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UniProtKB/Swiss-Prot entry P61086


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

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Entry information
Entry name UBE2K_HUMAN
Primary accession number P61086
Secondary accession numbers A6NJC1 B2RDF8 O54806 P27924 Q16721 Q9CVV9 Q9Y2D3
Integrated into Swiss-Prot on April 26, 2004
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 65)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 K
Synonyms EC 6.3.2.19
Ubiquitin-conjugating enzyme E2-25 kDa
E2(25K)
E2-25K
Ubiquitin-protein ligase
Ubiquitin carrier protein
Huntingtin-interacting protein 2
HIP-2
Gene name
Name: UBE2K
Synonyms: HIP2, LIG
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] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.271.32.19385; PubMed=8702625 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme.";
J. Biol. Chem. 271:19385-19394(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10634809 [NCBI, ExPASy, EBI, Israel, Japan]
Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M., Matsuda M., Sakurabayashi I.;
"Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for atherosclerosis.";
Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9; PubMed=10675012 [NCBI, ExPASy, EBI, Israel, Japan]
Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N., Sakurabayashi I.;
"Regulation of macrophage-specific gene expression by degenerated lipoproteins.";
Electrophoresis 21:338-346(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Uterus;
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 2-10; 62-72; 79-97 AND 166-186, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RNF138.
DOI=10.1074/jbc.M602089200; PubMed=16714285 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.;
"NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF).";
J. Biol. Chem. 281:20749-20760(2006).
[8]
PROTEIN SEQUENCE OF 2-8.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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
U58522; AAC50633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022435; BAA78555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022436; BAA78556.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC105287; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AK315524; BAG37905.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022804; AAH22804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050600; AAH50600.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00019894; -.
IPI00021370; -.
RefSeq NP_005330.1; -.
UniGene Hs.50308
3D structure databases
PDB
1YLA; X-ray; 2.40 A; A/B=1-200.[ExPASy / RCSB / EBI]
2O25; X-ray; 2.60 A; A/B=1-200.[ExPASy / RCSB / EBI]
3E46; X-ray; 1.86 A; A=1-200.[ExPASy / RCSB / EBI]
3F92; X-ray; 2.23 A; A=1-200.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1YLA; -.
2O25; -.
3E46; -.
3F92; -.
ModBase P61086.
Protein-protein interaction databases
IntAct P61086; 6.
Enzyme and pathway databases
BRENDA 6.3.2.19; 247.
2D gel databases
OGP P27924; -.
Organism-specific databases
GeneCards GC04P039377; -.
H-InvDB HIX0004166; -.
HGNC HGNC:4914; UBE2K.
GenAtlas UBE2K.
MIM 602846; gene. [NCBI / EBI]
PharmGKB PA29290; -.
Gene expression databases
ArrayExpress P61086; -.
Bgee P61086; -.
CleanEx HS_UBE2K; -.
GermOnline ENSG00000078140; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0031625; Molecular function: ubiquitin protein ligase binding (inferred from physical interaction from UniProtKB).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (traceable author statement from ProtInc).
GO:0043687; Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000449; UBA/transl_elong_EF1B_N.
IPR015940; UBA/transl_elong_EF1B_N_euk.
IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
Pfam PF00627; UBA; 1.
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 SM00165; UBA; 1.
SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS50030; UBA; 1.
PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P61086; -.
PRIDE P61086; -.
Genome annotation databases
Ensembl ENSG00000078140; Homo sapiens. [Contig view]
GeneID 3093; -.
Phylogenomic databases
HOGENOM P61086; -.
HOVERGEN P61086; -.
OMA P61086; MAVSRIK.
Other
NextBio 12275; -.
SOURCE UBE2K; Homo sapiens.
ProtoNet P61086.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Direct protein sequencing; Isopeptide bond; Ligase; Nucleotide-binding; Ubl conjugation; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   200  199     Ubiquitin-conjugating enzyme E2 K. PRO_0000082443
DOMAIN   160   200  41     UBA. 
ACT_SITE   92    92        Glycyl thioester intermediate (By similarity). 
CROSSLNK   14    14        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (By similarity). 
VAR_SEQ   22    72        Missing (in isoform 2). VSP_011798
HELIX   3    17  15      
HELIX   20    23  4      
STRAND   26    33  8      
STRAND   36    44  9      
STRAND   47    49  3      
TURN   50    53  4      
STRAND   55    61  7      
TURN   64    67  4      
STRAND   72    77  6      
TURN   86    88  3      
HELIX   94    96  3      
HELIX   106   118  13      
HELIX   128   136  9      
HELIX   138   153  16      
HELIX   160   171  12      
HELIX   176   185  10      
TURN   186   188  3      
HELIX   190   196  7      
Sequence information
Length: 200 AA [This is the length of the unprocessed precursor] Molecular weight: 22407 Da [This is the MW of the unprocessed precursor] CRC64: E40668099ED25828 [This is a checksum on the sequence]
        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 

P61086 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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