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PIM1

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Yarrowia lipolytica (strain CLIB 122 / E 150)
Length
1177 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
129.478 kDa
Sequence
MIDNKVSVCSVGKVVITEVATFASHPLYIDRKTALTMIRSTRAASRLRLGARYYASHAPYGVLSEHLKRTPRTNSQHYYPPPQGAHDLPKVSSMGDSIASIVRGRELWVQEKDKSDKPEKSDKPDKTDKTDKDKPEKQDKDKTDKPEKTKVSHTPSSTASTGAGEAAAPPSAPPSGSGSSSSSGGGSPPAKKKKSPAQTYPEILAVPISDRPLLPGFHRALVIRDPNVMKAIDEMITRGEPYLACFFLKEFSNADVIQDASEVHDIGVIAEIQIQSQDHKRSTVDASNEPVYVLILYPHKRVRLNSLKNPPSSGGAVSYASVSEDVAEDGELLLTSKDLEGYSEEFLEAREEAKKAKSGKTEDSKHDSKVTSKDGKETTEKYDSSTLQESPYSFLSTYDVSTAAISLIEDKPHDKNNRVITTLTNEILNVFKMLRAEDATLREQLSSVVGDILRTEPAVLQEPGRLADFAAALCAGEGKEIQAVLTALDLETRLNRALILLKREHTNAKLQQKIARDVENKLNSKHKKFLLTEQMKAIKKELGVDDGKEKLVEKFNERAEKLDMPENIQKVFEEEMTRLQSMEPSSSEYSVTRNYLDWITQIPWNKTTEDRFNLPQAKDVLDSEHYGMKEVKDRILEFIAVSRMKGGLTGKILLLQGPPGVGKTSIGKSIAKALNRQFYRFSVGGTNDASEVKGHRRTYVGAIPGRLVQALKQTQTENPLILIDEIDKLSSSRTQGDPGAALLEALDPEQNNAFLDHYLDVPIDLSKVLFVCTSNDLSTIPWPLLDRMEVIEMSGYVPDEKLNIANQYLVPQSKKETGLENVNVQVTDDAINALNRQYCRESGVRNLKKHIEKIFRKVVVKIVGEYGQDEVAAEKIIDVEPVEKDKESAEKKTTKSKSKEVNEEPAAKEEKDKATESAESSETKVGTKAPPVTVPEDYSLTIDEKDLYDYVNSPPYSSDRMFEDPPPGVVMGLAYSPLGGSALYIECILDGGLSADSSARLSSTGNLGNVMKESTNIAYSFAKSFMIRNFPANRFFERAGIHLHCPAGAISKDGPSAGCAVVTGLLSLALNHPIDSSISMTGEISLTGKVMKIGGLREKAVGAHSAGAKTIIIPKDNSGDWDELPDTVKEGLTPVFAGTYQDVYDVVFQGLDTKVAAEVWKKQFDLIDRKLDKRGSK

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
1133 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner (PubMed:15870080, PubMed:16428434, PubMed:8146662, PubMed:8276800, PubMed:8354406, PubMed:8810243, PubMed:9405361, PubMed:9724747). Endogenous substrates include ABF2, ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized proteins. The 2 nucleic acid-binding proteins ABF2 and MGM101 are protected from degradation by PIM1 when they are bound to DNA (PubMed:16428434, PubMed:20150421, PubMed:28377575).
Similarity
Belongs to the peptidase S16 family.
Mass
127.112 kDa
Sequence
MLRTRTTKTLSTVARTTRAIQYYRSIAKTAAVSQRRFASTLTVRDVENIKPSHIIKSPTWQEFQHQLKDPRYMEHFAQLDAQFARHFMATNSGKSILAKDDSTSQKKDEDVKIVPDEKDTDNDVEPTRDDEIVNKDQEGEASKNSRSSASGGGQSSSSRSDSGDGSSKQKPPKDVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITDKNDVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKSKEQAKDTDTETTVVEDANNPEDQESTSPATPKLEDIVVERIPDSELQHHKRVEATEEESEELDDIQEGEDINPTEFLKNYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERIKSLKLPDSVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSKEQYSIPRAKKILDEDHYGMVDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSADSKPKESVSSEEKAENNAKSSSEKTKDNNSEKTSDDIEALKTSEKINVSISQKNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFAKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMATSFLSLALNKSIDPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVNTKEGNSVWKAEFEILDAKKEKD

