ID HSE1_YEAST Reviewed; 452 AA. AC P38753; D3DKR2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1; GN Name=HSE1; OrderedLocusNames=YHL002W; 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 IDENTIFICATION IN THE ESCRT-0 COMPLEX, FUNCTION OF THE ESCRT-0 COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=12055639; DOI=10.1038/ncb815; RA Bilodeau P.S., Urbanowski J.L., Winistorfer S.C., Piper R.C.; RT "The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein RT sorting."; RL Nat. Cell Biol. 4:534-539(2002). RN [4] RP FUNCTION OF THE ESCRT-0 COMPLEX. RX PubMed=14581452; DOI=10.1083/jcb.200305007; RA Bilodeau P.S., Winistorfer S.C., Kearney W.R., Robertson A.D., Piper R.C.; RT "Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of RT sorting ubiquitinated proteins at the endosome."; RL J. Cell Biol. 163:237-243(2003). 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 INTERACTION WITH RSP5; VPS23 AND VPS27, AND FUNCTION OF THE ESCRT-0 RP COMPLEX. RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x; RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., RA Stevens T.H.; RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces RT cerevisiae."; RL Traffic 5:194-210(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, 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 [9] RP FUNCTION, AND INTERACTION WITH RSP5 AND UBP7. RX PubMed=17079730; DOI=10.1091/mbc.e06-06-0557; RA Ren J., Kee Y., Huibregtse J.M., Piper R.C.; RT "Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, RT associates with ubiquitin peptidases and a ligase to control sorting RT efficiency into multivesicular bodies."; RL Mol. Biol. Cell 18:324-335(2007). RN [10] RP IDENTIFICATION IN A COMPLEX WITH VPS27 AND DOA1, INTERACTION WITH DOA1, AND RP MUTAGENESIS OF 254-TRP-TRP-255. RX PubMed=18508771; DOI=10.1074/jbc.m802982200; RA Ren J., Pashkova N., Winistorfer S., Piper R.C.; RT "DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into RT multivesicular bodies."; RL J. Biol. Chem. 283:21599-21611(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, 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). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting CC receptor for ubiquitinated cargo proteins at the multivesicular body CC (MVB) and recruits ESCRT-I to the MVB outer membrane. CC {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14581452, CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:17079730}. CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27 CC (PubMed:12055639). Interacts with the ESCRT-I subunit VPS23, the UBP7 CC deubiquitinase and the E3 ligase RSP5 (PubMed:17079730, CC PubMed:15086794). May form a complex composed of VPS27, HSE1 and DOA1 CC (PubMed:18508771). Interacts (via SH3 domain) with DOA1 CC (PubMed:18508771). {ECO:0000269|PubMed:12055639, CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:17079730, CC ECO:0000269|PubMed:18508771}. CC -!- INTERACTION: CC P38753; Q12168: ACF2; NbExp=2; IntAct=EBI-1382, EBI-32973; CC P38753; P40563: AIM21; NbExp=4; IntAct=EBI-1382, EBI-25376; CC P38753; P36037: DOA1; NbExp=3; IntAct=EBI-1382, EBI-6017; CC P38753; P25604: STP22; NbExp=3; IntAct=EBI-1382, EBI-411625; CC P38753; P40453: UBP7; NbExp=4; IntAct=EBI-1382, EBI-19857; CC P38753; P40343: VPS27; NbExp=8; IntAct=EBI-1382, EBI-20380; CC P38753; P0CG53: UBB; Xeno; NbExp=2; IntAct=EBI-1382, EBI-5333021; CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12055639, CC ECO:0000269|PubMed:14562095}; Peripheral membrane protein CC {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14562095}; Cytoplasmic CC side {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10555; AAB68427.