SKG6_YEAST
ID SKG6_YEAST Reviewed; 734 AA.
AC P32900; D3DL98;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein SKG6;
DE AltName: Full=Suppressor of lethality of KEX2-GAS1 double null mutant 6;
GN Name=SKG6; OrderedLocusNames=YHR149C;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-734.
RX PubMed=8358820; DOI=10.1007/bf00324677;
RA Schwank S., Harrer R., Schueller H.-J., Schweizer E.;
RT "Molecular cloning and analysis of the nuclear gene MRP-L6 coding for a
RT putative mitochondrial ribosomal protein from Saccharomyces cerevisiae.";
RL Curr. Genet. 24:136-140(1993).
RN [5]
RP INTERACTION WITH ZDS1 AND ZDS2.
RX PubMed=11489916; DOI=10.1083/jcb.200104057;
RA Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W.,
RA Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R.,
RA McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P.,
RA Boone C., Pringle J.R., Davis T.N., Fields S., Drubin D.G.;
RT "A protein interaction map for cell polarity development.";
RL J. Cell Biol. 154:549-571(2001).
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 BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16314687; DOI=10.2323/jgam.51.323;
RA Tomishige N., Noda Y., Adachi H., Yoda K.;
RT "SKG6, a suppressor gene of synthetic lethality of kex2Delta gas1Delta
RT mutations, encodes a novel membrane protein showing polarized intracellular
RT localization.";
RL J. Gen. Appl. Microbiol. 51:323-326(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND IDENTIFICATION BY
RP 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 [10]
RP GENE NAME.
RX PubMed=15645486; DOI=10.1002/yea.1206;
RA Tomishige N., Noda Y., Adachi H., Shimoi H., Yoda K.;
RT "SKG1, a suppressor gene of synthetic lethality of kex2Deltagas1Delta
RT mutations, encodes a novel membrane protein that affects cell wall
RT composition.";
RL Yeast 22:141-155(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-222 AND SER-369, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-251, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-191; SER-193;
RP SER-219; THR-221; SER-222; SER-672 AND SER-717, AND IDENTIFICATION BY MASS
RP 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: May be involved in the polarity establishment process.
CC Suppresses the lethality of KEX2-GAS1 double null mutant when
CC overexpressed. {ECO:0000269|PubMed:16314687}.
CC -!- SUBUNIT: Interacts with ZDS1 and ZDS2.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16314687}; Single-
CC pass membrane protein {ECO:0000269|PubMed:16314687}. Note=Localizes
CC primarily to the growing sites, such as an incipient bud site in the
CC cells with emerging buds, a bud tip in small- or medium-budded cells,
CC or a cell periphery in large-budded cells.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SKG6/TOS2 family. {ECO:0000305}.
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DR EMBL; U10397; AAB68987.1; -; Genomic_DNA.
DR EMBL; AY723827; AAU09744.1; -; Genomic_DNA.
DR EMBL; X69480; CAA49235.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06842.1; -; Genomic_DNA.
DR PIR; S46765; S46765.
DR RefSeq; NP_012019.1; NM_001179280.1.
DR AlphaFoldDB; P32900; -.
DR BioGRID; 36583; 33.
DR DIP; DIP-4592N; -.
DR IntAct; P32900; 7.
DR MINT; P32900; -.
DR STRING; 4932.YHR149C; -.
DR iPTMnet; P32900; -.
DR MaxQB; P32900; -.
DR PaxDb; P32900; -.
DR PRIDE; P32900; -.
DR EnsemblFungi; YHR149C_mRNA; YHR149C; YHR149C.
DR GeneID; 856554; -.
DR KEGG; sce:YHR149C; -.
DR SGD; S000001192; SKG6.
DR VEuPathDB; FungiDB:YHR149C; -.
DR eggNOG; ENOG502REX9; Eukaryota.
DR GeneTree; ENSGT00940000176525; -.
DR HOGENOM; CLU_026020_0_0_1; -.
DR InParanoid; P32900; -.
DR OMA; RMKSIYQ; -.
DR BioCyc; YEAST:G3O-31184-MON; -.
DR PRO; PR:P32900; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32900; protein.
DR GO; GO:0071944; C:cell periphery; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:1902413; P:negative regulation of mitotic cytokinesis; IMP:SGD.
DR InterPro; IPR014805; SKG6/AXL2_alpha-helix_TM.
DR Pfam; PF08693; SKG6; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..734
FT /note="Protein SKG6"
FT /id="PRO_0000202924"
FT TRANSMEM 72..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 30..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 355
FT /note="L -> R (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="N -> D (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="M -> I (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="P -> A (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="Missing (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="Q -> R (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="P -> S (in Ref. 4; CAA49235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 81849 MW; 5F508A348DBB297F CRC64;
MYHTHMHESL ISVTSTVSVS DASYAYARLT RRDDSDSSSS SASSTKNSKS AECTGSKQQC
QLPTDSSHST SVTVGVAVAV PVGVIIIVLA VILCIVYRRS KKEAEEDNDP DFEGDSEFLP
TMKDYSPGIN HLYSSDSQQD FMEKTLQQPP SDPFVGSMHS SKYNVRSATP PAIGRSWYVD
PFQLPQESND SNSLRDFAMR VQEDGLGGYK VAAESRNASQ TSLHPDNFSN CTPIRASSRF
QESESFRSHG SPIHNNQLSR GSATEGANKQ FTFPNEDNDS SSVSEEAEVL NESNESASND
AFEFELDNSS EKTHERNLRF GKDDDNYELQ DIREAEHMND RSSSKSQDDD YYVSLLSPNE
EEDIKRMKSI YQVYLDRAKT MKKEEDKADN ANDISQEENR VDNIVQNPLP SIKINNNDNI
DNNEVPEAKH LVKEALPLNN TNLAEYGPEM AQSQKQYPVQ DTLTVNDTEA APSNRIASSI
YSEAIQPLNY QDQYQQQEQS PVYNGHTQYP GNGYSGNPQQ QGYTAQFVQN PQWYGVPTPQ
QQQHNHPQTL ETIGELPTPA YLAQSASSHS LTSFKRPNKQ QLLQLQTARL NGTALNPVDH
PEMFYSPTND AYYAPQQQGQ YMKFNENGAV PSPYQLRQSV VMTNPSDLTA KPSYKPAGSF
RSVSATNSRN NSLTTQNNIY LQQQQQQLYN SRVSGILEET DVVQPPSVGG ILPHSGSQDD
LRKQLGSSHN YTVN
