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P61086

- UBE2K_HUMAN

UniProt

P61086 - UBE2K_HUMAN

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Protein

Ubiquitin-conjugating enzyme E2 K

Gene

UBE2K

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 RB1.8 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. ubiquitin-ubiquitin ligase activity Source: UniProtKB

GO - Biological processi

  1. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  4. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP61086.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UBE2K
Synonyms:HIP2, LIG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4914. UBE2K.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941D → E: Decreased lysine reactivity and impaired formation of free polyubiquitin chains. 1 Publication

Organism-specific databases

PharmGKBiPA162407874.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 200199Ubiquitin-conjugating enzyme E2 KPRO_0000082443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei14 – 141N6-acetyllysine; alternate1 Publication
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity

Post-translational modificationi

Sumoylation at Lys-14 impairs catalytic activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61086.
PaxDbiP61086.
PeptideAtlasiP61086.
PRIDEiP61086.

2D gel databases

OGPiP27924.

PTM databases

PhosphoSiteiP61086.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

By aggregated low-density lipoprotein.2 Publications

Gene expression databases

BgeeiP61086.
CleanExiHS_UBE2K.
ExpressionAtlasiP61086. baseline and differential.
GenevestigatoriP61086.

Organism-specific databases

HPAiCAB033212.
CAB033515.
HPA028869.

Interactioni

Subunit structurei

Interacts with RNF138/NARF. Interacts with BRCA1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1P146352EBI-473850,EBI-495332
HTTP428583EBI-473850,EBI-466029
ospGQ99PZ62EBI-473850,EBI-9316527From a different organism.

Protein-protein interaction databases

BioGridi109340. 77 interactions.
DIPiDIP-32524N.
IntActiP61086. 13 interactions.
MINTiMINT-5000019.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources
Helixi20 – 234Combined sources
Beta strandi26 – 316Combined sources
Beta strandi33 – 353Combined sources
Beta strandi36 – 449Combined sources
Beta strandi47 – 493Combined sources
Turni50 – 534Combined sources
Beta strandi55 – 617Combined sources
Turni64 – 685Combined sources
Beta strandi72 – 776Combined sources
Turni86 – 883Combined sources
Helixi94 – 963Combined sources
Turni97 – 993Combined sources
Helixi106 – 11813Combined sources
Helixi128 – 1369Combined sources
Helixi138 – 15316Combined sources
Helixi160 – 17011Combined sources
Turni171 – 1733Combined sources
Helixi176 – 18510Combined sources
Turni186 – 1883Combined sources
Helixi190 – 19910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YLAX-ray2.40A/B1-200[»]
2O25X-ray2.60A/B1-200[»]
3E46X-ray1.86A1-200[»]
3F92X-ray2.23A13-200[»]
3K9OX-ray1.80A1-200[»]
3K9PX-ray2.80A1-200[»]
ProteinModelPortaliP61086.
SMRiP61086. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61086.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 20041UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00670000098059.
HOVERGENiHBG063308.
InParanoidiP61086.
KOiK04649.
OMAiKHWTNAY.
OrthoDBiEOG7F513F.
PhylomeDBiP61086.
TreeFamiTF101127.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTiSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61086-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP
60 70 80 90 100
YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW
110 120 130 140 150
AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH
160 170 180 190 200
VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN
Length:200
Mass (Da):22,407
Last modified:January 23, 2007 - v3
Checksum:iE40668099ED25828
GO
Isoform 2 (identifier: P61086-2) [UniParc]FASTAAdd to Basket

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

Note: May be inactive.

Show »
Length:149
Mass (Da):16,618
Checksum:iF029A8438A8E88DB
GO
Isoform 3 (identifier: P61086-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:157
Mass (Da):17,447
Checksum:iE1083BBDA3B3DC65
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 7251Missing in isoform 2. 3 PublicationsVSP_011798Add
BLAST
Alternative sequencei134 – 17643Missing in isoform 3. 1 PublicationVSP_046211Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33976.1. [P61086-1]
CCDS47043.1. [P61086-3]
CCDS47044.1. [P61086-2]
RefSeqiNP_001104582.1. NM_001111112.1. [P61086-3]
NP_001104583.1. NM_001111113.1. [P61086-2]
NP_005330.1. NM_005339.4. [P61086-1]
UniGeneiHs.50308.

Genome annotation databases

EnsembliENST00000261427; ENSP00000261427; ENSG00000078140. [P61086-1]
ENST00000445950; ENSP00000390483; ENSG00000078140. [P61086-3]
ENST00000503368; ENSP00000421203; ENSG00000078140. [P61086-2]
GeneIDi3093.
KEGGihsa:3093.
UCSCiuc003gut.4. human. [P61086-2]
uc003guu.4. human. [P61086-1]

Polymorphism databases

DMDMi46577658.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS33976.1. [P61086-1 ]
CCDS47043.1. [P61086-3 ]
CCDS47044.1. [P61086-2 ]
RefSeqi NP_001104582.1. NM_001111112.1. [P61086-3 ]
NP_001104583.1. NM_001111113.1. [P61086-2 ]
NP_005330.1. NM_005339.4. [P61086-1 ]
UniGenei Hs.50308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 13-200 [» ]
3K9O X-ray 1.80 A 1-200 [» ]
3K9P X-ray 2.80 A 1-200 [» ]
ProteinModelPortali P61086.
SMRi P61086. Positions 3-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109340. 77 interactions.
DIPi DIP-32524N.
IntActi P61086. 13 interactions.
MINTi MINT-5000019.

PTM databases

PhosphoSitei P61086.

Polymorphism databases

DMDMi 46577658.

2D gel databases

OGPi P27924.

Proteomic databases

MaxQBi P61086.
PaxDbi P61086.
PeptideAtlasi P61086.
PRIDEi P61086.

Protocols and materials databases

DNASUi 3093.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261427 ; ENSP00000261427 ; ENSG00000078140 . [P61086-1 ]
ENST00000445950 ; ENSP00000390483 ; ENSG00000078140 . [P61086-3 ]
ENST00000503368 ; ENSP00000421203 ; ENSG00000078140 . [P61086-2 ]
GeneIDi 3093.
KEGGi hsa:3093.
UCSCi uc003gut.4. human. [P61086-2 ]
uc003guu.4. human. [P61086-1 ]

Organism-specific databases

CTDi 3093.
GeneCardsi GC04P039700.
HGNCi HGNC:4914. UBE2K.
HPAi CAB033212.
CAB033515.
HPA028869.
MIMi 602846. gene.
neXtProti NX_P61086.
PharmGKBi PA162407874.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00670000098059.
HOVERGENi HBG063308.
InParanoidi P61086.
KOi K04649.
OMAi KHWTNAY.
OrthoDBi EOG7F513F.
PhylomeDBi P61086.
TreeFami TF101127.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P61086.

Miscellaneous databases

ChiTaRSi UBE2K. human.
EvolutionaryTracei P61086.
GeneWikii HIP2.
GenomeRNAii 3093.
NextBioi 12275.
PROi P61086.
SOURCEi Search...

Gene expression databases

Bgeei P61086.
CleanExi HS_UBE2K.
ExpressionAtlasi P61086. baseline and differential.
Genevestigatori P61086.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view ]
SMARTi SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEi PS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. 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. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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).
  22. "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.
  23. "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).

Entry informationi

Entry nameiUBE2K_HUMAN
AccessioniPrimary (citable) accession number: P61086
Secondary accession number(s): A6NJC1
, A8K5Y9, B2RDF8, C9JGP1, O54806, P27924, Q16721, Q9CVV9, Q9Y2D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3