P63165 (SUMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Chromosomal rearrangement
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA 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 component	cytoplasm 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 function	ubiquitin protein ligase binding Inferred from physical interaction Ref.28. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	7	EBI-80140,EBI-608057
DAXX	Q9UER7	5	EBI-80140,EBI-77321
DNMT3B	Q9UBC3	4	EBI-80140,EBI-80125
HIF1A	Q16665	2	EBI-80140,EBI-447269
MYB	P10242	3	EBI-80140,EBI-298355
RANGAP1	P46060	3	EBI-80140,EBI-396091
RWDD3	Q9Y3V2	2	EBI-80140,EBI-1549885
SART1	O43290	2	EBI-80140,EBI-607761
SATB1	Q01826	2	EBI-80140,EBI-743747

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 97

96

Small ubiquitin-related modifier 1

PRO_0000035939

Propeptide

98 – 101

4

PRO_0000035940

Regions

Domain

20 – 97

78

Ubiquitin-like

Sites

Site

36

1

Interaction with PIAS2

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.31

Modified residue

2

1

Phosphoserine Ref.22 Ref.25 Ref.26 Ref.29

Modified residue

9

1

Phosphoserine Ref.30

Cross-link

7

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.31

Cross-link

25

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.31

Cross-link

97

Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis

36

1

F → A: Abolishes binding to PIAS2. Ref.36

Sequence conflict

75

1

H → N in AAH66306. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

101

Helix Strand Turn

Details...

Beta strand

1 – 6

6

Turn

9 – 11

3

Beta strand

21 – 27

7

Beta strand

33 – 39

7

Helix

45 – 55

11

Helix

59 – 61

3

Beta strand

62 – 66

5

Helix

77 – 80

4

Beta strand

86 – 92

7

Sequences

	Sequence		Length	Mass (Da)
	P63165 [UniParc]. Last modified September 27, 2004. Version 1. Checksum: 89BE97D2D054FB33	FASTA	101	11,557
	10 20 30 40 50 60 MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 70 80 90 100 SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00303105.

RefSeq

NP_001005781.1. NM_001005781.1.
NP_003343.1. NM_003352.4.

UniGene

Hs.596171.
Hs.81424.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A5R	NMR	-	A	1-101	[»]
1TGZ	X-ray	2.80	B	18-97	[»]
1WYW	X-ray	2.10	B	1-97	[»]
1Y8R	X-ray	2.75	C/F	1-97	[»]
1Z5S	X-ray	3.01	B	18-97	[»]
2ASQ	NMR	-	A	1-97	[»]
2BF8	X-ray	2.30	B	21-97	[»]
2G4D	X-ray	2.80	B/D	20-97	[»]
2IO2	X-ray	2.90	B	18-97	[»]
2IY0	X-ray	2.77	B	20-101	[»]
2IY1	X-ray	2.46	B/D	20-101	[»]
2KQS	NMR	-	A	1-97	[»]
2PE6	X-ray	2.40	B	1-97	[»]
2UYZ	X-ray	1.40	B	20-97	[»]
2VRR	X-ray	2.22	B	20-97	[»]
3KYC	X-ray	2.45	D	1-97	[»]
3KYD	X-ray	2.61	D	1-94	[»]

ProteinModelPortal

P63165.

SMR

P63165. Positions 1-101.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29080N.

IntAct

P63165. 59 interactions.

MINT

MINT-137859.

STRING

P63165.

PTM databases

PhosphoSite

P63165.

Polymorphism databases

DMDM

52783799.

Proteomic databases

PRIDE

P63165.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000392245; ENSP00000376076; ENSG00000116030.
ENST00000392246; ENSP00000376077; ENSG00000116030.

GeneID

7341.

KEGG

hsa:7341.

UCSC

uc002uyz.1. human.

Organism-specific databases

CTD

7341.

GeneCards

GC02M203070.

H-InvDB

HIX0002747.

HGNC

HGNC:12502. SUMO1.

HPA

CAB004269.

MIM

601912. gene.
613705. phenotype.

neXtProt

NX_P63165.

Orphanet

1991. Cleft lip with or without cleft palate.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20914.

GeneTree

ENSGT00390000018808.

HOVERGEN

HBG053025.

OrthoDB

EOG42JNSX.

PhylomeDB

P63165.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_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.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P63165.

Bgee

P63165.

CleanEx

HS_SUMO1.

Genevestigator

P63165.

GermOnline

ENSG00000116030. Homo sapiens.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

KO

K12160.

Pfam

PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

28734.

PMAP-CutDB

P63165.

SOURCE

Search...

Entry information

Entry name

SUMO1_HUMAN

Accession

Primary (citable) accession number: P63165
Secondary accession number(s): B2R4I5 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.