CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
477ALLESSLKATRNFSIubiquitination[1]
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. 
Interpro
 IPR001298; Filamin.
 IPR017868; Filamin/ABP280_repeat-like.
 IPR000569; HECT.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set. 
Pfam
 PF00630; Filamin
 PF00632; HECT 
SMART
 SM00119; HECTc
 SM00557; IG_FLMN 
PROSITE
 PS50194; FILAMIN_REPEAT
 PS50237; HECT 
PRINTS