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Protein

Small ubiquitin-related modifier 3

Gene

SUMO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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).
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 3Curated
Short name:
SUMO-3Curated
Alternative name(s):
SMT3 homolog 1Imported
SUMO-21 Publication
Ubiquitin-like protein SMT3A1 Publication
Short name:
Smt3A1 Publication
Gene namesi
Name:SUMO3Imported
Synonyms:SMT3A1 Publication, SMT3H1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:11124. SUMO3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • kinetochore Source: ProtInc
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiSUMO3.
DMDMi23503102.

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

BgeeiP55854.
CleanExiHS_SUMO3.
ExpressionAtlasiP55854. baseline and differential.
GenevisibleiP55854. HS.

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
SENP2Q9HC624EBI-474067,EBI-714881
SP100P234972EBI-474067,EBI-751145
USPL1Q5W0Q716EBI-474067,EBI-2513899

Protein-protein interaction databases

BioGridi112496. 44 interactions.
DIPiDIP-29255N.
IntActiP55854. 50 interactions.
MINTiMINT-1398263.
STRINGi9606.ENSP00000330343.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 153Combined sources
Beta strandi16 – 227Combined sources
Turni24 – 263Combined sources
Beta strandi28 – 347Combined sources
Beta strandi35 – 373Combined sources
Helixi40 – 5011Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 615Combined sources
Turni72 – 765Combined sources
Beta strandi82 – 876Combined sources
Beta strandi90 – 923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U4ANMR-A14-92[»]
2IO1X-ray2.60B/D/F14-103[»]
2MP2NMR-A12-92[»]
B2-90[»]
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.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP55854.
KOiK12160.
OMAiYCLCART.
PhylomeDBiP55854.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ
60 70 80 90 100
GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGVPESSLAG

HSF
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 (Ref. 5) Curated
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000411651; ENSP00000409666; ENSG00000184900. [P55854-2]
GeneIDi6612.
KEGGihsa:6612.
UCSCiuc002zfz.1. human. [P55854-1]
uc011afi.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U4ANMR-A14-92[»]
2IO1X-ray2.60B/D/F14-103[»]
2MP2NMR-A12-92[»]
B2-90[»]
ProteinModelPortaliP55854.
SMRiP55854. Positions 14-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112496. 44 interactions.
DIPiDIP-29255N.
IntActiP55854. 50 interactions.
MINTiMINT-1398263.
STRINGi9606.ENSP00000330343.

PTM databases

PhosphoSiteiP55854.

Polymorphism and mutation databases

BioMutaiSUMO3.
DMDMi23503102.

Proteomic databases

MaxQBiP55854.
PaxDbiP55854.
PRIDEiP55854.

Protocols and materials databases

DNASUi6612.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332859; ENSP00000330343; ENSG00000184900.
ENST00000411651; ENSP00000409666; ENSG00000184900. [P55854-2]
GeneIDi6612.
KEGGihsa:6612.
UCSCiuc002zfz.1. human. [P55854-1]
uc011afi.1. human.

Organism-specific databases

CTDi6612.
GeneCardsiGC21M046735.
HGNCiHGNC:11124. SUMO3.
HPAiCAB012180.
HPA042123.
HPA048064.
MIMi602231. gene.
neXtProtiNX_P55854.
PharmGKBiPA35973.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP55854.
KOiK12160.
OMAiYCLCART.
PhylomeDBiP55854.
TreeFamiTF315116.

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).
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiSUMO3. human.
EvolutionaryTraceiP55854.
GeneWikiiSUMO3.
GenomeRNAii6612.
NextBioi25743.
PROiP55854.
SOURCEiSearch...

Gene expression databases

BgeeiP55854.
CleanExiHS_SUMO3.
ExpressionAtlasiP55854. baseline and differential.
GenevisibleiP55854. HS.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage."
    Richard P., Feng S., Manley J.L.
    Genes Dev. 27:2227-2232(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF SETX.
  20. "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.
  21. "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: July 22, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.