PIN4_YEAST
ID PIN4_YEAST Reviewed; 668 AA.
AC P34217; D6VPU8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=RNA-binding protein PIN4;
DE AltName: Full=Psi inducibility protein 4;
GN Name=PIN4; Synonyms=MDT1; OrderedLocusNames=YBL051C;
GN ORFNames=YBL0506, YBL0516;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH RAD53, PHOSPHORYLATION AT THR-305, AND
RP MUTAGENESIS OF THR-305.
RX PubMed=15024067; DOI=10.1128/mcb.24.7.2779-2788.2004;
RA Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.;
RT "Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage
RT tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:2779-2788(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 AND SER-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-466, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-653 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-191; SER-194;
RP SER-197; SER-393; SER-466; SER-636; SER-638; SER-640; SER-653 AND SER-655,
RP AND 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).
CC -!- FUNCTION: Involved in normal G2/M phase transition of the mitotic cell
CC cycle. In association with RAD53, also involved in checkpoint control
CC in response to DNA damage. {ECO:0000269|PubMed:15024067}.
CC -!- SUBUNIT: Interacts with RAD53. {ECO:0000269|PubMed:15024067}.
CC -!- INTERACTION:
CC P34217; P22216: RAD53; NbExp=3; IntAct=EBI-21256, EBI-17843;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Hyperphosphorylated in response to DNA damage by MEC1.
CC {ECO:0000269|PubMed:15024067}.
CC -!- MISCELLANEOUS: Present with 4630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z23261; CAA80795.1; -; Genomic_DNA.
DR EMBL; Z35812; CAA84871.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07068.1; -; Genomic_DNA.
DR PIR; S39836; S39836.
DR RefSeq; NP_009502.1; NM_001178291.1.
DR PDB; 2A0T; NMR; -; B=301-310.
DR PDBsum; 2A0T; -.
DR AlphaFoldDB; P34217; -.
DR SMR; P34217; -.
DR BioGRID; 32647; 325.
DR DIP; DIP-1905N; -.
DR ELM; P34217; -.
DR IntAct; P34217; 44.
DR MINT; P34217; -.
DR STRING; 4932.YBL051C; -.
DR iPTMnet; P34217; -.
DR MaxQB; P34217; -.
DR PaxDb; P34217; -.
DR PRIDE; P34217; -.
DR EnsemblFungi; YBL051C_mRNA; YBL051C; YBL051C.
DR GeneID; 852229; -.
DR KEGG; sce:YBL051C; -.
DR SGD; S000000147; PIN4.
DR VEuPathDB; FungiDB:YBL051C; -.
DR eggNOG; KOG0108; Eukaryota.
DR HOGENOM; CLU_029387_0_0_1; -.
DR OMA; PRFIIIR; -.
DR BioCyc; YEAST:G3O-28950-MON; -.
DR EvolutionaryTrace; P34217; -.
DR PRO; PR:P34217; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34217; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IGI:SGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR CDD; cd02639; R3H_RRM; 1.
DR CDD; cd12253; RRM_PIN4_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID50186; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034186; PIN4-like_RRM.
DR InterPro; IPR034069; R3H_Cip2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..668
FT /note="RNA-binding protein PIN4"
FT /id="PRO_0000082028"
FT DOMAIN 85..163
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:15024067"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 305
FT /note="T->A: No interaction with RAD53."
FT /evidence="ECO:0000269|PubMed:15024067"
SQ SEQUENCE 668 AA; 73776 MW; EA8EE581286436CB CRC64;
METSSFENAP PAAINDAQDN NINTETNDQE TNQQSIETRD AIDKENGVQT ETGENSAKNA
EQNVSSTNLN NAPTNGALDD DVIPNAIVIK NIPFAIKKEQ LLDIIEEMDL PLPYAFNYHF
DNGIFRGLAF ANFTTPEETT QVITSLNGKE ISGRKLKVEY KKMLPQAERE RIEREKREKR
GQLEEQHRSS SNLSLDSLSK MSGSGNNNTS NNQLFSTLMN GINANSMMNS PMNNTINNNS
SNNNNSGNII LNQPSLSAQH TSSSLYQTNV NNQAQMSTER FYAPLPSTST LPLPPQQLDF
NDPDTLEIYS QLLLFKDREK YYYELAYPMG ISASHKRIIN VLCSYLGLVE VYDPRFIIIR
RKILDHANLQ SHLQQQGQMT SAHPLQPNST GGSMNRSQSY TSLLQAHAAA AANSISNQAV
NNSSNSNTIN SNNGNGNNVI INNNSASSTP KISSQGQFSM QPTLTSPKMN IHHSSQYNSA
DQPQQPQPQT QQNVQSAAQQ QQSFLRQQAT LTPSSRIPSG YSANHYQINS VNPLLRNSQI
SPPNSQIPIN SQTLSQAQPP AQSQTQQRVP VAYQNASLSS QQLYNLNGPS SANSQSQLLP
QHTNGSVHSN FSYQSYHDES MLSAHNLNSA DLIYKSLSHS GLDDGLEQGL NRSLSGLDLQ
NQNKKNLW
