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Protein

DYRK-family kinase pom1

Gene

pom1

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

Functioni

Polarity factor involved in localization of polarized growth and cytokinesis (PubMed:11230130, PubMed:11950884, PubMed:14663827, PubMed:17077120). Forms an intracellular gradient that serves to measure cell length and control mitotic entry (PubMed:19474792, PubMed:19474789, PubMed:21703453, PubMed:24047646). Controls the timing of mitotic commitment by regulating the inhibitory impact of cdr1/cdr2 on wee1 activity (PubMed:19474792, PubMed:22684255, PubMed:24316795). Directly phosphorylates the tail of cdr2 which inhibits cdr2 activation by ssp1 (PubMed:19474792, PubMed:24508166). Cdr2 phosphorylation by pom1 also modulates cdr2 association with membranes and inhibits cdr2 interaction with mid1, reducing its clustering ability, possibly via the down-regulation of cdr2 kinase activity (PubMed:24982431). Acts as a negative regulator of mid1 distribution, excluding mid1 from non-growing ends, which prevents division-septum assembly at the cell ends (PubMed:17140794, PubMed:17077120, PubMed:17543869). The pom1 polar gradient also mediates mitotic entry by regulating cdk1 (PubMed:19474789). Plays an essential role in proper localization and phosphorylation of a GAP for cdc42, rga4, which ensures bipolar localization of GTP-bound, active cdc42 involved in F-actin formation (PubMed:18328707). Phosphorylates multiple other substrates that function in polarized cell growth, including tea4, mod5, pal1, the Rho GAP rga7, and the Arf GEF syt22 (PubMed:25720772).18 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei728ATPPROSITE-ProRule annotation1
Active sitei825Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi705 – 713ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • activation of bipolar cell growth Source: PomBase
  • cellular protein localization Source: PomBase
  • negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  • negative regulation of protein localization to cell tip Source: PomBase
  • negative regulation of protein localization to plasma membrane Source: PomBase
  • regulation of establishment of actomyosin contractile ring localization involved in mitotic cell cycle Source: PomBase
  • regulation of establishment or maintenance of cell polarity regulating cell shape Source: PomBase
  • regulation of G2/M transition of mitotic cell cycle Source: PomBase
  • signal transduction involved in G2 cell size control checkpoint Source: PomBase

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-6804756 Regulation of TP53 Activity through Phosphorylation

Names & Taxonomyi

Protein namesi
Recommended name:
DYRK-family kinase pom1 (EC:2.7.12.13 Publications)
Gene namesi
Name:pom11 Publication
ORF Names:SPAC2F7.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi

Organism-specific databases

EuPathDBiFungiDB:SPAC2F7.03c
PomBaseiSPAC2F7.03c pom1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865791 – 1087DYRK-family kinase pom1Add BLAST1087

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei513Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylates at the cell cortex to lower lipid affinity and promote membrane release (PubMed:21703453, PubMed:26150232). Dephosphorylation by dis2, regulated by tea4, triggers membrane association (PubMed:21703453).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09690
PaxDbiQ09690
PRIDEiQ09690

PTM databases

iPTMnetiQ09690

Interactioni

Subunit structurei

Interacts with rga4 (PubMed:18328707). Interacts with tea4; this interaction triggers pom1 plasma membrane association (PubMed:21703453).2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi278379, 198 interactors
DIPiDIP-59764N
ELMiQ09690
IntActiQ09690, 3 interactors
STRINGi4896.SPAC2F7.03c.1

Structurei

3D structure databases

ProteinModelPortaliQ09690
SMRiQ09690
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini699 – 995Protein kinasePROSITE-ProRule annotationAdd BLAST297

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi62 – 65Poly-Ser4

Sequence similaritiesi

Phylogenomic databases

InParanoidiQ09690
KOiK18669
OrthoDBiEOG092C2DKP
PhylomeDBiQ09690

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

Q09690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYLQSQKAV SLGDENTDAL FKLHTSNRKS ANMFGIKSEL LNPSELSAVG
60 70 80 90 100
SYSNDICPNR QSSSSTAADT SPSTNASNTN ISFPEQEHKD ELFMNVEPKG
110 120 130 140 150
VGSSMDNHAI TIHHSTGNGL LRSSFDHDYR QKNSPRNSIH RLSNISIGNN
160 170 180 190 200
PIDFESSQQN NPSSLNTSSH HRTSSISNSK SFGTSLSYYN RSSKPSDWNQ
210 220 230 240 250
QNNGGHLSGV ISITQDVSSV PLQSSVFSSG NHAYHASMAP KRSGSWRHTN
260 270 280 290 300
FHSTSHPRAA SIGNKSGIPP VPTIPPNIGH STDHQHPKAN ISGSLTKSSS
310 320 330 340 350
ESKNLSTIQS PLKTSNSFFK ELSPHSQITL SNVKNNHSHV GSQTKSHSFA
360 370 380 390 400
TPSVFDNNKP VSSDNHNNTT TSSQVHPDSR NPDPKAAPKA VSQKTNVDGH
410 420 430 440 450
RNHEAKHGNT VQNESKSQKS SNKEGRSSRG GFFSRLSFSR SSSRMKKGSK
460 470 480 490 500
AKHEDAPDVP AIPHAYIADS STKSSYRNGK KTPTRTKSRM QQFINWFKPS
510 520 530 540 550
KERSSNGNSD SASPPPVPRL SITRSQVSRE PEKPEEIPSV PPLPSNFKDK
560 570 580 590 600
GHVPQQRSVS YTPKRSSDTS ESLQPSLSFA SSNVLSEPFD RKVADLAMKA
610 620 630 640 650
INSKRINKLL DDAKVMQSLL DRACIITPVR NTEVQLINTA PLTEYEQDEI
660 670 680 690 700
NNYDNIYFTG LRNVDKRRSA DENTSSNFGF DDERGDYKVV LGDHIAYRYE
710 720 730 740 750
VVDFLGKGSF GQVLRCIDYE TGKLVALKII RNKKRFHMQA LVETKILQKI
760 770 780 790 800
REWDPLDEYC MVQYTDHFYF RDHLCVATEL LGKNLYELIK SNGFKGLPIV
810 820 830 840 850
VIKSITRQLI QCLTLLNEKH VIHCDLKPEN ILLCHPFKSQ VKVIDFGSSC
860 870 880 890 900
FEGECVYTYI QSRFYRSPEV ILGMGYGTPI DVWSLGCIIA EMYTGFPLFP
910 920 930 940 950
GENEQEQLAC IMEIFGPPDH SLIDKCSRKK VFFDSSGKPR PFVSSKGVSR
960 970 980 990 1000
RPFSKSLHQV LQCKDVSFLS FISDCLKWDP DERMTPQQAA QHDFLTGKQD
1010 1020 1030 1040 1050
VRRPNTAPAR QKFARPPNIE TAPIPRPLPN LPMEYNDHTL PSPKEPSNQA
1060 1070 1080
SNLVRSSDKF PNLLTNLDYS IISDNGFLRK PVEKSRP
Length:1,087
Mass (Da):121,146
Last modified:November 1, 1995 - v1
Checksum:i3277E7CA840F8BE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAA90490.1
PIRiS58147
RefSeqiNP_592974.1, NM_001018374.2

Genome annotation databases

EnsemblFungiiSPAC2F7.03c.1; SPAC2F7.03c.1:pep; SPAC2F7.03c
GeneIDi2541889
KEGGispo:SPAC2F7.03c

Similar proteinsi

Entry informationi

Entry nameiPOM1_SCHPO
AccessioniPrimary (citable) accession number: Q09690
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 149 of the entry and version 1 of the sequence. See 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

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