Q09690 (POM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase pom1
EC=2.7.12.1

Gene names

Name:	pom1
ORF Names:	SPAC2F7.03c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	1087 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 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 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_component	cell 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 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_function	ATP binding Inferred from sequence model. Source: PomBase 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: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tea4	O60132	5	EBI-4319163,EBI-1099982

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1087	1087	Dual specificity protein kinase pom1		PRO_0000086579
Regions
	Domain	699 – 995	297	Protein kinase
	Nucleotide binding	705 – 713	9	ATP By similarity
	Compositional bias	62 – 65	4	Poly-Ser
Sites
	Active site	825	1	Proton acceptor By similarity
	Binding site	728	1	ATP By similarity
Amino acid modifications
	Modified residue	513	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q09690 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 3277E7CA840F8BE2	FASTA	1,087	121,146
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA90490.1.
PIR	S58147.
RefSeq	NP_592974.1. NM_001018374.2.
3D structure databases
ProteinModelPortal	Q09690.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59764N.
IntAct	Q09690. 3 interactions.
MINT	MINT-4694097.
STRING	4896.SPAC2F7.03c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC2F7.03c.1; SPAC2F7.03c.1:pep; SPAC2F7.03c.
GeneID	2541889.
KEGG	spo:SPAC2F7.03c.
Organism-specific databases
PomBase	SPAC2F7.03c.
Phylogenomic databases
eggNOG	COG0515.
KO	K08825.
OMA	HESIGES.
OrthoDB	EOG415KP0.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802976.

Entry information

Entry name

POM1_SCHPO

Accession

Primary (citable) accession number: Q09690

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program