Reviewed, UniProtKB/Swiss-Prot P68036 (UB2L3_HUMAN)

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

Name:	UBE2L3
Synonyms:	UBCE7, UBCH7

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	Protein modification; protein ubiquitination.
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 process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB ubiquitin ligase complex Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	enzyme binding Ref.1 Traceable author statement. Source: UniProtKB ubiquitin-protein ligase activity Ref.1 Ref.2 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AURKA	O14965	1	EBI-711173,EBI-448680

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

1

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154

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P68036-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: F5A30243BE3C9985	FASTA	154	17,862
	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

References

	« Hide 'large scale' referencesShow '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

EMBLGenBankDDBJ

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

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C4Z	X-ray	2.60	D	1-154	[»]
1FBV	X-ray	2.90	C	1-154	[»]

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

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 25, 2008
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)