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Q9H832

- UBE2Z_HUMAN

UniProt

Q9H832 - UBE2Z_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 Z

Gene

UBE2Z

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins By similarity. Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.2 PublicationsPROSITE-ProRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei188 – 1881Glycyl 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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9H832.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 Z (EC:6.3.2.19)
    Alternative name(s):
    Uba6-specific E2 conjugating enzyme 1
    Short name:
    Use1
    Ubiquitin carrier protein Z
    Ubiquitin-protein ligase Z
    Gene namesi
    Name:UBE2Z
    ORF Names:HOYS7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:25847. UBE2Z.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670659.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Ubiquitin-conjugating enzyme E2 ZPRO_0000280515Add
    BLAST

    Proteomic databases

    MaxQBiQ9H832.
    PaxDbiQ9H832.
    PRIDEiQ9H832.

    PTM databases

    PhosphoSiteiQ9H832.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly in placenta, pancreas, spleen and testis.2 Publications

    Gene expression databases

    ArrayExpressiQ9H832.
    BgeeiQ9H832.
    CleanExiHS_UBE2Z.
    GenevestigatoriQ9H832.

    Organism-specific databases

    HPAiHPA007922.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBDO152052EBI-720977,EBI-6657186

    Protein-protein interaction databases

    BioGridi122419. 29 interactions.
    IntActiQ9H832. 30 interactions.
    MINTiMINT-1388629.
    STRINGi9606.ENSP00000354201.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H832.
    SMRiQ9H832. Positions 93-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233451.
    HOVERGENiHBG083204.
    InParanoidiQ9H832.
    KOiK10585.
    OMAiAVMANMS.
    OrthoDBiEOG7MSMP5.
    PhylomeDBiQ9H832.
    TreeFamiTF354204.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H832-1) [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

    MAESPTEEAA TAGAGAAGPG ASSVAGVVGV SGSGGGFGPP FLPDVWAAAA    50
    AAGGAGGPGS GLAPLPGLPP SAAAHGAALL SHWDPTLSSD WDGERTAPQC 100
    LLRIKRDIMS IYKEPPPGMF VVPDTVDMTK IHALITGPFD TPYEGGFFLF 150
    VFRCPPDYPI HPPRVKLMTT GNNTVRFNPN FYRNGKVCLS ILGTWTGPAW 200
    SPAQSISSVL ISIQSLMTEN PYHNEPGFEQ ERHPGDSKNY NECIRHETIR 250
    VAVCDMMEGK CPCPEPLRGV MEKSFLEYYD FYEVACKDRL HLQGQTMQDP 300
    FGEKRGHFDY QSLLMRLGLI RQKVLERLHN ENAEMDSDSS SSGTETDLHG 350
    SLRV 354
    Length:354
    Mass (Da):38,210
    Last modified:March 20, 2007 - v2
    Checksum:i5AFC148BD8D31356
    GO
    Isoform 2 (identifier: Q9H832-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:246
    Mass (Da):28,075
    Checksum:iA0AE68FB9430ACDB
    GO

    Sequence cautioni

    The sequence AAH15890.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14724.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_023747Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF623992 mRNA. Translation: ABR25252.1.
    AK023917 mRNA. Translation: BAB14724.1. Different initiation.
    AK024030 mRNA. Translation: BAB14789.1.
    AC091133 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94703.1.
    BC015169 mRNA. Translation: AAH15169.2.
    BC015890 mRNA. Translation: AAH15890.1. Different initiation.
    AB025426 mRNA. Translation: BAB87810.1.
    CR457322 mRNA. Translation: CAG33603.1.
    AL713782 mRNA. Translation: CAD28542.1.
    CCDSiCCDS11540.2. [Q9H832-1]
    RefSeqiNP_075567.2. NM_023079.4. [Q9H832-1]
    UniGeneiHs.514297.

    Genome annotation databases

    EnsembliENST00000360943; ENSP00000354201; ENSG00000159202. [Q9H832-1]
    GeneIDi65264.
    KEGGihsa:65264.
    UCSCiuc002ioi.3. human. [Q9H832-1]

    Polymorphism databases

    DMDMi134035344.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF623992 mRNA. Translation: ABR25252.1 .
    AK023917 mRNA. Translation: BAB14724.1 . Different initiation.
    AK024030 mRNA. Translation: BAB14789.1 .
    AC091133 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94703.1 .
    BC015169 mRNA. Translation: AAH15169.2 .
    BC015890 mRNA. Translation: AAH15890.1 . Different initiation.
    AB025426 mRNA. Translation: BAB87810.1 .
    CR457322 mRNA. Translation: CAG33603.1 .
    AL713782 mRNA. Translation: CAD28542.1 .
    CCDSi CCDS11540.2. [Q9H832-1 ]
    RefSeqi NP_075567.2. NM_023079.4. [Q9H832-1 ]
    UniGenei Hs.514297.

    3D structure databases

    ProteinModelPortali Q9H832.
    SMRi Q9H832. Positions 93-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122419. 29 interactions.
    IntActi Q9H832. 30 interactions.
    MINTi MINT-1388629.
    STRINGi 9606.ENSP00000354201.

    PTM databases

    PhosphoSitei Q9H832.

    Polymorphism databases

    DMDMi 134035344.

    Proteomic databases

    MaxQBi Q9H832.
    PaxDbi Q9H832.
    PRIDEi Q9H832.

    Protocols and materials databases

    DNASUi 65264.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360943 ; ENSP00000354201 ; ENSG00000159202 . [Q9H832-1 ]
    GeneIDi 65264.
    KEGGi hsa:65264.
    UCSCi uc002ioi.3. human. [Q9H832-1 ]

    Organism-specific databases

    CTDi 65264.
    GeneCardsi GC17P046985.
    HGNCi HGNC:25847. UBE2Z.
    HPAi HPA007922.
    MIMi 611362. gene.
    neXtProti NX_Q9H832.
    PharmGKBi PA142670659.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233451.
    HOVERGENi HBG083204.
    InParanoidi Q9H832.
    KOi K10585.
    OMAi AVMANMS.
    OrthoDBi EOG7MSMP5.
    PhylomeDBi Q9H832.
    TreeFami TF354204.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9H832.

    Miscellaneous databases

    GenomeRNAii 65264.
    NextBioi 67390.
    PROi Q9H832.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H832.
    Bgeei Q9H832.
    CleanExi HS_UBE2Z.
    Genevestigatori Q9H832.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging."
      Jin J., Li X., Gygi S.P., Harper J.W.
      Nature 447:1135-1138(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. "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] (ISOFORM 2).
      Tissue: Retinoblastoma and Thyroid.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Skin.
    6. "Molecular cloning of an osteocyte derived gene."
      Ikeda A., Turitani K.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-354.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-354.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-354.
      Tissue: Brain and Pancreas.
    9. "Cloning and characterization of a gene encoding the human putative ubiquitin conjugating enzyme E2Z (UBE2Z)."
      Gu X., Zhao F., Zheng M., Fei X., Chen X., Huang S., Xie Y., Mao Y.
      Mol. Biol. Rep. 34:183-188(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "Identification of novel regulators of apoptosis using a high-throughput cell-based screen."
      Park K.M., Kang E., Jeon Y.-J., Kim N., Kim N.-S., Yoo H.-S., Yeom Y.I., Kim S.J.
      Mol. Cells 23:170-174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBE2Z_HUMAN
    AccessioniPrimary (citable) accession number: Q9H832
    Secondary accession number(s): A6N8M6
    , A6NC60, Q7L354, Q8TCM4, Q9H893
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3