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Q09690 (POM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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:
Dual specificity protein kinase pom1

EC=2.7.12.1
Gene names
Name:pom1
ORF Names:SPAC2F7.03c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in localization of polarized growth and cytokinesis. May interact with both the actin and microtubule cytoskeleton. Requires tea1 for localization to the cell ends but not to the cell center. Ref.2 Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cell tip. Cell septum. Note: Present at both poles of the cell throughout the cell cycle irrespective of whether the tips are growing or not. Localized to the septum at the time of cytokinesis. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle distribution

Traceable author statement PubMed 18328707. Source: PomBase

activation of bipolar cell growth

Inferred from mutant phenotype PubMed 20501954Ref.2. Source: PomBase

cell morphogenesis involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 11950884. Source: PomBase

cellular protein localization

Inferred from mutant phenotype PubMed 18328707PubMed 19474789. Source: PomBase

negative regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 19474792PubMed 22624651. Source: PomBase

negative regulation of establishment of actomyosin contractile ring localization

Traceable author statement PubMed 17543869. Source: PomBase

protein localization to medial cortex

Inferred from mutant phenotype PubMed 19474792. Source: PomBase

protein localization to nucleus

Inferred from mutant phenotype PubMed 9852154. Source: PomBase

protein phosphorylation

Inferred from direct assay PubMed 11230130. Source: PomBase

regulation of actomyosin contractile ring localization

Inferred from mutant phenotype PubMed 9852154. Source: PomBase

regulation of cell size

Inferred from genetic interaction PubMed 19474792. Source: PomBase

regulation of establishment or maintenance of cell polarity regulating cell shape

Inferred from mutant phenotype Ref.2. Source: PomBase

signal transduction

Inferred from direct assay PubMed 11230130. Source: PomBase

   Cellular_componentcell cortex of cell tip

Inferred from direct assay PubMed 11230130. Source: PomBase

cell division site

Inferred from direct assay PubMed 22174761Ref.2. Source: PomBase

cell septum

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell tip

Inferred from direct assay PubMed 20870879PubMed 22174761Ref.2. Source: PomBase

non-growing cell tip

Inferred from direct assay PubMed 20870879. Source: PomBase

site of polarized growth

Inferred from direct assay PubMed 11230130. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay PubMed 11230130PubMed 19474792. Source: PomBase

protein serine/threonine/tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tea4O601325EBI-4319163,EBI-1099982

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10871087Dual specificity protein kinase pom1
PRO_0000086579

Regions

Domain699 – 995297Protein kinase
Nucleotide binding705 – 7139ATP By similarity
Compositional bias62 – 654Poly-Ser

Sites

Active site8251Proton acceptor By similarity
Binding site7281ATP By similarity

Amino acid modifications

Modified residue5131Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q09690 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3277E7CA840F8BE2

FASTA1,087121,146
        10         20         30         40         50         60 
MGYLQSQKAV SLGDENTDAL FKLHTSNRKS ANMFGIKSEL LNPSELSAVG SYSNDICPNR 

        70         80         90        100        110        120 
QSSSSTAADT SPSTNASNTN ISFPEQEHKD ELFMNVEPKG VGSSMDNHAI TIHHSTGNGL 

       130        140        150        160        170        180 
LRSSFDHDYR QKNSPRNSIH RLSNISIGNN PIDFESSQQN NPSSLNTSSH HRTSSISNSK 

       190        200        210        220        230        240 
SFGTSLSYYN RSSKPSDWNQ QNNGGHLSGV ISITQDVSSV PLQSSVFSSG NHAYHASMAP 

       250        260        270        280        290        300 
KRSGSWRHTN FHSTSHPRAA SIGNKSGIPP VPTIPPNIGH STDHQHPKAN ISGSLTKSSS 

       310        320        330        340        350        360 
ESKNLSTIQS PLKTSNSFFK ELSPHSQITL SNVKNNHSHV GSQTKSHSFA TPSVFDNNKP 

       370        380        390        400        410        420 
VSSDNHNNTT TSSQVHPDSR NPDPKAAPKA VSQKTNVDGH RNHEAKHGNT VQNESKSQKS 

       430        440        450        460        470        480 
SNKEGRSSRG GFFSRLSFSR SSSRMKKGSK AKHEDAPDVP AIPHAYIADS STKSSYRNGK 

       490        500        510        520        530        540 
KTPTRTKSRM QQFINWFKPS KERSSNGNSD SASPPPVPRL SITRSQVSRE PEKPEEIPSV 

       550        560        570        580        590        600 
PPLPSNFKDK GHVPQQRSVS YTPKRSSDTS ESLQPSLSFA SSNVLSEPFD RKVADLAMKA 

       610        620        630        640        650        660 
INSKRINKLL DDAKVMQSLL DRACIITPVR NTEVQLINTA PLTEYEQDEI NNYDNIYFTG 

       670        680        690        700        710        720 
LRNVDKRRSA DENTSSNFGF DDERGDYKVV LGDHIAYRYE VVDFLGKGSF GQVLRCIDYE 

       730        740        750        760        770        780 
TGKLVALKII RNKKRFHMQA LVETKILQKI REWDPLDEYC MVQYTDHFYF RDHLCVATEL 

       790        800        810        820        830        840 
LGKNLYELIK SNGFKGLPIV VIKSITRQLI QCLTLLNEKH VIHCDLKPEN ILLCHPFKSQ 

       850        860        870        880        890        900 
VKVIDFGSSC FEGECVYTYI QSRFYRSPEV ILGMGYGTPI DVWSLGCIIA EMYTGFPLFP 

       910        920        930        940        950        960 
GENEQEQLAC IMEIFGPPDH SLIDKCSRKK VFFDSSGKPR PFVSSKGVSR RPFSKSLHQV 

       970        980        990       1000       1010       1020 
LQCKDVSFLS FISDCLKWDP DERMTPQQAA QHDFLTGKQD VRRPNTAPAR QKFARPPNIE 

      1030       1040       1050       1060       1070       1080 
TAPIPRPLPN LPMEYNDHTL PSPKEPSNQA SNLVRSSDKF PNLLTNLDYS IISDNGFLRK 


PVEKSRP 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis."
Baehler J., Pringle J.R.
Genes Dev. 12:1356-1370(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 972 / ATCC 24843.
[3]"Role of Tea1p, Tea3p and Pom1p in the determination of cell ends in Schizosaccharomyces pombe."
Niccoli T., Arellano M., Nurse P.
Yeast 20:1349-1358(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"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-513, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA90490.1.
PIRS58147.
RefSeqNP_592974.1. NM_001018374.2.

3D structure databases

ProteinModelPortalQ09690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278379. 193 interactions.
DIPDIP-59764N.
IntActQ09690. 3 interactions.
MINTMINT-4694097.
STRING4896.SPAC2F7.03c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC2F7.03c.1; SPAC2F7.03c.1:pep; SPAC2F7.03c.
GeneID2541889.
KEGGspo:SPAC2F7.03c.

Organism-specific databases

PomBaseSPAC2F7.03c.

Phylogenomic databases

eggNOGCOG0515.
KOK08825.
OMAHESIGES.
OrthoDBEOG7WDNBB.
PhylomeDBQ09690.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802976.

Entry information

Entry namePOM1_SCHPO
AccessionPrimary (citable) accession number: Q09690
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 115 of the entry and version 1 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