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P63166

- SUMO1_MOUSE

UniProt

P63166 - SUMO1_MOUSE

Protein

Small ubiquitin-related modifier 1

Gene

Sumo1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei36 – 361Interaction with PIAS2By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. SUMO ligase activity Source: MGI
    3. transcription factor binding Source: MGI
    4. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of DNA binding Source: Ensembl
    2. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    3. negative regulation of transcription, DNA-templated Source: Ensembl
    4. palate development Source: UniProtKB
    5. PML body organization Source: MGI
    6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    7. positive regulation of protein complex assembly Source: Ensembl
    8. protein localization to nuclear pore Source: MGI
    9. protein sumoylation Source: UniProtKB
    10. regulation of transcription, DNA-templated Source: MGI
    11. response to stress Source: UniProtKB-KW

    Keywords - Biological processi

    Stress response, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
    REACT_196649. SUMO is proteolytically processed.
    REACT_198645. Regulation of IFNG signaling.
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small ubiquitin-related modifier 1
    Short name:
    SUMO-1
    Alternative name(s):
    SMT3 homolog 3
    Ubiquitin-homology domain protein PIC1
    Ubiquitin-like protein SMT3C
    Short name:
    Smt3C
    Gene namesi
    Name:Sumo1
    Synonyms:Smt3c, Smt3h3, Ubl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1197010. Sumo1.

    Subcellular locationi

    Nucleus membrane. Nucleus speckle. Cytoplasm. NucleusPML body By similarity
    Note: Recruited by BCL11A into the nuclear body.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. dendrite Source: Ensembl
    3. nuclear body Source: UniProtKB
    4. nuclear membrane Source: UniProtKB-SubCell
    5. nuclear speck Source: UniProtKB-SubCell
    6. nucleus Source: MGI
    7. PML body Source: UniProtKB
    8. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 9796Small ubiquitin-related modifier 1PRO_0000035941Add
    BLAST
    Propeptidei98 – 1014By similarityPRO_0000035942

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21Phosphoserine1 Publication
    Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
    Modified residuei9 – 91PhosphoserineBy similarity
    Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
    Cross-linki97 – 97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

    Post-translational modificationi

    Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
    Polymeric SUMO1 chains undergo polyubiquitination by RNF4.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP63166.
    PaxDbiP63166.
    PRIDEiP63166.

    PTM databases

    PhosphoSiteiP63166.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Developmental stagei

    Expressed at E13.5 strongly in the upper lip, primary palate and medial edge epithelia of the secondary palate. At E14.5 expression could be seen in the medial edge epithelial seam.1 Publication

    Inductioni

    By hypoxia.1 Publication

    Gene expression databases

    BgeeiP63166.
    CleanExiMM_SUMO1.
    GenevestigatoriP63166.

    Interactioni

    Subunit structurei

    Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25 By similarity. Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ikzf1Q032672EBI-80152,EBI-908572
    PTPN1P180312EBI-80152,EBI-968788From a different organism.

    Protein-protein interaction databases

    BioGridi204420. 32 interactions.
    DIPiDIP-29278N.
    IntActiP63166. 7 interactions.
    MINTiMINT-154756.

    Structurei

    3D structure databases

    ProteinModelPortaliP63166.
    SMRiP63166. Positions 1-101.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 9778Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin family. SUMO subfamily.Curated
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5227.
    GeneTreeiENSGT00390000018808.
    HOGENOMiHOG000207495.
    HOVERGENiHBG053025.
    InParanoidiP63166.
    KOiK12160.
    OMAiITDNHTP.
    OrthoDBiEOG76X62R.
    PhylomeDBiP63166.
    TreeFamiTF315116.

    Family and domain databases

    InterProiIPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P63166-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES    50
    YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST 100
    V 101
    Length:101
    Mass (Da):11,557
    Last modified:September 27, 2004 - v1
    Checksum:i89BE97D2D054FB33
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033353 mRNA. Translation: AAC39959.1.
    AK002536 mRNA. Translation: BAB22172.1.
    AK011074 mRNA. Translation: BAB27379.1.
    AK089081 mRNA. Translation: BAC40739.1.
    AK159366 mRNA. Translation: BAE35024.1.
    BC082566 mRNA. Translation: AAH82566.1.
    BC083158 mRNA. Translation: AAH83158.1.
    CCDSiCCDS35586.1.
    RefSeqiNP_033486.1. NM_009460.2.
    UniGeneiMm.362118.

    Genome annotation databases

    EnsembliENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
    GeneIDi22218.
    KEGGimmu:22218.
    UCSCiuc007bdx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033353 mRNA. Translation: AAC39959.1 .
    AK002536 mRNA. Translation: BAB22172.1 .
    AK011074 mRNA. Translation: BAB27379.1 .
    AK089081 mRNA. Translation: BAC40739.1 .
    AK159366 mRNA. Translation: BAE35024.1 .
    BC082566 mRNA. Translation: AAH82566.1 .
    BC083158 mRNA. Translation: AAH83158.1 .
    CCDSi CCDS35586.1.
    RefSeqi NP_033486.1. NM_009460.2.
    UniGenei Mm.362118.

    3D structure databases

    ProteinModelPortali P63166.
    SMRi P63166. Positions 1-101.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204420. 32 interactions.
    DIPi DIP-29278N.
    IntActi P63166. 7 interactions.
    MINTi MINT-154756.

    PTM databases

    PhosphoSitei P63166.

    Proteomic databases

    MaxQBi P63166.
    PaxDbi P63166.
    PRIDEi P63166.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091374 ; ENSMUSP00000088935 ; ENSMUSG00000026021 .
    GeneIDi 22218.
    KEGGi mmu:22218.
    UCSCi uc007bdx.1. mouse.

    Organism-specific databases

    CTDi 7341.
    MGIi MGI:1197010. Sumo1.

    Phylogenomic databases

    eggNOGi COG5227.
    GeneTreei ENSGT00390000018808.
    HOGENOMi HOG000207495.
    HOVERGENi HBG053025.
    InParanoidi P63166.
    KOi K12160.
    OMAi ITDNHTP.
    OrthoDBi EOG76X62R.
    PhylomeDBi P63166.
    TreeFami TF315116.

    Enzyme and pathway databases

    Reactomei REACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
    REACT_196649. SUMO is proteolytically processed.
    REACT_198645. Regulation of IFNG signaling.
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

    Miscellaneous databases

    NextBioi 28734.
    PROi P63166.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63166.
    CleanExi MM_SUMO1.
    Genevestigatori P63166.

    Family and domain databases

    InterProi IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The ubiquitin-homology gene PIC1: characterization of mouse (Pic1) and human (UBL1) genes and pseudogenes."
      Howe K., Williamson J., Boddy M.N., Sheer D., Freemont P.S., Solomon E.
      Genomics 47:92-100(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ICR.
    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: Kidney, Liver 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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Colon and Eye.
    4. "Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1alpha in adult mouse brain and heart in vivo."
      Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X., Sjoeland H., Billig H.
      FEBS Lett. 569:293-300(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH HIF1A.
    5. Cited for: INTERACTION WITH IKFZ1.
    6. "SUMO1 haploinsufficiency leads to cleft lip and palate."
      Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.
      Science 313:1751-1751(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    7. "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body."
      Kuwata T., Nakamura T.
      Genes Cells 13:931-940(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSUMO1_MOUSE
    AccessioniPrimary (citable) accession number: P63166
    Secondary accession number(s): P55856, Q3TX92, Q93068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 106 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3