[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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 [GENOMIC DNA / MRNA]. DOI=10.1006/bbrc.1997.6709; PubMed=9175795 [NCBI, ExPASy, EBI, Israel, Japan] Choudhury B.K., Li S.S.; "Identification and characterization of the SMT3 cDNA and gene from nematode Caenorhabditis elegans."; Biochem. Biophys. Res. Commun. 234:788-791(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[4]	FUNCTION. PubMed=11806825 [NCBI, ExPASy, EBI, Israel, Japan] Jones D., Crowe E., Stevens T.A., Candido E.P.M.; "Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins."; Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002).
[5]	FUNCTION. DOI=10.1101/gad.1227104; PubMed=15466489 [NCBI, ExPASy, EBI, Israel, Japan] Broday L., Kolotuev I., Didier C., Bhoumik A., Gupta B.P., Sternberg P.W., Podbilewicz B., Ronai Z.; "The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans."; Genes Dev. 18:2380-2391(2004).
[6]	FUNCTION. DOI=10.1038/ng1336; PubMed=15107848 [NCBI, ExPASy, EBI, Israel, Japan] Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S., Haber D.A.; "SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2."; Nat. Genet. 36:507-511(2004).
[7]	FUNCTION. DOI=10.1242/dev.01664; PubMed=15689373 [NCBI, ExPASy, EBI, Israel, Japan] Leight E.R., Glossip D., Kornfeld K.; "Sumoylation of LIN-1 promotes transcriptional repression and inhibition of vulval cell fates."; Development 132:1047-1056(2005).
[8]	FUNCTION. DOI=10.1038/sj.emboj.7600726; PubMed=15990876 [NCBI, ExPASy, EBI, Israel, Japan] Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.; "Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans."; EMBO J. 24:2613-2623(2005).
[9]	FUNCTION. DOI=10.1016/j.ydbio.2006.04.001; PubMed=16701625 [NCBI, ExPASy, EBI, Israel, Japan] Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.; "The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required for ABa-derived pharyngeal muscle in C. elegans."; Dev. Biol. 295:664-677(2006).

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. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates.
SUBUNIT: Covalently attached to a number of proteins such as tbx-2, lin-1, lin-11 and sop-2.
INTERACTION:
O62195:-; NbExp=1; IntAct=EBI-313647, EBI-315940;
P90740:-; NbExp=1; IntAct=EBI-313647, EBI-313626;
Q23158:atn-1; NbExp=1; IntAct=EBI-313647, EBI-314014;
Q22799:dlc-1; NbExp=1; IntAct=EBI-313647, EBI-328324;
O16299:figl-1; NbExp=1; IntAct=EBI-313647, EBI-320880;
Q94420:mel-26; NbExp=1; IntAct=EBI-313647, EBI-320790;
Q19905:sqv-4; NbExp=1; IntAct=EBI-313647, EBI-320696;
PTM: Cleavage of precursor form by ulp-1 is necessary for function (Probable).
SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
SIMILARITY: Contains 1 ubiquitin-like domain.

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

X99600; CAA67914.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U94830; AAB67608.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043701; AAK18969.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JC5582; JC5582.

NP_490842.1; -.

3D structure databases

HSSP

Q93068; 1A5R. [HSSP ENTRY / PDB]

ModBase

P55853.

Protein-protein interaction databases

DIP

DIP:25461N; -.

IntAct

P55853; 18.

Organism-specific databases

WormBase

WBGene00004888; smo-1.

WormPep

K12C11.2; CE18056. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

P55853; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0010171;	Biological process: body morphogenesis (inferred from mutant phenotype from WormBase).
GO:0040002;	Biological process: collagen and cuticulin-based cuticle development (inferred from mutant phenotype from WormBase).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0001703;	Biological process: gastrulation with mouth forming first (inferred from mutant phenotype from WormBase).
GO:0040035;	Biological process: hermaphrodite genitalia development (inferred from mutant phenotype from WormBase).
GO:0040027;	Biological process: negative regulation of vulval development (inferred from mutant phenotype from WormBase).
GO:0040010;	Biological process: positive regulation of growth rate (inferred from mutant phenotype from WormBase).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from InterPro).
GO:0006511;	Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
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).

Genome annotation databases

Ensembl

K12C11.2; Caenorhabditis elegans. [Contig view]

GeneID

266820; -.

KEGG

cel:K12C11.2; -.

NMPDR

fig|6239.3.peg.221; -.

Other

953156; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Developmental protein; Ubl conjugation pathway.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 91`	`91`	`Small ubiquitin-related modifier.`	`PRO_0000114890`
`PROPEP`	`91 91`	`1`	`By similarity.`	`PRO_0000271227`
`DOMAIN`	`13 91`	`79`	`Ubiquitin-like.`
`CROSSLNK`	`90 90`		`Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) (By similarity).`

Sequence information

Length: 91 AA [This is the length of the unprocessed precursor]

Molecular weight: 10222 Da [This is the MW of the unprocessed precursor]

CRC64: 0894E99B6F7B37F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV AVNSLRFLFD 

        70         80         90 
GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F

P55853 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools