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P63165 (SUMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. 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·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)
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.27 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. Ref.16 Ref.18 Ref.19 Ref.21 Ref.23 Ref.27

Subcellular location

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

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

Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:613705]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is 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=A chromosomal aberation 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 diversityChromosomal rearrangement
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA repair

Traceable author statement. Source: ProtInc

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of DNA binding

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of transcription, DNA-dependent

Inferred from direct assay. 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. Source: BHF-UCL

protein sumoylation

Inferred from direct assay. Source: UniProtKB

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of protein localization

Traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Traceable author statement. Source: ProtInc

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionubiquitin protein ligase binding

Inferred from physical interaction Ref.28. Source: UniProtKB

Complete GO annotation...

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.31
Modified residue21Phosphoserine Ref.22 Ref.25 Ref.26 Ref.29
Modified residue91Phosphoserine Ref.30
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.31
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.31
Cross-link97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis361F → A: Abolishes binding to PIAS2. Ref.36
Sequence conflict751H → N in AAH66306. Ref.13

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P63165 [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

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: 9119407] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 8806687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 8812453] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 9019411] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 8978815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8906799] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
[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].
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 15815621] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 9162015] [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: 10574707] [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: 10961991] [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: 12383504] [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: 12924945] [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: 12565818] [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: 15487983] [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: 15608651] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
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: 16955485] [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: 16990542] [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: 18707152] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2.
[26]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[27]"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: 18538659] [Abstract]
Cited for: FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25.
[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: 18408734] [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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[30]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[31]"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: 20388717] [Abstract]
Cited for: SUMOYLATION AT LYS-7 AND LYS-25, ACETYLATION AT SER-2.
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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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: 9654451] [Abstract]
Cited for: STRUCTURE BY NMR.
[34]"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: 15296745] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2, CLEAVAGE.
[35]"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: 15660128] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1; SAE2 AND ATP.
[36]"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: 16204249] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, MUTAGENESIS OF PHE-36.
[37]"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed: 15931224] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I; RANGAP1 AND RANBP2.
[38]"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: 15959518] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
[39]"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: 15723079] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
[40]"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: 16712526] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
[41]"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: 17099698] [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.
BC006462 mRNA. Translation: AAH06462.1.
BC053528 mRNA. Translation: AAH53528.1.
BC066306 mRNA. Translation: AAH66306.1.
IPIIPI00303105.
RefSeqNP_001005781.1. NM_001005781.1.
NP_003343.1. NM_003352.4.
UniGeneHs.596171.
Hs.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[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
ProteinModelPortalP63165.
SMRP63165. Positions 1-101.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29080N.
IntActP63165. 59 interactions.
MINTMINT-137859.
STRINGP63165.

PTM databases

PhosphoSiteP63165.

Polymorphism databases

DMDM52783799.

Proteomic databases

PRIDEP63165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392245; ENSP00000376076; ENSG00000116030.
ENST00000392246; ENSP00000376077; ENSG00000116030.
GeneID7341.
KEGGhsa:7341.
UCSCuc002uyz.1. human.

Organism-specific databases

CTD7341.
GeneCardsGC02M203070.
H-InvDBHIX0002747.
HGNCHGNC:12502. SUMO1.
HPACAB004269.
MIM601912. gene.
613705. phenotype.
neXtProtNX_P63165.
Orphanet1991. Cleft lip with or without cleft palate.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20914.
GeneTreeENSGT00390000018808.
HOVERGENHBG053025.
OrthoDBEOG42JNSX.
PhylomeDBP63165.

Enzyme and pathway databases

Pathway_Interaction_DBhdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP63165.
BgeeP63165.
CleanExHS_SUMO1.
GenevestigatorP63165.
GermOnlineENSG00000116030. Homo sapiens.

Family and domain databases

InterProIPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
KOK12160.
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio28734.
PMAP-CutDBP63165.
SOURCESearch...

Entry information

Entry nameSUMO1_HUMAN
AccessionPrimary (citable) accession number: P63165
Secondary accession number(s): B2R4I5 expand/collapse secondary AC list , P55856, Q6FGG0, Q6NZ62, Q93068
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: January 25, 2012
This is version 100 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

Human chromosome 2

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families