SAP1_YEAST
ID SAP1_YEAST Reviewed; 897 AA.
AC P39955; D3DLU8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein SAP1;
DE AltName: Full=SIN1-associated protein;
GN Name=SAP1; OrderedLocusNames=YER047C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 CHARACTERIZATION.
RX PubMed=8654588; DOI=10.1016/0014-5793(96)00500-5;
RA Liberzon A., Shpungin S., Bangio H., Yona E., Katcoff D.J.;
RT "Association of yeast SAP1, a novel member of the 'AAA' ATPase family of
RT proteins, with the chromatin protein SIN1.";
RL FEBS Lett. 388:5-10(1996).
RN [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, 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 -!- SUBUNIT: Interacts with SPT2/SIN1.
CC -!- INTERACTION:
CC P39955; Q05080: HOF1; NbExp=4; IntAct=EBI-16463, EBI-5412;
CC P39955; P36006: MYO3; NbExp=3; IntAct=EBI-16463, EBI-11670;
CC P39955; Q04439: MYO5; NbExp=4; IntAct=EBI-16463, EBI-11687;
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; U18796; AAB64582.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07702.1; -; Genomic_DNA.
DR PIR; S50550; S50550.
DR RefSeq; NP_010966.1; NM_001178938.1.
DR AlphaFoldDB; P39955; -.
DR SMR; P39955; -.
DR BioGRID; 36784; 91.
DR DIP; DIP-1550N; -.
DR ELM; P39955; -.
DR IntAct; P39955; 17.
DR MINT; P39955; -.
DR STRING; 4932.YER047C; -.
DR CarbonylDB; P39955; -.
DR iPTMnet; P39955; -.
DR MaxQB; P39955; -.
DR PaxDb; P39955; -.
DR PRIDE; P39955; -.
DR TopDownProteomics; P39955; -.
DR EnsemblFungi; YER047C_mRNA; YER047C; YER047C.
DR GeneID; 856771; -.
DR KEGG; sce:YER047C; -.
DR SGD; S000000849; SAP1.
DR VEuPathDB; FungiDB:YER047C; -.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000176549; -.
DR HOGENOM; CLU_000688_15_2_1; -.
DR InParanoid; P39955; -.
DR OMA; HNYPNTQ; -.
DR BioCyc; YEAST:G3O-30226-MON; -.
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P39955; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39955; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..897
FT /note="Protein SAP1"
FT /id="PRO_0000084761"
FT REGION 112..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 645..652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 897 AA; 100332 MW; E9780B269700144C CRC64;
MDSQRSHHIL TRLTKIRRRP QQPLTDFTEL YSRIANETIY YLNLEEKKRY KEALQGWKAL
TTDVLFKQTL IEHNYPNTQS YTKDEVSLQN GIRELYHKSV MHLKRVKKLV REEPAPRNDM
PSSKTYTNHS SSFTRSTEPP PVFQMVPGRM MKTLRNRNAC GYKTAYSNPS LSSYGNSTSI
KRGEDAENIR VNFVPSKPLS NNASRQHKNP IEHNDPPLKK ETELYSDKYI SEPILIDLTN
DEDDHDVGIL KGHNVFDEEE SDGFEFDVSD YYDNFSEVDV EEEEEEKEER RRIKTLEAIQ
QQMSDLSVTS STSSNKSVSS SENVPGSCIQ SLPTTAPALP SLPPPPLLNV DRASSTGALK
PHSLETSTTM DSSKIRNPQI SKLMKNNHVP YLKGTKSTPT LITKSTPTFI TRSKSNTKPI
IKSNASSPTS SLTVPNSVIQ KPKTAAMAAK RVLNSKKVAS NPALNTTKKS HPILKSKTAK
VPNSSSKKTS SHPSRPVSNS KPYSHGASQN KKPSKNQTTS MSKTNRKIPA QKKIGSPKIE
DVGTEDATEH ATSLNEQREE PEIDKKVLRE ILEDEIIDSL QGVDRQAAKQ IFAEIVVHGD
EVHWDDIAGL ESAKYSLKEA VVYPFLRPDL FRGLREPVRG MLLFGPPGTG KTMLARAVAT
ESHSTFFSIS ASSLTSKYLG ESEKLVRALF AIAKKLSPSI IFVDEIDSIM GSRNNENENE
SSRRIKNEFL VQWSSLSSAA AGSNKSNTNN SDTNGDEDDT RVLVLAATNL PWSIDEAARR
RFVRRQYIPL PEDQTRHVQF KKLLSHQKHT LTESDFDELV KITEGYSGSD ITSLAKDAAM
GPLRDLGDKL LETEREMIRP IGLVDFKNSL VYIKPSVSQD GLVKYEKWAS QFGSSGS
