SPP41_YEAST
ID SPP41_YEAST Reviewed; 1435 AA.
AC P38904; D6VT89; Q03291;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein SPP41;
GN Name=SPP41; OrderedLocusNames=YDR464W;
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 204626 / S288c / A364A;
RX PubMed=8005438; DOI=10.1093/genetics/136.3.833;
RA Maddock J.R., Weidenhammer E.M., Adams C.C., Lunz R.L., Woolford J.L. Jr.;
RT "Extragenic suppressors of Saccharomyces cerevisiae prp4 mutations identify
RT a negative regulator of PRP genes.";
RL Genetics 136:833-847(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-981 AND LYS-1154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1014, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1014, AND IDENTIFICATION BY
RP 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 -!- FUNCTION: Negative regulator of PRP3 and PRP4 genes.
CC -!- SUBUNIT: Interacts with PRP8 and RAP1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U03673; AAA20494.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U33050; AAB64901.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12299.1; -; Genomic_DNA.
DR PIR; S69632; S69632.
DR RefSeq; NP_010752.3; NM_001180772.3.
DR AlphaFoldDB; P38904; -.
DR SMR; P38904; -.
DR BioGRID; 32518; 285.
DR DIP; DIP-2331N; -.
DR STRING; 4932.YDR464W; -.
DR iPTMnet; P38904; -.
DR MaxQB; P38904; -.
DR PaxDb; P38904; -.
DR PRIDE; P38904; -.
DR EnsemblFungi; YDR464W_mRNA; YDR464W; YDR464W.
DR GeneID; 852075; -.
DR KEGG; sce:YDR464W; -.
DR SGD; S000002872; SPP41.
DR VEuPathDB; FungiDB:YDR464W; -.
DR eggNOG; ENOG502S97X; Eukaryota.
DR HOGENOM; CLU_251351_0_0_1; -.
DR InParanoid; P38904; -.
DR OMA; VAKGPPY; -.
DR BioCyc; YEAST:G3O-29992-MON; -.
DR PRO; PR:P38904; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38904; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR021386; SPP41_DUF3020.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF11223; DUF3020; 2.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50330; UIM; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1435
FT /note="Protein SPP41"
FT /id="PRO_0000072147"
FT DOMAIN 171..190
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 16..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 683..699
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 16..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CROSSLNK 981
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
FT CROSSLNK 1154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
SQ SEQUENCE 1435 AA; 161597 MW; 7C18CF349FD647E8 CRC64;
MAYDEDDGEI NFNELVGNLL SSHNQEGQEE GEVQGGEQEG DDFEKIYPTS ENIEPKHPDD
SQHMHNSPDQ NIEIPHFVDE EDELVSVVAN AVQNIDDEQA KPENHLENGS EHVTSDTADD
NHEKEQQQEW AHILQQEILK SDGEPLRENT ERRVSTSQHH PSQRTDDALD QDDENLRMAI
LESLQELNTN EEEEKEPEKH EHAAPNDKLS SKKSSKKKKK DKSKNRESSK DKSSKKSKSS
SHSKKHAKDR NKEKQSKPTN NENTLDLSNI LENLIHENDN AAIDTAKQTV DIQDNSHTDN
TNNEDVEAQA LVEATLKAFE NELLSSAPTE EPSQEQSIGP VSSRKAVEPP RKPTADDIPL
AMLQAFKPKK RPPQEKKKTK SKTSKAASTA NKSPASESTS KKKKKKKTVK ESNKSQEAYE
DDEFSRILAD MVNQVVNTSL KETSTHTATQ DNKLESESDF TSPVQSQYTT EDASTANDDS
LDLNQIMQNA MAMVFQNQND DEFDENIVED FNRGLGDLSV SDLLPHDNLS RMEKKSVPKS
SSKSEKKTAI SRRASKKASR DASSVELTEV PSKPKKPSKT EVSLEKKLRK KYVSIANEAA
SVARKKRWAK NKELKEKEKL ERQTAREERR HKKKLEKQRL AEEQEELKKI VERGPPYPPD
LRLTKSGKPK KPYRRWTPEE LLKRSQEAEK PRKVKKERKK KEKKMKVPSS ALKKIPLFNF
VKGNVQPSAR HRLNDIEGSL STIGLHKSPD GVRRILSRPK SEDHEWPLSD SSASQNYDAH
LKTVVHKEKI PFHPPWTIPS QPPFALPVAR RKKIPNIKKY RKRTNNSFRV SKEGTASTRN
RILPAILLPI INTLKAAAKS QTAAGATPEE ARKRLATIIQ HAKSTVIRAA LQARKNSMQA
AHSKGTTTEL ATTASRMKNP LKMIPIFNTS RVKQQLDKQL PARSAGTEIS SSESPDKATP
DPHSNSTIAG HTLKGVTTPI KIEDSDANVP PVSIAVSTIE PSQDKLELTK RAESVEPVEN
NVETAKETQS VQEIKENVGT KASEEVTLTE DKTNGDPKNE KRILIESPVE KTDKKKPGEK
IATDLNEDAS LSDKKDGDEK STLHSDAAQL TGNEPDSVNT TTGKPKLIDV SLKPLNEAKP
KIPIIFPLKR PQIKPEVSVI NLVQNLVNTK IPEIKNESVD LGSNITDILS STITNILPEI
TATDVKNYQY EDENVKYLKK TPRQVLNLDG LVPPSGRCIT KAKRVRRIKK LSADATTAPE
ADGKANSESI TYTFDIPSPE EVQSKRSVVL KFAKARLTEA ELSCLKKEIN NVRKRRWREM
NSTKNWEYDV KSRLKKRANA FFGEGESETK SKWIEERFQE KVSQEKYKDR LETTETQANN
TKIVIDDKEI LNILAVNMNN LNKARCIEKD IQESFREEKL ASLQPKKKRK KSILH
