rnf145

RING finger protein 145

695 amino acids

78.494 kDa

MGAKEKLEAMLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLNKNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLAKLYLYFVAALLLFAGHQISRDYVRSELESGYEGPMHLEPLSMNRFITALVGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLIPIETIVVINKFAMIFTGLEVLYFLASNLLVPFNLAKSAYRELAQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYTYFSTRDQPTSRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPSYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFVYVLFMIEEFRKEPVENVDDAIYYVNGTYRLLEFLVALCVVAYGVSETVFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPVSTKEQLEQHNDICSICYQDMNSAVITPCSHFFHPGCLKKWLYVQETCPLCHCQLKSLSQQAVAESGSSTNPVVEQSANNPPQEPLSAVAATTETLGTVPTCSALEQEPTMDIEPAESLVERRGELEVHVSQEEANSNSNEVLQRILTTGKVQPEDLNVKALPPESEVCAGI

rnf145

RING finger protein 145

695 amino acids

78.567 kDa

MGAKEKLEAMLNVALRVPSIMLLDVLYRWDVSSFFKQIQRSSLNNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLAKLYLYFVAALLLYAGHQISRDYVRSELESGYEGPMHIEPLSMNRFITALVGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPIETIVVINKFAMIFTGLEVLYFLASNLLVPFNLAKSAYRELAQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYTYFSTRDQPTSRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPSYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMIEEFRKEPVENMDDVIYYVNGTYRLLEFLVALCVVAYGVSETVFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPVATKEQLEQHNDICSICYQDMNSAVITPCSHFFHPGCLKKWLYVQETCPLCHCQLKSLSQQATGESGSSTNPVSEQSATNPPLGPVSRAEVTTEPLAAVPTRSALEQEPTMDIKVSGSVEKRIGELEAHFSQGEANLNSNEVLQRLQAKGEANPEDLNVKALPPECEHCAEI

rnf145

RING finger protein 145

685 amino acids

77.649 kDa

MAMKARLESVLNVGLRIPSIMLLEVLYRWDVSSFFQKIQRSSLNNNPVFQYKYIALYLHYVGYILSLVLLTLPRQHLVQLYLYVLTALLLFAGHQLSRDYVRGELDSGYEGPLYLEPLSMNRFTTALIGQVVVCTLCSCVMQTRQIWLFSAHLLPLVARLCLVPLETIVFINRFAMIFTGLEVLYFIASNLLVPYNLAKTAYRELVQVVEVYGLLALGMSLWNQLVLPVLFMCFWLVLFALQIYTYFSTRDQPPSRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDNAMHRGMTEGITLLILAVQTGLIELQVIHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFRMDFWLLIIISSSILTSLQVLGTLLIYVLFMVEEFRKAPVENMDEVIYYVNGTYRLLEFLVAVCVVAYGVSETLFGEWTVMGSTIILVHSYYNVWLRAQLGWQSFLLRRDAVHKIQSMPTASTLQLQQHNDICSICFQDMKSAVITPCSHFFHAACLKKWLYVQETCPLCHGQLKSQLQPTSSPGTPTQGTPAANQNPREVEQEQRQPQVELNTEEGIRAEEMKTSAEQKLGMDLLPGSLNTQPKECDLVAEGSAGTASNLKGDDYYDDDDVSTSDVNCAS

RNF145

RING finger protein 145

663 amino acids

E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species. Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function. In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately downregulating cholesterol biosynthesis.

75.617 kDa

MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLSNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFLTALLLYAGHQISRDYVRSELEFAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFLVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPIATKEQLEKHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLCHCHLKNSSQLPGLGTEPVLQPHAGAEQNVMFQEGTEPPGQEHTPGTRIQEGSRDNNEYIARRPDNQEGAFDPKEYPHSAKDEAHPVESA

Rnf145

RING finger protein 145

663 amino acids

E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species (PubMed:26194095). Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function (PubMed:29374057). In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately downregulating cholesterol biosynthesis (PubMed:29068315).

74.648 kDa

MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLNNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFVTALLLYAGHQISRDYVRSELESAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFVVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPVATQEQLEKHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQDTCPLCHCHLKNSSQLPGLGTEAAPQPPAGAEQNIVLQEGPEPPDHESPPGTGTQEGSGDSSEHINRGSASQEGAADAGEGPQIPEGEVCPVESA