CKI1_SCHPO
ID CKI1_SCHPO Reviewed; 446 AA.
AC P40233; Q9UUL9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Casein kinase I homolog 1;
DE EC=2.7.11.1;
GN Name=cki1; ORFNames=SPBC1347.06c;
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 [MRNA].
RC STRAIN=SP66;
RX PubMed=8163505; DOI=10.1016/s0021-9258(17)32675-3;
RA Wang P.-C., Vancura A., Desai A., Carmel G., Kuret J.;
RT "Cytoplasmic forms of fission yeast casein kinase-1 associate primarily
RT with the particulate fraction of the cell.";
RL J. Biol. Chem. 269:12014-12023(1994).
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-298.
RX PubMed=7889932; DOI=10.1002/j.1460-2075.1995.tb07082.x;
RA Xu R.-M., Carmel G., Sweet R.M., Kuret J., Cheng X.;
RT "Crystal structure of casein kinase-1, a phosphate-directed protein
RT kinase.";
RL EMBO J. 14:1015-1023(1995).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U06929; AAA19019.1; -; mRNA.
DR EMBL; CU329671; CAB37437.1; -; Genomic_DNA.
DR PIR; A53581; A53581.
DR RefSeq; NP_596698.1; NM_001022622.2.
DR PDB; 1CSN; X-ray; 2.00 A; A=1-298.
DR PDB; 1EH4; X-ray; 2.80 A; A/B=1-298.
DR PDB; 2CSN; X-ray; 2.50 A; A=2-298.
DR PDBsum; 1CSN; -.
DR PDBsum; 1EH4; -.
DR PDBsum; 2CSN; -.
DR AlphaFoldDB; P40233; -.
DR SMR; P40233; -.
DR BioGRID; 276168; 2.
DR IntAct; P40233; 1.
DR MINT; P40233; -.
DR STRING; 4896.SPBC1347.06c.1; -.
DR iPTMnet; P40233; -.
DR MaxQB; P40233; -.
DR PaxDb; P40233; -.
DR PRIDE; P40233; -.
DR EnsemblFungi; SPBC1347.06c.1; SPBC1347.06c.1:pep; SPBC1347.06c.
DR PomBase; SPBC1347.06c; cki1.
DR VEuPathDB; FungiDB:SPBC1347.06c; -.
DR eggNOG; KOG1165; Eukaryota.
DR HOGENOM; CLU_019279_1_0_1; -.
DR InParanoid; P40233; -.
DR OMA; HANMIHI; -.
DR PhylomeDB; P40233; -.
DR BRENDA; 2.7.11.1; 5613.
DR EvolutionaryTrace; P40233; -.
DR PRO; PR:P40233; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:PomBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:PomBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..446
FT /note="Casein kinase I homolog 1"
FT /id="PRO_0000192861"
FT DOMAIN 12..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 308..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 82
FT /note="I -> V (in Ref. 1; AAA19019)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> Q (in Ref. 1; AAA19019)"
FT /evidence="ECO:0000305"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1EH4"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 105..123
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1CSN"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1CSN"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:1CSN"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1CSN"
SQ SEQUENCE 446 AA; 50425 MW; D813483056CD8FD8 CRC64;
MSGQNNVVGV HYKVGRRIGE GSFGVIFEGT NLLNNQQVAI KFEPRRSDAP QLRDEYRTYK
LLAGCTGIPN VYYFGQEGLH NILVIDLLGP SLEDLLDLCG RKFSVKTVAM AAKQMLARVQ
SIHEKSLVYR DIKPDNFLIG RPNSKNANMI YVVDFGMVKF YRDPVTKQHI PYREKKNLSG
TARYMSINTH LGREQSRRDD LEALGHVFMY FLRGSLPWQG LKAATNKQKY ERIGEKKQST
PLRELCAGFP EEFYKYMHYA RNLAFDATPD YDYLQGLFSK VLERLNTTED ENFDWNLLNN
GKGWQSLKSR NAETENQRSS KPPAPKLESK SPALQNHAST QNVVSKRSDY EKPFAEPHLN
SASDSAEPNQ NSLPNPPTET KATTTVPDRS GLATNQPAPV DVHDSSEERV TREQVQNATK
ETEAPKKKKS FWASILSCCS GSNEDT
