CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039591
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
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40LKCCVCKKNGASIGCubiquitination[1, 2]
120ILRSPCCKNAWFHRDubiquitination[1]
154NNSDIFQKEMLRMGIubiquitination[1]
206DYNAPDSKWEIKRCQubiquitination[1]
210PDSKWEIKRCQCCGSubiquitination[1]
251YNSGEFQKAKKHVLPubiquitination[1]
253SGEFQKAKKHVLPNSubiquitination[2]
276LLEESSPKLPRQSPGubiquitination[1, 2]
287QSPGSQSKDLLRQGSubiquitination[1, 2]
396SLNSQALKENLYYEAubiquitination[3]
525KTLGVLEKIQAYPEAubiquitination[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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Ligase; Metal-binding; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 660 AA 
Protein Sequence
MSSGIWQRGK EEEGVYGFLI EDIRKEVNRA SKLKCCVCKK NGASIGCVAP RCKRSYHFPC 60
GLQRECIFQF TGNFASFCWD HRPVQIITSN NYRESLPCTI CLEFIEPIPS YNILRSPCCK 120
NAWFHRDCLQ VQAINAGVFF FRCTICNNSD IFQKEMLRMG IHIPEKDASW ELEENAYQEL 180
LQHYERCDVR RCRCKEGRDY NAPDSKWEIK RCQCCGSSGT HLACSSLRSW EQNWECLECR 240
GIIYNSGEFQ KAKKHVLPNS NNVGITDCLL EESSPKLPRQ SPGSQSKDLL RQGSKFRRNV 300
STLLIELGFQ IKKKTKRLYI NKANIWNSAL DAFRNRNFNP SYAIEVAYVI ENDNFGSEHP 360
GSKQEFLSLL MQHLENSSLF EGSLSKNLSL NSQALKENLY YEAGKMLAIS LVHGGPSPGF 420
FSKTLFNCLV YGPENTQPIL DDVSDFDVAQ IIIRINTATT VADLKSIINE CYNYLELIGC 480
LRLITTLSDK YMLVKDILGY HVIQRVHTPF ESFKQGLKTL GVLEKIQAYP EAFCSILCHK 540
PESLSAKILS ELFTVHTLPD VKALGFWNSY LQAVEDGKST TTMEDILIFA TGCSSIPPAG 600
FKPTPSIECL HVDFPVGNKC NNCLAIPITN TYKEFQENMD FTIRNTLRLE KEESSHYIGH 660 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 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 
PRINTS