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)

Q9R1T2

- SAE1_MOUSE

UniProt

Q9R1T2 - SAE1_MOUSE

Protein

SUMO-activating enzyme subunit 1

Gene

Sae1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein C-terminus binding Source: UniProtKB
    3. SUMO activating enzyme activity Source: RefGenome

    GO - Biological processi

    1. protein sumoylation Source: UniProtKB
    2. regulation of mitotic cell cycle Source: RefGenome
    3. SMT3-dependent protein catabolic process Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SUMO-activating enzyme subunit 1
    Alternative name(s):
    Ubiquitin-like 1-activating enzyme E1A
    Cleaved into the following chain:
    Gene namesi
    Name:Sae1
    Synonyms:Aos1, Sua1, Ubl1a1, Uble1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1929264. Sae1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350SUMO-activating enzyme subunit 1PRO_0000194967Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 350349SUMO-activating enzyme subunit 1, N-terminally processedPRO_0000423291Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processedBy similarity
    Modified residuei202 – 2021N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R1T2.
    PaxDbiQ9R1T2.
    PRIDEiQ9R1T2.

    2D gel databases

    REPRODUCTION-2DPAGEQ9R1T2.

    PTM databases

    PhosphoSiteiQ9R1T2.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in testis.1 Publication

    Gene expression databases

    BgeeiQ9R1T2.
    CleanExiMM_SAE1.
    GenevestigatoriQ9R1T2.

    Interactioni

    Subunit structurei

    Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I By similarity.By similarity

    Protein-protein interaction databases

    BioGridi207998. 3 interactions.
    IntActiQ9R1T2. 1 interaction.
    MINTiMINT-4139487.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R1T2.
    SMRiQ9R1T2. Positions 29-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00550000075007.
    HOGENOMiHOG000172217.
    HOVERGENiHBG080782.
    InParanoidiQ9R1T2.
    KOiK10684.
    OMAiRTPVDYF.
    OrthoDBiEOG7FR7GW.
    PhylomeDBiQ9R1T2.
    TreeFamiTF315037.

    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.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SUPFAMiSSF69572. SSF69572. 1 hit.

    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 splicing. Align

    Isoform 1 (identifier: Q9R1T2-1) [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

    MVEKEEAGGG GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG    50
    LGAEIAKNLI LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL 100
    ERAQNLNPMV DVKVDTEDVE KKPESFFTKF DAVCLTCCSR DVIIKVDQIC 150
    HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE EKTKVAKVSQ GVEDGPEAKR 200
    AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT APDYFLLQVL 250
    LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF 300
    SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ 350
    Length:350
    Mass (Da):38,620
    Last modified:May 1, 2000 - v1
    Checksum:i333108F6E98BABAA
    GO
    Isoform 2 (identifier: Q9R1T2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         321-350: ALSQRDPPHNNFFFFDGMKGSGIVECLGPQ → VCLGTMCV

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):36,135
    Checksum:iD979A4D5950C2E4F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei321 – 35030ALSQR…CLGPQ → VCLGTMCV in isoform 2. 1 PublicationVSP_022004Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024303 mRNA. Translation: BAA82876.1.
    AK010313 mRNA. Translation: BAB26845.1.
    AK011783 mRNA. Translation: BAB27838.1.
    AK087556 mRNA. Translation: BAC39925.1.
    AK090012 mRNA. Translation: BAC41044.1.
    AK154139 mRNA. Translation: BAE32401.1.
    AK159672 mRNA. Translation: BAE35276.1.
    AK162789 mRNA. Translation: BAE37060.1.
    BC068164 mRNA. Translation: AAH68164.1.
    CCDSiCCDS20848.1. [Q9R1T2-1]
    RefSeqiNP_001272820.1. NM_001285891.1. [Q9R1T2-1]
    NP_001272821.1. NM_001285892.1. [Q9R1T2-2]
    NP_062722.1. NM_019748.3. [Q9R1T2-1]
    UniGeneiMm.258530.

    Genome annotation databases

    EnsembliENSMUST00000094815; ENSMUSP00000092409; ENSMUSG00000052833. [Q9R1T2-1]
    GeneIDi56459.
    KEGGimmu:56459.
    UCSCiuc009fhp.1. mouse. [Q9R1T2-1]
    uc009fhq.1. mouse. [Q9R1T2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024303 mRNA. Translation: BAA82876.1 .
    AK010313 mRNA. Translation: BAB26845.1 .
    AK011783 mRNA. Translation: BAB27838.1 .
    AK087556 mRNA. Translation: BAC39925.1 .
    AK090012 mRNA. Translation: BAC41044.1 .
    AK154139 mRNA. Translation: BAE32401.1 .
    AK159672 mRNA. Translation: BAE35276.1 .
    AK162789 mRNA. Translation: BAE37060.1 .
    BC068164 mRNA. Translation: AAH68164.1 .
    CCDSi CCDS20848.1. [Q9R1T2-1 ]
    RefSeqi NP_001272820.1. NM_001285891.1. [Q9R1T2-1 ]
    NP_001272821.1. NM_001285892.1. [Q9R1T2-2 ]
    NP_062722.1. NM_019748.3. [Q9R1T2-1 ]
    UniGenei Mm.258530.

    3D structure databases

    ProteinModelPortali Q9R1T2.
    SMRi Q9R1T2. Positions 29-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207998. 3 interactions.
    IntActi Q9R1T2. 1 interaction.
    MINTi MINT-4139487.

    PTM databases

    PhosphoSitei Q9R1T2.

    2D gel databases

    REPRODUCTION-2DPAGE Q9R1T2.

    Proteomic databases

    MaxQBi Q9R1T2.
    PaxDbi Q9R1T2.
    PRIDEi Q9R1T2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000094815 ; ENSMUSP00000092409 ; ENSMUSG00000052833 . [Q9R1T2-1 ]
    GeneIDi 56459.
    KEGGi mmu:56459.
    UCSCi uc009fhp.1. mouse. [Q9R1T2-1 ]
    uc009fhq.1. mouse. [Q9R1T2-2 ]

    Organism-specific databases

    CTDi 10055.
    MGIi MGI:1929264. Sae1.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00550000075007.
    HOGENOMi HOG000172217.
    HOVERGENi HBG080782.
    InParanoidi Q9R1T2.
    KOi K10684.
    OMAi RTPVDYF.
    OrthoDBi EOG7FR7GW.
    PhylomeDBi Q9R1T2.
    TreeFami TF315037.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

    Miscellaneous databases

    NextBioi 312702.
    PROi Q9R1T2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R1T2.
    CleanExi MM_SAE1.
    Genevestigatori Q9R1T2.

    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.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SUPFAMi SSF69572. SSF69572. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Mus musculus cDNA similar to human Sua1 complete cds, complete cds."
      Kaneta Y., Takada S., Itoh M., Takagi N.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Strain: BALB/c, C57BL/6J and NOD.
      Tissue: Embryo, Embryonic stem cell, Eye and Thymus.
    3. "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).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Expression and regulation of the mammalian SUMO-1 E1 enzyme."
      Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
      FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
    5. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSAE1_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1T2
    Secondary accession number(s): Q3TRG9, Q3TWJ0, Q9CSW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3