Reviewed, UniProtKB/Swiss-Prot P62837 (UB2D2_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 D2
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase D2
    Ubiquitin carrier protein D2
    Ubiquitin-conjugating enzyme E2-17 kDa 2
    E2(17)KB 2

Gene names

Name:	UBE2D2
Synonyms:	UBC4, UBCH5B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
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	Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex and with E3 ubiquitin-protein ligase PJA2 By similarity. Ref.8
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	3D-structure Complete proteome 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.2 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB ubiquitin-protein ligase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNF11	Q9Y3C5	1	EBI-347677,EBI-396669
RNF5	Q99942	2	EBI-347677,EBI-348482
TRAF6	Q9Y4K3	1	EBI-347677,EBI-359276
TRIM5	Q9C035-4	1	EBI-347677,EBI-924243
XIAP	P98170	1	EBI-347677,EBI-517127
ZNRF1	Q8ND25	1	EBI-347677,EBI-2129250

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 147

147

Ubiquitin-conjugating enzyme E2 D2

PRO_0000082462

Sites

Active site

85

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

8

1

N6-acetyllysine Ref.10

Experimental info

Sequence conflict

128

1

K → Q in AAC41750. Ref.2

Secondary structure

1

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147

Helix Strand Turn

Details...

Helix

1 – 15

15

Beta strand

19 – 28

10

Beta strand

32 – 38

7

Turn

44 – 47

4

Beta strand

49 – 55

7

Turn

58 – 61

4

Beta strand

66 – 71

6

Helix

87 – 89

3

Turn

90 – 92

3

Helix

99 – 111

13

Helix

121 – 129

9

Helix

131 – 145

15

Sequences

	Sequence		Length	Mass (Da)
	P62837-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: C942BE7853CBC355	FASTA	147	16,735
	10 20 30 40 50 60 MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 70 80 90 100 110 120 PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 130 140 PEIARIYKTD REKYNRIARE WTQKYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a family of closely related human ubiquitin conjugating enzymes." Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M. J. Biol. Chem. 270:30408-30414(1995) [PubMed: 8530467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)." Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., Theodoras A., Pagano M., Draetta G. Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995) [PubMed: 7724550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia." Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J. Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed: 16112646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Testis.
[7]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 73-90, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[8]	"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4." Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M. Oncogene 19:3529-3536(2000) [PubMed: 10918611] [Abstract] Cited for: INTERACTION WITH SCF COMPLEX.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39317 mRNA. Translation: AAA91460.1.
L40146 Genomic DNA. Translation: AAC41750.1.
AY651263 mRNA. Translation: AAX35690.1.
AK001311 mRNA. Translation: BAG50891.1.
AK001428 mRNA. Translation: BAG50911.1.
CH471062 Genomic DNA. Translation: EAW62095.1.
BC033349 mRNA. Translation: AAH33349.1.

IPI

IPI00332376.

PIR

I59365.

RefSeq

NP_003330.1.
NP_862821.1.

UniGene

Hs.108332

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UR6	NMR	-	A	1-147	[»]
1W4U	NMR	-	A	1-147	[»]
2C4O	X-ray	1.94	A/B/C/D	1-147	[»]
2CLW	X-ray	1.94	A/B/C/D	1-147	[»]
2ESK	X-ray	1.36	A	1-147	[»]
2ESO	X-ray	1.50	A	1-147	[»]
2ESP	X-ray	1.52	A	1-147	[»]
2ESQ	X-ray	1.44	A	1-147	[»]
3A33	X-ray	2.20	A	1-147	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29267N.

IntAct

P62837. 64 interactions.

STRING

P62837.

Proteomic databases

PRIDE

P62837.

Genome annotation databases

Ensembl

ENST00000398733; ENSP00000381717; ENSG00000131508; Homo sapiens. [Genome view]

GeneID

7322.

KEGG

hsa:7322.

UCSC

uc003ler.1. human.

Organism-specific databases

CTD

7322.

GeneCards

GC05P138920.

H-InvDB

HIX0005224.
HIX0006636.
HIX0019025.
HIX0028451.

HGNC

HGNC:12475. UBE2D2.

HPA

HPA003920.

MIM

602962. gene.

PharmGKB

PA37125.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG756483.

HOVERGEN

P62837.

OMA

RKKYEAT.

PhylomeDB

P62837.

Enzyme and pathway databases

BRENDA

6.3.2.19. 247.

Gene expression databases

ArrayExpress

P62837.

Bgee

P62837.

CleanEx

HS_UBE2D2.

Genevestigator

P62837.

GermOnline

ENSG00000131508. 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.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

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

NextBio

28630.

SOURCE

Search...

Entry information

Entry name

UB2D2_HUMAN

Accession

Primary (citable) accession number: P62837
Secondary accession number(s): P51669, Q3MN78

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 19, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.