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UniProtKB/Swiss-Prot entry P63165


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SUMO1_HUMAN
Primary accession number P63165
Secondary accession numbers P55856 Q6FGG0 Q6NZ62 Q93068
Integrated into Swiss-Prot on September 27, 2004
Sequence was last modified on September 27, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name Small ubiquitin-related modifier 1 [Precursor]
Synonyms SUMO-1
Sentrin
Ubiquitin-like protein SMT3C
SMT3 homolog 3
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein UBL1
GAP-modifying protein 1
GMP1
Gene name
Name: SUMO1
Synonyms: SMT3C, SMT3H3, UBL1
ORFNames: OK/SW-cl.43
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1006/geno.1996.4556; PubMed=9119407 [NCBI, ExPASy, EBI, Israel, Japan]
Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C.;
"SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family.";
Genomics 40:362-367(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Placenta;
PubMed=8806687 [NCBI, ExPASy, EBI, Israel, Japan]
Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.;
"PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.";
Oncogene 13:971-982(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/geno.1996.0462; PubMed=8812453 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K., Chen D.J.;
"UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins.";
Genomics 36:271-279(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
DOI=10.1016/S0092-8674(00)81862-0; PubMed=9019411 [NCBI, ExPASy, EBI, Israel, Japan]
Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.;
"A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.";
Cell 88:97-107(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1083/jcb.135.6.1457; PubMed=8978815 [NCBI, ExPASy, EBI, Israel, Japan]
Matunis M.J., Coutavas E., Blobel G.;
"A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.";
J. Cell Biol. 135:1457-1470(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8906799 [NCBI, ExPASy, EBI, Israel, Japan]
Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F., Chang H.M., Yeh E.T.H.;
"Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.";
J. Immunol. 157:4277-4281(1996).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
DOI=10.1074/jbc.272.22.14001; PubMed=9162015 [NCBI, ExPASy, EBI, Israel, Japan]
Kamitani T., Nguyen H.P., Yeh E.T.H.;
"Preferential modification of nuclear proteins by a novel ubiquitin-like molecule.";
J. Biol. Chem. 272:14001-14004(1997).
[13]
SUBCELLULAR LOCATION.
PubMed=10574707 [NCBI, ExPASy, EBI, Israel, Japan]
Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.;
"Cell cycle regulation of PML modification and ND10 composition.";
J. Cell Sci. 112:4581-4588(1999).
[14]
INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
DOI=10.1074/jbc.M004293200; PubMed=10961991 [NCBI, ExPASy, EBI, Israel, Japan]
Minty A., Dumont X., Kaghad M., Caput D.;
"Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.";
J. Biol. Chem. 275:36316-36323(2000).
[15]
SUBCELLULAR LOCATION.
DOI=10.1016/S0378-1119(02)00843-0; PubMed=12383504 [NCBI, ExPASy, EBI, Israel, Japan]
Su H.-L., Li S.S.-L.;
"Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.";
Gene 296:65-73(2002).
[16]
INTERACTION WITH UBE2I.
DOI=10.1021/bi0345283; PubMed=12924945 [NCBI, ExPASy, EBI, Israel, Japan]
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.;
"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.";
Biochemistry 42:9959-9969(2003).
[17]
INTERACTION WITH HIPK2.
DOI=10.1016/S0014-4827(02)00025-3; PubMed=12565818 [NCBI, ExPASy, EBI, Israel, Japan]
Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O., Everett R.D.;
"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.";
Exp. Cell Res. 283:36-50(2003).
[18]
CLEAVAGE.
DOI=10.1042/BJ20041210; PubMed=15487983 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Z., Au S.W.N.;
"Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1.";
Biochem. J. 386:325-330(2005).
[19]
INTERACTION WITH RANBP2.
DOI=10.1038/nsmb878; PubMed=15608651 [NCBI, ExPASy, EBI, Israel, Japan]
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection.";
Nat. Struct. Mol. Biol. 12:67-74(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[21]
INTERACTION WITH PARK2.
DOI=10.1002/jnr.21041; PubMed=16955485 [NCBI, ExPASy, EBI, Israel, Japan]
Um J.W., Chung K.C.;
"Functional modulation of parkin through physical interaction with SUMO-1.";
J. Neurosci. Res. 84:1543-1554(2006).
[22]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1998.1839; PubMed=9654451 [NCBI, ExPASy, EBI, Israel, Japan]
Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R., Becker J.;
"Structure determination of the small ubiquitin-related modifier SUMO-1.";
J. Mol. Biol. 280:275-286(1998).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2, AND CLEAVAGE.
DOI=10.1016/j.str.2004.05.023; PubMed=15296745 [NCBI, ExPASy, EBI, Israel, Japan]
Reverter D., Lima C.D.;
"A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.";
Structure 12:1519-1531(2004).
[24]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1; SAE2 AND ATP.
DOI=10.1038/sj.emboj.7600552; PubMed=15660128 [NCBI, ExPASy, EBI, Israel, Japan]
Lois L.M., Lima C.D.;
"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.";
EMBO J. 24:439-451(2005).
[25]
STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, AND MUTAGENESIS OF PHE-36.
DOI=10.1074/jbc.M507059200; PubMed=16204249 [NCBI, ExPASy, EBI, Israel, Japan]
Song J., Zhang Z., Hu W., Chen Y.;
"Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation.";
J. Biol. Chem. 280:40122-40129(2005).
[26]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I; RANGAP1 AND RANBP2.
DOI=10.1038/nature03588; PubMed=15931224 [NCBI, ExPASy, EBI, Israel, Japan]
Reverter D., Lima C.D.;
"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.";
Nature 435:687-692(2005).
[27]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
DOI=10.1038/nature03634; PubMed=15959518 [NCBI, ExPASy, EBI, Israel, Japan]
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
"Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.";
Nature 435:979-982(2005).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
DOI=10.1038/nsmb903; PubMed=15723079 [NCBI, ExPASy, EBI, Israel, Japan]
Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R., Olsen J.V., Jentsch S., Melchior F., Sixma T.K.;
"SUMO modification of the ubiquitin-conjugating enzyme E2-25K.";
Nat. Struct. Mol. Biol. 12:264-269(2005).
[29]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
DOI=10.1042/BJ20060526; PubMed=16712526 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.;
"Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease.";
Biochem. J. 398:345-352(2006).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
Dong C., Shen L., Taitham M., Hay R.T., Naismith J.H.;
"Complexes of SEN protease.";
Submitted (AUG-2006) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X99586; CAA67898.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U61397; AAB40388.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U38784; AAC50733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67122; AAC50996.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U72722; AAB40390.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U83117; AAB39999.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062294; BAB93477.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006632; AAP35278.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542147; CAG46944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542156; CAG46953.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079354; AAY24035.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006462; AAH06462.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053528; AAH53528.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066306; AAH66306.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001005781.1; -.
NP_003343.1; -.
UniGene Hs.81424
3D structure databases
PDB
1A5R; NMR; -; A=1-101.[ExPASy / RCSB / EBI]
1TGZ; X-ray; 2.80 A; B=18-97.[ExPASy / RCSB / EBI]
1WYW; X-ray; 2.10 A; B=1-97.[ExPASy / RCSB / EBI]
1Y8R; X-ray; 2.75 A; C/F=1-97.[ExPASy / RCSB / EBI]
1Z5S; X-ray; 3.01 A; B=18-97.[ExPASy / RCSB / EBI]
2ASQ; NMR; -; A=1-97.[ExPASy / RCSB / EBI]
2BF8; X-ray; 2.30 A; B=21-97.[ExPASy / RCSB / EBI]
2G4D; X-ray; 2.80 A; B/D=20-97.[ExPASy / RCSB / EBI]
2IO2; X-ray; 2.90 A; B=18-97.[ExPASy / RCSB / EBI]
2IY0; X-ray; 2.77 A; B=20-101.[ExPASy / RCSB / EBI]
2IY1; X-ray; 2.46 A; B/D=20-101.[ExPASy / RCSB / EBI]
2PE6; X-ray; 2.40 A; B=1-97.[ExPASy / RCSB / EBI]
2UYZ; X-ray; 1.40 A; B=20-97.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A5R; -.
1TGZ; -.
1WYW; -.
1Y8R; -.
1Z5S; -.
2ASQ; -.
2BF8; -.
2G4D; -.
2IO2; -.
2IY0; -.
2IY1; -.
2PE6; -.
2UYZ; -.
ModBase P63165.
Protein-protein interaction databases
DIP DIP:29080N; -.
IntAct P63165; -.
Organism-specific databases
H-InvDB HIX0002747; -.
HIX0029725; -.
HIX0040593; -.
HIX0042122; -.
HGNC HGNC:12502; SUMO1.
GenAtlas SUMO1.
HPA CAB004269; -.
MIM 601912; gene. [NCBI / EBI]
PharmGKB PA37149; -.
GeneCards P63165.
Gene expression databases
ArrayExpress P63165; -.
CleanEx HS_SUMO1; -.
GermOnline ENSG00000116030; Homo sapiens.
Ontologies
GO
GO:0005643; Cellular component: nuclear pore (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0016481; Biological process: negative regulation of transcription (inferred from direct assay from UniProtKB).
GO:0043433; Biological process: negative regulation of transcription factor activity (inferred from mutant phenotype from UniProtKB).
GO:0016925; Biological process: protein sumoylation (inferred from direct assay from UniProtKB).
GO:0032880; Biological process: regulation of protein localization (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000626; Ubiquitin.
Graphical view of domain structure.
Pfam PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.
SMART SM00213; UBQ; 1.
SMART graphical view of domain structure.
PROSITE PS50053; UBIQUITIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P63165.
Genome annotation databases
Ensembl ENSG00000116030; Homo sapiens. [Contig view]
GeneID 7341; -.
KEGG hsa:7341; -.
Phylogenomic databases
HOGENOM P63165; -.
HOVERGEN P63165; -.
Other
LinkHub P63165; -.
SOURCE SUMO1; Homo sapiens.
ProtoNet P63165.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Membrane; Nucleus; Phosphoprotein; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1    97  97     Small ubiquitin-related modifier 1. PRO_0000035939
PROPEP   98   101  4      PRO_0000035940
DOMAIN   20    97  78     Ubiquitin-like. 
SITE   36    36  1     Interaction with PIAS2. 
MOD_RES   2     2        Phosphoserine. 
CROSSLNK   97    97        Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins). 
MUTAGEN   36    36        F->A: Abolishes binding to PIAS2. 
CONFLICT   75    75        H -> N (in Ref. 11; AAH66306). 
STRAND   21    27  7      
STRAND   33    39  7      
HELIX   45    55  11      
HELIX   59    61  3      
STRAND   62    66  5      
HELIX   77    80  4      
STRAND   86    92  7      
Sequence information
Length: 101 AA [This is the length of the unprocessed precursor] Molecular weight: 11557 Da [This is the MW of the unprocessed precursor] CRC64: 89BE97D2D054FB33 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 

        70         80         90        100 
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V 

P63165 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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