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P61086

- UBE2K_HUMAN

UniProt

P61086 - UBE2K_HUMAN

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
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. 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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_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-SubCell
    2. extracellular vesicular exosome Source: UniProt

    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

    ArrayExpressiP61086.
    BgeeiP61086.
    CleanExiHS_UBE2K.
    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

    Protein-protein interaction databases

    BioGridi109340. 77 interactions.
    DIPiDIP-32524N.
    IntActiP61086. 12 interactions.
    MINTiMINT-5000019.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP    50
    YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW 100
    AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH 150
    VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN 200
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 12 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.
    HOVERGENi HBG063308.
    InParanoidi P61086.
    KOi K04649.
    OMAi KHWTNAY.
    OrthoDBi EOG7F513F.
    PhylomeDBi P61086.
    TreeFami TF101127.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P61086.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P61086.
    Bgeei P61086.
    CleanExi HS_UBE2K.
    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

    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: October 1, 2014
    This is version 121 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