Reviewed, UniProtKB/Swiss-Prot P61956 (SUMO2_HUMAN)

Names and origin

Protein names

Recommended name:
    Small ubiquitin-related modifier 2
      Short name=SUMO-2
Alternative name(s):
    Ubiquitin-like protein SMT3B
    SMT3 homolog 2
    Sentrin-2
    HSMT3
    SUMO-3

Gene names

Name:	SUMO2
Synonyms:	SMT3B, SMT3H2

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	95 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 either as a monomer or as a lysine-linked polymer. 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. 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	Homotrimer Potential. Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1.
Subcellular location	Nucleus. Note= Nuclear bodies.
Tissue specificity	Broadly expressed.
Post-translational modification	Polymeric chains can be formed through Lys-11 cross-linking. 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	Nucleus
Coding sequence diversity	Polymorphism
PTM	Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIAS4	Q8N2W9	1	EBI-473220,EBI-473160

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 93

93

Small ubiquitin-related modifier 2

PRO_0000035949

Propeptide

94 – 95

2

PRO_0000035950

Regions

Domain

16 – 95

80

Ubiquitin-like

Amino acid modifications

Cross-link

11

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Cross-link

93

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

Natural variations

Natural variant

16

1

D → N: dbSNP rs17850328.

VAR_047508

Experimental info

Mutagenesis

11

1

K → R: Abolishes the formation of poly(SUMO) chains

Sequence conflict

55

1

M → V in AC005000. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

95

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Beta strand

27 – 34

8

Helix

41 – 51

11

Turn

55 – 57

3

Beta strand

59 – 62

4

Turn

73 – 77

5

Beta strand

82 – 87

6

Sequences

	Sequence		Length	Mass (Da)
	P61956-1 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: F8F0426849BEF08B	FASTA	95	10,871
	10 20 30 40 50 60 MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSMRQIRF 70 80 90 RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene." Mannen H., Tseng H.M., Cho C.L., Li S.S.-L. Biochem. Biophys. Res. Commun. 222:178-180(1996) [PubMed: 8630065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"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.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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], VARIANT ASN-16. Tissue: Blood vessel, Bone, Bone marrow, Brain, Lung and Testis.
[5]	"Characterization of a second member of the sentrin family of ubiquitin-like proteins." Kamitani T., Kito K., Nguyen H.P., Fukuda-Kamitani T., Yeh E.T.H. J. Biol. Chem. 273:11349-11353(1998) [PubMed: 9556629] [Abstract] Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9." Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T. J. Biol. Chem. 276:35368-35374(2001) [PubMed: 11451954] [Abstract] Cited for: SUMOYLATION AT LYS-11, MUTAGENESIS OF LYS-11.
[7]	"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.
[8]	"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.
[9]	"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: CLEAVAGE.
[10]	"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.
[11]	"NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression." Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G. Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed: 16567619] [Abstract] Cited for: INTERACTION WITH PELP1.
[12]	"Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins." Huang W.-C., Ko T.-P., Li S.S.-L., Wang A.H.-J. Eur. J. Biochem. 271:4114-4122(2004) [PubMed: 15479240] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 9-93, SUBUNIT.
[13]	"Solution structure of human SUMO-2 (SMT3B), a ubiquitin-like protein." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-93.
[14]	"Crystal structure of SUMO-3-modified thymine-DNA glycosylase." Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M. J. Mol. Biol. 359:137-147(2006) [PubMed: 16626738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-93 CONJUGATED TO TDG.
[15]	"Solution structure of human small ubiquitin-like modifier protein isoform 2 (SUMO-2)." Chang C.K., Wang Y.H., Chung T.L., Chang C.F., Li S.S.L., Huang T.H. Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-95.
+	Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

L76416 mRNA. Translation: AAD45399.1.
X99585 mRNA. Translation: CAA67897.1.
AC005000 Genomic DNA. No translation available.
BC008450 mRNA. Translation: AAH08450.1.
BC016775 mRNA. Translation: AAH16775.1.
BC022340 mRNA. Translation: AAH22340.1.
BC062713 mRNA. Translation: AAH62713.1.
BC068465 mRNA. Translation: AAH68465.1.
BC070159 mRNA. Translation: AAH70159.1.
BC071645 mRNA. Translation: AAH71645.1.
BC071646 mRNA. Translation: AAH71646.1.
BC107853 mRNA. Translation: AAI07854.1.

PIR

JC4760.

RefSeq

NP_001005849.1.
NP_008868.3.

UniGene

Hs.380973
Hs.546298

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WM2	X-ray	1.60	A	12-89	[»]
1WM3	X-ray	1.20	A	17-88	[»]
1WZ0	NMR	-	A	1-93	[»]
1Z5Q	model	-	B	15-93	[»]
2AWT	NMR	-	A	1-95	[»]
2CKH	X-ray	3.20	B	15-93	[»]
2D07	X-ray	2.10	B	1-93	[»]
2IO0	X-ray	2.30	B	15-95	[»]
2IO3	X-ray	3.20	B	15-93	[»]
2IYD	X-ray	3.20	B	15-95	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P61956.

PTM databases

PhosphoSite

P61956.

Genome annotation databases

GeneID

6613.

KEGG

hsa:6613.

Organism-specific databases

H-InvDB

HIX0014166.
HIX0034144.

HGNC

HGNC:11125. SUMO2.

HPA

CAB012180.

MIM

603042. gene.

PharmGKB

PA134914683.

GenAtlas

Search...

GeneCards

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Phylogenomic databases

HOGENOM

P61956.

HOVERGEN

P61956.

Gene expression databases

CleanEx

HS_SUMO2.

GermOnline

ENSG00000188612. 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

P61956.

NextBio

25747.

SOURCE

Search...

Entry information

Entry name

SUMO2_HUMAN

Accession

Primary (citable) accession number: P61956
Secondary accession number(s): P55855 , Q32Q42, Q6IPZ6, Q96HK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	November 25, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)