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Protein

Cell division control protein 15

Gene

cdc15

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. protein anchor Source: PomBase

GO - Biological processi

  1. actin cytoskeleton organization Source: PomBase
  2. cortical actin cytoskeleton organization Source: PomBase
  3. establishment of endoplasmic reticulum localization involved in endoplasmic reticulum polarization at cell division site Source: PomBase
  4. mitotic actomyosin contractile ring assembly Source: PomBase
  5. mitotic actomyosin contractile ring localization Source: PomBase
  6. mitotic nuclear division Source: UniProtKB-KW
  7. protein localization to cell division site involved in cytokinesis, actomyosin contractile ring assembly Source: PomBase
  8. regulation of actin nucleation Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 15
Gene namesi
Name:cdc15
ORF Names:SPAC20G8.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC20G8.05c.

Subcellular locationi

GO - Cellular componenti

  1. cell division site Source: PomBase
  2. cell tip Source: PomBase
  3. cytoplasm Source: PomBase
  4. cytoskeleton Source: UniProtKB-SubCell
  5. medial membrane band Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 927927Cell division control protein 15PRO_0000089443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei332 – 3321Phosphoserine1 Publication
Modified residuei529 – 5291Phosphothreonine1 Publication
Modified residuei636 – 6361Phosphoserine1 Publication
Modified residuei639 – 6391Phosphoserine1 Publication
Modified residuei700 – 7001Phosphoserine1 Publication
Modified residuei774 – 7741Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09822.

Expressioni

Developmental stagei

Peaks in early mitosis before septation.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cdc12Q100594EBI-1148185,EBI-1148281
myo1Q9Y7Z84EBI-1148185,EBI-1148082

Protein-protein interaction databases

BioGridi278460. 46 interactions.
DIPiDIP-35649N.
IntActiQ09822. 3 interactions.
MINTiMINT-4695421.
STRINGi4896.SPAC20G8.05c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09822.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10182FCHPROSITE-ProRule annotationAdd
BLAST
Domaini866 – 92762SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 207100Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 FCH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG303711.
InParanoidiQ09822.
OMAiTARWNRE.
OrthoDBiEOG7F7WKS.
PhylomeDBiQ09822.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09822-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVNGVSQSE AAPYVTKSSV KFRDNFWGSE DAGMDALMSR TKSSLSVLES
60 70 80 90 100
IDEFYAKRAS IEREYASKLQ ELAASSADIP EVGSTLNNIL SMRTETGSMA
110 120 130 140 150
KAHEEVSQQI NTELRNKIRE YIDQTEQQKV VAANAIEELY QKKTALEIDL
160 170 180 190 200
SEKKDAYEYS CNKLNSYMRQ TKKMTGRELD KYNLKIRQAA LAVKKMDAEY
210 220 230 240 250
RETNELLLTV TREWIDRWTE VCDAFQHIEE YRLEFLKTNM WAYANIISTA
260 270 280 290 300
CVKDDESCEK IRLTLENTNI DEDITQMIQN EGTGTTIPPL PEFNDYFKEN
310 320 330 340 350
GLNYDIDQLI SKAPSYPYSS SRPSASASLA SSPTRSAFRP KTSETVSSEV
360 370 380 390 400
VSSPPTSPLH SPVKPVSNEQ VEQVTEVELS IPVPSIQEAE SQKPVLTGSS
410 420 430 440 450
MRRPSVTSPT FEVAARPLTS MDVRSSHNAE TEVQAIPAAT DISPEVKEGK
460 470 480 490 500
NSENAITKDN DDIILSSQLQ PTATGSRSSR LSFSRHGHGS QTSLGSIKRK
510 520 530 540 550
SIMERMGRPT SPFMGSSFSN MGSRSTSPTK EGFASNQHAT GASVQSDELE
560 570 580 590 600
DIDPRANVVL NVGPNMLSVG EAPVESTSKE EDKDVPDPIA NAMAELSSSM
610 620 630 640 650
RRRQSTSVDD EAPVSLSKTS SSTRLNGLGY HSRNTSIASD IDGVPKKSTL
660 670 680 690 700
GAPPAAHTSA QMQRMSNSFA SQTKQVFGEQ RTENSARESL RHSRSNMSRS
710 720 730 740 750
PSPMLSRRSS TLRPSFERSA SSLSVRQSDV VSPAPSTRAR GQSVSGQQRP
760 770 780 790 800
SSSMSLYGEY NKSQPQLSMQ RSVSPNPLGP NRRSSSVLQS QKSTSSNTSN
810 820 830 840 850
RNNGGYSGSR PSSEMGHRYG SMSGRSMRQV SQRSTSRARS PEPTNRNSVQ
860 870 880 890 900
SKNVDPRATF TAEGEPILGY VIALYDYQAQ IPEEISFQKG DTLMVLRTQE
910 920
DGWWDGEIIN VPNSKRGLFP SNFVQTV
Length:927
Mass (Da):102,119
Last modified:May 30, 2000 - v2
Checksum:iFDCE7E0AAA3D247D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86179 Genomic DNA. Translation: CAA60115.1.
CU329670 Genomic DNA. Translation: CAB08599.2.
AB027810 Genomic DNA. Translation: BAA87114.1.
PIRiT38127.
RefSeqiNP_593322.1. NM_001018753.2.

Genome annotation databases

EnsemblFungiiSPAC20G8.05c.1; SPAC20G8.05c.1:pep; SPAC20G8.05c.
GeneIDi2541975.
KEGGispo:SPAC20G8.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86179 Genomic DNA. Translation: CAA60115.1.
CU329670 Genomic DNA. Translation: CAB08599.2.
AB027810 Genomic DNA. Translation: BAA87114.1.
PIRiT38127.
RefSeqiNP_593322.1. NM_001018753.2.

3D structure databases

ProteinModelPortaliQ09822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278460. 46 interactions.
DIPiDIP-35649N.
IntActiQ09822. 3 interactions.
MINTiMINT-4695421.
STRINGi4896.SPAC20G8.05c-1.

Proteomic databases

MaxQBiQ09822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC20G8.05c.1; SPAC20G8.05c.1:pep; SPAC20G8.05c.
GeneIDi2541975.
KEGGispo:SPAC20G8.05c.

Organism-specific databases

PomBaseiSPAC20G8.05c.

Phylogenomic databases

eggNOGiNOG303711.
InParanoidiQ09822.
OMAiTARWNRE.
OrthoDBiEOG7F7WKS.
PhylomeDBiQ09822.

Miscellaneous databases

NextBioi20803057.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiCDC15_SCHPO
AccessioniPrimary (citable) accession number: Q09822
Secondary accession number(s): O14365, Q9UU50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 30, 2000
Last modified: February 4, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.