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Protein Page:
UBE2L3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
UBE2L3 Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down- regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A; used by the papilloma virus HPV-16 E6 protein to ubiquitinate p53/TP53. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity. May interact with NR3C1. Ubiquitous, with highest expression in testis. Belongs to the ubiquitin-conjugating enzyme family. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Ubiquitin conjugating system; Ubiquitin ligase; EC 6.3.2.19; Ligase
Chromosomal Location of Human Ortholog: 22q11.21
Cellular Component: cytoplasm; nucleus; ubiquitin ligase complex
Molecular Function: protein binding; acid-amino acid ligase activity; enzyme binding; ubiquitin protein ligase binding; transcription coactivator activity; ubiquitin-protein ligase activity; ATP binding
Biological Process: ubiquitin-dependent protein catabolic process; cell proliferation; protein polyubiquitination; transcription, DNA-dependent; regulation of transcription, DNA-dependent; protein modification process; protein ubiquitination
Reference #:  P68036 (UniProtKB)
Alt. Names/Synonyms: E2-F1; L-UBC; UB2L3; UBCE7; UBCH7; UbcM4; UBE2L3; Ubiquitin carrier protein L3; Ubiquitin-conjugating enzyme E2 L3; Ubiquitin-conjugating enzyme E2-F1; ubiquitin-conjugating enzyme E2L 3; ubiquitin-conjugating enzyme UBCH7; Ubiquitin-protein ligase L3
Gene Symbols: UBE2L3
Molecular weight: 17,862 Da
Basal Isoelectric point: 8.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

UBE2L3

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 K9-ac AASRRLMkELEEIRK
0 1 K9-ub AASRRLMkELEEIRK
0 3 K20-ac EIRKCGMkNFRNIQV
0 25 K20-ub EIRKCGMkNFRNIQV
0 1 K48-ub PDNPPYDkGAFRIEI
0 8 K64-ub FPAEYPFkPPkITFk
0 2 K67-ub EYPFkPPkITFkTkI
0 2 K71-ub kPPkITFkTkIYHPN
0 62 K73-ub PkITFkTkIYHPNID
0 81 K82-ub YHPNIDEkGQVCLPV
0 4 K82-ac YHPNIDEkGQVCLPV
0 2 K96-ac VISAENWkPATkTDQ
0 3 K96-ub VISAENWkPATkTDQ
0 1 K100-ub ENWkPATkTDQVIQS
0 6 Y129-p RADLAEEySkDRKKF
0 2 K131-ac DLAEEySkDRKKFCk
0 11 K131-ub DLAEEySkDRKKFCk
0 1 K134 EEySkDRKKFCkNAE
0 1 K135 EySkDRKKFCkNAEE
0 2 K138-ac kDRKKFCkNAEEFTk
0 2 K138-ub kDRKKFCkNAEEFTk
0 2 K145-ub kNAEEFTkKyGEkRP
0 1 K145-sc kNAEEFTkKyGEkRP
0 4 K145-ac kNAEEFTkKyGEkRP
0 3 Y147-p AEEFTkKyGEkRPVD
0 2 K150-ub FTkKyGEkRPVD___
  mouse

 
K9 AASRRLMKELEEIRK
K9 AASRRLMKELEEIRK
K20 EIRKCGMKNFRNIQV
K20-ub EIRKCGMkNFRNIQV
K48 PDNPPYDKGAFRIEI
K64-ub FPAEYPFkPPKITFK
K67 EYPFkPPKITFKTkI
K71 kPPKITFKTkIYHPN
K73-ub PKITFKTkIYHPNID
K82-ub YHPNIDEkGQVCLPV
K82 YHPNIDEKGQVCLPV
K96 VISAENWKPATKTDQ
K96-ub VISAENWkPATKTDQ
K100 ENWkPATKTDQVIQS
Y129 RADLAEEYSkDRkkF
K131-ac DLAEEYSkDRkkFCk
K131-ub DLAEEYSkDRkkFCk
K134-ac EEYSkDRkkFCkNAE
K135-ac EYSkDRkkFCkNAEE
K138 kDRkkFCKNAEEFTk
K138-ub kDRkkFCkNAEEFTk
K145 kNAEEFTKKYGEKRP
K145 kNAEEFTKKYGEKRP
K145-ac kNAEEFTkKYGEKRP
Y147 AEEFTkKYGEKRPVD
K150 FTkKYGEKRPVD___
  rat

 
K9-ac AASRRLMkELEEIRK
K9 AASRRLMKELEEIRK
K20 EIRKCGMKNFRNIQV
K20-ub EIRKCGMkNFRNIQV
K48 PDNPPYDKGAFRIEI
K64 FPAEYPFKPPKITFK
K67 EYPFKPPKITFKTkI
K71 KPPKITFKTkIYHPN
K73-ub PKITFKTkIYHPNID
K82-ub YHPNIDEkGQVCLPV
K82 YHPNIDEKGQVCLPV
K96-ac VISAENWkPATKTDQ
K96 VISAENWKPATKTDQ
K100 ENWkPATKTDQVIQS
Y129 RADLAEEYSkDRKKF
K131-ac DLAEEYSkDRKKFCk
K131 DLAEEYSKDRKKFCk
K134 EEYSkDRKKFCkNAE
K135 EYSkDRKKFCkNAEE
K138-ac kDRKKFCkNAEEFTk
K138 kDRKKFCKNAEEFTk
K145-ub kNAEEFTkKYGEKRP
K145 kNAEEFTKKYGEKRP
K145 kNAEEFTKKYGEKRP
Y147 AEEFTkKYGEKRPVD
K150 FTkKYGEKRPVD___
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