Reviewed,
UniProtKB/Swiss-Prot P68036 (UB2L3_HUMAN)
Last modified
November 25, 2008.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ubiquitin-conjugating enzyme E2 L3 EC=6.3.2.19 Alternative name(s): Ubiquitin-protein ligase L3 Ubiquitin carrier protein L3 UbcH7 E2-F1 L-UBC | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. |
| Catalytic activity | ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. |
| Pathway | |
| Subunit structure | Binds UBE3A, HEI10, CBL, ZAP70, RNF19A, RNF19B and RNF144B. |
| Tissue specificity | Ubiquitous, with highest expression in testis. |
| Sequence similarities | Belongs to the ubiquitin-conjugating enzyme family. |
| Caution | Ref.8 reported that UBE2L1, UBE2L2 and UBE2L4 are most likely pseudogenes and the only expressed member of this subfamily seems to be UBE2L3. |
Ontologies
Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Molecular function | Ligase |
| Technical term | 3D-structure Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | protein ubiquitination Inferred from direct assay. Source: UniProtKB regulation of protein metabolic processInferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Ref.1Traceable author statement. Source: UniProtKB |
| Cellular component | cytoplasm Inferred from direct assay. Source: UniProtKB ubiquitin ligase complex Ref.1Traceable author statement. Source: UniProtKB |
| Molecular function | enzyme binding Ref.1 Traceable author statement. Source: UniProtKB ubiquitin-protein ligase activity Ref.1 Ref.2Traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 154 | 154 | Ubiquitin-conjugating enzyme E2 L3 | PRO_0000082476 | ||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||
| Active site | 86 | 1 | Glycyl thioester intermediate By similarity | |||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 23 | 1 | R → C in AAG17922. Ref.4 | |||||||||||||||||||||||||||||||
| Sequence conflict | 118 | 1 | E → K in AAG17922. Ref.4 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Helix | 7 – 11 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 15 – 17 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 23 – 25 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 30 – 39 | 10 | ||||||||||||||||||||||||||||||||
| Beta strand | 43 – 45 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 51 – 56 | 6 | ||||||||||||||||||||||||||||||||
| Turn | 59 – 63 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 67 – 72 | 6 | ||||||||||||||||||||||||||||||||
| Turn | 88 – 90 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 91 – 94 | 4 | ||||||||||||||||||||||||||||||||
| Helix | 101 – 113 | 13 | ||||||||||||||||||||||||||||||||
| Helix | 123 – 130 | 8 | ||||||||||||||||||||||||||||||||
| Helix | 137 – 144 | 8 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3." Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P., Coletta P.L., Lench N.J., Markham A.F. Mamm. Genome 6:725-731(1995) [PubMed: 8563171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5." Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M. J. Biol. Chem. 271:2795-2800(1996) [PubMed: 8576257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3." Moynihan T.P., Cole C.G., Dunham I., O'Neil L., Markham A.F., Robinson P.A. Genomics 51:124-127(1998) [PubMed: 9693040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
| [4] | "Is retroposition a common way of spreading ubiquitin-conjugating enzyme genes throughout mammalian genomes?" Poloumienko A. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood. |
| [5] | "A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [7] | "Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-'N-end rule' protein substrates." Blumenfeld N., Gonen H., Mayer A., Smith C.E., Siegel N.R., Schwartz A.L., Ciechanover A. J. Biol. Chem. 269:9574-9581(1994) [PubMed: 8144544] [Abstract] Cited for: PROTEIN SEQUENCE OF 53-67; 67-74 AND 101-122. |
| [8] | "Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7." Ardley H.C., Moynihan T.P., Markham A.F., Robinson P.A. Biochim. Biophys. Acta 1491:57-64(2000) [PubMed: 10760570] [Abstract] Cited for: PROMOTER ANALYSIS. |
| [9] | "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity." Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G. Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed: 11237715] [Abstract] Cited for: INTERACTION WITH RNF19A. |
| [10] | "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis." Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B. FEBS Lett. 580:940-947(2006) [PubMed: 16427630] [Abstract] Cited for: INTERACTION WITH RNF144B. |
| [11] | "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase." Fortier J.M., Kornbluth J. J. Immunol. 176:6454-6463(2006) [PubMed: 16709802] [Abstract] Cited for: INTERACTION WITH RNF19B. |
| [12] | "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade." Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P. Science 286:1321-1326(1999) [PubMed: 10558980] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE3A. |
| [13] | "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases." Zheng N., Wang P., Jeffrey P.D., Pavletich N.P. Cell 102:533-539(2000) [PubMed: 10966114] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH 47-434 OF CBL AND ZAP70. |
| [14] | "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels." Toby G.G., Gherraby W., Coleman T.R., Golemis E.A. Mol. Cell. Biol. 23:2109-2122(2003) [PubMed: 12612082] [Abstract] Cited for: INTERACTION WITH HEI10. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| S81003 mRNA. Translation: AAB36017.1. X92962 mRNA. Translation: CAA63538.1. AJ000519 mRNA. Translation: CAA04156.1. AF300336 Genomic DNA. Translation: AAG17922.1. CR456606 mRNA. Translation: CAG30492.1. BC053368 mRNA. Translation: AAH53368.1. | |||||||||||||||||||
| RefSeq | NP_003338.1. NP_937800.1. | ||||||||||||||||||
| UniGene | Hs.108104 Hs.603229 Hs.705512 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P68036. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P68036. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| OGP | P51966. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSG00000185651. Homo sapiens. [Contig view] | ||||||||||||||||||
| GeneID | 7332. | ||||||||||||||||||
| KEGG | hsa:7332. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| H-InvDB | HIX0027846. | ||||||||||||||||||
| HGNC | HGNC:12488. UBE2L3. | ||||||||||||||||||
| MIM | 603721. gene. | ||||||||||||||||||
| PharmGKB | PA37137. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
| GeneCards | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | P68036. | ||||||||||||||||||
| HOVERGEN | P68036. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P68036. | ||||||||||||||||||
| CleanEx | HS_UBE2L3. | ||||||||||||||||||
| GermOnline | ENSG00000185651. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit. | ||||||||||||||||||
| PANTHER | PTHR11621. UBQ-conjugat_E2. 1 hit. | ||||||||||||||||||
| Pfam | PF00179. UQ_con. 1 hit. [Graphical view] | ||||||||||||||||||
| ProDom | PD000461. UBQ_conjugat. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| SMART | SM00212. UBCc. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| LinkHub | P68036. | ||||||||||||||||||
| NextBio | 28696. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | UB2L3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P68036 Secondary accession number(s): P51966, P70653, Q9HAV1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