Gene
pim1
Protein
Lon protease homolog, mitochondrial
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Length
1113 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
122.528 kDa
Sequence
MLRGQTLPWRAALQQVSRPFIPRPLLAPSRYNVTARSILNASRLHRSLPTSRAFSSSSIRRREKPPPGDEKDDPAQKEQKDANEEKDVERAPDARRKAADPSGKQGSSHEPGAPTSGFARRKEKAGADKEQRGLEEDSKKDGNAVEGKGNSSDTPSPIPVNGGSDSRPSGANNGGNEDGGKKGKKGSGEKALQKPSVPEVYPQVMAIPIAKRPLFPGFYKAITIRDPNVAAAIQDMMKRGQPYVGAFLFKDENADGDVIENLDDVYDVGVFAQITAAYPLRGEASGVTAVLYPHRRIKVSSLLPPSDAAKAGTTDEKTSERRGDVVASFEEGTAELAPKDHYEPTSFLRKYPVSLVNVENLAEEPYDKKSAIIRAVTSEIVNVCKEIASLNPLFRDQISAFYTDQFPGNLSDEPAKLADFAAAVSAGELNEMQEVLELMNIEERLPKALVVLKKELMNAQLQSKISKDVEAKIQKRQREYWLMEQMKGIKRELGIESDGKDKLVEKFKEKAEKLAMPDAVKKVFDEELNKLAHLEPAASEFNVTRNYLDWLTQIPWGQKSVENFGIQHAVKVLDEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCLVGPPGVGKTSIGKSIARALNRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEIDKIGRGHQGDPSSALLELLDPEQNSSFLDHYMDVPVDLSKVLFVCTANVTDTIPRPLLDRMELIELSGYVADEKMAIAQRYLAPAARELTGLKEVDVNLTEEAVEELIKSYCRESGVRNLKKQIEKVYRKAAYKIVRDLGEDVLAEEKALTDEGKAVQEESQKETESPDSKSPVDPEKSTTETPRVALKVPESVQLSIGKDSLTDYVGPPIFTADRLYDTFPPGVTMGLAWTSMGGAALYVESILENALTPQSRPGIDITGNLQNVMKESSQIAYSFAKSVMAKQFPENRFFEKAKLHMHCPEGAVPKDGPSAGITMATSLLSLALNHPLDPTIAMTGELTVTGKVLRIGGLREKTVAARRAGAKKIVFPADNMSDWLELPENIKEGIEGHAVGWYSEVFDLLFTDLDKGAANHVWQKQLAEKPEKKSNEVEEDE

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Length
1111 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
124.188 kDa
Sequence
MLRSSRSRLVTRNILLRQFKNGNNVRLMNATRFQHNGIVGNEKLASDSQKFVDESYHWMQYRKQMNDPVSRQRLEQLESQWVKSIQLKQDDKGKDIDQPESENRKKEEEQVPTEEKDNDTAKESETSQQRDSVAETQGPASTSGGASGNGESSGNGSGDDGNNGSGNGKPSKNAKQPFPEVYPQVMALPISRRPLFPGFYKAVVISDERVMKAIKDMSDRQQPYIGAFLLKDSTVDTDVIHKADEVYNVGVFAQVTSAFPSKDEKTGAETMTALLYPHRRIKLDELIPPTSEQNLKDESDVSKSEGVENNEQEVVKASLQKMENMKDVEEDDDENLTGFLKDYDVSLVNVSNLADKEFNPNSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEEELQEILESLDIEQRLEKALTVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIESFKDRVSKLQLPETVQKVFDDEITKLATLETSQSEFGVIRNYLDWITSLPWGIISKEQYSIPKAKKILDEDHYGMKDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARSLNRQFFRFSVGGMTDVAEIKGHRRTYIGALPGRVIQALKKCQTQNPLILIDEIDKIGHGGIHGDPAAALLELLDPEQNNSFLDNYMDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEEKVKIAENYLSPSAKKSAGLDNANVNITENAIVSLMKHYCRESGVRSLKKHIEKIYRKAALNVVKQLSIDDKPMENEEVKDQKDIKVKQSENKSSAEASTVESTTEENELIKTQKSHDNKGSLEVPETVSVTVDENNLKDYVGPPIFTTDRLYESTPPGVVMGLAWTSMGGCAMYVESVLEQPLTHSTQPTLERTGQLGDVMKESSRLAYSFSKMYLAKKFPENRFFEVAKIHLHCPEGATPKDGPSAGVTMASSFLSLALNKGLDPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLSDWAELPENVKEGLEPLAADWYEDVFQRLFGDVDTNKGNTVWSEDFKKIDEKRNKETK

Gene
pim1
Protein
Lon protease homolog, mitochondrial
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Length
1108 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
121.963 kDa
Sequence
MLRGQSLPWRAALHQTPRPTVLRPLLPFARNNGPVRSNLSISRLSRSPSLSPRAFSTSSIRRKEKPPSDEKEDSNLQEQKDPNEQKDSDRSPEGRRRSPDSTGREPGAPTSASGRRRDKVAGEKEQRGVEEDAKKENVSIEGKSDPTEDPSPIPVNGGGSSDTKSSASNGGNEDGGRKGKKGSGDRALQKPSVPEVYPQVMAIPIAKRPLFPGFYKAITIRDPNVATAIQEMMKRGQPYVGAFLFKDENADGDVIENLDDVYDVGVFAQITAAYPLRGEASGVTAVLYPHRRIKISSLLPPGEQSKAGNTEDKAPEKKGDVVASFEEGVAEPAPKDLYEPTSFLRKYPVSLVNVENLAEEPFDKKSAIIRAVTSEIVNVCKEIASLNPLFRDQISAFYTDQFPGNLSDEPAKLADFAAAVSAGELHEMQEVLEIMNIEERLPKALVVLKKELMNAQLQSKISKDVEAKIQKRQREYWLMEQMKGIKRELGIESDGKDKLVEKFKEKASKLAMPDAVKKVFDEEINKLAHLEPAASEFNVTRNYLDWLTQIPWGQKSVENFGIKHAMTVLDEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCLVGPPGVGKTSIGKSIARALNRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEVDKIGRGHQGDPSSALLELLDPEQNSSFLDHYMDVPVDLSKVLFVCTANVTDTIPRPLLDRMELIELSGYVADEKMAIAERYLAPAARELTGLKDVDVNLQKDAIEELIKSYARESGVRNLKKQIEKVYRKAAFKIVQDLGEEVLGEDKALTDEGKAAQEESKKETEEGDPKDPPADPEKSTTETPRLALKVPESVHLSIGKDSLTDYLGPPVFTADRLYDTFPPGVTMGLAWTSMGGAALYVESILENALTPESRPGIDITGNLQPVMKESTQIAYSFAKSVLAKQFPENKFFEKAKLHMHCPEGAVPKDGPSAGITMATSLLSLALDHPLDPTIAMTGELTVTGKVLRIGGLREKTVAARRAGAKKIIFPADNMSDWLELPENIKDGIEGHAVSWYSEVFNILFAELDKDAANKLWQKQLAGKPKKGPLEEDD

Gene
pim1
Protein
Lon protease homolog, mitochondrial
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Length
1107 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
121.2 kDa
Sequence
MLSRQRIPRILASRTSLAHSIRSFTSTTSSIRPVAAAGQHAVTRPRHERPTNLSSFSTYTALGKKNDKGFFDNSIEPLSEEERKANVEHAEAEAKEAESKQAKSKSSTSDAPPPAPEDGKAGAAGGSSAGSGSGADGGSGDGGKRGRKPGDKALAKPVVPEIYPQVMAIPIAKRPLFPGFYKAITIKDPNVAAAITEMIKRGQPYVGAFLFKDENADDDVIRNRDDVYDVGVFAQITSAFPMNNQNGEGASLTAILYPHRRIKLSELIPPGSPEAASIDGAKEGAAPEPVPEPIPKVTDESEQKGDVVASFEESAVTPRPEPSQKPYEPTSFLKKYPVSLVNVENLTEEPYDPKSQVIRAVTNEIVNVFKEVASMNSLFRDQISTFSMSQSTGNVMAEPAKLADFAAAVSAGEPAELQEVLSSLNVEERMHKALLVLKKEHVNAQLQSKITKDVEQKITKRQREYWLMEQMKGIRRELGIESDGKDKLVEKFKELADKLAMPEAVRKVFDDELNKLAHLEPAASEFNVTRNYLDWLTNIPWGQSSAENFDILNAVKVLDEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCFVGPPGVGKTSIGKSIARALGRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRVIQALKKCKTENPLILIDEIDKIGRGYQGDPSSALLELLDPEQNGSFLDHYLDVPVDLSKVLFVCTANLTDTIPRPLLDRMEVIRLSGYVADEKMAIAEKYLAPQAQEMAGLKGVDVQLTKDAIEELNKSYCRESGVRNLKKKIEQVYRKSALKIVQDLGEQALPESEALTEEGKAAQEETEKKKSEEAASGETSSPKAATEASEKETTEKPRVAMKIPEGVHVVINKDNLKDYVGPPIFTSDRLYDVTPPGVTMGLAWTSMGGAAMYVESILQSALTSKSAPSLEITGNLKTVMKESSAIAYSYAKAVMAKDFPKNRFFDKAKIHVHVPEGAVQKDGPSAGITMTTSLLSLALDTPIDPQIAMTGELTLTGKVLRIGGLREKTVAARRAGCKMVVFPEDNMSDWLELPENVKEGIEGRPVRWYSEVFDLIFPKLDREKANKSRIIEDDKSEKEESKKKNDDDE

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
Length
1104 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
120.467 kDa
Sequence
MLPLRAFARLAQRPRLSRPTQLARSSLPRPSPSRPAAHYLALAPAPSTRFLHSSPPVLKEKRWLNNTPPEDDGEDGQNPKQDDQVEKPLPDAESSKSAEERAKSQSSKPDIKASSSDSVSSSAPAPGSADGGSPPGAGGPKEVAKPVIPEIYPQVLAIPITHRPLFPGFYKAVTVRSPPVIKAIRELQAHGQPYVGAFLLKDSTVDSDVVTDINQVQPVGVFCQITSCFTSQEGEGKPEALTAVLFPHRRIKINELVKSSGTKGDGTVGVGGLVEGSQDSAKGEGEVKSFESEVPGVEEVREELGTVSIDSEQPDVHKENRDLETKEVTQIDFLHSLLPQVSLTNVSNLSTEPYEKDSQVIRAIMSELISVFKEIAQLQPMFREQVTSFAISNTSSQVFDEPDKLADLAAVVSTADVSDLQAVLSSTSIEDRLQRALVLLKKELINAQLQFKISRDVDTKIQKRQREYYLMEQLKGIKKELGMESDGKDKLVEGFKEKASKLAMPEGVRKVFDEELNKLVHLEPAASEFNVTRNYIDWLTQVPWGVHTPENYNISHAIKILDEDHYGLKDVKDRILEFMAIGKLRGSVEGKILCLVGPPGVGKTSIGKSIAKALGRQFFRFSVGGLTDVAEIKGHRRTYIGAMPGKPIQALKKVATENPLILIDEVDKISKAYNGDPASALLEMLDPEQNKSFLDHYLDVPIDLSKVLFVCTANVLETIPGPLLDRMEVLEVSGYVSAEKMNIAERYLSPQAKVAAGLEDVNIELEPGAIEALIRYYCRESGVRNLKKHIDKIYRKAAFKIVTDLGESGLPEPATPPAENQVEAQYPDIKPASELTSNVIPGTEVSGVDTKTDVTTVPREPMKVPAGIHVKVTQENLKDYVGPPLYHKDRLYTHSPPAGVSTGLGYLGNGSGAVMPVEINSMPGKGNLQLTGKLGEVIRESAQIAMSWVKSNAYLLGITKSEAEATLNDRDVHLHMPEGGIGKEGPSAGTAILTAFVSLFTKTRVDPDIAMTGEISLLGQVLPVGGLKEKILAAHRAGIKKLIVPAGCKPDIDENVPESVKGGIEFVFVEDVRQVLHEAFRGTEVEKRWQETLPMEEEPQRERH

