Tag | Content |
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CPLM ID | CPLM-000351 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Apoptosis-resistant E3 ubiquitin protein ligase 1 |
Protein Synonyms/Alias | |
Gene Name | AREL1 |
Gene Synonyms/Alias | KIAA0317 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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477 | ALLESSLKATRNFSI | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits apoptosis by ubiquitinating and targeting for degradation a number of proapoptotic proteins including DIABLO/SMAC, HTRA2 and SEPT4/ARTS which are released from the mitochondrion into the cytosol following apoptotic stimulation. |
Sequence Annotation | REPEAT 52 158 Filamin. DOMAIN 483 823 HECT. ACT_SITE 790 790 Glycyl thioester intermediate (By CARBOHYD 210 210 N-linked (GlcNAc...) (Potential). CARBOHYD 306 306 N-linked (GlcNAc...) (Potential). |
Keyword | Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Glycoprotein; Ligase; Membrane; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 823 AA |
Protein Sequence | MFYVIGGITV SVVAFFFTIK FLFELAARVV SFLQNEDRER RGDRTIYDYV RGNYLDPRSC 60 KVSWDWKDPY EVGHSMAFRV HLFYKNGQPF PAHRPVGLRV HISHVELAVE IPVTQEVLQE 120 PNSNVVKVAF TVRKAGRYEI TVKLGGLNVA YSPYYKIFQP GMVVPSKTKI VCHFSTLVLT 180 CGQPHTLQIV PRDEYDNPTN NSMSLRDEHN YTLSIHELGP QEEESTGVSF EKSVTSNRQT 240 FQVFLRLTLH SRGCFHACIS YQNQPINNGE FDIIVLSEDE KNIVERNVST SGVSIYFEAY 300 LYNATNCSST PWHLPPMHMT SSQRRPSTAV DEEDEDSPSE CHTPEKVKKP KKVYCYVSPK 360 QFSVKEFYLK IIPWRLYTFR VCPGTKFSYL GPDPVHKLLT LVVDDGIQPP VELSCKERNI 420 LAATFIRSLH KNIGGSETFQ DKVNFFQREL RQVHMKRPHS KVTLKVSRHA LLESSLKATR 480 NFSISDWSKN FEVVFQDEEA LDWGGPRREW FELICKALFD TTNQLFTRFS DNNQALVHPN 540 PNRPAHLRLK MYEFAGRLVG KCLYESSLGG AYKQLVRARF TRSFLAQIIG LRMHYKYFET 600 DDPEFYKSKV CFILNNDMSE MELVFAEEKY NKSGQLDKVV ELMTGGAQTP VTNANKIFYL 660 NLLAQYRLAS QVKEEVEHFL KGLNELVPEN LLAIFDENEL ELLMCGTGDI SVSDFKAHAV 720 VVGGSWHFRE KVMRWFWTVV SSLTQEELAR LLQFTTGSSQ LPPGGFAALC PSFQIIAAPT 780 HSTLPTAHTC FNQLCLPTYD SYEEVHRMLQ LAISEGCEGF GML 823 |
Gene Ontology | GO:0005829; C:cytosol; IDA:UniProtKB. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005634; C:nucleus; IBA:RefGenome. GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB. GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB. |
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SMART | |
PROSITE | |
PRINTS | |