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P55854

- SUMO3_HUMAN

UniProt

P55854 - SUMO3_HUMAN

Protein

Small ubiquitin-related modifier 3

Gene

SUMO3

Organism
Homo sapiens (Human)
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 CBX4.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. post-translational protein modification Source: Reactome
    3. protein sumoylation Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_163725. SUMO is proteolytically processed.
    REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small ubiquitin-related modifier 3
    Short name:
    SUMO-3
    Alternative name(s):
    SMT3 homolog 1
    SUMO-2
    Ubiquitin-like protein SMT3B
    Short name:
    Smt3B
    Gene namesi
    Name:SUMO3
    Synonyms:SMT3B, SMT3H1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:11124. SUMO3.

    Subcellular locationi

    Cytoplasm. Nucleus. NucleusPML body By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. kinetochore Source: ProtInc
    4. nucleoplasm Source: Reactome
    5. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111K → R: Abolishes the formation of poly(SUMO) chains. 1 Publication
    Mutagenesisi33 – 331I → A: Impaired interaction with USP25; when associated with A-34. 1 Publication
    Mutagenesisi34 – 341K → A: Impaired interaction with USP25; when associated with A-33. 1 Publication

    Organism-specific databases

    PharmGKBiPA35973.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9292Small ubiquitin-related modifier 3PRO_0000035957Add
    BLAST
    Propeptidei93 – 10311PRO_0000035958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki92 – 92Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

    Post-translational modificationi

    Polymeric chains can be formed through Lys-11 cross-linking.
    Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP55854.
    PaxDbiP55854.
    PRIDEiP55854.

    PTM databases

    PhosphoSiteiP55854.

    Expressioni

    Tissue specificityi

    Expressed predominantly in liver.1 Publication

    Gene expression databases

    ArrayExpressiP55854.
    BgeeiP55854.
    CleanExiHS_SUMO3.
    GenevestigatoriP55854.

    Organism-specific databases

    HPAiCAB012180.
    HPA042123.
    HPA048064.

    Interactioni

    Subunit structurei

    Covalently attached to a number of proteins. Interacts with ARNTL/BMAL1 By similarity. Interacts with USP25 (via ts SIM domain); the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity. Interacts with SAE2 and UBE2I.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SART1O432902EBI-474067,EBI-607761
    SP100P234972EBI-474067,EBI-751145
    USPL1Q5W0Q713EBI-474067,EBI-2513899

    Protein-protein interaction databases

    BioGridi112496. 138 interactions.
    DIPiDIP-29255N.
    IntActiP55854. 49 interactions.
    MINTiMINT-1398263.
    STRINGi9606.ENSP00000330343.

    Structurei

    Secondary structure

    1
    103
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 227
    Turni24 – 263
    Beta strandi28 – 347
    Beta strandi35 – 373
    Helixi40 – 5011
    Helixi54 – 563
    Beta strandi57 – 615
    Turni72 – 765
    Beta strandi82 – 876
    Beta strandi90 – 923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U4ANMR-A14-92[»]
    2IO1X-ray2.60B/D/F14-103[»]
    ProteinModelPortaliP55854.
    SMRiP55854. Positions 14-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55854.

    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.
    HOGENOMiHOG000207495.
    HOVERGENiHBG053025.
    KOiK12160.
    PhylomeDBiP55854.
    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: P55854-1) [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 GGVPESSLAG 100
    HSF 103
    Length:103
    Mass (Da):11,637
    Last modified:September 19, 2002 - v2
    Checksum:iE337E34CB5B3B187
    GO
    Isoform 2 (identifier: P55854-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-50: Q → QVRHLAPPQSLPVCALVLCVPGIPRARASRGWTQMQLPE

    Note: No experimental confirmation available.

    Show »
    Length:141
    Mass (Da):15,768
    Checksum:iB4D3FDFE12CD6B12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321K → E in BAD96311. 1 PublicationCurated
    Sequence conflicti76 – 761E → R in CAA67896. (PubMed:9119407)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381P → S.1 Publication
    Corresponds to variant rs1051311 [ dbSNP | Ensembl ].
    VAR_052692

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 501Q → QVRHLAPPQSLPVCALVLCV PGIPRARASRGWTQMQLPE in isoform 2. 1 PublicationVSP_054693

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99584 mRNA. Translation: CAA67896.1.
    BT007008 mRNA. Translation: AAP35654.1.
    CR542173 mRNA. Translation: CAG46970.1.
    CR542188 mRNA. Translation: CAG46985.1.
    AK222591 mRNA. Translation: BAD96311.1.
    AK300822 mRNA. Translation: BAG62476.1.
    AK312350 mRNA. Translation: BAG35271.1.
    AL773603 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09392.1.
    BC000036 mRNA. Translation: AAH00036.1.
    BC008420 mRNA. Translation: AAH08420.1.
    CCDSiCCDS33587.1. [P55854-1]
    CCDS68220.1. [P55854-2]
    RefSeqiNP_001273345.1. NM_001286416.1. [P55854-2]
    NP_008867.2. NM_006936.2. [P55854-1]
    UniGeneiHs.474005.

    Genome annotation databases

    EnsembliENST00000332859; ENSP00000330343; ENSG00000184900. [P55854-1]
    ENST00000411651; ENSP00000409666; ENSG00000184900. [P55854-2]
    GeneIDi6612.
    KEGGihsa:6612.
    UCSCiuc002zfz.1. human. [P55854-1]

    Polymorphism databases

    DMDMi23503102.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    SUMO protein entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99584 mRNA. Translation: CAA67896.1 .
    BT007008 mRNA. Translation: AAP35654.1 .
    CR542173 mRNA. Translation: CAG46970.1 .
    CR542188 mRNA. Translation: CAG46985.1 .
    AK222591 mRNA. Translation: BAD96311.1 .
    AK300822 mRNA. Translation: BAG62476.1 .
    AK312350 mRNA. Translation: BAG35271.1 .
    AL773603 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09392.1 .
    BC000036 mRNA. Translation: AAH00036.1 .
    BC008420 mRNA. Translation: AAH08420.1 .
    CCDSi CCDS33587.1. [P55854-1 ]
    CCDS68220.1. [P55854-2 ]
    RefSeqi NP_001273345.1. NM_001286416.1. [P55854-2 ]
    NP_008867.2. NM_006936.2. [P55854-1 ]
    UniGenei Hs.474005.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U4A NMR - A 14-92 [» ]
    2IO1 X-ray 2.60 B/D/F 14-103 [» ]
    ProteinModelPortali P55854.
    SMRi P55854. Positions 14-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112496. 138 interactions.
    DIPi DIP-29255N.
    IntActi P55854. 49 interactions.
    MINTi MINT-1398263.
    STRINGi 9606.ENSP00000330343.

    PTM databases

    PhosphoSitei P55854.

    Polymorphism databases

    DMDMi 23503102.

    Proteomic databases

    MaxQBi P55854.
    PaxDbi P55854.
    PRIDEi P55854.

    Protocols and materials databases

    DNASUi 6612.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332859 ; ENSP00000330343 ; ENSG00000184900 . [P55854-1 ]
    ENST00000411651 ; ENSP00000409666 ; ENSG00000184900 . [P55854-2 ]
    GeneIDi 6612.
    KEGGi hsa:6612.
    UCSCi uc002zfz.1. human. [P55854-1 ]

    Organism-specific databases

    CTDi 6612.
    GeneCardsi GC21M046548.
    HGNCi HGNC:11124. SUMO3.
    HPAi CAB012180.
    HPA042123.
    HPA048064.
    MIMi 602231. gene.
    neXtProti NX_P55854.
    PharmGKBi PA35973.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5227.
    HOGENOMi HOG000207495.
    HOVERGENi HBG053025.
    KOi K12160.
    PhylomeDBi P55854.
    TreeFami TF315116.

    Enzyme and pathway databases

    Reactomei REACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_163725. SUMO is proteolytically processed.
    REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

    Miscellaneous databases

    ChiTaRSi SUMO3. human.
    EvolutionaryTracei P55854.
    GeneWikii SUMO3.
    GenomeRNAii 6612.
    NextBioi 25743.
    PROi P55854.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55854.
    Bgeei P55854.
    CleanExi HS_SUMO3.
    Genevestigatori P55854.

    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. "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family."
      Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C.
      Genomics 40:362-367(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-38.
      Tissue: Brain.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain cortex.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Coronary artery.
    6. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Bone marrow and Kidney.
    9. "Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3."
      Saitoh H., Hinchey J.
      J. Biol. Chem. 275:6252-6258(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    10. "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
      Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
      J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF PML, POLYSUMOYLATION, INTERACTION WITH SAE1 AND UBE2I, SUMOYLATION AT LYS-11, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-11.
    11. "Molecular features of human ubiquitin-like SUMO genes and their encoded proteins."
      Su H.-L., Li S.S.-L.
      Gene 296:65-73(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
      Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
      Biochemistry 42:9959-9969(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I.
    13. "A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex."
      Reverter D., Lima C.D.
      Structure 12:1519-1531(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE.
    14. "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
      Xu Z., Au S.W.N.
      Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE, TISSUE SPECIFICITY.
    15. "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3."
      Gong L., Yeh E.T.H.
      J. Biol. Chem. 281:15869-15877(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE.
    16. "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25."
      Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.
      Mol. Cell 30:610-619(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25, MUTAGENESIS OF ILE-33 AND LYS-34.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
      Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
      J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. "Solution structure of human SUMO-3 C47S and its binding surface for Ubc9."
      Ding H., Xu Y., Chen Q., Dai H., Tang Y., Wu J., Shi Y.
      Biochemistry 44:2790-2799(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 14-92.
    20. "The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing."
      Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T.
      Biochem. J. 397:279-288(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH SENP1, CLEAVAGE.

    Entry informationi

    Entry nameiSUMO3_HUMAN
    AccessioniPrimary (citable) accession number: P55854
    Secondary accession number(s): B2R5X4
    , B4DUW4, Q53HI9, Q6FGD4, Q9BWR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3