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Q10199 (IMP2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Septation protein imp2
Gene names
Name:imp2
ORF Names:SPBC11C11.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal septation. Involved in the disassembly of the medial ring during septation. Ref.1

Subcellular location

Cytoplasm › cytoskeleton. Note: Associates with the medial ring during septation. Ref.1

Sequence similarities

Contains 1 FCH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   DomainSH3 domain
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis, actomyosin contractile ring assembly

Inferred from mutant phenotype Ref.1. Source: PomBase

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentactomyosin contractile ring

Inferred from direct assay Ref.1. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670Septation protein imp2
PRO_0000084186

Regions

Domain16 – 9782FCH
Domain607 – 67064SH3

Amino acid modifications

Modified residue3971Phosphoserine Ref.3
Modified residue5031Phosphoserine Ref.3
Modified residue5311Phosphothreonine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q10199 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 03551FBB56FC91AE

FASTA67075,167
        10         20         30         40         50         60 
MSQQLSFNAS SAKPDKSFSN YFWGANDEGY HALLSRFSDV KHINEELRSF YHERANIEED 

        70         80         90        100        110        120 
YAKRMAKLSR TTFSSLETGC LKESVQVMKA EVDNMAKSHL QISQLLQDDV ENAFTRYAAS 

       130        140        150        160        170        180 
LKDKKKMIVS GIEKVHKDKL SKHQALVKAQ DKYHYLCKKV NYYVSQQNML FGKELEKNNA 

       190        200        210        220        230        240 
KLNKTQNAIT ASSSDYQSAV AAVRDSYARW TNEWRSTCDK LQDIEEERRH FLKSVMWTFT 

       250        260        270        280        290        300 
LLISRSCFND DQACERIRKN LEQCSVSQDV LEFIDAKSTG TGIPQPPKFY DYYKGEVPDD 

       310        320        330        340        350        360 
SVELVQANFQ RAQTKIENDN MPLNRPYVLS ATARNESSFE NTLPNTPSAI QSLTTVSSNS 

       370        380        390        400        410        420 
SQNGRSSPKK SFLSKFKLTS RPSTPNVGNT APDALSSPRN DSPLTSAADE QMKHLSLQEE 

       430        440        450        460        470        480 
PKQNPTPAAP GAFPNSNTLP PRYNELGSLP SPNSVSFTED SRPNVNTPSR RQQIQEEFGS 

       490        500        510        520        530        540 
VLQMENRAVS PVYDSRKNGS RSSFTLRKSR SPKRPSSSLS QNASRLPRSL TPGNLEPNYD 

       550        560        570        580        590        600 
FGVRVDPASG TAPTDDEPYT DRDSSFVDDT INTKATGNTS NRLSLPAYPT DGGDTSIDNP 

       610        620        630        640        650        660 
TSTDGQRILG YVSALYDYDA AIPEEISFRK GDTIAVLKLY EDGWWEGFVV GEDDHNRGQF 

       670 
PSNFVREIEV

« Hide

References

« Hide 'large scale' references
[1]"imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe."
Demeter J., Sazer S.
J. Cell Biol. 143:415-427(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-503 AND THR-531, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA20684.1.
PIRS67383. T39317.
RefSeqNP_596391.1. NM_001022312.2.

3D structure databases

ProteinModelPortalQ10199.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC11C11.02-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC11C11.02.1; SPBC11C11.02.1:pep; SPBC11C11.02.
GeneID2540112.
KEGGspo:SPBC11C11.02.

Organism-specific databases

PomBaseSPBC11C11.02.

Phylogenomic databases

eggNOGNOG303711.
OMAFAKSWNS.
OrthoDBEOG4N07PQ.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801248.

Entry information

Entry nameIMP2_SCHPO
AccessionPrimary (citable) accession number: Q10199
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents