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P55854

- SUMO3_HUMAN

UniProt

P55854 - SUMO3_HUMAN

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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

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. SUMO ligase activity Source: Ensembl

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  3. post-translational protein modification Source: Reactome
  4. protein localization to nucleus Source: Ensembl
  5. protein sumoylation Source: UniProtKB
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).

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: Chromosome 21

Organism-specific databases

HGNCiHGNC:11124. SUMO3.

Subcellular locationi

Cytoplasm. Nucleus. NucleusPML body By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. kinetochore Source: ProtInc
  4. nuclear body Source: Ensembl
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
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.

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.
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. 392 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 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.
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

        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. 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:
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. [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:
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 .
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U4A NMR - A 14-92 [» ]
2IO1 X-ray 2.60 B/D/F 14-103 [» ]
2MP2 NMR - A 12-92 [» ]
B 2-90 [» ]
ProteinModelPortali P55854.
SMRi P55854. Positions 14-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112496. 392 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 GC21M046735.
HGNCi HGNC:11124. SUMO3.
HPAi CAB012180.
HPA042123.
HPA048064.
MIMi 602231. gene.
neXtProti NX_P55854.
PharmGKBi PA35973.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5227.
GeneTreei ENSGT00390000018808.
HOGENOMi HOG000207495.
HOVERGENi HBG053025.
InParanoidi P55854.
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

Bgeei P55854.
CleanExi HS_SUMO3.
ExpressionAtlasi P55854. baseline and differential.
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

« 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. "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: November 26, 2014
This is version 133 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

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