Reviewed, UniProtKB/Swiss-Prot P63165 (SUMO1_HUMAN)

Names and origin

Protein names

Recommended name:
    Small ubiquitin-related modifier 1
      Short name=SUMO-1
Alternative name(s):
    Sentrin
    Ubiquitin-like protein SMT3C
    SMT3 homolog 3
    Ubiquitin-homology domain protein PIC1
    Ubiquitin-like protein UBL1
    GAP-modifying protein 1
      Short name=GMP1

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 which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.
Subunit structure	Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52.
Subcellular location	Nucleus membrane. Nucleus speckle. Cytoplasm.
Post-translational modification	Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
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
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA repair Ref.3 Traceable author statement. Source: ProtInc negative regulation of transcription Inferred from direct assay. Source: UniProtKB negative regulation of transcription factor activity Inferred from mutant phenotype. Source: UniProtKB protein sumoylation Inferred from direct assay. Source: UniProtKB regulation of protein localization Traceable author statement. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Ref.4 Traceable author statement. Source: ProtInc nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.23 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAXX	Q9UER7	4	EBI-80140,EBI-77321
DNMT3B	Q9UBC3	1	EBI-80140,EBI-80125
RANGAP1	P46060	1	EBI-80140,EBI-396091
RWDD3	Q08AJ7	1	EBI-80140,EBI-1549885
SENP2	Q9HC62	1	EBI-80140,EBI-714881
UBE2I	P63279	1	EBI-80140,EBI-80168

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 97

97

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

Phosphoserine

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

Sequence conflict

75

1

H → N in AAH66306. Ref.11

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)
	P63165-1 [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]	"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].
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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: Epithelium.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"Complexes of SEN protease." Dong C., Shen L., Taitham M., Hay R.T., Naismith J.H. Submitted (AUG-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
+	Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AC079354 Genomic DNA. Translation: AAY24035.1.
BC006462 mRNA. Translation: AAH06462.1.
BC053528 mRNA. Translation: AAH53528.1.
BC066306 mRNA. Translation: AAH66306.1.

RefSeq

NP_001005781.1.
NP_003343.1.

UniGene

Hs.81424

3D structure databases

PDBMSD

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	[»]
2PE6	X-ray	2.40	B	1-97	[»]
2UYZ	X-ray	1.40	B	20-97	[»]
2VRR	X-ray	2.22	B	20-97	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29080N.

IntAct

P63165.

PTM databases

PhosphoSite

P63165.

Genome annotation databases

Ensembl

ENSG00000116030. Homo sapiens. [Contig view]

GeneID

7341.

KEGG

hsa:7341.

Organism-specific databases

H-InvDB

HIX0002747.
HIX0029725.
HIX0040593.
HIX0042122.

HGNC

HGNC:12502. SUMO1.

HPA

CAB004269.

MIM

601912. gene.

Orphanet

1991. Cleft lip with or without cleft palate.

PharmGKB

PA37149.

GenAtlas

Search...

GeneCards

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Phylogenomic databases

HOGENOM

P63165.

HOVERGEN

P63165.

Gene expression databases

ArrayExpress

P63165.

CleanEx

HS_SUMO1.

GermOnline

ENSG00000116030. Homo sapiens.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
[Graphical view]

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 Resources

LinkHub

P63165.

NextBio

28734.

SOURCE

Search...

Entry information