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
Length
1104 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
120.556 kDa
Sequence
MLPLRAFARLAQRPRLSRPTQLARSSLPRPSPSRPAAHYLALAPAPSTRFLHSSPPVLKEKRWLNNTPPEDDGEDGQNPKQDDQVEKPLPDAESSKSAEERAKSQSSKPDIKASSSDSVSSSAPAPGSADGGSPPGAGGPKEVAKPVIPEIYPQVLAIPITHRPLFPGFYKAVTVRSPPVIKAIRELQAHGQPYVGAFLLKDSTVDSDVVTDINQVQPVGVFCQITSCFTSQEGEGKPEALTAVLFPHRRIKINELVKSSGTKGDGTVGVGGLVEGSQDSAKGEGEVKSFESEVPGVEEVREELGTVSIDSEQPDVHKENRDLETKEVTQIDFLHSLLPQVSLTNVSNLSIEPYEKDSQVIRAIMSELISVFKEIAQLQPMFREQVTSFAISNTSSQVFDEPDKLADLAAVVSTADVSDLQAVLSSTSIEDRLQRALVLLKKELINAQLQFKISRDVDTKIQKRQREYYLMEQLKGIKKELGMESDGKDKLVEGFKEKASKLAMPEGVRKVFDEELNKLVHLEPAASEFNVTRNYIDWLTQVPWGVHTPENYNISHAIKILDEDHYGLKDVKDRILEFMAIGKLRGSVEGKILCLVGPPGVGKTSIGKSIAKALGRQFFRFSVGGLTDVAEIKGHRRTYIGAMPGKPIQALKKVATENPLILIDEVDKISKAYNGDPASALLEMLDPEQNKSFLDHYLDVPIDLSKVLFVCTANVLETIPGPLLDRMEVLEVSGYVSAEKMNIAERYLSPQAKVAAGLEDVNIELEPGAIEALIRYYCRESGVRNLKKHIDKIYRKAAFKIVTDLGESGLPEPATPPAENQVEAQYPDIKPASELTYNVIPGTEVSGVDTKTDVTTVPREPMKVPAGIHVKVTQENLKDYVGPPLYHKDRLYTHSPPAGVSTGLGYLGNGSGAVMPVEINSMPGKGNLQLTGKLGEVIRESAQIAMSWVKSNAYLLGITKSEAEATLNDRDVHLHMPEGGIGKEGPSAGTAILTAFVSLFTKTRVDPDIAMTGEISLLGQVLPVGGLKEKILAAHRAGIKKLIVPAGCKPDIDENVPESVKGGIEFVFVEDVRQVLHEAFRGTEVEKRWQETLPMEEEPQRERH

Gene
pim1
Protein
Lon protease homolog, mitochondrial
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Length
1104 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
121.838 kDa
Sequence
MLRGQTLRWRAALQTPRSLILRPLFAPGGYNVGPRSVLETSRRFRSLPPSLRTFSSSTARRKEKPPPGDEKEDSNKKENKDNDDGTEDKEVERDPRRKQADSSGKHGSSVDPGAPTSGFARRREKAADRDQRSVTEDAKREAEAKGNSSDTPSAIPVSDSSSESKPSGSHNGGDDGGKKGKKNDKALQKPSVPDVYPQVMAIPIAKRPLFPGFYKAITIRDPNVATAIQEMMKRGQPYVGAFLFKDENADGDVIESTDDVYDTGVFAQVTAAYPLRGEQSGVTAVLYPHRRIKISSLIPPGDSTKSGNSEDKTTEKRGDVVASFEENAAELVTKDHYEPTSFLRKYPVSLVNVENLTEEPFDKKSAIIRAVTSEIVNVCKEIATLNPLFRDQISAFYTDQFPGNLSDEPAKLADFAAAVSGGELHELQEVLESMNIEERLPKGLVVLKKELMNAQLQTKISKDVEAKIQKRQREYWLMEQMKGIKRELGIESDGKDKLVEKFKEKAEKLAMPEAVKKVFDEELNKLAHLEPAASEFNVTRNYLDWLTQIPWGQKSVENFGISHATDVLNEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCLVGPPGVGKTSIGKSIARALNRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEVDKIGRGHQGDPSSALLELLDPEQNSSFLDHYMDVPVDLSKVLFVCTANVTDTIPRPLLDRMELIELSGYVADEKMAIAQKYLAPAARELTGLKNVDVTLTEEAIEELIKSYCRESGVRNLKKQIEKVYRKAAFKIVSDLGEDVLAEDKALTAEGKAAQEESEKETGPIESTSEQEKATTENPRVALNVPDSVHLSIGKDSLTDYVGPPIFTTDRLYDTFPPGVTMGLAWTSMGGAALYVESILENALTPESQPGLDITGNLQNVMKESTQIAYSFVKSVMAKQFPENRFFEKAKLHMHCPEGAVPKDGPSAGITMATSLLSLALNHPLDPTIAMTGELTVTGKVLRIGGLREKTVAARRAGAKTIIFPADNMSDWLELPENIKSGIEGHAVSWYSEVFDILFADLDKQAANRVWQKQLSKEPKKSNDKDDH

