Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q02053

- UBA1_MOUSE

UniProt

Q02053 - UBA1_MOUSE

Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity
    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.

    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. protein binding Source: MGI
    3. ubiquitin activating enzyme activity Source: RefGenome
    4. ubiquitin-protein transferase activity Source: RefGenome

    GO - Biological processi

    1. modification-dependent protein catabolic process Source: RefGenome
    2. 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_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme 1
    Alternative name(s):
    Ubiquitin-activating enzyme E1
    Ubiquitin-activating enzyme E1 X
    Ubiquitin-like modifier-activating enzyme 1 X
    Gene namesi
    Name:Uba1
    Synonyms:Sbx, Ube1, Ube1ax, Ube1x
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:98890. Uba1.

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. mitochondrion Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000194935Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei4 – 41PhosphoserineBy similarity
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei46 – 461PhosphoserineBy similarity
    Modified residuei55 – 551Phosphotyrosine1 Publication
    Modified residuei528 – 5281N6-succinyllysine1 Publication
    Modified residuei671 – 6711N6-acetyllysine1 Publication
    Modified residuei800 – 8001PhosphothreonineBy similarity
    Modified residuei810 – 8101PhosphoserineBy similarity
    Modified residuei816 – 8161Phosphoserine1 Publication
    Modified residuei820 – 8201Phosphoserine1 Publication
    Modified residuei835 – 8351PhosphoserineBy similarity
    Modified residuei980 – 9801N6-acetyllysineBy similarity

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ02053.
    PaxDbiQ02053.
    PRIDEiQ02053.

    PTM databases

    PhosphoSiteiQ02053.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. In testis, expressed in A spermatogonia and spermatids but at very low levels in pachytene spermatocytes.1 Publication

    Developmental stagei

    In testis, highly expressed from 14.5 days post coitum (dpc) until the day of birth, with levels falling after 10 days post partum (dpp) but peaking again at 28 dpp.1 Publication

    Inductioni

    May be modulated by the thyroid hormone receptor.

    Gene expression databases

    ArrayExpressiQ02053.
    BgeeiQ02053.
    CleanExiMM_UBA1.
    GenevestigatoriQ02053.

    Interactioni

    Subunit structurei

    Monomer. Interacts with GAN (via BTB domain).

    Protein-protein interaction databases

    BioGridi204410. 6 interactions.
    IntActiQ02053. 7 interactions.
    MINTiMINT-1869675.

    Structurei

    Secondary structure

    1
    1058
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni203 – 2053
    Beta strandi218 – 2258
    Beta strandi227 – 2348
    Beta strandi246 – 25510
    Helixi257 – 2604
    Beta strandi265 – 27814
    Helixi280 – 2823
    Beta strandi288 – 2947
    Helixi631 – 6355
    Helixi641 – 65616
    Helixi658 – 6669
    Helixi671 – 6777
    Helixi683 – 69513
    Turni696 – 6983
    Helixi703 – 71816
    Helixi720 – 7289
    Beta strandi740 – 7423
    Helixi759 – 77517
    Helixi784 – 7929
    Beta strandi809 – 8113
    Helixi824 – 8329
    Helixi836 – 8383
    Helixi858 – 87215
    Helixi880 – 8867

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z7LX-ray2.80A/B/C626-891[»]
    2LZJNMR-A202-312[»]
    2V31NMR-A202-312[»]
    ProteinModelPortaliQ02053.
    SMRiQ02053. Positions 50-1053.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02053.

    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
    Regioni63 – 6115492 approximate repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00390000016689.
    HOGENOMiHOG000167329.
    HOVERGENiHBG054199.
    InParanoidiQ02053.
    KOiK03178.
    OMAiPFFAFSE.
    OrthoDBiEOG74R1PV.
    PhylomeDBiQ02053.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q02053-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI     50
    DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT 100
    LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP 150
    LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH SRGIKLVVAD TRGLFGQLFC 200
    DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF 250
    SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 300
    ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR 350
    NEEDATELVG LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF 400
    IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EEKCLPRQNR 450
    YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV 500
    VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN 550
    RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT 600
    LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD 650
    EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP 700
    QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH 750
    PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT 800
    PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE 850
    KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 900
    VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ 950
    EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF 1000
    FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV 1050
    PYVRYTIR 1058
    Length:1,058
    Mass (Da):117,809
    Last modified:April 1, 1993 - v1
    Checksum:i95D8152ED5C8E037
    GO

    Sequence cautioni

    The sequence CAA44465.1 differs from that shown. Reason: Frameshift at position 1033.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti963 – 9631L → V in CAA44465. (PubMed:1684224)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10576 mRNA. Translation: BAA01433.1.
    AK088057 mRNA. Translation: BAC40121.1.
    AK088528 mRNA. Translation: BAC40405.1.
    AK143416 mRNA. Translation: BAE25369.1.
    AK171667 mRNA. Translation: BAE42599.1.
    AL807240 Genomic DNA. Translation: CAM23092.1.
    BC058630 mRNA. Translation: AAH58630.1.
    BC145984 mRNA. Translation: AAI45985.1.
    X62580 mRNA. Translation: CAA44465.1. Frameshift.
    U09051 Genomic DNA. Translation: AAC52169.1.
    U09055 Genomic DNA. Translation: AAC52171.1.
    CCDSiCCDS30044.1.
    PIRiI48756.
    I63168.
    JC1254.
    RefSeqiNP_001129557.1. NM_001136085.2.
    NP_001263245.1. NM_001276316.1.
    NP_001263246.1. NM_001276317.1.
    NP_033483.2. NM_009457.4.
    UniGeneiMm.1104.

