Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P29355 (SEM5_CAEEL)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sex muscle abnormal protein 5
Gene names
Name: sem-5
ORF Names: C14F5.5
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts both in vulval induction and sex myoblast migration. Presumably interacts with the kinase receptor let-23 and with a target that modifies the Ras-like protein let-60.

Sequence similarities

Belongs to the GRB2/sem-5/DRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9XVW81EBI-315286,EBI-315348

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228Sex muscle abnormal protein 5
PRO_0000088212

Regions

Domain1 – 5858SH3 1
Domain60 – 15293SH2
Domain154 – 21360SH3 2

Experimental info

Mutagenesis491P → L in N1619. Ref.1
Mutagenesis901E → K in N1779. Ref.1
Mutagenesis911S → N in N1781. Ref.1
Mutagenesis2011G → R in N2195. Ref.1

Secondary structure

........... 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29355-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 2D684C9520646C41

FASTA22826,210
        10         20         30         40         50         60 
MEAVAEHDFQ AGSPDELSFK RGNTLKVLNK DEDPHWYKAE LDGNEGFIPS NYIRMTECNW 

        70         80         90        100        110        120 
YLGKITRNDA EVLLKKPTVR DGHFLVRQCE SSPGEFSISV RFQDSVQHFK VLRDQNGKYY 

       130        140        150        160        170        180 
LWAVKFNSLN ELVAYHRTAS VSRTHTILLS DMNVETKFVQ ALFDFNPQES GELAFKRGDV 

       190        200        210        220 
ITLINKDDPN WWEGQLNNRR GIFPSNYVCP YNSNKSNSNV APGFNFGN 

« Hide

References

« Hide 'large scale' references
[1]"C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains."
Clark S.G., Stern M.J., Horvitz H.R.
Nature 356:340-344(1992) [PubMed: 1372395] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-49; GLU-90; SER-91 AND GLY-201.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains."
Lim W.A., Richards F.M., Fox R.O.
Nature 372:375-379(1994) [PubMed: 7802869] [Abstract]
Cited for: STRUCTURE BY NMR OF 153-214.
[4]"Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors."
Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.
Science 282:2088-2092(1998) [PubMed: 9851931] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 155-214.
+Additional computationally mapped references.

Cross-references

Sequence databases

S88446 mRNA. Translation: AAB21850.1.
U29082 Genomic DNA. Translation: AAA68405.1.
PIRS25730.
RefSeqNP_509342.1.
UniGeneCel.19703

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1K76NMR-A155-214[»]
1KFZNMR-A155-214[»]
1SEMX-ray2.00A/B155-212[»]
2SEMX-ray2.20A/B155-214[»]
3SEMX-ray2.20A/B155-214[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:27394N.
IntActP29355. 13 interactions.

Genome annotation databases

EnsemblC14F5.5. Caenorhabditis elegans. [Contig view]
GeneID181055.
KEGGcel:C14F5.5.
NMPDRfig|6239.3.peg.23897.

Organism-specific databases

WormBaseWBGene00004774. sem-5.
WormPepC14F5.5. CE01784. [WorfDB]

Phylogenomic databases

OMAP29355. AFLIRIS.

Gene expression databases

ArrayExpressP29355.

Family and domain databases

InterProIPR000108. Neu_cyt_fact_2.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00499. P67PHOX.
PR00401. SH2DOMAIN.
ProDomPD000093. SH2. 1 hit.
PD000066. SH3. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio912202.

Entry information

Entry nameSEM5_CAEEL
AccessionPrimary (citable) accession number: P29355
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents