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KEL2_YEAST
ID   KEL2_YEAST              Reviewed;         882 AA.
AC   P50090; D6VV18;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Kelch repeat-containing protein 2;
GN   Name=KEL2; OrderedLocusNames=YGR238C; ORFNames=G8585;
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=8701610;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA   van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT   "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT   region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 12:385-390(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   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   [5]
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   [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 THR-455 AND SER-509, 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   [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).
CC   -!- SUBUNIT: Interacts with KEL1.
CC   -!- INTERACTION:
CC       P50090; P38853: KEL1; NbExp=6; IntAct=EBI-9630, EBI-9619;
CC   -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X87941; CAA61189.1; -; Genomic_DNA.
DR   EMBL; Z73023; CAA97266.1; -; Genomic_DNA.
DR   EMBL; AY693035; AAT93054.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08329.1; -; Genomic_DNA.
DR   PIR; S57704; S57704.
DR   RefSeq; NP_011754.3; NM_001181367.3.
DR   AlphaFoldDB; P50090; -.
DR   SMR; P50090; -.
DR   BioGRID; 33490; 160.
DR   ComplexPortal; CPX-36; Kelch-containing Formin Regulatory Complex.
DR   DIP; DIP-4229N; -.
DR   IntAct; P50090; 10.
DR   MINT; P50090; -.
DR   STRING; 4932.YGR238C; -.
DR   iPTMnet; P50090; -.
DR   MaxQB; P50090; -.
DR   PaxDb; P50090; -.
DR   PRIDE; P50090; -.
DR   EnsemblFungi; YGR238C_mRNA; YGR238C; YGR238C.
DR   GeneID; 853153; -.
DR   KEGG; sce:YGR238C; -.
DR   SGD; S000003470; KEL2.
DR   VEuPathDB; FungiDB:YGR238C; -.
DR   eggNOG; KOG0379; Eukaryota.
DR   GeneTree; ENSGT00940000176597; -.
DR   HOGENOM; CLU_005472_0_0_1; -.
DR   InParanoid; P50090; -.
DR   BioCyc; YEAST:G3O-30916-MON; -.
DR   PRO; PR:P50090; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P50090; protein.
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:1990615; C:Kelch-containing formin regulatory complex; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
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; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Kelch repeat; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..882
FT                   /note="Kelch repeat-containing protein 2"
FT                   /id="PRO_0000119097"
FT   REPEAT          99..143
FT                   /note="Kelch 1"
FT   REPEAT          153..207
FT                   /note="Kelch 2"
FT   REPEAT          213..267
FT                   /note="Kelch 3"
FT   REPEAT          268..317
FT                   /note="Kelch 4"
FT   REPEAT          319..369
FT                   /note="Kelch 5"
FT   REPEAT          371..417
FT                   /note="Kelch 6"
FT   REGION          41..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          550..685
FT                   /evidence="ECO:0000255"
FT   COILED          728..881
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        481..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         455
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   882 AA;  99975 MW;  63B9772FF017E6D9 CRC64;
     MVPFKLTNKV PTDTGPSLIS AQSVPRPIVF MDNRNNTRIV TPTLPPNQHR GISGASTALP
     WSPESKNTGK YIWNRVKLKN SPFPRYRHSS SFIVTNDNRI FVTGGLHDQS VYGDVWQIAA
     NADGTSFTSK RIDIDQNTPP PRVGHASTIC GNAYVVFGGD THKLNKNGLL DDDLYLFNIN
     SYKWTIPQPI GRRPLGRYGH KISIIASNPM QTKLYLFGGQ VDETYFNDLV VFDLSSFRRP
     NSHWEFLEPV GDLPPPLTNH TMVAYDNKLW VFGGETPKTI SNDTYRYDPA QSEWSKVKTT
     GEKPPPIQEH ASVVYKHLMC VLGGKDTHNA YSNDVYFLNL LSLKWYKLPR MKEGIPQERS
     GHSLTLMKNE KLLIMGGDKT DYASPNIHDL QTSETDQGEG TLLYTLDLSS LNELCPGIMC
     ESLHAGESFS NSLSGGFTPS KSTESENQEI INILTPRLPD SKVLSYNDID EGAGSYSSAL
     DDKAFERKSD REEKKPQSSK VDSSINKESP GTGIKVSKKN FPVLRGLTVD SEEYGSSSYK
     DTSCQKGIPK NLFDDLNLNL QTLRLEAQQK ELETARHISQ LEKEVQRLMV IKEASKDSNF
     QTARLKNLEI QKTFLESRIN DLKNLLMVKL SQASKLCDQI TIQNNGLKTC SEHVTIKRDI
     IDLENKCDVL KRQNEILVNN MQKITPELHT YLNESSCYLG KLLKSYPTSA RPPSSEKDNQ
     IYEKDSLNKI EKVINEMHET VRAKEKLHLE TQKLNDERDS LRANLLDNNN KLDALRKLSD
     GSSKSMDLTK KAIHLSQSEL EKYRKNNDDL QKEIDRIKTE QAEQDDKQEQ RGAITHGNFD
     AFHRMKINNL KAELYMSKEN RDSLKDELLA LKKKLYTLEQ KK
 
 
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