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P63165 (SUMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 1

Short name=SUMO-1
Alternative name(s):
GAP-modifying protein 1
Short name=GMP1
SMT3 homolog 3
Sentrin
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name=Smt3C
Ubiquitin-like protein UBL1
Gene names
Name:SUMO1
Synonyms:SMT3C, SMT3H3, UBL1
ORF Names:OK/SW-cl.43
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Ref.4 Ref.14 Ref.26 Ref.28

Subunit structure

Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Ref.16 Ref.18 Ref.19 Ref.21 Ref.23 Ref.26 Ref.33 Ref.36

Subcellular location

Nucleus membrane. Nucleus speckle. Cytoplasm. NucleusPML body. Note: Recruited by BCL11A into the nuclear body By similarity. Ref.14 Ref.15 Ref.17 Ref.35

Post-translational modification

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.

Polymeric SUMO1 chains undergo polyubiquitination by RNF4.

Involvement in disease

Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays. Ref.24

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement Ref.3. Source: ProtInc

PML body organization

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of DNA binding

Inferred from mutant phenotype PubMed 15637059. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 12072434. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15572661. Source: UniProtKB

palate development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of protein complex assembly

Inferred from direct assay PubMed 18579533. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

protein localization to nuclear pore

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from direct assay PubMed 14752048PubMed 15572661PubMed 15637059PubMed 17696781. Source: UniProtKB

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of protein localization

Traceable author statement PubMed 15637059. Source: UniProtKB

   Cellular_componentPML body

Inferred from direct assay Ref.35. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Traceable author statement Ref.4. Source: ProtInc

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 9412458. Source: BHF-UCL

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSUMO ligase activity

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12072434PubMed 14516784PubMed 17081985PubMed 9885291. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.28. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63165-1)

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.
Isoform 2 (identifier: P63165-2)

The sequence of this isoform differs from the canonical sequence as follows:
     4-28: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 9796Small ubiquitin-related modifier 1
PRO_0000035939
Propeptide98 – 1014
PRO_0000035940

Regions

Domain20 – 9778Ubiquitin-like

Sites

Site361Interaction with PIAS2

Amino acid modifications

Modified residue21N-acetylserine Ref.29 Ref.30 Ref.31 Ref.34
Modified residue21Phosphoserine Ref.22 Ref.25 Ref.27 Ref.31 Ref.34
Modified residue91Phosphoserine Ref.31
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.30
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.30
Cross-link97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Natural variations

Alternative sequence4 – 2825Missing in isoform 2.
VSP_046756

Experimental info

Mutagenesis361F → A: Abolishes binding to PIAS2. Ref.40
Sequence conflict751H → N in AAH66306. Ref.13

Secondary structure

....................... 101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: 89BE97D2D054FB33

FASTA10111,557
        10         20         30         40         50         60 
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 

        70         80         90        100 
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V 

« Hide

Isoform 2 [UniParc].

Checksum: 709FCA25A95F9020
Show »

FASTA768,799

References

« Hide 'large scale' references
[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).
Tissue: Brain.
[2]"PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia."
Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.
Oncogene 13:971-982(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain and Placenta.
[3]"UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins."
Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K., Chen D.J.
Genomics 36:271-279(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2."
Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.
Cell 88:97-107(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[5]"A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex."
Matunis M.J., Coutavas E., Blobel G.
J. Cell Biol. 135:1457-1470(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin."
Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F., Chang H.M., Yeh E.T.H.
J. Immunol. 157:4277-4281(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[7]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[8]"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Amygdala.
[11]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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: Placenta.
[14]"Preferential modification of nuclear proteins by a novel ubiquitin-like molecule."
Kamitani T., Nguyen H.P., Yeh E.T.H.
J. Biol. Chem. 272:14001-14004(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
[15]"Cell cycle regulation of PML modification and ND10 composition."
Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.
J. Cell Sci. 112:4581-4588(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif."
Minty A., Dumont X., Kaghad M., Caput D.
J. Biol. Chem. 275:36316-36323(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
[17]"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.
[18]"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.
[19]"The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML."
Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O., Everett R.D.
Exp. Cell Res. 283:36-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK2.
[20]"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.
[21]"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP2.
[22]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Functional modulation of parkin through physical interaction with SUMO-1."
Um J.W., Chung K.C.
J. Neurosci. Res. 84:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARK2.
[24]"SUMO1 haploinsufficiency leads to cleft lip and palate."
Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.
Science 313:1751-1751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION, INVOLVEMENT IN OFC10.
[25]"Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution."
Matic I., Macek B., Hilger M., Walther T.C., Mann M.
J. Proteome Res. 7:4050-4057(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2.
[26]"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.
[27]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-7 AND LYS-25, ACETYLATION AT SER-2.
Tissue: Cervix carcinoma.
[31]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BHLHE40/DEC1.
[34]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[36]"PolySUMO-binding proteins identified through a string search."
Sun H., Hunter T.
J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SIMC1; CASP8AP2; RNF111 AND SOBP.
[37]"Structure determination of the small ubiquitin-related modifier SUMO-1."
Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R., Becker J.
J. Mol. Biol. 280:275-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[38]"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: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2, CLEAVAGE.
[39]"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
Lois L.M., Lima C.D.
EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1; SAE2 AND ATP.
[40]"Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation."
Song J., Zhang Z., Hu W., Chen Y.
J. Biol. Chem. 280:40122-40129(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, MUTAGENESIS OF PHE-36.
[41]"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I; RANGAP1 AND RANBP2.
[42]"Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
[43]"SUMO modification of the ubiquitin-conjugating enzyme E2-25K."
Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R., Olsen J.V., Jentsch S., Melchior F., Sixma T.K.
Nat. Struct. Mol. Biol. 12:264-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
[44]"Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."
Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.
Biochem. J. 398:345-352(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
[45]"SUMO protease SENP1 induces isomerization of the scissile peptide bond."
Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND SENP1.
+Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99586 mRNA. Translation: CAA67898.1.
U61397 mRNA. Translation: AAB40388.1.
U38784 mRNA. Translation: AAC50733.1.
U67122 mRNA. Translation: AAC50996.1.
U72722 mRNA. Translation: AAB40390.1.
U83117 mRNA. Translation: AAB39999.1.
AB062294 mRNA. Translation: BAB93477.1.
BT006632 mRNA. Translation: AAP35278.1.
CR542147 mRNA. Translation: CAG46944.1.
CR542156 mRNA. Translation: CAG46953.1.
AK311840 mRNA. Translation: BAG34782.1.
AC079354 Genomic DNA. Translation: AAY24035.1.
CH471063 Genomic DNA. Translation: EAW70304.1.
CH471063 Genomic DNA. Translation: EAW70307.1.
BC006462 mRNA. Translation: AAH06462.1.
BC053528 mRNA. Translation: AAH53528.1.
BC066306 mRNA. Translation: AAH66306.1.
CCDSCCDS2352.1. [P63165-1]
CCDS46493.1. [P63165-2]
RefSeqNP_001005781.1. NM_001005781.1. [P63165-1]
NP_001005782.1. NM_001005782.1. [P63165-2]
NP_003343.1. NM_003352.4. [P63165-1]
UniGeneHs.81424.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5RNMR-A1-101[»]
1TGZX-ray2.80B18-97[»]
1WYWX-ray2.10B1-97[»]
1Y8RX-ray2.75C/F1-97[»]
1Z5SX-ray3.01B18-97[»]
2ASQNMR-A1-97[»]
2BF8X-ray2.30B21-97[»]
2G4DX-ray2.80B/D20-97[»]
2IO2X-ray2.90B18-97[»]
2IY0X-ray2.77B20-101[»]
2IY1X-ray2.46B/D20-101[»]
2KQSNMR-A1-97[»]
2LASNMR-A20-97[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
3RZWX-ray2.15C/D1-97[»]
3UIPX-ray2.29B18-97[»]
ProteinModelPortalP63165.
SMRP63165. Positions 1-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113188. 777 interactions.
DIPDIP-29080N.
IntActP63165. 91 interactions.
MINTMINT-137859.
STRING9606.ENSP00000376076.

Chemistry

ChEMBLCHEMBL2146296.

PTM databases

PhosphoSiteP63165.

Polymorphism databases

DMDM52783799.

Proteomic databases

MaxQBP63165.
PaxDbP63165.
PRIDEP63165.

Protocols and materials databases

DNASU7341.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392244; ENSP00000376075; ENSG00000116030. [P63165-2]
ENST00000392245; ENSP00000376076; ENSG00000116030. [P63165-1]
ENST00000392246; ENSP00000376077; ENSG00000116030. [P63165-1]
GeneID7341.
KEGGhsa:7341.
UCSCuc002uyz.1. human. [P63165-1]

Organism-specific databases

CTD7341.
GeneCardsGC02M203070.
HGNCHGNC:12502. SUMO1.
HPACAB004269.
HPA056956.
MIM601912. gene.
613705. phenotype.
neXtProtNX_P63165.
Orphanet1991. Cleft lip with or without cleft palate.
PharmGKBPA37149.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5227.
HOGENOMHOG000207495.
HOVERGENHBG053025.
KOK12160.
OrthoDBEOG76X62R.
PhylomeDBP63165.
TreeFamTF315116.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000116030-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
SignaLinkP63165.

Gene expression databases

ArrayExpressP63165.
BgeeP63165.
CleanExHS_SUMO1.
GenevestigatorP63165.

Family and domain databases

InterProIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63165.
GeneWikiSmall_ubiquitin-related_modifier_1.
GenomeRNAi7341.
NextBio28734.
PMAP-CutDBP63165.
PROP63165.
SOURCESearch...

Entry information

Entry nameSUMO1_HUMAN
AccessionPrimary (citable) accession number: P63165
Secondary accession number(s): A8MUS8 expand/collapse secondary AC list , B2R4I5, P55856, Q6FGG0, Q6NZ62, Q93068
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM