GIP4_YEAST
ID GIP4_YEAST Reviewed; 760 AA.
AC P39732; D6VPI7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=GLC7-interacting protein 4;
GN Name=GIP4; Synonyms=FUN21; OrderedLocusNames=YAL031C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP SEQUENCE REVISION.
RA Vo D.T.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-760.
RX PubMed=1583694; DOI=10.1016/0022-2836(92)91025-k;
RA Harris S.D., Cheng J., Pugh T.A., Pringle J.R.;
RT "Molecular analysis of Saccharomyces cerevisiae chromosome I. On the number
RT of genes and the identification of essential genes using temperature-
RT sensitive-lethal mutations.";
RL J. Mol. Biol. 225:53-65(1992).
RN [5]
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 [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 INTERACTION WITH GLC7, AND FUNCTION.
RX PubMed=16537909; DOI=10.1128/mcb.26.7.2648-2660.2006;
RA Pinsky B.A., Kotwaliwale C.V., Tatsutani S.Y., Breed C.A., Biggins S.;
RT "Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora
RT protein kinase by redistributing Glc7.";
RL Mol. Cell. Biol. 26:2648-2660(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-501, 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-609, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609, AND IDENTIFICATION BY
RP 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: GLC7 phosphatase-regulatory protein involved in GLC7
CC subcellular redistribution and chromosome segregation.
CC {ECO:0000269|PubMed:16537909}.
CC -!- SUBUNIT: Interacts with GLC7. {ECO:0000269|PubMed:16537909}.
CC -!- INTERACTION:
CC P39732; P32598: GLC7; NbExp=4; IntAct=EBI-20636, EBI-13715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 227 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GIP4 family. {ECO:0000305}.
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DR EMBL; U12980; AAC05001.1; -; Genomic_DNA.
DR EMBL; X62577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006935; DAA06957.1; -; Genomic_DNA.
DR PIR; S70294; S70294.
DR RefSeq; NP_009371.1; NM_001178176.1.
DR AlphaFoldDB; P39732; -.
DR SMR; P39732; -.
DR BioGRID; 31735; 55.
DR DIP; DIP-6268N; -.
DR IntAct; P39732; 3.
DR MINT; P39732; -.
DR STRING; 4932.YAL031C; -.
DR iPTMnet; P39732; -.
DR MaxQB; P39732; -.
DR PaxDb; P39732; -.
DR PRIDE; P39732; -.
DR EnsemblFungi; YAL031C_mRNA; YAL031C; YAL031C.
DR GeneID; 851202; -.
DR KEGG; sce:YAL031C; -.
DR SGD; S000000029; GIP4.
DR VEuPathDB; FungiDB:YAL031C; -.
DR eggNOG; ENOG502QRIU; Eukaryota.
DR HOGENOM; CLU_021324_0_0_1; -.
DR InParanoid; P39732; -.
DR OMA; WYKKPAV; -.
DR BioCyc; YEAST:G3O-28842-MON; -.
DR PRO; PR:P39732; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39732; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:SGD.
DR InterPro; IPR026241; GIP4.
DR PRINTS; PR02082; GLC7IP4.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..760
FT /note="GLC7-interacting protein 4"
FT /id="PRO_0000202416"
FT REGION 449..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 760 AA; 86636 MW; 95C5C7DAD4B5D2C8 CRC64;
MVDVQKRKKL LAKAAASASI PAIKGSVPLD SYDIKIIQYK NALYKLNELN RLLNVLVPHL
KKKRDNDESY KIIPLVNFIL SLCEGPIFNV SPVLAKRYHL LCRFQLIKLS EVQQRLSTNF
IDVEGWMFPE EVPLDHYKSC IYNNSLQWKI LNSLSCIAQN AIKIYNAKLR QILLERDAYK
ARSLPFDTSI IEDLLNPVEM TLILDLAVLI NDPVRDKSTH SFYKLQWQVM EKLNSCVHSK
IFPILRTYYN QLQKFSETRP TSLSNLQKDL PHWEWTLHRI YTFHLRVFSV LCVIISFSRQ
IFLPNKQHFL DIKTRLSSEN VYHYDLIICE LMALLSPECD DVTALFELQE NLKFWTQTAR
TDNNSSRTPI FHLQPGLVVE LFNNHICKII PKLRSIMGLL SNWMDCWKYI EKNYKTFDET
NDLRENLKEK LERDKALYLE VKNAKSKLKK KPSITKLPAS SSPSPSPTSS ASPSRQASLE
SIRTRARAHL ASNSSRSPSV SPVRTTFNNK NAETKKSVVS PEKRKLINGR RPRSSSLQSY
TNKQQTSYLN STRHPSIAPP SKLNNQRSNS LQSSTMTLNQ KIVQDTVRHL MNKSASTPNP
SASSSLAPSP KVSSINNTSS GKSSSTLIAN SSDTLAIETL TLDPESNSSE LSIKRVRFAG
VPPMTEAENP KPTKVGWYKK PAVLHYPPIP ASAMIKPLQH KSKYNTLRQE EGFTFRKSLR
DGLEWENGES GSETTMMPFG IEIKESTGHR IASKIRSKLR
