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P61957

- SUMO2_MOUSE

UniProt

P61957 - SUMO2_MOUSE

Protein

Small ubiquitin-related modifier 2

Gene

Sumo2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as 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 an E3 ligase 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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins By similarity.By similarity

    GO - Molecular functioni

    1. SUMO ligase activity Source: MGI
    2. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    2. protein sumoylation Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small ubiquitin-related modifier 2
    Short name:
    SUMO-2
    Alternative name(s):
    SMT3 homolog 2
    Sentrin-2
    Ubiquitin-like protein SMT3A
    Short name:
    Smt3A
    Gene namesi
    Name:Sumo2
    Synonyms:Smt3a, Smt3h2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:2158813. Sumo2.

    Subcellular locationi

    Nucleus By similarity. NucleusPML body By similarity

    GO - Cellular componenti

    1. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9393Small ubiquitin-related modifier 2PRO_0000035951Add
    BLAST
    Propeptidei94 – 952By similarityPRO_0000035952

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei11 – 111N6-acetyllysine; alternate1 Publication
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Cross-linki93 – 93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

    Post-translational modificationi

    Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 By similarity.By similarity
    Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
    Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP61957.
    PaxDbiP61957.
    PRIDEiP61957.

    PTM databases

    PhosphoSiteiP61957.

    Expressioni

    Gene expression databases

    BgeeiP61957.
    CleanExiMM_SUMO2.
    GenevestigatoriP61957.

    Interactioni

    Subunit structurei

    Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25 By similarity. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with MTA1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi228466. 16 interactions.
    STRINGi10090.ENSMUSP00000115044.

    Structurei

    3D structure databases

    ProteinModelPortaliP61957.
    SMRiP61957. Positions 1-95.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 9580Ubiquitin-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.
    InParanoidiA2A9X2.
    KOiK12160.
    OMAiDISAKHP.
    OrthoDBiEOG76X62R.
    PhylomeDBiP61957.
    TreeFamiTF315116.

    Family and domain databases

    InterProiIPR022617. Rad60/SUMO_like.
    IPR027218. SUMO_chordates.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
    PfamiPF11976. Rad60-SLD. 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.

    P61957-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER   50
    QGLSMRQIRF RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY 95
    Length:95
    Mass (Da):10,871
    Last modified:June 7, 2004 - v1
    Checksum:iF8F0426849BEF08B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L79948 mRNA. Translation: AAL40136.1.
    AK012619 mRNA. Translation: BAB28360.1.
    AK085238 mRNA. Translation: BAC39397.1.
    AK132213 mRNA. Translation: BAE21037.1.
    AK160404 mRNA. Translation: BAE35772.1.
    AK167308 mRNA. Translation: BAE39412.1.
    AL645470 Genomic DNA. Translation: CAM23014.1.
    BC017522 mRNA. Translation: AAH17522.1.
    BC083326 mRNA. Translation: AAH83326.1.
    BC095930 mRNA. Translation: AAH95930.1.
    CCDSiCCDS36374.1.
    RefSeqiNP_579932.1. NM_133354.2.
    UniGeneiMm.29923.

    Genome annotation databases

    EnsembliENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
    GeneIDi170930.
    KEGGimmu:170930.
    UCSCiuc007mhw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L79948 mRNA. Translation: AAL40136.1 .
    AK012619 mRNA. Translation: BAB28360.1 .
    AK085238 mRNA. Translation: BAC39397.1 .
    AK132213 mRNA. Translation: BAE21037.1 .
    AK160404 mRNA. Translation: BAE35772.1 .
    AK167308 mRNA. Translation: BAE39412.1 .
    AL645470 Genomic DNA. Translation: CAM23014.1 .
    BC017522 mRNA. Translation: AAH17522.1 .
    BC083326 mRNA. Translation: AAH83326.1 .
    BC095930 mRNA. Translation: AAH95930.1 .
    CCDSi CCDS36374.1.
    RefSeqi NP_579932.1. NM_133354.2.
    UniGenei Mm.29923.

    3D structure databases

    ProteinModelPortali P61957.
    SMRi P61957. Positions 1-95.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 228466. 16 interactions.
    STRINGi 10090.ENSMUSP00000115044.

    PTM databases

    PhosphoSitei P61957.

    Proteomic databases

    MaxQBi P61957.
    PaxDbi P61957.
    PRIDEi P61957.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000153892 ; ENSMUSP00000115044 ; ENSMUSG00000020738 .
    GeneIDi 170930.
    KEGGi mmu:170930.
    UCSCi uc007mhw.1. mouse.

    Organism-specific databases

    CTDi 6613.
    MGIi MGI:2158813. Sumo2.

    Phylogenomic databases

    eggNOGi COG5227.
    GeneTreei ENSGT00390000018808.
    HOGENOMi HOG000207495.
    HOVERGENi HBG053025.
    InParanoidi A2A9X2.
    KOi K12160.
    OMAi DISAKHP.
    OrthoDBi EOG76X62R.
    PhylomeDBi P61957.
    TreeFami TF315116.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 370513.
    PROi P61957.
    SOURCEi Search...

    Gene expression databases

    Bgeei P61957.
    CleanExi MM_SUMO2.
    Genevestigatori P61957.

    Family and domain databases

    InterProi IPR022617. Rad60/SUMO_like.
    IPR027218. SUMO_chordates.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10562:SF10. PTHR10562:SF10. 1 hit.
    Pfami PF11976. Rad60-SLD. 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. "Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes."
      Chen A., Mannen H., Li S.S.-L.
      Biochem. Mol. Biol. Int. 46:1161-1174(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    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.
      Tissue: Cerebellum, Embryo, Placenta and Stomach.
    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, Eye and Mammary tumor.
    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-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSUMO2_MOUSE
    AccessioniPrimary (citable) accession number: P61957
    Secondary accession number(s): A2A9X2, P55855, Q542L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 103 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