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Q9GZZ9

- UBA5_HUMAN

UniProt

Q9GZZ9 - UBA5_HUMAN

Protein

Ubiquitin-like modifier-activating enzyme 5

Gene

UBA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    E1-like enzyme which activates UFM1 and SUMO2.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei83 – 831ATP; via amide nitrogen1 Publication
    Binding sitei104 – 1041ATP1 Publication
    Binding sitei127 – 1271ATP1 Publication
    Binding sitei150 – 1501ATP1 Publication
    Binding sitei184 – 1841ATP1 Publication
    Metal bindingi226 – 2261Zinc1 Publication
    Metal bindingi229 – 2291Zinc1 Publication
    Active sitei250 – 2501Glycyl thioester intermediate1 Publication
    Metal bindingi303 – 3031Zinc1 Publication
    Metal bindingi308 – 3081Zinc1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cofactor binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
    5. protein binding Source: IntAct
    6. UFM1 activating enzyme activity Source: UniProtKB

    GO - Biological processi

    1. protein ufmylation Source: UniProtKB
    2. response to endoplasmic reticulum stress Source: MGI

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme 5
    Short name:
    Ubiquitin-activating enzyme 5
    Alternative name(s):
    ThiFP1
    UFM1-activating enzyme
    Ubiquitin-activating enzyme E1 domain-containing protein 1
    Gene namesi
    Name:UBA5
    Synonyms:UBE1DC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:23230. UBA5.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Localizes mainly in cytoplasm, while it mainly localizes to the nucleus in presence of SUMO2.

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: RefGenome
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi250 – 2501C → S: Forms a stable intermediate complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA162407661.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Ubiquitin-like modifier-activating enzyme 5PRO_0000194970Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei358 – 3581Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9GZZ9.
    PaxDbiQ9GZZ9.
    PRIDEiQ9GZZ9.

    PTM databases

    PhosphoSiteiQ9GZZ9.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZZ9.
    BgeeiQ9GZZ9.
    CleanExiHS_UBA5.
    GenevestigatoriQ9GZZ9.

    Organism-specific databases

    HPAiHPA017235.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951662EBI-747805,EBI-712001
    GABARAPL1Q9H0R82EBI-747805,EBI-746969
    GABARAPL2P6052010EBI-747805,EBI-720116
    MAP1LC3BQ9GZQ82EBI-747805,EBI-373144
    MAP1LC3CQ9BXW42EBI-747805,EBI-2603996

    Protein-protein interaction databases

    BioGridi122964. 50 interactions.
    IntActiQ9GZZ9. 37 interactions.
    MINTiMINT-1475093.
    STRINGi9606.ENSP00000348565.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi70 – 734
    Beta strandi75 – 795
    Helixi83 – 9513
    Beta strandi98 – 1036
    Helixi120 – 1223
    Helixi127 – 13812
    Beta strandi142 – 1476
    Helixi154 – 16613
    Beta strandi167 – 1704
    Beta strandi176 – 1805
    Helixi185 – 19814
    Beta strandi202 – 2076
    Beta strandi211 – 2199
    Turni221 – 2233
    Beta strandi229 – 2313
    Helixi247 – 27428
    Beta strandi281 – 2866
    Turni287 – 2904
    Helixi306 – 31712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GUCX-ray2.25A/B57-329[»]
    3H8VX-ray2.00A/B57-329[»]
    ProteinModelPortaliQ9GZZ9.
    SMRiQ9GZZ9. Positions 43-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZZ9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family. UBA5 subfamily.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000256352.
    HOVERGENiHBG056496.
    InParanoidiQ9GZZ9.
    KOiK12164.
    OMAiNYNITTM.
    OrthoDBiEOG7N63MX.
    PhylomeDBiQ9GZZ9.
    TreeFamiTF314168.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9GZZ9-1) [UniParc]FASTAAdd to Basket

    Also known as: UBE1DC1A

    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

    MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS    50
    NPYSRLMALK RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL 100
    LLFDYDKVEL ANMNRLFFQP HQAGLSKVQA AEHTLRNINP DVLFEVHNYN 150
    ITTVENFQHF MDRISNGGLE EGKPVDLVLS CVDNFEARMT INTACNELGQ 200
    TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID EKTLKREGVC 250
    AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN 300
    PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS 350
    EEELKNFSGP VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK 400
    MKNM 404
    Length:404
    Mass (Da):44,863
    Last modified:March 1, 2001 - v1
    Checksum:i02F0F64FEAA1E880
    GO
    Isoform 2 (identifier: Q9GZZ9-2) [UniParc]FASTAAdd to Basket

    Also known as: UBE1DC1B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.

    Show »
    Length:348
    Mass (Da):38,537
    Checksum:i127B3CB48EB035B1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031N → S in BAB55199. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 2. CuratedVSP_038528Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB154406 mRNA. Translation: BAD15375.1.
    AY253672 mRNA. Translation: AAP79600.1.
    AL136757 mRNA. Translation: CAB66691.1.
    AK026904 mRNA. Translation: BAB15587.1.
    AK027563 mRNA. Translation: BAB55199.1.
    AC020632 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79192.1.
    CH471052 Genomic DNA. Translation: EAW79189.1.
    CH471052 Genomic DNA. Translation: EAW79191.1.
    BC009737 mRNA. Translation: AAH09737.1.
    CCDSiCCDS3076.1. [Q9GZZ9-1]
    CCDS3077.1. [Q9GZZ9-2]
    RefSeqiNP_079094.1. NM_024818.3. [Q9GZZ9-1]
    NP_938143.1. NM_198329.2. [Q9GZZ9-2]
    XP_005247844.1. XM_005247787.2. [Q9GZZ9-2]
    UniGeneiHs.170737.

