P61086 (UBE2K_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 K
EC=6.3.2.19

Alternative name(s):
Huntingtin-interacting protein 2
Short name=HIP-2
Ubiquitin carrier protein
Ubiquitin-conjugating enzyme E2-25 kDa
Short name=Ubiquitin-conjugating enzyme E2(25K)
Short name=Ubiquitin-conjugating enzyme E2-25K
Ubiquitin-protein ligase

Gene names

Name:	UBE2K
Synonyms:	HIP2, LIG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1. Ref.1 Ref.2 Ref.3 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with RNF138/NARF. Interacts with BRCA1. Ref.9 Ref.13
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem. Ref.1 Ref.2 Ref.3
Induction	By aggregated low-density lipoprotein. Ref.2 Ref.3
Post-translational modification	Sumoylation at Lys-14 impairs catalytic activity By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family. Contains 1 UBA domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein K48-linked ubiquitination Inferred from direct assay Ref.15. Source: UniProtKB ubiquitin-dependent protein catabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-ubiquitin ligase activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P61086-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P61086-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-72: Missing.

Note: May be inactive.

Isoform 3 (identifier: P61086-3)

The sequence of this isoform differs from the canonical sequence as follows:
     134-176: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10 Ref.11

Chain

2 – 200

199

Ubiquitin-conjugating enzyme E2 K

PRO_0000082443

Regions

Domain

160 – 200

41

UBA

Sites

Active site

92

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

14

1

N6-acetyllysine; alternate Ref.14

Cross-link

14

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Natural variations

Alternative sequence

22 – 72

51

Missing in isoform 2.

VSP_011798

Alternative sequence

134 – 176

43

Missing in isoform 3.

VSP_046211

Experimental info

Mutagenesis

94

1

D → E: Decreased lysine reactivity and impaired formation of free polyubiquitin chains. Ref.18

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

200

Helix Strand Turn

Details...

