KEL1_YEAST
ID KEL1_YEAST Reviewed; 1164 AA.
AC P38853; D3DLA7; E9P8X4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Kelch repeat-containing protein 1;
GN Name=KEL1; OrderedLocusNames=YHR158C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9786949; DOI=10.1083/jcb.143.2.375;
RA Philips J., Herskowitz I.;
RT "Identification of Kel1p, a kelch domain-containing protein involved in
RT cell fusion and morphology in Saccharomyces cerevisiae.";
RL J. Cell Biol. 143:375-389(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-613, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-477; SER-613; SER-691 AND
RP SER-1022, AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; THR-467; SER-503;
RP THR-604; SER-613; THR-626; SER-748; SER-837; SER-997 AND SER-1022, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-503; SER-613;
RP SER-689; SER-691; SER-717; SER-748; SER-848; SER-958 AND SER-1022, AND
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).
CC -!- FUNCTION: Has a role in cell morphogenesis and cell fusion and may
CC antagonize the PKC1 pathway.
CC -!- SUBUNIT: Interacts with KEL2.
CC -!- INTERACTION:
CC P38853; P33306: BCK2; NbExp=2; IntAct=EBI-9619, EBI-3480;
CC P38853; P38853: KEL1; NbExp=6; IntAct=EBI-9619, EBI-9619;
CC P38853; P50090: KEL2; NbExp=6; IntAct=EBI-9619, EBI-9630;
CC P38853; P07866: LTE1; NbExp=3; IntAct=EBI-9619, EBI-10243;
CC P38853; P39946: PAC1; NbExp=3; IntAct=EBI-9619, EBI-12838;
CC -!- MISCELLANEOUS: Present with 1350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U10397; AAB68991.1; -; Genomic_DNA.
DR EMBL; AY692803; AAT92822.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06851.1; -; Genomic_DNA.
DR PIR; S46769; S46769.
DR RefSeq; NP_012028.1; NM_001179289.1.
DR AlphaFoldDB; P38853; -.
DR SMR; P38853; -.
DR BioGRID; 36592; 227.
DR ComplexPortal; CPX-36; Kelch-containing Formin Regulatory Complex.
DR DIP; DIP-1403N; -.
DR IntAct; P38853; 33.
DR MINT; P38853; -.
DR STRING; 4932.YHR158C; -.
DR iPTMnet; P38853; -.
DR COMPLUYEAST-2DPAGE; P38853; -.
DR MaxQB; P38853; -.
DR PaxDb; P38853; -.
DR PRIDE; P38853; -.
DR EnsemblFungi; YHR158C_mRNA; YHR158C; YHR158C.
DR GeneID; 856563; -.
DR KEGG; sce:YHR158C; -.
DR SGD; S000001201; KEL1.
DR VEuPathDB; FungiDB:YHR158C; -.
DR eggNOG; KOG0379; Eukaryota.
DR GeneTree; ENSGT00940000176597; -.
DR HOGENOM; CLU_005472_0_0_1; -.
DR InParanoid; P38853; -.
DR OMA; WNRIKLQ; -.
DR BioCyc; YEAST:G3O-31193-MON; -.
DR PRO; PR:P38853; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38853; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0051285; C:cell cortex of cell tip; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990615; C:Kelch-containing formin regulatory complex; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000755; P:cytogamy; IMP:SGD.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IMP:SGD.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI:SGD.
DR GO; GO:0090337; P:regulation of formin-nucleated actin cable assembly; IGI:SGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:SGD.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Kelch repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1164
FT /note="Kelch repeat-containing protein 1"
FT /id="PRO_0000119096"
FT REPEAT 139..186
FT /note="Kelch 1"
FT REPEAT 253..307
FT /note="Kelch 2"
FT REPEAT 308..357
FT /note="Kelch 3"
FT REPEAT 359..409
FT /note="Kelch 4"
FT REPEAT 411..460
FT /note="Kelch 5"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 777..931
FT /evidence="ECO:0000255"
FT COILED 974..1163
FT /evidence="ECO:0000255"
FT COMPBIAS 21..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 447
FT /note="D -> A (in Ref. 3; AAT92822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1164 AA; 131094 MW; 43D0FC570F1D5E4D CRC64;
MAGFSFAKKF THKKHGKTPS DASISDQSRE ASLSTPPNEK FFTKQETPQK GRQFSQGYHS
NVNKTSSPPM FARKQVSESR IQPSAVPPQQ RNVSGPSTTL HKQLSKQREY TVWNRIKLQN
SPFPRYRHVA SAYVTDKNQI YVIGGLHDQS VYGDTWILTA FDNATRFSTT TIDISEATPP
PRVGHAAVLC GNAFVVFGGD THKVNKEGLM DDDIYLLNIN SYKWTVPAPV GPRPLGRYGH
KISIIATTQM KTKLYVFGGQ FDDTYFNDLA VYDLSSFRRP DSHWEFLKPR TFTPPPITNF
TMISYDSKLW VFGGDTLQGL VNDVFMYDPA INDWFIIDTT GEKPPPVQEH ATVVYNDLMC
VVGGKDEHDA YLNSVYFLNL KSRKWFKLPV FTAGIPQGRS GHSLTLLKND KILIMGGDKF
DYARVEEYDL HTSDIDMQRG TIVYTLDLAR IKDLCPGVMD VPTDTPTPRN GNLDLATPVT
PTSHQTKNMN VPISAAPLAS APSPAPKDFS DADRLNREVH NRNVSTEHQN QSHPVNSESH
LIAEPNILTP YVPSESSQTP VMKITSNKPF DTPTIQKEPD LSETMDPTVG NQRIPSSIYG
DNLTPANQIK NNSPILETLP SNEIKTPQNG NIEEIKHLPD ADEKIDSTTT FDQEINGDKL
GTSSMSKVEE DGNVADEDDE IGVAQMASSP SKDQFKIKHY NESSELSQNN TEIDKLSEPV
DITIKKSDTA GHDSANHVID ASDEKNVSPM GDVPTDTKNE EASVPINRDA TTEVVDRALF
EKLRSELQSL KELTHEKALE AGAHIKELET ELWQLKSQKN SGTTKEIDEL DSVRLQSKCE
ILEADNHSLE DKVNELEELV NSKFLDIENL NEVIQFQNEK IKSLELEPNY KEKLEELQIE
HENLSRENER LKNESKQHNE DIINNVANYS SQLGSLISHW KENRANSSFL ESSSSLISVS
DENGEKTVGE PYGDQSRHHR VVINKLTNRL DDLLERSQEL TISKEKLSSE YHALKMEHSS
LSQDVLVKEN EIKKIQNDYK ESISSMDSAS KALMVSQREL EKYKSLNKKL IDELDELKFK
NGVCSENFEN GLRSTEESSN NVKNSNSIRE NQFNIKINDL KAELFITNQE RDDLKSEVLE
LKKRLLNLEN NTKQVNEDAD SDLL
