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 27-MAR-2024, entry version 156. 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}. 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; 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; 62. DR DIP; DIP-6268N; -. DR IntAct; P39732; 3. DR MINT; P39732; -. DR STRING; 4932.YAL031C; -. DR iPTMnet; P39732; -. DR MaxQB; P39732; -. DR PaxDb; 4932-YAL031C; -. DR PeptideAtlas; P39732; -. DR EnsemblFungi; YAL031C_mRNA; YAL031C; YAL031C. DR GeneID; 851202; -. DR KEGG; sce:YAL031C; -. DR AGR; SGD:S000000029; -. 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 OrthoDB; 2034742at2759; -. DR BioCyc; YEAST:G3O-28842-MONOMER; -. DR BioGRID-ORCS; 851202; 0 hits in 10 CRISPR screens. 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 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 //