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
Length
1086 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
120.08 kDa
Fragment
single
Sequence
MLRTSCTSSLRRVVGKYVVSPLVASQIRFATSSVRSQPYLLNSELTELPAQFKRYSSILLTEKPEGDVPESGPEPSGESGISEKSNVENDKHDGNDEIKPEAEKNEKDEIEKPEIDKDAIVETDGVSESSVENVSGSSSAAGGASAPPSGNSNNNNNNNNNNNDNDEPNEIVTNAGTGLYPPLLAIPMKDRPPLPGRPFAINITDPEVIRSIYTIIDKREPYFVLFHVKDPNEGDTDVINSKDSVYNIGVHCQIIRHTTPRPGVFNVLGYPLERCSLADLSTPSEKKGETETRKEGENFPTSYLKGLKVSYATVKPVKDEPFDKTSTDIKSLVESLKALLSKMGAKNPLEKLQIKEGTELVNDPPRFADFVGSTIHGDPKKIQEILESLNIQTRLSKALELLKVELKASLIKENTIHNLSTKADEYQTRLFIKEFIKELQKRAGIVESDDKKTSKFDERLKHLKMTEEALEAYNAEKAKMESQNEHSSELGVSERYLDWLTSIPWGIYSKDRFNIKQAREILDRDHYGLKDVKDRILEFISMGRVSGKVDGKILCLTGPPGTGKTSIAKSIAESLNRKYVRIAMGGIQDVHEVKGHRRTYVGSIPGRIISALKQAKTSNPLMLIDEIDKLDLSRSGGASSAFLEILDPEQNNAFVDNYIDVKVDLSKVLFVCTANYLGNISPPLRDRMEIIEVNGYTNNEKIEIAKRHLIPDAAKKAGLEGGHVVIETKTISRLIEKYCRESGLRNIKKLITRIFSKASLKIVEEVEAREGESKSKSEEAKSEAITGSVTEISVEDATVKAQSIEEPSVESASQKVDEAKPVESEELKSDEEEEEVVKLEIPDDIKLEITSANLKDYVGPEIYTRDRVYDIPPPGVATGLSYSTSGNGDALYIESILTHSIGSGSGHASIHVTGSLKDVMKESASIAYSFAKSYMVKNYPENRFFEAAEIHVHCPDGAIPKDGPSAGISFTSSLISLALQKPLPPTIAMTGEITVTGRVLAVGGLREKILGAKRYGCNTIIFPKDIENELEEIPEEVKEGVKFIPVEWYQDVFDEIFPNLSSDEGNEVWKEEFNKLDKKKASNKKK

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
Length
1079 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
119.97 kDa
Sequence
MLRPRTYVRKLAWRCPRKSQLGLRLATSVSSHKSLPLPMNFDISHSQSAFRAYQDIIHRNKSVGDDEPSQRSENENNPSESDKDSNQDPETPKKDKESENDKEPEKEKDIENDNKVSSESNENVTLASSNTGGAAPPNGNNNGDDPDDSNPSLPVDPVTGLYPPLLAIPMKDRPPLPGRPFAINVTDPEVIRSIYTIIDKREPYFVLFHVKDSNEPDTDVINKKDSVYDIGVHCQIIRHTTPRPGVFNVLGYPLERCKLEELTTPSSEKEAKSEEPSKEDAESFPTSYLKGLNVSYATVKPVEDEPYDKSSAEIRSLVESLKTLLSKMGGKNPLEKLQIKEGTDLISDPSKFADFVGSTIHGDPKKIQEILETLNIETRLSRALELLKVELKASLIKESTIHNLSTKADEYQTRLFIKEFIKELQKRAGISESEDKKTSKFDERLKHLKLTEEAMEAYNAEKAKMENQNEHSSELGVSERYLDWLTSIPWGVYSKDHFNIKQAREVLERDHYGLKDVKDRILEFISLGKVSGKVDGKILCLAGPPGTGKTSIAKSIAESLNRKYVRIAMGGIQDVHEVKGHRRTYVGSIPGRIISALKQAKTSNPLMLIDEIDKLDLSRGGGAASAFLEILDPEQNNSFVDNYIDVKVDLSKVLFVCTANYLGNIPAPLRDRMEIIDVSGYTNNEKIEIAKRHLIPEASKKAGLETNHVSITNETISRLIEKYCRESGLRNVKKLITRIFSKASLKIVEEIEAKEALDSSKEKEGVTASSEEANVNSESTKSNTSQAEPVAESSTDISTKSKVASEKIETKEKKETNKENGQSEEDQQPEPKFVIPEDIKLEITPANLKDYVGPEIYTRDRVYEFPPPGVATGLSYSTSGNGDALYIESILTHSIGSGSGVPGMHVTGSLKDVMKESASIAYSFTKSFMAKNYPDNRFFEAADIHVHCPDGAIPKDGPSAGISFTSSLVSLAINESLPPTVAMTGEITVTGRVLPVGGLREKILGAKRYGCDTIIFPKDIENELEEIPDEVKDGVTFIPVEWYQEVFDKIFPNATAQKCNEVWKEEFAKLDSKKKNKKK

