ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P68036


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name UB2L3_HUMAN
Primary accession number P68036
Secondary accession numbers P51966 P70653 Q9HAV1
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 46)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 L3
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase L3
Ubiquitin carrier protein L3
UbcH7
E2-F1
L-UBC
Gene name
Name: UBE2L3
Synonyms: UBCE7, UBCH7
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF00354295; PubMed=8563171 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3.";
Mamm. Genome 6:725-731(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.271.5.2795; PubMed=8576257 [NCBI, ExPASy, EBI, Israel, Japan]
Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.;
"Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5.";
J. Biol. Chem. 271:2795-2800(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1006/geno.1998.5257; PubMed=9693040 [NCBI, ExPASy, EBI, Israel, Japan]
Moynihan T.P., Cole C.G., Dunham I., O'Neil L., Markham A.F., Robinson P.A.;
"Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3.";
Genomics 51:124-127(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
Poloumienko A.;
"Is retroposition a common way of spreading ubiquitin-conjugating enzyme genes throughout mammalian genomes?";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 53-67; 67-74 AND 101-122.
PubMed=8144544 [NCBI, ExPASy, EBI, Israel, Japan]
Blumenfeld N., Gonen H., Mayer A., Smith C.E., Siegel N.R., Schwartz A.L., Ciechanover A.;
"Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-'N-end rule' protein substrates.";
J. Biol. Chem. 269:9574-9581(1994).
[8]
PROMOTER ANALYSIS.
DOI=10.1016/S0167-4781(00)00024-5; PubMed=10760570 [NCBI, ExPASy, EBI, Israel, Japan]
Ardley H.C., Moynihan T.P., Markham A.F., Robinson P.A.;
"Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7.";
Biochim. Biophys. Acta 1491:57-64(2000).
[9]
INTERACTION WITH RNF19A.
DOI=10.1006/bbrc.2001.4414; PubMed=11237715 [NCBI, ExPASy, EBI, Israel, Japan]
Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.;
"A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity.";
Biochem. Biophys. Res. Commun. 281:706-713(2001).
[10]
INTERACTION WITH RNF144B.
DOI=10.1016/j.febslet.2005.09.105; PubMed=16427630 [NCBI, ExPASy, EBI, Israel, Japan]
Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.;
"The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis.";
FEBS Lett. 580:940-947(2006).
[11]
INTERACTION WITH RNF19B.
PubMed=16709802 [NCBI, ExPASy, EBI, Israel, Japan]
Fortier J.M., Kornbluth J.;
"NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase.";
J. Immunol. 176:6454-6463(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE3A.
DOI=10.1126/science.286.5443.1321; PubMed=10558980 [NCBI, ExPASy, EBI, Israel, Japan]
Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P.;
"Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade.";
Science 286:1321-1326(1999).
[13]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH 47-434 OF CBL AND ZAP70.
DOI=10.1016/S0092-8674(00)00057-X; PubMed=10966114 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.;
"Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.";
Cell 102:533-539(2000).
[14]
INTERACTION WITH HEI10.
DOI=10.1128/MCB.23.6.2109-2122.2003; PubMed=12612082 [NCBI, ExPASy, EBI, Israel, Japan]
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
"A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels.";
Mol. Cell. Biol. 23:2109-2122(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S81003; AAB36017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X92962; CAA63538.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000519; CAA04156.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF300336; AAG17922.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456606; CAG30492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053368; AAH53368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003338.1; -.
NP_937800.1; -.
UniGene Hs.108104
3D structure databases
PDB
1C4Z; X-ray; 2.60 A; D=1-154.[ExPASy / RCSB / EBI]
1FBV; X-ray; 2.90 A; C=1-154.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C4Z; -.
1FBV; -.
ModBase P68036.
Protein-protein interaction databases
IntAct P68036; -.
2D gel databases
OGP P51966; -.
Organism-specific databases
H-InvDB HIX0027846; -.
HGNC HGNC:12488; UBE2L3.
GenAtlas UBE2L3.
MIM 603721; gene. [NCBI / EBI]
PharmGKB PA37137; -.
GeneCards P68036.
Gene expression databases
ArrayExpress P68036; -.
CleanEx HS_UBE2L3; -.
GermOnline ENSG00000185651; Homo sapiens.
Ontologies
GO
GO:0000151; Cellular component: ubiquitin ligase complex (traceable author statement from UniProtKB).
GO:0019899; Molecular function: enzyme binding (traceable author statement from UniProtKB).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (traceable author statement from UniProtKB).
GO:0006464; Biological process: protein modification process (traceable author statement from UniProtKB).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P68036.
Genome annotation databases
Ensembl ENSG00000185651; Homo sapiens. [Contig view]
GeneID 7332; -.
KEGG hsa:7332; -.
Phylogenomic databases
HOGENOM P68036; -.
HOVERGEN P68036; -.
Other
LinkHub P68036; -.
SOURCE UBE2L3; Homo sapiens.
ProtoNet P68036.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   154  154     Ubiquitin-conjugating enzyme E2 L3. PRO_0000082476
ACT_SITE   86    86        Glycyl thioester intermediate (By similarity). 
CONFLICT   23    23        R -> C (in Ref. 4; AAG17922). 
CONFLICT   118   118        E -> K (in Ref. 4; AAG17922). 
HELIX   7    11  5      
STRAND   15    17  3      
STRAND   23    25  3      
STRAND   30    39  10      
STRAND   43    45  3      
STRAND   51    56  6      
TURN   59    63  5      
STRAND   67    72  6      
TURN   88    90  3      
STRAND   91    94  4      
HELIX   101   113  13      
HELIX   123   130  8      
HELIX   137   144  8      
Sequence information
Length: 154 AA [This is the length of the unprocessed precursor] Molecular weight: 17862 Da [This is the MW of the unprocessed precursor] CRC64: F5A30243BE3C9985 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE 

        70         80         90        100        110        120 
YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP 

       130        140        150 
LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD 

P68036 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!