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HUA1_YEAST
ID   HUA1_YEAST              Reviewed;         198 AA.
AC   P40325; D6VV46;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Proline-rich protein HUA1;
GN   Name=HUA1; OrderedLocusNames=YGR268C;
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 96604 / S288c / FY1679;
RX   PubMed=9605509;
RX   DOI=10.1002/(sici)1097-0061(19980430)14:6<587::aid-yea268>3.0.co;2-i;
RA   Agostoni Carbone M.L., Lucchini G., Melchioretto P., Nardese V., Vanoni M.,
RA   Panzeri L.;
RT   "A 9359 bp fragment from the right arm of Saccharomyces cerevisiae
RT   chromosome VII includes the FOL2 and YTA7 genes and three unknown open
RT   reading frames.";
RL   Yeast 14:587-591(1998).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
RC   STRAIN=C836;
RX   PubMed=7754704; DOI=10.1002/yea.320100903;
RA   Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C.,
RA   Vetter I., Feldmann H.;
RT   "Identification of a set of yeast genes coding for a novel family of
RT   putative ATPases with high similarity to constituents of the 26S protease
RT   complex.";
RL   Yeast 10:1141-1155(1994).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=11914276; DOI=10.1101/gad.970902;
RA   Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA   Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA   Gerstein M., Roeder G.S., Snyder M.;
RT   "Subcellular localization of the yeast proteome.";
RL   Genes Dev. 16:707-719(2002).
RN   [7]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-18, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=14566057; DOI=10.1073/pnas.2132527100;
RA   Samanta M.P., Liang S.;
RT   "Predicting protein functions from redundancies in large-scale protein
RT   interaction networks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12579-12583(2003).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: May be involved in assembly and disassembly of the actin
CC       cytoskeleton. {ECO:0000269|PubMed:14566057}.
CC   -!- INTERACTION:
CC       P40325; P43603: LSB3; NbExp=5; IntAct=EBI-23614, EBI-22980;
CC       P40325; P32793: YSC84; NbExp=3; IntAct=EBI-23614, EBI-24460;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
CC   -!- SIMILARITY: Belongs to the HUA1 family. {ECO:0000305}.
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DR   EMBL; Y07893; CAA69199.1; -; Genomic_DNA.
DR   EMBL; Z73053; CAA97298.1; -; Genomic_DNA.
DR   EMBL; AY558512; AAS56838.1; -; Genomic_DNA.
DR   EMBL; X81072; CAA56961.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08357.1; -; Genomic_DNA.
DR   PIR; S64601; S64601.
DR   RefSeq; NP_011784.3; NM_001181397.3.
DR   AlphaFoldDB; P40325; -.
DR   BioGRID; 33518; 78.
DR   DIP; DIP-1987N; -.
DR   IntAct; P40325; 12.
DR   MINT; P40325; -.
DR   STRING; 4932.YGR268C; -.
DR   iPTMnet; P40325; -.
DR   MaxQB; P40325; -.
DR   PaxDb; P40325; -.
DR   PRIDE; P40325; -.
DR   EnsemblFungi; YGR268C_mRNA; YGR268C; YGR268C.
DR   GeneID; 853185; -.
DR   KEGG; sce:YGR268C; -.
DR   SGD; S000003500; HUA1.
DR   VEuPathDB; FungiDB:YGR268C; -.
DR   eggNOG; ENOG502S12N; Eukaryota.
DR   HOGENOM; CLU_078573_1_0_1; -.
DR   InParanoid; P40325; -.
DR   OMA; KNGKSCQ; -.
DR   BioCyc; YEAST:G3O-30935-MON; -.
DR   PRO; PR:P40325; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P40325; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   InterPro; IPR038910; Hua1-like.
DR   PANTHER; PTHR28031; PTHR28031; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..198
FT                   /note="Proline-rich protein HUA1"
FT                   /id="PRO_0000202865"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..86
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CROSSLNK        3
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
SQ   SEQUENCE   198 AA;  22435 MW;  78029FD484168793 CRC64;
     MSKDTHDDEL PSYEDVIKEE ERLQSQPPRP PRPAANLAQG HQSRPHQRPS TMPATSSSQT
     YAHSHSYTPT SSQPRPPPRP QQNPSLPWTY PPRFYCSKCG NTGYKLKNGR SCKSCWRRFA
     PQNNVVSAPT YYTNYTMPVY TNAWQGNRPL YVQPGDPRLG GVLCGECRGS GRTRFLLDED
     ICPLCHGVGR IITQPQRY
 
 
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