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876)
Length
1078 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
120.913 kDa
Sequence
MIKASKCNKPRALFLVRVSIPRTFIRNATSAVPTTIKLNDLASLPPITKSLPTNLPFLMPDTLQSLLRFDSEKEKQPSTDKSNDKDKPSRKEKGKDKEKENEEKKDINMDEKYEINEETDTKPTIDPNNPVSSKSNISSSSGGDNNNNNNNNNNNNDSDGKNDDGSPKDKEFLSPSDSGLHPPFLAIAMKDRPFLPGATRHLHVSDPEVIKCVNHMINSNIKSPYFVLFHVRDTNSEDAALDVIKDRDFVHEVGTLCQIIKTTGSEILVYPHYRVKLVDISTPNSRSESIEKEQDNSQTSYLKKFEVSYAVTQQLKDEPYDEQSITINAWTRRIKELYEKLAPKYDQPENKEEIMSNPSMLADFIASKVHAKPEQIQEILESSNVETKLELSLQLLQVEADADEMRQTALKNIRERTEKAYAQSLIKEYTKELLKAAGIGENSKVHKFDERIKHLKMPEEAMKAYKTEKERLGTQSDMEQNVVERYLDWLTQIPFGVYTKDSFNVKKAREILDRDHYGLKDVKDRILEFISVGKISGNVDGKILCLAGPPGTGKTSIAKSIAEALNRKYTRIAVGGVQDVHDVKGHRRTYVASIPGRIVTALTQAKTSNPLMLIDEIDKLDTTSHGGAARAFLEILDPEQNNSFVDNFIEVKVDLSKVLFVCTANYLGSIPGPLRDRMEIIEVNGYTKNDKIEITKRHLIPAAAKKVGLDEGRVVIPDETISRLIDKYCRESGLRHIKSLINRIFSKASRKIVEELEETDVDSHNKDTVEGTLVAKESEKVISDKAKIDTENSPIEYIQSNTEVKAETTTESQQEQEKEKEKDEEIKKLDLPADLKIEVKPETLKDFVGPEIYIKDRLYETLNPGVATGLAYNTSGDGDALYIESILTDSISSDLGNAGLHVTGSLKDVMKESASIAYSFAKQFMVRQFPDNRFFEAAHIHVHCPGGAIPKDGPSAGIAFTSSLVSLALNKSLPNDTAMTGEITLTGKVLAIGGLREKSLGAKRAGYTKIIFPKDCEYQLDEIPDEVKEGLTYIPVEWYSEVFEHLFQGISKEEGNSVWKEEFAKLEDKKKSKKTNTK

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
Length
1073 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
120.378 kDa
Sequence
MIKASKCNKARALFLVRTSIPRTFIRNATSAIPTTVKLKDLSSLPPLTKSLPTNLPFLMPDTLHNLLRFDSKKEKQPSTDKSNDKDKPSRKEKGKDKEKENEERKDINEDEKYDIKEETDSKPTIDPNNPVSSKSSISSSSGGANNNNNNDDSDGRDDDGSPKDKEFLSPSDAGLHPPFLAIAMKDRPFLPGATRHLHVTDPEVIKCVNHMINSNIKSPYFVLFHVRDTNSEDAALDVIKDRDFVHEVGTLCQIIKTTGSEILVYPHYRVKLVDISTPNSRSERIEMEQDNSQTSYLKKFEVSYAVTQQLKDEPYDEQSITINAWTRRIKELYEKLAPKYEQPENKEEIMNNPSMLADFIASKVHAKPEQIQQILESSNVETKLELSLQLLQVEADADEMRQTALKNIRERTEKAYAQSLIKEYTKELLKAAGIGENSKVHKFDERIKHLKMPEEAMKAYKTEKERLGTQSDMEQNVVERYLDWLTQIPFGVYTKDSFNVKKAREILDRDHYGLKDVKDRILEFISVGKISGNVDGRILCLAGPPGTGKTSIAKSIAEALNRKYTRIAVGGVQDVHDVKGHRRTYVASIPGRIVTALTQAKTSNPLMLIDEIDKLDTTSHGGAARAFLEILDPEQNNSFVDNFIEVKVDLSKVLFVCTANYLGSIPAPLRDRMEIIEVNGYTKNDKIEITKRHLIPAAAKKVGLEEGRVVIPDETILRLIDKYCRESGLRHIKSLINRIFSKASRKIVEELEDTDADPHSREIVEESLVAKENESVISDKAKKDAGSSSIESNDSNTEAKVSTTTENEKKQEQKQKQDEEIKKLDLPADLKIEVKPETLKDFVGPEIYIKDRLYETLNPGVATGLAYNTSGDGDALYIESILTDSISSDLGNAGLHVTGSLKEVMKESASIAYSFAKQFMVRQFPDNRFFEAAHIHVHCPGGAIPKDGPSAGIAFTSSLVSLALNKSLPNDTAMTGEITLTGKVLAIGGLREKSLGAKRAGYTKIIFPKDCEYQLDEIPDEVKEGLTYIPVEWYSEVFEHLFKGISKEEGNSVWKEEFAKLEEKKKSKKTHTV

Gene
pim1
Protein
Lon protease homolog, mitochondrial
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
1067 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
118.642 kDa
Sequence
MITRLSGACLRRSGAKRNWPREHLVHRSLLASFSTTQRVLKCSVGPFRTSNVVFKSKEPKDNKPLDNKNDPKKTHNEDESHTNESLPSTDKKKKKDNDDFKQNLKSSSNKTEEKYSATQASKSKNDEFELGGEENEDEMPLNGEFNKNVPAKYSVPDVYPQLLALPIARRPLFPGFYKAIVTKNPSVSEAIKELIKKRQPYIGAFLLKDENTDTDVITNIDQVYPVGVFAQITSIFPAKSGSEPALTAVLYPHRRIRITELIPPKEDADSAASSDAAELETDKSSNLSSNGEVKSDLKQDNGKEEPEKEVESTPSILQNFKVSLVNVENVPNEPFKRQDPVIKAVTSEIMNVFKDIANVSPLFREQIANFSISQTSGNVFDEPAKLADFAAAVSAADHRELQEVLEATNIGDRLQKALYVLKKELLNAQLQHKINKEIEQKITQRHKEYLLTEQLKQIKRELGQELDSKEALVTEFKKRTESLSMPDHVKKVFNDELSKFQHLEPMAAEFNITRNYLDWITQLPWGKRSVENFDLDHAKEVLDRDHYGLKDVKDRVLELVAVGKLRGTMQGKIMCLVGPPGVGKTSVGKSIASALNREFFRFSVGGLTDVAEIKGHRRTYIGAMPGKIVQALKKVQTENPLILIDEIDKVGKSHQGDPASALLELLDSEQNSAFLDYYMDIPLDVSSVLFVCTANTIDTIPPPLLDRMEVIELSGYVSAEKVNIAKGYLIPQAKAACGLKDANVNISDDAIKGLISYYAHESGVRNLKKSIEKIFRKTSFSIVKEIDDELNSKEKSTGKSGKKTSPQSSEDAANKEASSVPLKVPDKVNIEIEEKDLTKYLGPPIYTSQRLYDTTPPGVVMGLGWTPMGGVSMYVETIVKNILSSNSTPSLERTGQLGDVMKESSEISYSFSKSFLSKHFPNNKFFEHARLHMHCPEGSISKDGPSAGITMATSLLSLALDTPVPATTAMTGELTLTGKILRIGGLREKTVAAKLSGMKEILFPKSNLADWEQLPDYVKEGLTGVPVAWYDDVFKRVFSNIDAEKCNNLWPNLIKSSSKQHQISPSH

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
Length
1058 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
116.15 kDa
Sequence
MLTRIRNAGVGGNAARRVRLLAGYTGARMAHAAALNSTTGAGGAARAAGAGRRAHSDVHVWALRQQSGIHRGGQCILKQDREPDQSDDKKVPPRAEEGRDEEAVRDEEAERQPREEQANRSSEASSSRGSGGSASSAGGGGRSNPPSEGEVPRKYEELMVLPMSNRPLFPGYYKSVTVYDPAVIEAICGLLRRNIPYLGAFLLKDRSMDKDSIDSIEEVHRVGVFAQITSVHHGVDVDGRKAMSMVLYPHRRVQLDELVSTPKLVAEAKEKATDDGLVQAKKEKFRDMSEGGEEEENPTEFLLETGVTVGNFSDHLDLPVDHSSVMLNALTSETLNTFKHLSSINATVKQQLIALSSITTSLKPNIFESPSLLADFAAAISVGDPNELQDVLETRDVEQRLEKALVFIKKEVYVAELQQKIEKETDAKVQKRYKDQVLTEQMRGIKKEMGVEDAKDKAIATFRERAEKLKFPEHVKKIFDEELARLSGLESAMSEYSVTKNYLDWITSLPWGIASTDQYSILSARKVLDNDHYGMQDVKDRILEFIAVGKLKGQIDGKIICLVGPPGVGKTSIGQSISRALNRTFFRFSVGGMSDVSEIKGHRRTYIGALPGRLIHALKRCQTENPLILIDEIDKLGRTGHQGDPASALLELLDPEQNKTFLDTYLDFPVDMSKVLFVCTANTLDTIPRPLLDRMEVIELSGYVADEKVKIAERHLIPAAKKSTGLGSANINLTSDSIVALLKNYCRESGVRSLKKHIEKIYRKAALKIVQQLSIDDTPKSAPAETNIEPENGKPDASAKPLTNNLPAPEPLNIPDSVKIDITPETLVEYLGPPVFTADRIYEKTPAGVVMGLAYTYLGGCTMYVESVLGQPLSKDSNPSLEHTGQLGDVMKESSRLAYSFSKMFMSRRFPNNRFFEKAAIHLHCPEGATPKDGPSAGITMASSLLSLAMNKPLDPTIAMTGELTLTGKVLRIGGIKEKTVAAKRSGAKTIIFPKDNMADWEDLPAHVKEGLIPVAAEWYDDVFNVLFGSVTEEEGNNVWKDQFDLIERSKATASSSN

