SKB15_SCHPO
ID SKB15_SCHPO Reviewed; 341 AA.
AC O74453; Q96VR0;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Shk1 kinase-binding protein 15;
GN Name=skb15; ORFNames=SPCC16C4.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11389855; DOI=10.1016/s1097-2765(01)00248-9;
RA Kim H.W., Yang P., Qyang Y., Lai H., Du H., Henkel J.S., Kumar K., Bao S.,
RA Liu M., Marcus S.;
RT "Genetic and molecular characterization of Skb15, a highly conserved
RT inhibitor of the fission yeast PAK, Shk1.";
RL Mol. Cell 7:1095-1101(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Negatively regulates pak1/shk1 kinase activity leading to
CC proper execution of cytoskeletal remodeling and cytokinetic functions.
CC {ECO:0000269|PubMed:11389855}.
CC -!- FUNCTION: Interacts with pak1/shk1. {ECO:0000269|PubMed:11389855}.
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DR EMBL; AY030407; AAK51600.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20747.1; -; Genomic_DNA.
DR PIR; T41098; T41098.
DR RefSeq; NP_587918.1; NM_001022909.2.
DR AlphaFoldDB; O74453; -.
DR SMR; O74453; -.
DR BioGRID; 275340; 2.
DR STRING; 4896.SPCC16C4.08c.1; -.
DR iPTMnet; O74453; -.
DR MaxQB; O74453; -.
DR PaxDb; O74453; -.
DR PRIDE; O74453; -.
DR EnsemblFungi; SPCC16C4.08c.1; SPCC16C4.08c.1:pep; SPCC16C4.08c.
DR GeneID; 2538757; -.
DR KEGG; spo:SPCC16C4.08c; -.
DR PomBase; SPCC16C4.08c; skb15.
DR VEuPathDB; FungiDB:SPCC16C4.08c; -.
DR eggNOG; KOG0294; Eukaryota.
DR HOGENOM; CLU_031466_2_0_1; -.
DR InParanoid; O74453; -.
DR OMA; FGYRVKT; -.
DR PhylomeDB; O74453; -.
DR PRO; PR:O74453; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030685; C:nucleolar preribosome; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:PomBase.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00564; PQQ; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..341
FT /note="Shk1 kinase-binding protein 15"
FT /id="PRO_0000051217"
FT REPEAT 33..70
FT /note="WD 1"
FT REPEAT 77..114
FT /note="WD 2"
FT REPEAT 119..157
FT /note="WD 3"
FT REPEAT 197..234
FT /note="WD 4"
FT REPEAT 237..274
FT /note="WD 5"
FT REGION 293..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 122
FT /note="G -> C (in Ref. 1; AAK51600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37710 MW; 08E7A14D5C215BC4 CRC64;
MLRFVVGTYT HLIYGVDADI ERKKCKPLWL FEAHEGALTA LAVDGIYLAS TSSDETIKIF
DHTRNVQIAD VSVPTDIANA CIRDMCFTKN HLLACHDNGQ ISMWSKGSWL LVHTLKSSSH
KGITGIAVHP SEKLALTVGG DGKLRLWDLV RGKGGKVLPL STIPESILFL NESSFVIMSR
RGIDAFKLDL TSLFSFSSKS QLNALCLYQS KLIVGRDNGT VLVLDTSDGK ILHEFTAHKK
RVKSVYPVDD YLITASSDGS VCIWDKDWNL VIEHNIPEGN RITCMVAMLA DSNSEPKNVE
DEAAKRQSLD SETSETSSES ESESEYYSTS KQPPVKRTKH A
