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Q09822 (CDC15_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division control protein 15
Gene names
Name:cdc15
ORF Names:SPAC20G8.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length927 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Appears to mediate cytoskeletal rearrangements required for cytokinesis. Essential for viability.

Subcellular location

Cytoplasmcytoskeleton.

Developmental stage

Peaks in early mitosis before septation.

Domain

The N-terminal region is in a coiled coil structure.

Sequence similarities

Contains 1 FCH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   DomainCoiled coil
SH3 domain
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: PomBase

actomyosin contractile ring assembly

Inferred from mutant phenotype Ref.1. Source: PomBase

contractile ring localization

Inferred from mutant phenotype PubMed 19139265. Source: PomBase

cortical actin cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: PomBase

establishment of endoplasmic reticulum localization involved in endoplasmic reticulum polarization at cell division site

Inferred from mutant phenotype PubMed 18184749. Source: PomBase

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

protein localization to cell division site involved in cytokinesis, actomyosin contractile ring assembly

Inferred from mutant phenotype PubMed 24127216. Source: PomBase

regulation of actin nucleation

Inferred from genetic interaction PubMed 12939254. Source: PomBase

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 958201. Source: PomBase

   Cellular_componentcell division site

Inferred from direct assay PubMed 14602073PubMed 16823372PubMed 9786952. Source: PomBase

cell tip

Inferred from direct assay PubMed 16823372. Source: PomBase

cytoplasm

Inferred from direct assay Ref.4. Source: PomBase

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

medial membrane band

Inferred from direct assay PubMed 15517003. Source: PomBase

   Molecular_functionprotein anchor

Traceable author statement PubMed 15517003. Source: PomBase

protein binding

Inferred from physical interaction PubMed 12939254. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 927927Cell division control protein 15
PRO_0000089443

Regions

Domain20 – 10182FCH
Domain866 – 92762SH3
Coiled coil108 – 207100 Potential

Amino acid modifications

Modified residue3311Phosphoserine Ref.5
Modified residue3321Phosphoserine Ref.5
Modified residue5291Phosphothreonine Ref.5
Modified residue6361Phosphoserine Ref.5
Modified residue6391Phosphoserine Ref.5
Modified residue7001Phosphoserine Ref.5
Modified residue7741Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q09822 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: FDCE7E0AAA3D247D

FASTA927102,119
        10         20         30         40         50         60 
MEVNGVSQSE AAPYVTKSSV KFRDNFWGSE DAGMDALMSR TKSSLSVLES IDEFYAKRAS 

        70         80         90        100        110        120 
IEREYASKLQ ELAASSADIP EVGSTLNNIL SMRTETGSMA KAHEEVSQQI NTELRNKIRE 

       130        140        150        160        170        180 
YIDQTEQQKV VAANAIEELY QKKTALEIDL SEKKDAYEYS CNKLNSYMRQ TKKMTGRELD 

       190        200        210        220        230        240 
KYNLKIRQAA LAVKKMDAEY RETNELLLTV TREWIDRWTE VCDAFQHIEE YRLEFLKTNM 

       250        260        270        280        290        300 
WAYANIISTA CVKDDESCEK IRLTLENTNI DEDITQMIQN EGTGTTIPPL PEFNDYFKEN 

       310        320        330        340        350        360 
GLNYDIDQLI SKAPSYPYSS SRPSASASLA SSPTRSAFRP KTSETVSSEV VSSPPTSPLH 

       370        380        390        400        410        420 
SPVKPVSNEQ VEQVTEVELS IPVPSIQEAE SQKPVLTGSS MRRPSVTSPT FEVAARPLTS 

       430        440        450        460        470        480 
MDVRSSHNAE TEVQAIPAAT DISPEVKEGK NSENAITKDN DDIILSSQLQ PTATGSRSSR 

       490        500        510        520        530        540 
LSFSRHGHGS QTSLGSIKRK SIMERMGRPT SPFMGSSFSN MGSRSTSPTK EGFASNQHAT 

       550        560        570        580        590        600 
GASVQSDELE DIDPRANVVL NVGPNMLSVG EAPVESTSKE EDKDVPDPIA NAMAELSSSM 

       610        620        630        640        650        660 
RRRQSTSVDD EAPVSLSKTS SSTRLNGLGY HSRNTSIASD IDGVPKKSTL GAPPAAHTSA 

       670        680        690        700        710        720 
QMQRMSNSFA SQTKQVFGEQ RTENSARESL RHSRSNMSRS PSPMLSRRSS TLRPSFERSA 

       730        740        750        760        770        780 
SSLSVRQSDV VSPAPSTRAR GQSVSGQQRP SSSMSLYGEY NKSQPQLSMQ RSVSPNPLGP 

       790        800        810        820        830        840 
NRRSSSVLQS QKSTSSNTSN RNNGGYSGSR PSSEMGHRYG SMSGRSMRQV SQRSTSRARS 

       850        860        870        880        890        900 
PEPTNRNSVQ SKNVDPRATF TAEGEPILGY VIALYDYQAQ IPEEISFQKG DTLMVLRTQE 

       910        920 
DGWWDGEIIN VPNSKRGLFP SNFVQTV 

« Hide

References

« Hide 'large scale' references
[1]"The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis."
Fankhauser C., Reymond A., Cerutti L., Utzig S., Hofmann K., Simanis V.
Cell 82:435-444(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]Fankhauser C., Reymond A., Cerutti L., Utzig S., Hofmann K., Simanis V.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]"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.
[4]"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 286-425.
Strain: ATCC 38364 / 968.
[5]"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-331; SER-332; THR-529; SER-636; SER-639; SER-700 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86179 Genomic DNA. Translation: CAA60115.1.
CU329670 Genomic DNA. Translation: CAB08599.2.
AB027810 Genomic DNA. Translation: BAA87114.1.
PIRT38127.
RefSeqNP_593322.1. NM_001018753.2.

3D structure databases

ProteinModelPortalQ09822.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278460. 43 interactions.
DIPDIP-35649N.
IntActQ09822. 3 interactions.
MINTMINT-4695421.
STRING4896.SPAC20G8.05c-1.

Proteomic databases

MaxQBQ09822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC20G8.05c.1; SPAC20G8.05c.1:pep; SPAC20G8.05c.
GeneID2541975.
KEGGspo:SPAC20G8.05c.

Organism-specific databases

PomBaseSPAC20G8.05c.

Phylogenomic databases

eggNOGNOG303711.
OMATARWNRE.
OrthoDBEOG7F7WKS.
PhylomeDBQ09822.

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. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803057.

Entry information

Entry nameCDC15_SCHPO
AccessionPrimary (citable) accession number: Q09822
Secondary accession number(s): O14365, Q9UU50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names