clu

Protein clueless

1494 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

164.45 kDa

MALEIDAKNATAATGDAGGATGGKAKAKENKTNNNNNAAGEKNLVNGSSSSSAAAAAKKKGKKNRNKSPPQQDAIEAEAGAALSNGHAVNGVGDGDADAADANANVLADKPDKATAAAEEKSATPDDEAAAAVAAGDDADLDALNDIGITVNISSPGTDVLSVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKTIEPLEQGSTIRVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPDYVTPGVREPPLLPLHPNIKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFYINQSTDDNFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQAIQKRRTMRHAFERVATPYQVYQWSAPQLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDAKMQMFIWNNIFFSLGFDVRDHYKELGGDHAAFVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRLAGKHLKILPHSVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLEDVQMSKDLSEMGFPIEHRHKLCCLRQELLEAFIEDRYVTFIRIAAAHLQRLNAKKQADKDLPEEQSTEKPTEQSAEKDPMEKEQDKEKEKDKEAKPNTSSTETKSAEAMVNAIREAQSNVAVSNEVQAAEVVKRACATVGSLKEKEFDFRFNPDVFSPGIRHIDGPDGGGQSLAKQKRLVQDAAEFLVLKQIPAFIKEHTAHSSPPIDGQSLTESLHSHGINVRYLGKVIKMLGQMPRMDYLHRIAILELIVRATKHIYYTYMQSTEPLHLSAAISHFLNCLLTTGPVNPAVSSEEVHKKQLRNNGGKHNKHNKSSKSQAKPQSSSSSSSSAAASTQNGGNNHNSNNSTAAAAGAASSSSASNNSSADWTLVTPRSLWQQIRKETKAYWNFELDCDSVETAGAKYGFLRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPVVKHISPRATDAYNFYTTGQAKIQQGLLKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAGDALAIQQRAVIMSERVNGIDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNRKYFGDKAMHVAVSYHLMARTQSCMGDFRSALSNEKETYSIYKSQMGEKHEKTRESAECLRLLTHEAVALQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLEMLNTINGILFVHISQKDIVKVRSEIEKHLKTNTDENEITDALKTIVAAANNNENATETTKDEGAAAAGAAPGAGETPVQLTNGGGEETTATATATVSS

clu

Protein clueless

1487 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

164.596 kDa

MALEIDAKNAAAAATGDGGAPGKAKAKENKSNSNSNNNNVPAAGEKNLVNGSSAATKKKGKKNRNKSPPQQDVSAAGAALSNGHAEKASVNGDAADANANVLDKKVEEEGATAAAGATEAAAEVGSSGDGGAATEGEAAASGEDVDLDALHDVGITVNISSPGADVLSVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKTIEGLEQGSTIRVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLITITQGDLLDKKRTRPDSVDCTPPDYVIPGVREPPLLPLHPNIKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFYINQSTDECFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWSAPQLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDPKMQMFIWNNIFFSLGFDVRDHYKELGGDHAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRLAGKHLKILPHSVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELTDMGFPIEHRHKLCCLRQELLEAFIEDRYVTFIRIAAVHLQQLNAKKQAEKELPSITEKQEEPEKEQAEKSSAEQPEKEKEKEKDKEDEQKESKPSPTETKSAEAMVNAIREAQSNVAVSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHVDSPESGAQSLAKQKRLVQDAAEFLVLKQIPAFIKEHMAHSSPPIDGQSLTESLHSHGINVRYLGKVIKMLSQMPRMDYLHRIAILELIVRATKHIYYTYMQSTEPLHLSAAISHFLNCLLTTGPVNPAVSSEEVHKKQSRNNGGKHNKHNKSNKSGKPQSTSAAAATQNGHSSTAANGSANSAANTASTSGNSNYDWTLVTPRSLWQQIRKEIKSYWNWELDCDSIESACAKYGLLRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPVVKHISPRATDAYNFYTTGQAKIQQGLLKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLVCGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGNKAMHVAVSYHLMARIQSCMGDFRSALNNEKETYSIYKSQLGEKHDKTRESAECLRLLTHEAVALQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLEMLNTINGILFVHISQKDIVKVRSQIEKHLKTSDESGPNDDNEVTAALKTFVAAINYNDTEQPKEGSEVEGATATQLTNGSEDSTTTVSS

clu

Protein clueless

1465 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

161.824 kDa

MALEIDAKNAAATGDAGTIGKAKAKENKNHNNNNNAPAAGEKNLVNGSSAATKKKGKKNRNKSPPQNAVEAEASAALSNGHSENGDAADANANVLAEKGEGVAAGAVVGDGAEGGASAEGAVAEGDAAAAGEDVDLDALHDIGITVNISSPGTDVLSVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKTIESLEQGSTIRVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPDYVTPGVREPPLLPLHPNIKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFYINQSTDECFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQAIQKRRTMRHAFERVATPYQVYQWAAPQLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDAKMQMFIWNNIFFSLGFDVRDHYKELGGDHAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHSVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELTEMGFPIEHRHKLCCLRQELLEAFIEDRYVTFIRIAAVHLQQLNAKKQAATANAEKELPAIAEKQEEPNEEQPEKTEEQPAEKEESKPTPSETKSAEAMVNAIREAQSNVAVSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHVDGPDGGVQSLAKQKRLVQDAAEFLVLKQIPAFIKEHMAHSSPPIDGQSLTESLHSHGINVRYLGKVIKMLGQMPRMDYLHRIAILEIIVRATKHIYYTYMQSTEPLHLSAAISHFLNCLLTTGPVNPAVSSDELHKKQPRNNSGKHNKHKAAKASKPQAAAAQNGNATAAGSGGAGATTSGATSSNSDWTLVTPRSLWQQIRKEVKAYWNWELDCDSIESAGAKYGLLRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPVVKHISPRATDAYNFYTTGQAKIQQGMLKEGYELISEALNLLNNVFGAMHQENDSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGNKAMHVAVSYHLMARIQSCMGDFRSALNNEKETYSIYKSQLGEKHEKTRESAECLRLLTHEAVALQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLEMLNTINGILFVHISQKDIVKVRSEIEKHLKTNTDENDVPDESEITSALKTIVAAVNNNDNASETEQPKDEASAAGTPTQLTNGSEESTATVSS

clu

Protein clueless

1452 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.882 kDa

MALETEAKNSNATATSDATATKASGKAKETNNTAGGKKNLNPIPNSNHQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPPEPTTEAVLSNGHAEKSTLVDAVEDNADADANANVEKPEDGGAPDAEADGEDIDLDALQDVGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNATLDNFAELKAISNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKKTRPDSVDCTPPEYVTPGVSEPPLLPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEEKRFHISACSKGFYINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWASPTLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDPKMQMFIWNNIFFSLGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHAVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVSFIRIAAVHLQQLNAKKQSEKAEGNPVPALEGAEAVSKVNGADKTDVKEEKNEENEKAQSTAGDTKTAEAMVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHVDGEEGTCSSLAKQKVLVQEAAEFLVLKQIPAFVKEHMTHSSPPIDGQSLTESLHSHGINVRYLGKVIKILNQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQATGNQNGSSSGSSNGSSVSDWTLMTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPVVKHISPRATDAYNFYTTGQAKIQQGMFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKAMPVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTKDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKADSPENEVNDAISSIVAAANNNGEAEDAVPKDVEEQKEAGTQLTNGEKAAATEATSS

clu

Protein clueless

1451 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.766 kDa

MALETEAKNSNATATGDATATKASSKAKENNNTAGGKKNLNPIPSQQNSNQNLVNGNGTAADGPAGKKKGKKNRNKSPPEPTTEAVLSNGHAEKSTAEYAAEDNADADANANVEKPEDGGAPDAEADGEDIDLDALQDVGITVNISSPGADVLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNATLDNFAELKAISNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKKTRPDSVDCTPPEYVTPGVSEPPLLPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEEKRFHISACSKGFYINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWASPTLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDPKMQMFIWNNIFFSLGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHAVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVSFIRIAAVHLQQLNAKKQSEKTEGKPVPALEGADAASKVNGADKTDVKEEKNEENEEKAQSTTGESKTAEAMVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHVDGEEGTCSSLAKQKVLVQEAAEFLVLKQIPAFIKEHMTHSSPPIDGQSLTESLHSHGINVRYLGKVIKILGQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQTTGNQNGSSSGTSNGSSVSDWTLVTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDDDVVNVFPVVKHISPRATDAYNFYTTGQAKIQQGMFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKAMPVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTRDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKADSPENEVNDAINSIVAAANNNGEAEDADPKDVKEQAQAGTQLTNGEKAAATEATSS

clu

Protein clueless

1450 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

161.078 kDa

MALETDAKNSNAVAPGDAATVATTKAKENNSSAGKKQQQQQQPNQNQNLVNGNGNAADGPAAKKKGKKNRNKSPPEPAAEPVEASLSNGHAEKTTSEEGGDTAAPDTNANVGEKSEDGGGAAPGSELETEDIDLDALHEVGITVNISSPGADILSVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKTIEQLEQGSTIRVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKKTRPDSVDCTPPEYVTPGVSEPPLLPLHPNIKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFYINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTTRHAFERVATPYQVYQWASPVLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDAKMQMFIWNNIFFSLGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLDLLRQAGKHLKILPHAVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLPEVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRYVSFIRIAAVHLQQLNAKKQSEKTEEKALPALEEAEKESSETKEAEAEKPVEKKEEEKQQPSSNETKTAEAMVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSNGIRHVDGEEGTCSSLAKQKVLVQDAAEFLVVKQIPAFIKEHLAHSSPPIDGQSLTESLHSHGINVRYLGKVIKLLAQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTTGPVNPAVSSEEAHKKRSNGNKHNKHKSKGNKQQASGNQNGSSAGSSSGGSSSSSDWTLVTPRSLWQQIRREAKSYWDWELDCDSIETAVSKYGILRISLLRAFCLKVGIQVLLREYNFESKHKPTFGDEDIVNVFPVVKHISPRATDAYNFYTTGQAKIQQGMFKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNIKYFGSKAMHVAFSYHLMARTQSCMGDFRSALNNEKETYSIYKSQVGEKHEKTRDSAECLRLLTQQAVLLQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVQISQKDIVKVRSEIEKHFKANSAENEVNDAIKSIVAAANNNGDTEAETKDATKDNKDLAGASTQLTNGDKDAETAVASS

clu

Protein clueless

1448 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.852 kDa

MALETEAKNSNATATGDATATATKASGKAKENNNTAGGKKNLNPNSNQQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPTEPTTEAVLSNGHAEKPTVVDAVEDNADTNANVEKPQEGGAPDAEADGDDIDLDALQDIGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKSINNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPEYVTPGVSDPPILPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFFINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWAAPILEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDTKMQMFIWNNIFFSMGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVVDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHVVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVNFIRIAAARLQQLTTIKQSEKSEANPVPALEGAEAASKVNGAEKPDDKEKKNEEEEKKERSTSGEARAAAIVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHADGEEGTSLAKQKVLVQEAAEFLVLKQIPAFIKEHMSHSSSPIDGQSLTESLHSHGINVRYLGKVIKILSQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQTTGNQNGSSSGSSNSSSASDWTLMTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLMRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPIVKHISPRATDAYNFYTTGQAKIQQGLFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKDMHVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTRDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKTDSTENEVNDAINSIVAAANNNGEAEDAVSKDIKEQPEAGKQLTNGDKAAATEATSS

clu

Protein clueless

1441 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.067 kDa

MALDIDTKNSSSAATGDANTVKANNNSSAASTGNKKTENLVNGNNNSAADGPAAKKKGKKNRNKSPPIATDAETTEAATTTAVTNGHEGEALVNGDAVAPDANANVAANDESESAEQQAAENAASSGELESEDVDLDALHDVGITVNISSPGADIISVQLSSMELVQEIHQLLMDREETCHRTCFSLQLGNNTLDNFAELKTVENLEQGSTIKVVEDPYTMREARIHVRHVRDLLKNLDPTDAYNGIDCTSLTYLNTITQGDLLDKKKTRPDSVDCTPPEYVTPGVKEPPLLPLHPNIKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEEKRFHISACSKGFFINQSTDENFNPKPDNPSHLSHSLIDLLSTISPIFRRAFQTIQKRRTLRHAFERVATPYQVYQWASPQLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLMRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDSKMQMFIWNNIFFSLGFDVRDHYKELGGDHAAFVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHSVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVKLSKELTEMGFPIEHRHKLCCLRQELLEAFIEDRYVSFIRIAAVHLQQLNAKKQDEAKEGTKEPASETEKESPPKAITEKEEEESKDQPTVGETKSAEAMVNAIREAQSNMATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHVDGEEGTSSSIVKQKRLVQDAAEFLVLKQIPTFIKEHLAHSSPPIDGQTLTESLHNNGINVRYLGKVIKMLSQMPRMEYLYRIANLELIVRATKHIYYTYMQGTEPLHLSAAISHFLNCLLTNGPVNPAISKEEIHKKRTNTKYNKHKSSKSSGSGSKQSGQTSNQNGTSTSPSSSTASGGTSSNVAIDWTLVTPRSLWQQIRKEAKAYWDWDLECDAIDIALTKYGISRISLLRGFCQKVGIQVLLREYNFESKHKPTFGDDDIVNVFPVVKHISPRSTDAYNFYTTGQSKIQQGLFKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGAKAMHVAVSYHLMARTQSCMGDFRSALNNEKETYTIYKSQLGEKHEKTRDSAECLRLLTQQAVLLQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVQISQNDIVKVRSEIEKHLKANGEESEVNDAIKSIVDASGNNNGETEALINGGEESTVTVTATS

clu

Protein clueless

1435 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.351 kDa

MALEMDSKNSNSAVTGDAAAATTKTNKAKENNNLAGSKKNQSQNLVNGNGTAADGPATKKKGKKNRNKSPPVSTDEAALSNGHVEEKKPEGDGDADADANANVVAVKDEKAEGGDEADAAELDTEDIDLDALHDAGIHVNISCPGSELLTVQLSSMELVQEIHQLLMDREESCHRTCFSLQLDNVTLDNFAELKTIEQLESGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIECTSLTYLNTITQGDLLDKKKTRPDSVDCTPPDYVTPGVFEPPLLPLHPNFKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVITMEEKRYHISACSRGFFINQSTDDTFNPKPDNPSYLSHSLIDLLSHISPSFRRAFQAIQKRRTLRHAFERVATPYQVYQWAAPNLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDSKMQMFIWNNIFFSLGFDVRDHYKELGGDYAAYVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHSVYNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQEVKLSTELVEMGFPIEHRHKLCCLRQELLEAFVEDRYVNFIRIAAVHLQQLNAKKPEETQSEEKKQLPAIEEAEKENKENLNVNETPNEKEKDTPVETKNAEAMVNAIREAQSNVATSNEIQAAEVVKQACAAVGSMKEKEFDFRFNPDVFSPGIRHVDGEEGTSGSVAKQKLLVQDAAEFLVVKQIPAFVKEHLSHSSPPIDGQNLTESLHSHGINVRYLGKVIKTLGQMPRMDYLYRIAVMELIVRATKHIYYTYMQSTDPMHLSVAISHFLNCLLTNGPINPVVSNDEMHKKRGGNGGKHNKHKSSKGGKGQQQPAINQNGGSTTSSSSSANAYDWTLVTPRSLWQQIRKESKAYWDWDLDCDSMDSAMNKFGIMRICLLRAFCLKVGIQVLLREYNFDSKHKPTFGDDDIVNVFPVVKHISPRASDAYNFYTTGQAKIQQGLFKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDNPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLTCGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGNKAMHVAVSYHLMARTQSCMGDFRSALNNEKETYSIYKSQLGEKHEKTRDSAECLRLLTQQAVLLQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLEMLNTINGILFVQISQRDIVKVRSEIEKRMKANTDVNEAIKSMVAAANNNGESEVLAPQDNNKEQAATAQQLTNGDKVAVSS

clu

Protein clueless

1435 amino acids

mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.

Belongs to the CLU family.

160.221 kDa

MALEMDSKNSNSAVTGDAAAATTKTNKAKENNNLAGSKKNQSQNLVNGNGTAADGPATKKKGKKNRNKSPPVSTDEAALSNGHVEEKKPEGDGDADADANANVVAVKDEKAEGGDGADAAELDTEDIDLDALHDAGIHVNISCPGSELLTVQLSSMELVQEIHQLLMDREESCHRTCFSLQLDNVTLDNFAELKTIEQLESGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIECTSLTYLNTITQGDLLDKKKTRPDSVDCTPPDYVTPGVFEPPLLPLHPNFKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVITMEEKRYHISACSRGFFINQSTDDTFNPKPDNPSYLSHSLIDLLSHISPSFRRAFQAIQKRRTLRHAFERVATPYQVYQWAAPNLEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDSKMQMFIWNNIFFSLGFDVRDHYKELGGDYAAYVAPRYDLHGVRVYNAVDVEGLYTLGTVVIDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHSVYNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQEVKLSTELVEMGFPIEHRHKLCCLRQELLEAFVEDRYVNFIRIAAVHLQQLNAKKPEETQSEEKKQLPAIEEAEKENKENLNVNETPNEKEKDTPVETKNAEAMVNAIREAQSNVATSNEIQAAEVVKQACAAVGSMKEKEFDFRFNPDVFSPGIRHVDGEEGTSGSVAKQKLLVQDAAEFLVVKQIPAFVKEHLSHSSPPIDGQNLTESLHSHGINVRYLGKVIKALGQMPRMDYLYRIAVMELIVRATKHIYYTYMQSTDPMHLSVAISHFLNCLLTNGPINPVVSNDEMHKKRGGNGGKHNKHKSSKGGKGQQQPAINQNGGSTTSSSSSANAYDWTLVTPRSLWQQIRKESKAYWDWDLDCDSMDSAMSKFGIMRICLLRAFCLKVGIQVLLREYNFDSKHKPTFGDDDIVNVFPVVKHISPRASDAYNFYTTGQAKIQQGLFKEGYELISEALNLLNNVFGAMHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGIDNPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLLVLTCGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGNKAMHVAVSYHLMARTQSCMGDFRSALNNEKETYSIYKSQLGEKHEKTRDSAECLRLLTQQAVLLQRKMNDIYSNGKLTSDLPPIHITPPSMGSVLEMLNTINGILFVQISQRDIVKVRSEIEKRMKANTDVNEAIKSMVAAANNNGESEVLAPQDNNKEQAATAQQLTNGDKVAVSS

CLU

Clusterin

451 amino acids

Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity).

Belongs to the clusterin family.

51.801 kDa

MELPLLALLSLGLVCQGGQGLVPPNELKQLSAAGSKYIDAEVENAINGVKQMKTLMDKTSKEHQAMLHTLEETKKKKEEAVKLALEKEKQLAEKQEVCNETMLSLWEECKPCLKHTCMRVYSKMCHSGSGLVGRQLEEFLNRSSPFSIWVNGERIDDLLDREQRQERRFEDLEERFGLMEDGVEDIFQDSTQLYGPAFPFFRTPPFGGFREAFVPPVQRVHLVPRRRLSRELHPFFQHPMHGFHRLFQPLFEMTQHMLDGGHGAWEHPLGGFATESRNFSTDRMVCREIRRNSAGCLRMRDECEKCREILAVDCSQTDPVQSQLREQFEDALRLAERFTRRYDDLLSAFQAEMLNTSSLLDQLNRQFGWVSRLGNLTQGNDGFLQVTTVFSKTPNLEDPSAPADTQVTVQLFDSEPLSLTVPGDISWDDPRFMEIVAEQALQHYKQNNTIE

CLU

Clusterin

449 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

52.154 kDa

MKTLLLLVGLLLTLENGQVLGDKAVSDRELQEMSTQGSNYINKEIKNALKGVKQIKNLIEQTNEERKSLLGTLEEAKKKKEGALNDTKDSEMKLKESQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLLENDRQQTHVLDVMQDSFDRASSIMDELFQDRFFTREPQDTYYYSPFSSPHRRSSLLFNPKSRFARNIMHFPMYRHLNFNDMFQPFFDMIHQAQQAMNLHLHRLPDQLPMTEFSEGDNHDRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSTNNPSQMQLRQELNNSLQLAEKFTKLYDELLQSYQEKMLNTSSLLKQLNEQFSWVSQLANLTQGEDQYYLQVTTVSSHNSDSEVPSGLTRVVVKLFDSYPITVTVPEVVSRNNPKFMETVAEKALQEYRQKNREE

CLU

Clusterin

449 amino acids

Isoform 4: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405).

Belongs to the clusterin family.

52.495 kDa

MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE

Clu

Clusterin

448 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins (By similarity). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:14741101). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (PubMed:12551933). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. Following ER stress, suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. When secreted, does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). When secreted, acts as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (PubMed:11865066).

Belongs to the clusterin family.

51.656 kDa

MKILLLCVALLLIWDNGMVLGEQEVSDNELQELSTQGSRYINKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEDALEDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGQQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFARASGIIDTLFQDRFFARELHDPHYFSPIGFPHKRPHFLYPKSRLVRSLMSPSHYGPPSFHNMFQPFFEMIHQAQQAMDVQLHSPAFQFPDVDFLREGEDDRTVCKEIRRNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTEQYKELLQSFQSKMLNTSSLLEQLNDQFNWVSQLANLTQGEDKYYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRAE

CLU

Clusterin

447 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

51.851 kDa

MKTLLLCVGLLLSWERGQVLGDQLVSDNELQEMSTQGSKYIDREIQNAVKGVQEIKTLIEKTNEERKTLLSVLEEAKKNKEDALNETRDSETKLKAFPEVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWINGDRIDSLLENDRQQSHVLDVMQDSFNRATGIMDELFQDRFFTHKPQDTFYHSPFSYFRRPPLHYAKSRLVRNIMPLSLYGPLNFQDMFQPFFEMIHQAQQAMDVHLHSPAYQTPNVEFITGGPDDRAVCKEIRHNSTGCLRMKDQCAKCQEILSVDCSANNPSQNQLRQELNDSLRLAEELTKRYNELLQSYQWKMLNTSSLLDQPNEQFNWVSQLANLTQGPDQYYLRVSTVTSHTSESEAPSRVTEVVVKLFDSDPITITIPEEVSRDNPKFMETVAEKALQEYRKKKRVE

Clu

Clusterin

447 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (PubMed:16038898). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

51.375 kDa

MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME

CLU

Clusterin

446 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

51.775 kDa

MKTLLLLVGLLLTWENGPWVLGDKAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTLIEQSNEERKSLLSSLEEAKKKKEDALNDTRDTETKLKGSQGLCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMENDRQQSHVMDIMEDSFNRASNIMDELFQDRFFNREPFDTQFFSPFGSSHRGSLFFNPKSRFARNIMPFPLFTDLNYHDMFQPFFDMIHQAQQAMDAHLHRIPYHFPEAGVPENSNDRAVCKEIRHNSTGCLRMKDQCEKCREILSVDCSASNSSQMQLRQELYTSLQMAEKFSKLYDQLLQSYQQKMLNTSSLLKQLNEQFSWVSQLANLTQNDDRYYLQVTTVNSHGSDPSVPSGLTKVVVKLFDSYPITLIIPQEVSDPKFMETVAEEALQQYRQRSREE

CLU

Clusterin

445 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:11697889). When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

51.79 kDa

MMKTLLLLVGLLLTWDNGRVLGDQAVSDTELQEMSTEGSKYINKEIKNALKGVKQIKTLIEQTNEERKSLLSNLEEAKKKKEDALNDTKDSETKLKASQGVCNDTMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHALDVMQDSFNRASSIMDELFQDRFFTREPQDTYHYSPFSLFQRRPFFNPKFRIARNIIPFPRFQPLNFHDMFQPFFDMIHQAQQAMDVNLHRIPYHFPIEFPEEDNRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSSNNPAQVQLRQELSNSLQIAEKFTKLYDELLQSYQEKMFNTSSLLKQLNEQFSWVSQLANLTQSEDPFYLQVTTVGSQTSDSNVPVGFTKVVVKLFDSDPITVMIPEAVSRNNPKFMETVAEKALQEYRQKHREE

CLU

Clusterin

439 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

51.114 kDa

MKTLLLLMGLLLSWESGWAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTQIEQTNEERKLLLSSLEEAKKKKEDALNDTRDSENKLKASQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMENDREQSHVMDVMEDSFTRASSIMDELFQDRFFLRRPQDTQYYSPFSSFPRGSLFFNPKSRFARNVMPFPLLEPFNFHDVFQPFYDMIHQAQQAMDAHLQRTPYHFPTMEFTENNDRTVCKEIRHNSTGCLRMKDQCEKCQEILEVDCSASNPTQTLLRQQLNASLQLAEKFSRLYDQLLQSYQQKMLNTSALLKQLNEQFTWVSQLANLTQSDDQHYLQVFTVNSHNSDPSIPSGLTKVIVKLFNSFPITVTVPQEVSSPNFMENVAEKALQQYRRKSQEE

CLU

Clusterin

191 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

22.099 kDa

single

NRRPHFLYPKSRLIRSLLPPPHYGPLSFHDMFQPFLEMIHQAQQAMDVQFHSPAFQFPDMDLLREGEDDRAVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSANNPAQAHLRQELNDSLQVAERLTQRYNELLHSLQTKMLNTSSLLEQLNEQFNWVSQLANLTQGEDQYYLRVSTVTTHSSDSEVPSRVT

CLU

Clusterin

66 amino acids

Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Belongs to the clusterin family.

7.659 kDa

multiple

ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY