YGI2_YEAST
ID YGI2_YEAST Reviewed; 381 AA.
AC P53155; D6VU62; Q6Q536;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Uncharacterized protein YGL082W;
GN OrderedLocusNames=YGL082W;
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=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
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 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 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72604; CAA96787.1; -; Genomic_DNA.
DR EMBL; AY558581; AAS56907.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08023.1; -; Genomic_DNA.
DR PIR; S64089; S64089.
DR RefSeq; NP_011433.3; NM_001180947.3.
DR PDB; 6K6L; X-ray; 1.77 A; A/B=1-279.
DR PDBsum; 6K6L; -.
DR AlphaFoldDB; P53155; -.
DR SMR; P53155; -.
DR BioGRID; 33168; 26.
DR IntAct; P53155; 4.
DR MINT; P53155; -.
DR STRING; 4932.YGL082W; -.
DR iPTMnet; P53155; -.
DR MaxQB; P53155; -.
DR PaxDb; P53155; -.
DR PRIDE; P53155; -.
DR TopDownProteomics; P53155; -.
DR EnsemblFungi; YGL082W_mRNA; YGL082W; YGL082W.
DR GeneID; 852798; -.
DR KEGG; sce:YGL082W; -.
DR SGD; S000003050; YGL082W.
DR VEuPathDB; FungiDB:YGL082W; -.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_0_0_1; -.
DR InParanoid; P53155; -.
DR OMA; QDSYYTG; -.
DR BioCyc; YEAST:G3O-30583-MON; -.
DR PRO; PR:P53155; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53155; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; PTHR18063; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..381
FT /note="Uncharacterized protein YGL082W"
FT /id="PRO_0000202757"
FT REGION 331..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 263
FT /note="I -> T (in Ref. 4; AAS56907)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6K6L"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6K6L"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6K6L"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6K6L"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6K6L"
SQ SEQUENCE 381 AA; 43321 MW; 7F1047CF01FC40D5 CRC64;
MDVTFLTKNV QINGTQFKIL LQNGQGECAL IALANVLLIS PAHARYAQEI SRLVRGKETV
TLNELVQTLA DMGVQNPNGT DVDKQQLLQI LPQLYSGLNI NPEFNGSFED GVEMSIFRLY
NVGIVHGWII DGDNDPNSYE HVSKYSYMGA QKVLVQSYEI QKNNAQFENS EQIQSDAPYL
KSFLARSATQ LTEYGLTHLR EILVERSYAV LFRNDHFCTL YKNNGELFTL VTDPTYRNRK
DINWQSLKSV NGSQDSYYTG NFIPTSLERT ETTATGQNES YISNPFSDQN TGHVTSNQVN
SGASGVQQIE DDEELARRLQ EQEDMRAANN MQNGYANNGR NHQRERFERP EKNSKKNKFL
PFNGSNKEKK RDKLKKNCVI M