Helix

6 – 17

12

Helix

20 – 23

4

Beta strand

26 – 31

6

Beta strand

33 – 35

3

Beta strand

36 – 44

9

Beta strand

47 – 49

3

Turn

50 – 53

4

Beta strand

55 – 61

7

Turn

64 – 68

5

Beta strand

72 – 77

6

Turn

86 – 88

3

Helix

94 – 96

3

Turn

97 – 99

3

Helix

106 – 118

13

Helix

128 – 136

9

Helix

138 – 153

16

Helix

160 – 170

11

Turn

171 – 173

3

Helix

176 – 185

10

Turn

186 – 188

3

Helix

190 – 199

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E40668099ED25828	FASTA	200	22,407
	10 20 30 40 50 60 MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI 70 80 90 100 110 120 KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA 130 140 150 160 170 180 EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI 190 200 VALSSKSWDV ETATELLLSN
	Isoform 2 [UniParc]. Checksum: F029A8438A8E88DB	FASTA	149	16,618
	10 20 30 40 50 60 MANIAVQRIK REFKEVLKSE EVRFITKIWH PNISSVTGAI CLDILKDQWA AAMTLRTVLL 70 80 90 100 110 120 SLQALLAAAE PDDPQDAVVA NQYKQNPEMF KQTARLWAHV YAGAPVSSPE YTKKIENLCA 130 140 MGFDRNAVIV ALSSKSWDVE TATELLLSN
	Isoform 3 [UniParc]. Checksum: E1083BBDA3B3DC65	FASTA	157	17,447
	10 20 30 40 50 60 MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI 70 80 90 100 110 120 KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA 130 140 150 EPDDPQDAVV ANQNAVIVAL SSKSWDVETA TELLLSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme." Kalchman M.A., Graham R.K., Xia G., Koide H.B., Hodgson J.G., Graham K.C., Goldberg Y.P., Gietz R.D., Pickart C.M., Hayden M.R. J. Biol. Chem. 271:19385-19394(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]	"Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for atherosclerosis." Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M., Matsuda M., Sakurabayashi I. Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[3]	"Regulation of macrophage-specific gene expression by degenerated lipoproteins." Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N., Sakurabayashi I. Electrophoresis 21:338-346(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[4]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Placenta.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Uterus.
[9]	"NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)." Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H. J. Biol. Chem. 281:20749-20760(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10; 62-72; 79-97 AND 166-186, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNF138.
[10]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Tissue: Platelet.
[11]	Bienvenut W.V., Bilsland A.E., Keith W.N. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-8; 56-72 AND 177-186, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[12]	"E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system." Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V. Proc. Natl. Acad. Sci. U.S.A. 103:11589-11594(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF MHC CLASS I HEAVY CHAINS.
[13]	"E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages." Christensen D.E., Brzovic P.S., Klevit R.E. Nat. Struct. Mol. Biol. 14:941-948(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN POLYUBIQUITINATION, INTERACTION WITH BRCA1.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, MASS SPECTROMETRY.
[15]	"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines." David Y., Ziv T., Admon A., Navon A. J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Destabilization of Rb by human papillomavirus E7 is cell cycle dependent: E2-25K is involved in the proteolysis." Oh K.J., Kalinina A., Bagchi S. Virology 396:118-124(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN VIRUS-INDUCED DEGRADATION OF RB1.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids." Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E. Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-94.
[19]	"Structure of full-length ubiquitin-conjugating enzyme E2-25K (Huntingtin-interacting protein 2)." Wilson R.C., Hughes R.C., Flatt J.W., Meehan E.J., Ng J.D., Twigg P.D. Acta Crystallogr. F 65:440-444(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
[20]	"A novel and unexpected complex between the SUMO-1-conjugating enzyme UBC9 and the ubiquitin-conjugating enzyme E2-25 kDA." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE2I.
[21]	"Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting protein 2)." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U58522 mRNA. Translation: AAC50633.1.
AB022435 mRNA. Translation: BAA78555.1.
AB022436 mRNA. Translation: BAA78556.1.
BX339118 mRNA. No translation available.
AK291454 mRNA. Translation: BAF84143.1.
AK315524 mRNA. Translation: BAG37905.1.
AC105287 Genomic DNA. No translation available.
AC108471 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW92948.1.
BC022804 mRNA. Translation: AAH22804.1.
BC050600 mRNA. Translation: AAH50600.1.

IPI

IPI00019894.
IPI00021370.
IPI00878126.

RefSeq

NP_001104582.1. NM_001111112.1.
NP_001104583.1. NM_001111113.1.
NP_005330.1. NM_005339.4.

UniGene

Hs.50308.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YLA	X-ray	2.40	A/B	1-200	[»]
2O25	X-ray	2.60	A/B	1-200	[»]
3E46	X-ray	1.86	A	1-200	[»]
3F92	X-ray	2.23	A	1-200	[»]
3K9O	X-ray	1.80	A	1-200	[»]
3K9P	X-ray	2.80	A	1-200	[»]

ProteinModelPortal

P61086.

ModBase

Search...

Protein-protein interaction databases

IntAct

P61086. 8 interactions.

MINT

MINT-5000019.

PTM databases

PhosphoSite

P61086.

Polymorphism databases

DMDM

46577658.

2D gel databases

OGP

P27924.

Proteomic databases

PaxDb

P61086.

PeptideAtlas

P61086.

PRIDE

P61086.

Protocols and materials databases

DNASU

3093.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261427; ENSP00000261427; ENSG00000078140.
ENST00000445950; ENSP00000390483; ENSG00000078140.
ENST00000503368; ENSP00000421203; ENSG00000078140.

GeneID

3093.

KEGG

hsa:3093.

UCSC

uc003gus.4. human.
uc003gut.4. human.
uc003guu.4. human.

Organism-specific databases

CTD

3093.

GeneCards

GC04P039700.

HGNC

HGNC:4914. UBE2K.

HPA

CAB033212.
CAB033515.
HPA028869.

MIM

602846. gene.

neXtProt

NX_P61086.

PharmGKB

PA162407874.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOVERGEN

HBG063308.

InParanoid

P61086.

KO

K04649.

OMA

MAVSRIK.

OrthoDB

EOG4CC42C.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.
REACT_6900. Immune System.

SignaLink

P61086.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P61086.

Bgee

P61086.

CleanEx

HS_UBE2K.

Genevestigator

P61086.

GermOnline

ENSG00000078140. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]

SMART

SM00165. UBA. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.
SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P61086.

GenomeRNAi

3093.

NextBio

12275.

SOURCE

Search...

Entry information

Entry name

UBE2K_HUMAN

Accession

Primary (citable) accession number: P61086
Secondary accession number(s): A6NJC1 , A8K5Y9, B2RDF8, C9JGP1, O54806, P27924, Q16721, Q9CVV9, Q9Y2D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.