Gene
PIM1
Protein
Lon protease homolog, mitochondrial
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Length
1026 amino acids
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Similarity
Belongs to the peptidase S16 family.
Mass
114.998 kDa
Sequence
MLGTRVTRAVYTRAPLKLQLRALGLHRRYVHNGSKNDEGSSTSTTTNKEENDKKLPDVYPQMLALPISRRPLFPGFYKAVVISEPRVMKAITDMVERQQPYIGAFMLKDSNNDTDIIHDISEVHELGVLAQVTSAFPSKDEKTGKETMTALLYPHKRIKIDQLIPPKDVKIEDIVVEKVVDNEVASEETKDEETVDKTESATDKVSEEITEEIAKAPSTEVTEDPDNYENPTDFLKDYNVTLVNVSNLEDEPFDIKSPIINALTSEILKVFKEISQLNSMFREQIATFSASIQSATTNIFEEPAKLADFAAAVSAGEEEELQEVLESLNIEQRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQKEYYLMEQLKGIKRELGIDDGRDKLVDTYKKRVEKLNLPENVQKTFDEEITKLATLETSMSEFGVIRNYLDWLTSLPWGINSKEQYSIPRARKILDEDHYGMKDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSISRALNRQFFRFSVGGMTDVAEIKGHRRTYIGALPGRIIQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLDTIPRPLLDRMEVIELTGYVAEDKIKIAEQYLVPSAKKTAGLQNATVSMDEEAINALMKYYCRESGVRNLKKHIEKIYRKAALEVVKKMSIEDTEPLVSTSEEPQLSQTNQNISSSSAEDSTTDLEDSVNPDTAKEASKPNNSQEGASVEETKKAVKTEEEEDTSMIVPEDIKVEITPEDLKKYVGPPIYTTDRLYETTPPGVIMGLAWTNMGGCSLYVESVLEQPLHNCKHANLERTGQLGDVMKESSRLAYSFSKMYLSKKFPENRFFEKAAIHLHCPEGATPKDGPSAGVTMATSFLSLALNKPVDPTVAMTGELTLTGKVLRIGGLREKVVAAKRSGAKTVIFPKDNLNDWEELPENVKEGMEPLAADWYDDIYKRLFSGVKKSEGNNVWKSEFELIDKKKKEND

Gene
pim1
Protein
Protein pim1
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
539 amino acids
Function
Promotes the exchange of Ran(spi1)-bound GDP by GTP. Involved in the control of mitosis. Regulates a variety of nuclear events, including mitotic check-point, chromosome decondensation and mRNA processing/transport.
Mass
58.349 kDa
Sequence
MTSNRSTRSSTKREEVSKNGVEKRELDESDVMKNGKKPVKRAKVSSLPKPVRVPGSAKRINKIPELPTERLNVYVFGSGSMNELGMGEEEMDVVYRPRLNPILSTDKVGVVDLAVGGMHSAALSHDGRVYTWGVNDDYALGRLTKDQKDENGDKVDNDLLEGTPSKVEGALSHLRVTKVICSDNLTAAITDNGCCFTWGTFRCSDGVLGYSDSQKRTAEPTQMRLPEICQLATGTDHIIALTTTGKVYTWGNGQQFQLGRRMLERRRLQGLTPQPLALKNIISVGAGSYHSFAIDNKGRVYAWGLNITRQCGIEVEDEEEGAVITKPTLVDALEGYNVKSITGGEHHTLALLEDGRVLAWGRDDRHQLGIPDNALPETVVKDEKGNNYYLSTPTIIPGLTNVIQVVCGTHHNLAVTSDGKVYSWGSAENYEVGQGDNDEDVAVPTLVRSKAIKEVAIRVAGAGGQFSIIAGIPNASEEPVANGIKSEPENEKKLKTEETSKTDDSPVTDAKPDVTSNGEPSTATSESKDSVLEPSSTTA

Gene
PIM1
Protein
Serine/threonine-protein kinase pim-1
Organism
Bos taurus
Length
313 amino acids
Function
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3 protein binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity).
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Mass
35.63 kDa
Sequence
MLLSKINSLAHLRAAPCSDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHDCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIVRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK

Gene
PIM1
Protein
Serine/threonine-protein kinase pim-1
Organism
Felis catus
Length
313 amino acids
Function
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3 binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity).
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Mass
35.686 kDa
Sequence
MLLSKINSLAHLRTAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPSFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK

Gene
PIM1
Protein
Serine/threonine-protein kinase pim-1
Organism
Homo sapiens
Length
313 amino acids
Function
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Mass
35.686 kDa
Sequence
MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK

Gene
Pim1
Protein
Serine/threonine-protein kinase pim-1
Organism
Mus musculus
Length
313 amino acids
Function
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3 binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity).
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Mass
35.451 kDa
Sequence
MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK

Gene
Pim1
Protein
Serine/threonine-protein kinase pim-1
Organism
Rattus norvegicus
Length
313 amino acids
Function
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-protein binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity).
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Mass
35.631 kDa
Sequence
MLLSKINSLAHLRAAPCNDLHANKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIVKGQVYFRQRVSSECQHLIRWCLSLRPSDRPSFEEIQNHPWMQDVLLPQATAEIHLHSLSPSPSK