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06685.1; -; Genomic_DNA. DR PIR; S46798; S46798. DR RefSeq; NP_011861.1; NM_001179082.1. DR PDB; 2PJW; X-ray; 3.01 A; H=288-375. DR PDBsum; 2PJW; -. DR AlphaFoldDB; P38753; -. DR SMR; P38753; -. DR BioGRID; 36423; 349. DR ComplexPortal; CPX-1622; ESCRT-0 complex. DR DIP; DIP-1742N; -. DR IntAct; P38753; 44. DR MINT; P38753; -. DR STRING; 4932.YHL002W; -. DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family. DR iPTMnet; P38753; -. DR MaxQB; P38753; -. DR PaxDb; 4932-YHL002W; -. DR PeptideAtlas; P38753; -. DR EnsemblFungi; YHL002W_mRNA; YHL002W; YHL002W. DR GeneID; 856387; -. DR KEGG; sce:YHL002W; -. DR AGR; SGD:S000000994; -. DR SGD; S000000994; HSE1. DR VEuPathDB; FungiDB:YHL002W; -. DR eggNOG; KOG2199; Eukaryota. DR GeneTree; ENSGT00940000168664; -. DR HOGENOM; CLU_010104_2_0_1; -. DR InParanoid; P38753; -. DR OMA; QVYRDWW; -. DR OrthoDB; 620063at2759; -. DR BioCyc; YEAST:G3O-31026-MONOMER; -. DR Reactome; R-SCE-9013420; RHOU GTPase cycle. DR BioGRID-ORCS; 856387; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P38753; -. DR PRO; PR:P38753; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38753; Protein. DR GO; GO:0005768; C:endosome; IDA:SGD. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033565; C:ESCRT-0 complex; IPI:SGD. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0005774; C:vacuolar membrane; IDA:SGD. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA. DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:1904669; P:ATP export; IMP:SGD. DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD. DR GO; GO:0016237; P:microautophagy; IMP:SGD. DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:CAFA. DR GO; GO:1903319; P:positive regulation of protein maturation; IMP:CAFA. DR GO; GO:0009306; P:protein secretion; IMP:CAFA. DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD. DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal. DR CDD; cd21386; GAT_Hse1; 1. DR CDD; cd11805; SH3_GRB2_like_C; 1. DR CDD; cd16978; VHS_HSE1; 1. DR Gene3D; 1.20.5.1940; -; 1. DR Gene3D; 1.25.40.90; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR003903; UIM_dom. DR InterPro; IPR002014; VHS_dom. DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1. DR PANTHER; PTHR45929:SF3; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF00790; VHS; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SMART; SM00726; UIM; 1. DR SMART; SM00288; VHS; 1. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50330; UIM; 1. DR PROSITE; PS50179; VHS; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endosome; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; SH3 domain; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..452 FT /note="Class E vacuolar protein-sorting machinery protein FT HSE1" FT /id="PRO_0000202885" FT DOMAIN 15..145 FT /note="VHS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218" FT DOMAIN 162..181 FT /note="UIM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 217..276 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 144..166 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..438 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MUTAGEN 254..255 FT /note="WW->AA: Loss of interaction with DOA1." FT /evidence="ECO:0000269|PubMed:18508771" FT HELIX 289..294 FT /evidence="ECO:0007829|PDB:2PJW" FT HELIX 296..310 FT /evidence="ECO:0007829|PDB:2PJW" FT HELIX 316..319 FT /evidence="ECO:0007829|PDB:2PJW" FT HELIX 322..331 FT /evidence="ECO:0007829|PDB:2PJW" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:2PJW" FT HELIX 335..371 FT /evidence="ECO:0007829|PDB:2PJW" FT TURN 372..374 FT /evidence="ECO:0007829|PDB:2PJW" SQ SEQUENCE 452 AA; 51161 MW; 026267836BBADF69 CRC64; MSSSAIKIRN ALLKATDPKL RSDNWQYILD VCDLVKEDPE DNGQEVMSLI EKRLEQQDAN VILRTLSLTV SLAENCGSRL RQEISSKNFT SLLYALIESH SVHITLKKAV TDVVKQLSDS FKDDPSLRAM GDLYDKIKRK APYLVQPNVP EKHNMSTQAD NSDDEELQKA LKMSLFEYEK QKKLQEQEKE SAEVLPQQQQ QHQQQNQAPA HKIPAQTVVR RVRALYDLTT NEPDELSFRK GDVITVLEQV YRDWWKGALR GNMGIFPLNY VTPIVEPSKE EIEKEKNKEA IVFSQKTTID QLHNSLNAAS KTGNSNEVLQ DPHIGDMYGS VTPLRPQVTR MLGKYAKEKE DMLSLRQVLA NAERSYNQLM DRAANAHISP PVPGPALYAG MTHANNTPVM PPQRQSYQSN EYSPYPSNLP IQHPTNSANN TPQYGYDLGY SVVSQPPPGY EQ //