Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Small ubiquitin-related modifier

Gene

smo-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). 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 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).8 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein tag Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processUbl conjugation pathway

Enzyme and pathway databases

ReactomeiR-CEL-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-CEL-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-CEL-3065679 SUMO is proteolytically processed
R-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-3232118 SUMOylation of transcription factors
R-CEL-3899300 SUMOylation of transcription cofactors
R-CEL-4085377 SUMOylation of SUMOylation proteins
R-CEL-4090294 SUMOylation of intracellular receptors
R-CEL-4551638 SUMOylation of chromatin organization proteins
R-CEL-4570464 SUMOylation of RNA binding proteins
R-CEL-4615885 SUMOylation of DNA replication proteins
R-CEL-5696395 Formation of Incision Complex in GG-NER
R-CEL-877312 Regulation of IFNG signaling
R-CEL-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

Protein family/group databases

MoonDBiP55853 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier
Short name:
SUMO
Alternative name(s):
Ubiquitin-like protein SMT3
Gene namesi
Name:smo-1
Synonyms:smt3, sumo
ORF Names:K12C11.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiK12C11.2 ; CE18056 ; WBGene00004888 ; smo-1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown causes chromosome misalignment and anaphase bridges during the first embryonic mitotic division (PubMed:25475837). 23 percent of mutant animals have impaired locomotion (PubMed:24285704). Ectopic expression of egl-17 in multiple vulva precursor cells and moderate increase in phosphorylation of mpk-1 (PubMed:24349540). Adult bet-1 and smo-1 double mutants have decreased myo-3 levels in muscles and increased transcription levels of egl-15, sur-1 and let-60 (PubMed:24285704).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001148901 – 90Small ubiquitin-related modifierAdd BLAST90
PropeptideiPRO_000027122791By similarity1

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki90Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Post-translational modificationi

Cleavage of precursor form by ulp-1 is necessary for function.Curated

Keywords - PTMi

Isopeptide bond

Proteomic databases

EPDiP55853
PaxDbiP55853
PeptideAtlasiP55853
PRIDEiP55853

PTM databases

iPTMnetiP55853

Expressioni

Gene expression databases

BgeeiWBGene00004888 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Interactioni

Subunit structurei

Covalently attached to tbx-2 (PubMed:16701625). Covalently attached to lin-1 (PubMed:15689373). Covalently attached to lin-11 (PubMed:15466489). Covalently attached to sop-2 (PubMed:15107848). Covalently attached to bet-1 (PubMed:24349540, PubMed:24285704).6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi57309, 30 interactors
DIPiDIP-25461N
IntActiP55853, 36 interactors
STRINGi6239.K12C11.2

Structurei

Secondary structure

191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP55853
SMRiP55853
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 91Ubiquitin-likePROSITE-ProRule annotationAdd BLAST79

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated

Phylogenomic databases

eggNOGiKOG1769 Eukaryota
COG5227 LUCA
GeneTreeiENSGT00390000018808
HOGENOMiHOG000207495
InParanoidiP55853
KOiK12160
OMAiIIEVYQE
OrthoDBiEOG091G10ZQ
PhylomeDBiP55853

Family and domain databases

CDDicd01763 Sumo, 1 hit
InterProiView protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF11976 Rad60-SLD, 1 hit
SMARTiView protein in SMART
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55853-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV
60 70 80 90
AVNSLRFLFD GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F
Length:91
Mass (Da):10,222
Last modified:November 1, 1997 - v1
Checksum:i0894E99B6F7B37F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99600 mRNA Translation: CAA67914.1
U94830 Genomic DNA Translation: AAB67608.1
FO081631 Genomic DNA Translation: CCD72942.1
PIRiJC5582
RefSeqiNP_490842.1, NM_058441.4
UniGeneiCel.18381

Genome annotation databases

EnsemblMetazoaiK12C11.2; K12C11.2; WBGene00004888
GeneIDi266820
KEGGicel:CELE_K12C11.2
UCSCiK12C11.2.1 c. elegans

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99600 mRNA Translation: CAA67914.1
U94830 Genomic DNA Translation: AAB67608.1
FO081631 Genomic DNA Translation: CCD72942.1
PIRiJC5582
RefSeqiNP_490842.1, NM_058441.4
UniGeneiCel.18381

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XQMNMR-A1-90[»]
ProteinModelPortaliP55853
SMRiP55853
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57309, 30 interactors
DIPiDIP-25461N
IntActiP55853, 36 interactors
STRINGi6239.K12C11.2

Protein family/group databases

MoonDBiP55853 Predicted

PTM databases

iPTMnetiP55853

Proteomic databases

EPDiP55853
PaxDbiP55853
PeptideAtlasiP55853
PRIDEiP55853

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK12C11.2; K12C11.2; WBGene00004888
GeneIDi266820
KEGGicel:CELE_K12C11.2
UCSCiK12C11.2.1 c. elegans

Organism-specific databases

CTDi266820
WormBaseiK12C11.2 ; CE18056 ; WBGene00004888 ; smo-1

Phylogenomic databases

eggNOGiKOG1769 Eukaryota
COG5227 LUCA
GeneTreeiENSGT00390000018808
HOGENOMiHOG000207495
InParanoidiP55853
KOiK12160
OMAiIIEVYQE
OrthoDBiEOG091G10ZQ
PhylomeDBiP55853

Enzyme and pathway databases

ReactomeiR-CEL-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-CEL-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-CEL-3065679 SUMO is proteolytically processed
R-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-3232118 SUMOylation of transcription factors
R-CEL-3899300 SUMOylation of transcription cofactors
R-CEL-4085377 SUMOylation of SUMOylation proteins
R-CEL-4090294 SUMOylation of intracellular receptors
R-CEL-4551638 SUMOylation of chromatin organization proteins
R-CEL-4570464 SUMOylation of RNA binding proteins
R-CEL-4615885 SUMOylation of DNA replication proteins
R-CEL-5696395 Formation of Incision Complex in GG-NER
R-CEL-877312 Regulation of IFNG signaling
R-CEL-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

Miscellaneous databases

PROiPR:P55853

Gene expression databases

BgeeiWBGene00004888 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Family and domain databases

CDDicd01763 Sumo, 1 hit
InterProiView protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF11976 Rad60-SLD, 1 hit
SMARTiView protein in SMART
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSUMO_CAEEL
AccessioniPrimary (citable) accession number: P55853
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 7, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again