    Genome annotation databases

    EnsembliENST00000264991; ENSP00000264991; ENSG00000081307. [Q9GZZ9-2]
    ENST00000356232; ENSP00000348565; ENSG00000081307. [Q9GZZ9-1]
    ENST00000494238; ENSP00000418807; ENSG00000081307. [Q9GZZ9-2]
    GeneIDi79876.
    KEGGihsa:79876.
    UCSCiuc003epa.4. human. [Q9GZZ9-1]

    Polymorphism databases

    DMDMi74733510.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB154406 mRNA. Translation: BAD15375.1 .
    AY253672 mRNA. Translation: AAP79600.1 .
    AL136757 mRNA. Translation: CAB66691.1 .
    AK026904 mRNA. Translation: BAB15587.1 .
    AK027563 mRNA. Translation: BAB55199.1 .
    AC020632 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79192.1 .
    CH471052 Genomic DNA. Translation: EAW79189.1 .
    CH471052 Genomic DNA. Translation: EAW79191.1 .
    BC009737 mRNA. Translation: AAH09737.1 .
    CCDSi CCDS3076.1. [Q9GZZ9-1 ]
    CCDS3077.1. [Q9GZZ9-2 ]
    RefSeqi NP_079094.1. NM_024818.3. [Q9GZZ9-1 ]
    NP_938143.1. NM_198329.2. [Q9GZZ9-2 ]
    XP_005247844.1. XM_005247787.2. [Q9GZZ9-2 ]
    UniGenei Hs.170737.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GUC X-ray 2.25 A/B 57-329 [» ]
    3H8V X-ray 2.00 A/B 57-329 [» ]
    ProteinModelPortali Q9GZZ9.
    SMRi Q9GZZ9. Positions 43-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122964. 50 interactions.
    IntActi Q9GZZ9. 37 interactions.
    MINTi MINT-1475093.
    STRINGi 9606.ENSP00000348565.

    Chemistry

    ChEMBLi CHEMBL2016429.

    PTM databases

    PhosphoSitei Q9GZZ9.

    Polymorphism databases

    DMDMi 74733510.

    Proteomic databases

    MaxQBi Q9GZZ9.
    PaxDbi Q9GZZ9.
    PRIDEi Q9GZZ9.

    Protocols and materials databases

    DNASUi 79876.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264991 ; ENSP00000264991 ; ENSG00000081307 . [Q9GZZ9-2 ]
    ENST00000356232 ; ENSP00000348565 ; ENSG00000081307 . [Q9GZZ9-1 ]
    ENST00000494238 ; ENSP00000418807 ; ENSG00000081307 . [Q9GZZ9-2 ]
    GeneIDi 79876.
    KEGGi hsa:79876.
    UCSCi uc003epa.4. human. [Q9GZZ9-1 ]

    Organism-specific databases

    CTDi 79876.
    GeneCardsi GC03P132373.
    HGNCi HGNC:23230. UBA5.
    HPAi HPA017235.
    MIMi 610552. gene.
    neXtProti NX_Q9GZZ9.
    PharmGKBi PA162407661.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000256352.
    HOVERGENi HBG056496.
    InParanoidi Q9GZZ9.
    KOi K12164.
    OMAi NYNITTM.
    OrthoDBi EOG7N63MX.
    PhylomeDBi Q9GZZ9.
    TreeFami TF314168.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q9GZZ9.
    GeneWikii UBE1DC1.
    GenomeRNAii 79876.
    NextBioi 69659.
    PROi Q9GZZ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZZ9.
    Bgeei Q9GZZ9.
    CleanExi HS_UBA5.
    Genevestigatori Q9GZZ9.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier."
      Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N., Ueno T., Kominami E., Natsume T., Tanaka K.
      EMBO J. 23:1977-1986(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-250.
    2. "Isolation and characterization of ubiquitin-activating enzyme E1-domain containing 1, UBE1DC1."
      Dou T., Gu S., Liu J., Chen F., Zeng L., Guo L., Xie Y., Mao Y.
      Mol. Biol. Rep. 32:265-271(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: TestisImported.
    4. "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 1).
      Tissue: ColonImported and TeratocarcinomaImported.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: LungImported.
    8. "UBE1DC1, an ubiquitin-activating enzyme, activates two different ubiquitin-like proteins."
      Zheng M., Gu X., Zheng D., Yang Z., Li F., Zhao J., Xie Y., Ji C., Mao Y.
      J. Cell. Biochem. 104:2324-2334(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme."
      Bacik J.P., Walker J.R., Ali M., Schimmer A.D., Dhe-Paganon S.
      J. Biol. Chem. 285:20273-20280(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP AND ZINC, FUNCTION, ACTIVE SITE.

    Entry informationi

    Entry nameiUBA5_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZZ9
    Secondary accession number(s): A6NJL3, D3DNC8, Q96ST1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3