Reviewed, UniProtKB/Swiss-Prot P55854 (SUMO3_HUMAN)

Names and origin

Protein names

Recommended name:
    Small ubiquitin-related modifier 3
      Short name=SUMO-3
Alternative name(s):
    Ubiquitin-like protein SMT3A
    SMT3 homolog 1
    SUMO-2

Gene names

Name:	SUMO3
Synonyms:	SMT3A, SMT3H1

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	103 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	Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins By similarity.
Subcellular location	Cytoplasm. Ref.8
Tissue specificity	Expressed predominantly in liver. Ref.11
Post-translational modification	Polymeric chains can be formed through Lys-11 cross-linking. Cleavage of precursor form by SENP1, SENP2 or SENP5 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
Coding sequence diversity	Polymorphism
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell kinetochore Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAE1	Q9UBE0	1	EBI-474067,EBI-743154
SP100	P23497	1	EBI-474067,EBI-751145
UBE2I	P63279	1	EBI-474067,EBI-80168

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 92

92

Small ubiquitin-related modifier 3

PRO_0000035957

Propeptide

93 – 103

11

PRO_0000035958

Regions

Domain

15 – 92

78

Ubiquitin-like

Amino acid modifications

Cross-link

11

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Cross-link

92

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

Natural variations

Natural variant

38

1

P → S: dbSNP rs1051311. Ref.1

VAR_052692

Experimental info

Mutagenesis

11

1

K → R: Abolishes the formation of poly(SUMO) chains. Ref.7

Sequence conflict

32

1

K → E in BAD96311. Ref.4

Sequence conflict

76

1

E → R in CAA67896. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

103

Helix Strand Turn

Details...

Beta strand

16 – 22

7

Beta strand

28 – 34

7

Helix

40 – 50

11

Helix

54 – 56

3

Beta strand

57 – 61

5

Turn

72 – 76

5

Beta strand

82 – 87

6

Beta strand

90 – 92

3

Sequences

	Sequence		Length	Mass (Da)
	P55854-1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: E337E34CB5B3B187	FASTA	103	11,637
	10 20 30 40 50 60 MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR 70 80 90 100 FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGVPESSLAG HSF

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], VARIANT SER-38. Tissue: Brain.
[2]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Coronary artery.
[5]	"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: Bone marrow and Kidney.
[6]	"Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3." Saitoh H., Hinchey J. J. Biol. Chem. 275:6252-6258(2000) [PubMed: 10692421] [Abstract] Cited for: IDENTIFICATION.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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, TISSUE SPECIFICITY.
[12]	"Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3." Gong L., Yeh E.T.H. J. Biol. Chem. 281:15869-15877(2006) [PubMed: 16608850] [Abstract] Cited for: CLEAVAGE.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Solution structure of human SUMO-3 C47S and its binding surface for Ubc9." Ding H., Xu Y., Chen Q., Dai H., Tang Y., Wu J., Shi Y. Biochemistry 44:2790-2799(2005) [PubMed: 15723523] [Abstract] Cited for: STRUCTURE BY NMR OF 14-92.
[15]	"The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T. Biochem. J. 397:279-288(2006) [PubMed: 16553580] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH SENP1, CLEAVAGE.
+	Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

X99584 mRNA. Translation: CAA67896.1.
BT007008 mRNA. Translation: AAP35654.1.
CR542173 mRNA. Translation: CAG46970.1.
CR542188 mRNA. Translation: CAG46985.1.
AK222591 mRNA. Translation: BAD96311.1.
BC000036 mRNA. Translation: AAH00036.1.
BC008420 mRNA. Translation: AAH08420.1.

IPI

IPI00299147.

RefSeq

NP_008867.2.

UniGene

Hs.474005

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U4A	NMR	-	A	14-92	[»]
2IO1	X-ray	2.60	B/D/F	14-103	[»]

SMR

P55854. Positions 1-93.

ModBase

Search...

Protein-protein interaction databases

IntAct

P55854. 33 interactions.

PTM databases

PhosphoSite

P55854.

Proteomic databases

PRIDE

P55854.

Genome annotation databases

Ensembl

ENSG00000184900. Homo sapiens. [Contig view]

GeneID

6612.

KEGG

hsa:6612.

Organism-specific databases

GeneCards

GC21M045049.

H-InvDB

HIX0016173.

HGNC

HGNC:11124. SUMO3.

MIM

602231. gene.

PharmGKB

PA35973.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P55854.

HOVERGEN

P55854.

Gene expression databases

ArrayExpress

P55854.

Bgee

P55854.

CleanEx

HS_SUMO3.

GermOnline

ENSG00000184900. Homo sapiens.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[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

NextBio

25743.

SOURCE

Search...

Entry information

Entry name

SUMO3_HUMAN

Accession

Primary (citable) accession number: P55854
Secondary accession number(s): Q53HI9, Q6FGD4, Q9BWR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2002
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)