SC160_YEAST
ID SC160_YEAST Reviewed; 1222 AA.
AC P06105; D6VWA3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein SCP160;
DE AltName: Full=Protein HX;
GN Name=SCP160; Synonyms=HX; OrderedLocusNames=YJL080C; ORFNames=J1017;
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].
RX PubMed=8533468; DOI=10.1002/yea.320111004;
RA Wintersberger U., Kuehne C., Karwan A.;
RT "Scp160p, a new yeast protein associated with the nuclear membrane and the
RT endoplasmic reticulum, is necessary for maintenance of exact ploidy.";
RL Yeast 11:929-944(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-1222.
RX PubMed=3537966; DOI=10.1093/nar/14.22.9213;
RA Delahodde A., Becam A.-M., Perea J., Jacq C.;
RT "A yeast protein HX has homologies with the histone H2AF expressed in
RT chicken embryo.";
RL Nucleic Acids Res. 14:9213-9214(1986).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; SER-85 AND SER-89, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; SER-63; SER-630 AND
RP SER-1112, AND 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; SER-54; SER-63; SER-87
RP AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Involved in the control of mitotic chromosome transmission.
CC Required during cell division for faithful partitioning of the ER-
CC nuclear envelope membranes which, in S.cerevisiae, enclose the
CC duplicated chromosomes.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic
CC surface of the ER-nuclear envelope membranes.
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DR EMBL; X65645; CAA46597.1; -; Genomic_DNA.
DR EMBL; Z49355; CAA89373.1; -; Genomic_DNA.
DR EMBL; Z49354; CAA89371.1; -; Genomic_DNA.
DR EMBL; X88851; CAA61316.1; -; Genomic_DNA.
DR EMBL; X83502; CAA58490.1; -; Genomic_DNA.
DR EMBL; X04679; CAA28383.1; -; mRNA.
DR EMBL; BK006943; DAA08719.1; -; Genomic_DNA.
DR PIR; S56030; S56030.
DR RefSeq; NP_012455.1; NM_001181513.1.
DR AlphaFoldDB; P06105; -.
DR SMR; P06105; -.
DR BioGRID; 33676; 263.
DR DIP; DIP-2742N; -.
DR IntAct; P06105; 33.
DR MINT; P06105; -.
DR STRING; 4932.YJL080C; -.
DR iPTMnet; P06105; -.
DR MaxQB; P06105; -.
DR PaxDb; P06105; -.
DR PRIDE; P06105; -.
DR EnsemblFungi; YJL080C_mRNA; YJL080C; YJL080C.
DR GeneID; 853365; -.
DR KEGG; sce:YJL080C; -.
DR SGD; S000003616; SCP160.
DR VEuPathDB; FungiDB:YJL080C; -.
DR eggNOG; KOG2208; Eukaryota.
DR GeneTree; ENSGT00940000168637; -.
DR HOGENOM; CLU_003293_1_0_1; -.
DR InParanoid; P06105; -.
DR OMA; LKQASAW; -.
DR BioCyc; YEAST:G3O-31537-MON; -.
DR PRO; PR:P06105; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P06105; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0043577; P:chemotropism; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:SGD.
DR GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IGI:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 3.30.1370.10; -; 7.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 7.
DR SMART; SM00322; KH; 7.
DR SUPFAM; SSF54791; SSF54791; 6.
DR PROSITE; PS50084; KH_TYPE_1; 7.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1222
FT /note="Protein SCP160"
FT /id="PRO_0000050128"
FT DOMAIN 177..249
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 634..702
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 712..771
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 782..851
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 861..929
FT /note="KH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 939..1001
FT /note="KH 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 1153..1216
FT /note="KH 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 287
FT /note="E -> G (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> S (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="K -> Q (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="E -> K (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="D -> G (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> N (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="L -> F (in Ref. 3; CAA28383)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="E -> D (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="I -> V (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="C -> R (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 1087
FT /note="A -> E (in Ref. 1; CAA46597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1222 AA; 134810 MW; 504BBC9CAFD40758 CRC64;
MSEEQTAIDS PPSTVEGSVE TVTTIDSPST TASTIAATAE EHPQLEKKPT PLPSLKDLPS
LGSNAAFANV KVSWGPNMKP AVSNSPSPSP SAPSLTTGLG AKRMRSKNIQ EAFTLDLQSQ
LSITKPELSR IVQSVKKNHD VSVESTLSKN ARTFLVSGVA ANVHEAKREL VKKLTKPINA
VIEVPSKCKA SIIGSGGRTI REISDAYEVK INVSKEVNEN SYDEDMDDTT SNVSLFGDFE
SVNLAKAKIL AIVKEETKNA TIKLVVEDEK YLPYIDVSEF ASDEGDEEVK VQFYKKSGDI
VILGPREKAK ATKTSIQDYL KKLASNLDEE KVKIPSKFQF LIDAEELKEK YNVIVTFPST
PDDELVSFVG LRDKVGEAIT YARSSSKSYV VESLDISKAH SKNLTHAKNL IMYFTKYSVL
KGLEESHPNV KISLPSIQSL PTAETVTIHI SAKSDEANDI KAVRKELISF VNNIPPSETL
VITDLDYELF GGSIKHCLLA SESSVAFVQF GDYYPNDNSI LLVALTEDED FKPSIEEIQA
SLNKANESLN SLRTKQNNME TKTYEFSEEV QDSLFKPSSA TWKLIMEDIS EQEGHLQIKL
HTPEENQLTV RGDEKAAKAA NKIFESILNS PSSKSKMTVN IPANSVARLI GNKGSNLQQI
REKFACQIDI PNEENNNASK DKTVEVTLTG LEYNLTHAKK YLAAEAKKWA DIITKELIVP
VKFHGSLIGP HGTYRNRLQE KYNVFINFPR DNEIVTIRGP SRGVNKAHEE LKALLDFEME
NGHKMVINVP AEHVPRIIGK NGDNINDIRA EYGVEMDFLQ KSTDPKAQET GEVELEITGS
RQNIKDAAKR VESIVAEASD FVTEVLKIDH KYHKSIVGSG GHILREIISK AGGEEIRNKS
VDIPNADSEN KDITVQGPQK FVKKVVEEIN KIVKDAENSV TKTIDIPAER KGALIGPGGI
VRRQLESEFN INLFVPNKDD PSGKITITGA PENVEKAEKK ILNEIIRENF DREVDVPASI
YEYVSERGAF IQKLRMDLSV NVRFGNTSKK ANKLARAPIE IPLEKVCGST EGENAEKTKF
TIEEVGAPTS SEEGDITMRL TYEPIDLSSI LSDGEEKEVT KDTSNDSAKK EEALDTAVKL
IKERIAKAPS ATYAGYVWGA DTRRFNMIVG PGGSNIKKIR EAADVIINVP RKSDKVNDVV
YIRGTKAGVE KAGEMVLKSL RR
