CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015778
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 G2/M phase-specific E3 ubiquitin-protein ligase 
Protein Synonyms/Alias
  
Gene Name
 G2E3 
Gene Synonyms/Alias
 KIAA1333 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
442SLNSQALKENLYYEAubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
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. Essential in early embryonic development to prevent apoptotic death. 
Sequence Annotation
 DOMAIN 371 698 HECT.
 ZN_FING 80 128 PHD-type 1.
 ZN_FING 143 193 PHD-type 2; degenerate.
 ZN_FING 237 286 PHD-type 3.  
Keyword
 Apoptosis; Complete proteome; Cytoplasm; Developmental protein; Ligase; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 706 AA 
Protein Sequence
MNESKPGDSQ NLACVFCRKH DDCPNKYGEK KTKEKWNLTV HYYCLLMSSG IWQRGKEEEG 60
VYGFLIEDIR KEVNRASKLK CCVCKKNGAS IGCVAPRCKR SYHFPCGLQR ECIFQFTGNF 120
ASFCWDHRPV QIITSNNYRE SLPCTICLEF IEPIPSYNIL RSPCCKNAWF HRDCLQVQAI 180
NAGVFFFRCT ICNNSDIFQK EMLRMGIHIP EKDASWELEE NAYQELLQHY ERCDVRRCRC 240
KEGRDYNAPD SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRGIIY NSGEFQKAKK 300
HVLPNSNNVG ITDCLLEESS PKLPRQSPGS QSKDLLRQGS KFRRNVSTLL IELGFQIKKK 360
TKRLYINKAN IWNSALDAFR NRNFNPSYAI EVAYVIENDN FGSEHPGSKQ EFLSLLMQHL 420
ENSSLFEGSL SKNLSLNSQA LKENLYYEAG KMLAISLVHG GPSPGFFSKT LFNCLVYGPE 480
NTQPILDDVS DFDVAQIIIR INTATTVADL KSIINECYNY LELIGCLRLI TTLSDKYMLV 540
KDILGYHVIQ RVHTPFESFK QGLKTLGVLE KIQAYPEAFC SILCHKPESL SAKILSELFT 600
VHTLPDVKAL GFWNSYLQAV EDGKSTTTME DILIFATGCS SIPPAGFKPT PSIECLHVDF 660
PVGNKCNNCL AIPITNTYKE FQENMDFTIR NTLRLEKEES SHYIGH 706 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0001824; P:blastocyst development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0000209; P:protein polyubiquitination; IEA:Compara. 
Interpro
 IPR000569; HECT.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00632; HECT 
SMART
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS50237; HECT
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS