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P22314

- UBA1_HUMAN

UniProt

P22314 - UBA1_HUMAN

Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

UBA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (25 Oct 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei632 – 6321Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi478 – 50730ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. ubiquitin activating enzyme activity Source: RefGenome
    5. ubiquitin-protein transferase activity Source: RefGenome

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. modification-dependent protein catabolic process Source: RefGenome
    4. protein ubiquitination Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme 1
    Alternative name(s):
    Protein A1S9
    Ubiquitin-activating enzyme E1
    Gene namesi
    Name:UBA1
    Synonyms:A1S9T, UBE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12469. UBA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Spinal muscular atrophy X-linked 2 (SMAX2) [MIM:301830]: A lethal infantile form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Clinical features include hypotonia, areflexia, and multiple congenital contractures.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti539 – 5391M → I in SMAX2. 1 Publication
    VAR_043501
    Natural varianti547 – 5471S → G in SMAX2. 1 Publication
    VAR_043502
    Natural varianti557 – 5571E → V in SMAX2. 1 Publication
    VAR_071121

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41S → A: Reduces phosphorylation. 1 Publication
    Mutagenesisi8 – 114KKRR → AAAA: Loss of nuclear localization and a 90-95% decrease in the phosphorylation.

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi301830. phenotype.
    Orphaneti1145. X-linked distal arthrogryposis multiplex congenita.
    PharmGKBiPA37119.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000194934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei46 – 461Phosphoserine4 Publications
    Modified residuei55 – 551PhosphotyrosineBy similarity
    Modified residuei528 – 5281N6-succinyllysineBy similarity
    Modified residuei671 – 6711N6-acetyllysine1 Publication
    Modified residuei800 – 8001Phosphothreonine1 Publication
    Modified residuei810 – 8101Phosphoserine2 Publications
    Modified residuei816 – 8161PhosphoserineBy similarity
    Modified residuei820 – 8201PhosphoserineBy similarity
    Modified residuei835 – 8351Phosphoserine1 Publication
    Modified residuei980 – 9801N6-acetyllysine1 Publication

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP22314.
    PaxDbiP22314.
    PeptideAtlasiP22314.
    PRIDEiP22314.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00645078.

    PTM databases

    PhosphoSiteiP22314.

    Expressioni

    Gene expression databases

    ArrayExpressiP22314.
    BgeeiP22314.
    CleanExiHS_UBA1.
    GenevestigatoriP22314.

    Organism-specific databases

    HPAiCAB019435.
    HPA000289.
    HPA001506.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with GAN (via BTB domain).By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q763532EBI-709688,EBI-6248077From a different organism.
    GANQ9H2C05EBI-709688,EBI-764342
    UBE2IP632792EBI-709688,EBI-80168

    Protein-protein interaction databases

    BioGridi113165. 89 interactions.
    DIPiDIP-33686N.
    IntActiP22314. 28 interactions.
    MINTiMINT-1130980.
    STRINGi9606.ENSP00000338413.

    Structurei

    3D structure databases

    ProteinModelPortaliP22314.
    SMRiP22314. Positions 50-1053.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati63 – 1991371-1Add
    BLAST
    Repeati459 – 6111531-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni5 – 117Nuclear localization signal
    Regioni63 – 6115492 approximate repeatsAdd
    BLAST

    Domaini

    The first 11 amino acids are essential for phosphorylation and exclusive nuclear localization.

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000167329.
    HOVERGENiHBG054199.
    InParanoidiP22314.
    KOiK03178.
    OMAiPFFAFSE.
    OrthoDBiEOG74R1PV.
    PhylomeDBiP22314.
    TreeFamiTF300586.

    Family and domain databases

    Gene3Di1.10.3240.10. 1 hit.
    3.40.50.720. 4 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SMARTiSM00985. UBA_e1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    TIGRFAMsiTIGR01408. Ube1. 1 hit.
    PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P22314-1) [UniParc]FASTAAdd to Basket

    Also known as: E1a

    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

    MSSSPLSKKR RVSGPDPKPG SNCSPAQSVL SEVPSVPTNG MAKNGSEADI     50
    DEGLYSRQLY VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT 100
    LHDQGTAQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP 150
    LVEDFLSGFQ VVVLTNTPLE DQLRVGEFCH NRGIKLVVAD TRGLFGQLFC 200
    DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFESGDFVSF 250
    SEVQGMVELN GNQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 300
    ISFKSLVASL AEPDFVVTDF AKFSRPAQLH IGFQALHQFC AQHGRPPRPR 350
    NEEDAAELVA LAQAVNARAL PAVQQNNLDE DLIRKLAYVA AGDLAPINAF 400
    IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEVLT EDKCLQRQNR 450
    YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEI 500
    IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PHIRVTSHQN 550
    RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT 600
    LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD 650
    EFEGLFKQPA ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP 700
    QTWADCVTWA CHHWHTQYSN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH 750
    PLTFDVNNPL HLDYVMAAAN LFAQTYGLTG SQDRAAVATF LQSVQVPEFT 800
    PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE 850
    KDDDSNFHMD FIVAASNLRA ENYDIPSADR HKSKLIAGKI IPAIATTTAA 900
    VVGLVCLELY KVVQGHRQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ 950
    EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF 1000
    FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV 1050
    PYVRYTIR 1058
    Length:1,058
    Mass (Da):117,849
    Last modified:October 25, 2002 - v3
    Checksum:i4B413AAA75FAA562
    GO
    Isoform 2 (identifier: P22314-2) [UniParc]FASTAAdd to Basket

    Also known as: E1b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

    Show »
    Length:1,018
    Mass (Da):113,800
    Checksum:i9A508347FE29FB19
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901D → G in CAA40296. (PubMed:1606621)Curated
    Sequence conflicti434 – 4341E → Q in CAA40296. (PubMed:1606621)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti447 – 4471R → H.
    Corresponds to variant rs2070169 [ dbSNP | Ensembl ].
    VAR_043500
    Natural varianti539 – 5391M → I in SMAX2. 1 Publication
    VAR_043501
    Natural varianti547 – 5471S → G in SMAX2. 1 Publication
    VAR_043502
    Natural varianti557 – 5571E → V in SMAX2. 1 Publication
    VAR_071121

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040Missing in isoform 2. CuratedVSP_055913Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56976 mRNA. Translation: CAA40296.1.
    M58028 mRNA. Translation: AAA61246.1.
    AL513366 Genomic DNA. Translation: CAI41708.1.
    CH471164 Genomic DNA. Translation: EAW59290.1.
    BC013041 mRNA. Translation: AAH13041.1.
    X52897 mRNA. Translation: CAA37078.1.
    CCDSiCCDS14275.1.
    PIRiA38564.
    RefSeqiNP_003325.2. NM_003334.3.
    NP_695012.1. NM_153280.2.
    XP_005272707.1. XM_005272650.1.
    UniGeneiHs.533273.

    Genome annotation databases

    EnsembliENST00000335972; ENSP00000338413; ENSG00000130985. [P22314-1]
    ENST00000377351; ENSP00000366568; ENSG00000130985. [P22314-1]
    GeneIDi7317.
    KEGGihsa:7317.
    UCSCiuc004dhj.4. human.

    Polymorphism databases

    DMDMi24418865.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56976 mRNA. Translation: CAA40296.1 .
    M58028 mRNA. Translation: AAA61246.1 .
    AL513366 Genomic DNA. Translation: CAI41708.1 .
    CH471164 Genomic DNA. Translation: EAW59290.1 .
    BC013041 mRNA. Translation: AAH13041.1 .
    X52897 mRNA. Translation: CAA37078.1 .
    CCDSi CCDS14275.1.
    PIRi A38564.
    RefSeqi NP_003325.2. NM_003334.3.
    NP_695012.1. NM_153280.2.
    XP_005272707.1. XM_005272650.1.
    UniGenei Hs.533273.

    3D structure databases

    ProteinModelPortali P22314.
    SMRi P22314. Positions 50-1053.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113165. 89 interactions.
    DIPi DIP-33686N.
    IntActi P22314. 28 interactions.
    MINTi MINT-1130980.
    STRINGi 9606.ENSP00000338413.

    Chemistry

    ChEMBLi CHEMBL5924.

    PTM databases

    PhosphoSitei P22314.

    Polymorphism databases

    DMDMi 24418865.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00645078.

    Proteomic databases

    MaxQBi P22314.
    PaxDbi P22314.
    PeptideAtlasi P22314.
    PRIDEi P22314.

    Protocols and materials databases

    DNASUi 7317.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335972 ; ENSP00000338413 ; ENSG00000130985 . [P22314-1 ]
    ENST00000377351 ; ENSP00000366568 ; ENSG00000130985 . [P22314-1 ]
    GeneIDi 7317.
    KEGGi hsa:7317.
    UCSCi uc004dhj.4. human.

    Organism-specific databases

    CTDi 7317.
    GeneCardsi GC0XP047050.
    GeneReviewsi UBA1.
    HGNCi HGNC:12469. UBA1.
    HPAi CAB019435.
    HPA000289.
    HPA001506.
    MIMi 301830. phenotype.
    314370. gene.
    neXtProti NX_P22314.
    Orphaneti 1145. X-linked distal arthrogryposis multiplex congenita.
    PharmGKBi PA37119.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000167329.
    HOVERGENi HBG054199.
    InParanoidi P22314.
    KOi K03178.
    OMAi PFFAFSE.
    OrthoDBi EOG74R1PV.
    PhylomeDBi P22314.
    TreeFami TF300586.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi UBA1. human.
    GeneWikii UBA1.
    GenomeRNAii 7317.
    NextBioi 28604.
    PROi P22314.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22314.
    Bgeei P22314.
    CleanExi HS_UBA1.
    Genevestigatori P22314.

    Family and domain databases

    Gene3Di 1.10.3240.10. 1 hit.
    3.40.50.720. 4 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SMARTi SM00985. UBA_e1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    TIGRFAMsi TIGR01408. Ube1. 1 hit.
    PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1."
      Ayusawa D., Kaneda S., Itoh Y., Yasuda H., Murakami Y., Sugasawa K., Hanaoka F., Seno T.
      Cell Struct. Funct. 17:113-122(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1."
      Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
      Proc. Natl. Acad. Sci. U.S.A. 88:258-262(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 136-158; 369-383; 417-430 AND 559-580.
      Tissue: Placenta.
    3. Erratum
      Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
      Proc. Natl. Acad. Sci. U.S.A. 88:7456-7456(1991) [PubMed] [Europe PMC] [Abstract]
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lymph.
    7. "Molecular cloning, primary structure and expression of the human X linked A1S9 gene cDNA which complements the ts A1S9 mouse L cell defect in DNA replication."
      Zacksenhaus E., Sheinin R.
      EMBO J. 9:2923-2929(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-989.
    8. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 559-581 AND 924-944, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    9. "Isoforms of mammalian ubiquitin-activating enzyme."
      Cook J.C., Chock P.B.
      J. Biol. Chem. 267:24315-24321(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    10. "Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells."
      Schwartz A.L., Trausch J.S., Ciechanover A., Slot J.W., Geuze H.
      Proc. Natl. Acad. Sci. U.S.A. 89:5542-5546(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs."
      Handley-Gearhart P.M., Stephen A.G., Trausch-Azar J.S., Ciechanover A., Schwartz A.L.
      J. Biol. Chem. 269:33171-33178(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2.
    12. "Identification of a region within the ubiquitin-activating enzyme required for nuclear targeting and phosphorylation."
      Stephen A.G., Trausch-Azar J.S., Handley-Gearhart P.M., Ciechanover A., Schwartz A.L.
      J. Biol. Chem. 272:10895-10903(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-4, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-4 AND 8-LYS--ARG-11.
    13. Cited for: ISGYLATION.
    14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
      Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
      Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAN.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-46; THR-800 AND SER-835, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-671 AND LYS-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage."
      Moudry P., Lukas C., Macurek L., Hanzlikova H., Hodny Z., Lukas J., Bartek J.
      Cell Cycle 11:1573-1582(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    25. "Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy."
      Ramser J., Ahearn M.E., Lenski C., Yariz K.O., Hellebrand H., von Rhein M., Clark R.D., Schmutzler R.K., Lichtner P., Hoffman E.P., Meindl A., Baumbach-Reardon L.
      Am. J. Hum. Genet. 82:188-193(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMAX2 ILE-539 AND GLY-547.
    26. "Clinical and neuropathological features of X-linked spinal muscular atrophy (SMAX2) associated with a novel mutation in the UBA1 gene."
      Dlamini N., Josifova D.J., Paine S.M., Wraige E., Pitt M., Murphy A.J., King A., Buk S., Smith F., Abbs S., Sewry C., Jacques T.S., Jungbluth H.
      Neuromuscul. Disord. 23:391-398(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMAX2 VAL-557.

    Entry informationi

    Entry nameiUBA1_HUMAN
    AccessioniPrimary (citable) accession number: P22314
    Secondary accession number(s): Q5JRR8, Q96E13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: October 25, 2002
    Last modified: October 1, 2014
    This is version 167 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

    Miscellaneous

    There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3