    Genome annotation databases

    EnsembliENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
    ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
    GeneIDi22201.
    KEGGimmu:22201.
    UCSCiuc009stl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10576 mRNA. Translation: BAA01433.1 .
    AK088057 mRNA. Translation: BAC40121.1 .
    AK088528 mRNA. Translation: BAC40405.1 .
    AK143416 mRNA. Translation: BAE25369.1 .
    AK171667 mRNA. Translation: BAE42599.1 .
    AL807240 Genomic DNA. Translation: CAM23092.1 .
    BC058630 mRNA. Translation: AAH58630.1 .
    BC145984 mRNA. Translation: AAI45985.1 .
    X62580 mRNA. Translation: CAA44465.1 . Frameshift.
    U09051 Genomic DNA. Translation: AAC52169.1 .
    U09055 Genomic DNA. Translation: AAC52171.1 .
    CCDSi CCDS30044.1.
    PIRi I48756.
    I63168.
    JC1254.
    RefSeqi NP_001129557.1. NM_001136085.2.
    NP_001263245.1. NM_001276316.1.
    NP_001263246.1. NM_001276317.1.
    NP_033483.2. NM_009457.4.
    UniGenei Mm.1104.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z7L X-ray 2.80 A/B/C 626-891 [» ]
    2LZJ NMR - A 202-312 [» ]
    2V31 NMR - A 202-312 [» ]
    ProteinModelPortali Q02053.
    SMRi Q02053. Positions 50-1053.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204410. 6 interactions.
    IntActi Q02053. 7 interactions.
    MINTi MINT-1869675.

    PTM databases

    PhosphoSitei Q02053.

    Proteomic databases

    MaxQBi Q02053.
    PaxDbi Q02053.
    PRIDEi Q02053.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001989 ; ENSMUSP00000001989 ; ENSMUSG00000001924 .
    ENSMUST00000089217 ; ENSMUSP00000086626 ; ENSMUSG00000001924 .
    GeneIDi 22201.
    KEGGi mmu:22201.
    UCSCi uc009stl.1. mouse.

    Organism-specific databases

    CTDi 7317.
    MGIi MGI:98890. Uba1.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00390000016689.
    HOGENOMi HOG000167329.
    HOVERGENi HBG054199.
    InParanoidi Q02053.
    KOi K03178.
    OMAi PFFAFSE.
    OrthoDBi EOG74R1PV.
    PhylomeDBi Q02053.
    TreeFami TF300586.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi UBA1. mouse.
    EvolutionaryTracei Q02053.
    NextBioi 302189.
    PROi Q02053.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02053.
    Bgeei Q02053.
    CleanExi MM_UBA1.
    Genevestigatori Q02053.

    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. "Cloning and sequence of a functionally active cDNA encoding the mouse ubiquitin-activating enzyme E1."
      Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F., Yamao F.
      Gene 118:279-282(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Ovary and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    5. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 69-81; 90-97; 175-182; 227-239; 351-368; 375-384; 386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671; 679-693; 785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1."
      Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.
      Nature 354:483-487(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
      Strain: 129/Sv.
    7. "Estimating the intensity of male-driven evolution in rodents by using X-linked and Y-linked Ube 1 genes and pseudogenes."
      Chang B.H.-J., Li W.H.
      J. Mol. Evol. 40:70-77(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
      Strain: BALB/c AnCr.
      Tissue: Liver.
    8. "Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor."
      Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A.
      Nucleic Acids Res. 22:4132-4138(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
    9. "Transcriptional analysis of the candidate spermatogenesis gene Ube1y and of the closely related Ube1x shows that they are coexpressed in spermatogonia and spermatids but are repressed in pachytene spermatocytes."
      Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.
      Dev. Biol. 180:336-343(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. Cited for: ISGYLATION.
    11. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-671, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    14. "Crystal structure of a fragment of mouse ubiquitin-activating enzyme."
      Szczepanowski R.H., Filipek R., Bochtler M.
      J. Biol. Chem. 280:22006-22011(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.

    Entry informationi

    Entry nameiUBA1_MOUSE
    AccessioniPrimary (citable) accession number: Q02053
    Secondary accession number(s): A6H6S6, P31253, Q542H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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