CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015869
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-conjugating enzyme E2 Q1 
Protein Synonyms/Alias
 Ubiquitin carrier protein Q1; Ubiquitin-protein ligase Q1 
Gene Name
 Ube2q1 
Gene Synonyms/Alias
 Ube2q 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
46PCLRRELKLLESIFHubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). 
Sequence Annotation
 ACT_SITE 351 351 Glycyl thioester intermediate (By
 MOD_RES 1 1 N-acetylmethionine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 422 AA 
Protein Sequence
MQQPQPQGQQ QPGPGQQLGV QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR 60
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPSRGSVPGD PVRIHCNITE SYPAVPPIWS 120
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC 180
TQEEVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD 240
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH 300
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW 360
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE 420
DG 422 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. 
Interpro
 IPR000608; UBQ-conjugat_E2.
 IPR016135; UBQ-conjugating_enzyme/RWD. 
Pfam
 PF00179; UQ_con 
SMART
  
PROSITE
 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 
PRINTS