HRR25_YEAST
ID HRR25_YEAST Reviewed; 494 AA.
AC P29295; D6W3G5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Casein kinase I homolog HRR25;
DE EC=2.7.11.1 {ECO:0000269|PubMed:1495994};
GN Name=HRR25; OrderedLocusNames=YPL204W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1887218; DOI=10.1126/science.1887218;
RA Hoekstra M.F., Liskay R.M., Ou A.C., Demaggio A.J., Burbee D.G.,
RA Heffron F.;
RT "HRR25, a putative protein kinase from budding yeast: association with
RT repair of damaged DNA.";
RL Science 253:1031-1034(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1495994; DOI=10.1073/pnas.89.15.7008;
RA Demaggio A.J., Lindberg R.A., Hunter T., Hoekstra M.F.;
RT "The budding yeast HRR25 gene product is a casein kinase I isoform.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7008-7012(1992).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP INTERACTION WITH HRI1.
RX PubMed=21460040; DOI=10.1101/gad.1998811;
RA Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
RA Gerstein M., Snyder M.;
RT "Diverse protein kinase interactions identified by protein microarrays
RT reveal novel connections between cellular processes.";
RL Genes Dev. 25:767-778(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH ELP1.
RX PubMed=25569479; DOI=10.1371/journal.pgen.1004931;
RA Abdel-Fattah W., Jablonowski D., Di Santo R., Thuering K.L., Scheidt V.,
RA Hammermeister A., Ten Have S., Helm M., Schaffrath R., Stark M.J.;
RT "Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA
RT modification in yeast.";
RL PLoS Genet. 11:e1004931-e1004931(2015).
CC -!- FUNCTION: Protein kinase which phosphorylates serine and threonine
CC residues (PubMed:1495994). Can use casein as a substrate
CC (PubMed:1495994). Phosphorylates elongator complex member ELP1/IKI3 on
CC 'Ser-1198' and 'Ser-1202' which promotes the tRNA modification function
CC of the complex (PubMed:25569479). Associated with repair of damaged DNA
CC and meiosis (PubMed:1887218). {ECO:0000269|PubMed:1495994,
CC ECO:0000269|PubMed:1887218, ECO:0000269|PubMed:25569479}.
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 Evidence={ECO:0000269|PubMed:1495994};
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; Evidence={ECO:0000269|PubMed:1495994};
CC -!- SUBUNIT: Interacts with HRI1 (PubMed:21460040). Interacts with
CC ELP1/IKI3; the interaction leads to ELP1/IKI3 phosphorylation
CC (PubMed:21460040). {ECO:0000269|PubMed:21460040}.
CC -!- INTERACTION:
CC P29295; P35193: ATG19; NbExp=2; IntAct=EBI-8536, EBI-29291;
CC P29295; Q12292: ATG34; NbExp=2; IntAct=EBI-8536, EBI-36362;
CC P29295; P15442: GCN2; NbExp=5; IntAct=EBI-8536, EBI-330;
CC P29295; P29295: HRR25; NbExp=3; IntAct=EBI-8536, EBI-8536;
CC P29295; P40065: MAM1; NbExp=3; IntAct=EBI-8536, EBI-22643;
CC P29295; P36003: NNK1; NbExp=4; IntAct=EBI-8536, EBI-9796;
CC P29295; P15303: SEC23; NbExp=5; IntAct=EBI-8536, EBI-16584;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12628929}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12628929}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:12628929}.
CC -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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; M68605; AAA34687.1; -; Genomic_DNA.
DR EMBL; Z73560; CAA97918.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11231.1; -; Genomic_DNA.
DR PIR; A40860; A40860.
DR RefSeq; NP_015120.1; NM_001184018.1.
DR PDB; 4XHL; X-ray; 3.01 A; A=1-394.
DR PDB; 5CYZ; X-ray; 1.84 A; A=1-394.
DR PDB; 5CZO; X-ray; 2.89 A; A/B=1-394.
DR PDBsum; 4XHL; -.
DR PDBsum; 5CYZ; -.
DR PDBsum; 5CZO; -.
DR AlphaFoldDB; P29295; -.
DR SMR; P29295; -.
DR BioGRID; 35980; 621.
DR ComplexPortal; CPX-1681; Monopolin complex.
DR DIP; DIP-157N; -.
DR IntAct; P29295; 151.
DR MINT; P29295; -.
DR STRING; 4932.YPL204W; -.
DR iPTMnet; P29295; -.
DR MaxQB; P29295; -.
DR PaxDb; P29295; -.
DR PRIDE; P29295; -.
DR EnsemblFungi; YPL204W_mRNA; YPL204W; YPL204W.
DR GeneID; 855897; -.
DR KEGG; sce:YPL204W; -.
DR SGD; S000006125; HRR25.
DR VEuPathDB; FungiDB:YPL204W; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000176141; -.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; P29295; -.
DR OMA; ESRVYKY; -.
DR BioCyc; YEAST:G3O-34096-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P29295; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P29295; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0033551; C:monopolin complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:SGD.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:SGD.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:2001159; P:regulation of protein localization by the Cvt pathway; IMP:SGD.
DR GO; GO:0106214; P:regulation of vesicle fusion with Golgi apparatus; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR InterPro; IPR030509; CK1.
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 PANTHER; PTHR11909:SF409; PTHR11909:SF409; 1.
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; DNA damage; DNA repair; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..494
FT /note="Casein kinase I homolog HRR25"
FT /id="PRO_0000192859"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 394..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:4XHL"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5CZO"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 289..307
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:5CYZ"
SQ SEQUENCE 494 AA; 57340 MW; C4D3107A470E8BAF CRC64;
MDLRVGRKFR IGRKIGSGSF GDIYHGTNLI SGEEVAIKLE SIRSRHPQLD YESRVYRYLS
GGVGIPFIRW FGREGEYNAM VIDLLGPSLE DLFNYCHRRF SFKTVIMLAL QMFCRIQYIH
GRSFIHRDIK PDNFLMGVGR RGSTVHVIDF GLSKKYRDFN THRHIPYREN KSLTGTARYA
SVNTHLGIEQ SRRDDLESLG YVLIYFCKGS LPWQGLKATT KKQKYDRIME KKLNVSVETL
CSGLPLEFQE YMAYCKNLKF DEKPDYLFLA RLFKDLSIKL EYHNDHLFDW TMLRYTKAMV
EKQRDLLIEK GDLNANSNAA SASNSTDNKS ETFNKIKLLA MKKFPTHFHY YKNEDKHNPS
PEEIKQQTIL NNNAASSLPE ELLNALDKGM ENLRQQQPQQ QVQSSQPQPQ PQQLQQQPNG
QRPNYYPEPL LQQQQRDSQE QQQQVPMATT RATQYPPQIN SNNFNTNQAS VPPQMRSNPQ
QPPQDKPAGQ SIWL
