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Q9Z172

- SUMO3_MOUSE

UniProt

Q9Z172 - SUMO3_MOUSE

Protein

Small ubiquitin-related modifier 3

Gene

Sumo3

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

    Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment 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 By similarity.By similarity

    GO - Molecular functioni

    1. SUMO ligase activity Source: MGI

    GO - Biological processi

    1. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
    2. protein localization to nucleus Source: MGI
    3. 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 3
    Short name:
    SUMO-3
    Alternative name(s):
    SMT3 homolog 1
    Ubiquitin-like protein SMT3B
    Short name:
    Smt3B
    Gene namesi
    Name:Sumo3
    Synonyms:Smt3b, Smt3h1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1336201. Sumo3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. NucleusPML body 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear body Source: MGI
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9292Small ubiquitin-related modifier 3PRO_0000035959Add
    BLAST
    Propeptidei93 – 11018By similarityPRO_0000035960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki92 – 92Glycyl 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.By similarity
    Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiQ9Z172.
    PRIDEiQ9Z172.

    PTM databases

    PhosphoSiteiQ9Z172.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z172.
    BgeeiQ9Z172.
    CleanExiMM_SUMO3.
    GenevestigatoriQ9Z172.

    Interactioni

    Subunit structurei

    Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with USP25 (via ts SIM domain); the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity By similarity. Interacts with ARNTL/BMAL1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi203358. 6 interactions.
    IntActiQ9Z172. 1 interaction.
    MINTiMINT-4134935.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z172.
    SMRiQ9Z172. Positions 14-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 9278Ubiquitin-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.
    InParanoidiQ9Z172.
    KOiK12160.
    OrthoDBiEOG76X62R.
    PhylomeDBiQ9Z172.
    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]

    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: Q9Z172-1) [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

    MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ    50
    GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGSASRGSVP 100
    TPNRCPDLCY 110
    Length:110
    Mass (Da):12,430
    Last modified:May 1, 1999 - v1
    Checksum:i2950B8B1A3F88DC8
    GO
    Isoform 2 (identifier: Q9Z172-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: MSEEKPK → MTTVLAQ

    Note: No experimental confirmation available.

    Show »
    Length:110
    Mass (Da):12,345
    Checksum:iC7BD3DAAB055D5F2
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 77MSEEKPK → MTTVLAQ in isoform 2. 1 PublicationVSP_021948

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063847 mRNA. Translation: AAC99333.1.
    AK012742 mRNA. Translation: BAB28442.1.
    AK013019 mRNA. Translation: BAB28601.1.
    AK148306 mRNA. Translation: BAE28469.1.
    AK150063 mRNA. Translation: BAE29276.1.
    AK150200 mRNA. Translation: BAE29374.1.
    AK160169 mRNA. Translation: BAE35670.1.
    AK162035 mRNA. Translation: BAE36692.1.
    AK167207 mRNA. Translation: BAE39334.1.
    AK168988 mRNA. Translation: BAE40788.1.
    AK171169 mRNA. Translation: BAE42290.1.
    AK170896 mRNA. Translation: BAE42100.1.
    BC115488 mRNA. Translation: AAI15489.1.
    BC115489 mRNA. Translation: AAI15490.1.
    CCDSiCCDS23958.1. [Q9Z172-1]
    RefSeqiNP_064313.1. NM_019929.3. [Q9Z172-1]
    XP_006513489.1. XM_006513426.1. [Q9Z172-2]
    UniGeneiMm.24433.

    Genome annotation databases

    EnsembliENSMUST00000020501; ENSMUSP00000020501; ENSMUSG00000020265. [Q9Z172-1]
    ENSMUST00000099538; ENSMUSP00000097136; ENSMUSG00000020265. [Q9Z172-2]
    GeneIDi20610.
    KEGGimmu:20610.
    UCSCiuc007fvy.1. mouse. [Q9Z172-1]
    uc007fvz.1. mouse. [Q9Z172-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063847 mRNA. Translation: AAC99333.1 .
    AK012742 mRNA. Translation: BAB28442.1 .
    AK013019 mRNA. Translation: BAB28601.1 .
    AK148306 mRNA. Translation: BAE28469.1 .
    AK150063 mRNA. Translation: BAE29276.1 .
    AK150200 mRNA. Translation: BAE29374.1 .
    AK160169 mRNA. Translation: BAE35670.1 .
    AK162035 mRNA. Translation: BAE36692.1 .
    AK167207 mRNA. Translation: BAE39334.1 .
    AK168988 mRNA. Translation: BAE40788.1 .
    AK171169 mRNA. Translation: BAE42290.1 .
    AK170896 mRNA. Translation: BAE42100.1 .
    BC115488 mRNA. Translation: AAI15489.1 .
    BC115489 mRNA. Translation: AAI15490.1 .
    CCDSi CCDS23958.1. [Q9Z172-1 ]
    RefSeqi NP_064313.1. NM_019929.3. [Q9Z172-1 ]
    XP_006513489.1. XM_006513426.1. [Q9Z172-2 ]
    UniGenei Mm.24433.

    3D structure databases

    ProteinModelPortali Q9Z172.
    SMRi Q9Z172. Positions 14-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203358. 6 interactions.
    IntActi Q9Z172. 1 interaction.
    MINTi MINT-4134935.

    PTM databases

    PhosphoSitei Q9Z172.

    Proteomic databases

    PaxDbi Q9Z172.
    PRIDEi Q9Z172.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020501 ; ENSMUSP00000020501 ; ENSMUSG00000020265 . [Q9Z172-1 ]
    ENSMUST00000099538 ; ENSMUSP00000097136 ; ENSMUSG00000020265 . [Q9Z172-2 ]
    GeneIDi 20610.
    KEGGi mmu:20610.
    UCSCi uc007fvy.1. mouse. [Q9Z172-1 ]
    uc007fvz.1. mouse. [Q9Z172-2 ]

    Organism-specific databases

    CTDi 6612.
    MGIi MGI:1336201. Sumo3.

    Phylogenomic databases

    eggNOGi COG5227.
    GeneTreei ENSGT00390000018808.
    HOGENOMi HOG000207495.
    HOVERGENi HBG053025.
    InParanoidi Q9Z172.
    KOi K12160.
    OrthoDBi EOG76X62R.
    PhylomeDBi Q9Z172.
    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

    ChiTaRSi SUMO3. mouse.
    NextBioi 298967.
    PROi Q9Z172.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z172.
    Bgeei Q9Z172.
    CleanExi MM_SUMO3.
    Genevestigatori Q9Z172.

    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] (ISOFORM 1).
      Tissue: Liver.
    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: C57BL/6J.
      Tissue: Bone marrow, Embryo, Kidney, Muellerian duct and Small intestine.
    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).
    4. "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex."
      Lee J., Lee Y., Lee M.J., Park E., Kang S.H., Chung C.H., Lee K.H., Kim K.
      Mol. Cell. Biol. 28:6056-6065(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ARNTL/BMAL1.

    Entry informationi

    Entry nameiSUMO3_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z172
    Secondary accession number(s): Q14C17, Q3TBL9, Q3UDI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 102 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