LSB1_YEAST
ID LSB1_YEAST Reviewed; 241 AA.
AC P53281; D6VUR8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=LAS seventeen-binding protein 1;
DE Short=LAS17-binding protein 1;
GN Name=LSB1; OrderedLocusNames=YGR136W;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 INTERACTION WITH LAS17.
RX PubMed=10512884; DOI=10.1091/mbc.10.10.3521;
RA Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C.,
RA Soulard A., Moreau V., Winsor B.;
RT "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome
RT protein Las17p interacts with the Arp2/3 complex.";
RL Mol. Biol. Cell 10:3521-3538(1999).
RN [4]
RP FUNCTION.
RX PubMed=10407277;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<973::aid-yea402>3.0.co;2-l;
RA Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P.,
RA Maundrell K.;
RT "Chemotyping of yeast mutants using robotics.";
RL Yeast 15:973-986(1999).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [8]
RP UBIQUITINATION BY RSP5.
RX PubMed=17551511; DOI=10.1038/msb4100159;
RA Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J.,
RA Parkinson J., Rotin D.;
RT "Ubiquitination screen using protein microarrays for comprehensive
RT identification of Rsp5 substrates in yeast.";
RL Mol. Syst. Biol. 3:116-116(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, 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 [11]
RP UBIQUITINATION BY RSP5, AND INTERACTION WITH RSP5.
RX PubMed=22000681; DOI=10.1016/j.ejcb.2011.08.002;
RA Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R.,
RA Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T.;
RT "Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in
RT vitro.";
RL Eur. J. Cell Biol. 90:1016-1028(2011).
RN [12]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-90, AND INTERACTION WITH LAS17 AND
RP SUP35.
RX PubMed=21777813; DOI=10.1016/j.molcel.2011.07.001;
RA Chernova T.A., Romanyuk A.V., Karpova T.S., Shanks J.R., Ali M.,
RA Moffatt N., Howie R.L., O'Dell A., McNally J.G., Liebman S.W.,
RA Chernoff Y.O., Wilkinson K.D.;
RT "Prion induction by the short-lived, stress-induced protein Lsb2 is
RT regulated by ubiquitination and association with the actin cytoskeleton.";
RL Mol. Cell 43:242-252(2011).
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).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-79; LYS-118 AND
RP LYS-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in resistance to EDTA.
CC {ECO:0000269|PubMed:10407277}.
CC -!- SUBUNIT: Interacts with LAS17, RSP5 and SUP35.
CC {ECO:0000269|PubMed:10512884, ECO:0000269|PubMed:21777813,
CC ECO:0000269|PubMed:22000681}.
CC -!- INTERACTION:
CC P53281; Q12168: ACF2; NbExp=4; IntAct=EBI-23329, EBI-32973;
CC P53281; P40563: AIM21; NbExp=5; IntAct=EBI-23329, EBI-25376;
CC P53281; P38266: AIM3; NbExp=3; IntAct=EBI-23329, EBI-21584;
CC P53281; P53933: APP1; NbExp=4; IntAct=EBI-23329, EBI-28798;
CC P53281; Q04322: GYL1; NbExp=2; IntAct=EBI-23329, EBI-27427;
CC P53281; P39940: RSP5; NbExp=2; IntAct=EBI-23329, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC actin patch.
CC -!- DOMAIN: The PY motif is recognized directly by the WW domains of RSP5.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RSP5. {ECO:0000269|PubMed:17551511,
CC ECO:0000269|PubMed:22000681}.
CC -!- SIMILARITY: Belongs to the LSB1 family. {ECO:0000305}.
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DR EMBL; Z72921; CAA97149.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08229.1; -; Genomic_DNA.
DR PIR; S64445; S64445.
DR RefSeq; NP_011652.1; NM_001181265.1.
DR AlphaFoldDB; P53281; -.
DR SMR; P53281; -.
DR BioGRID; 33384; 44.
DR DIP; DIP-1863N; -.
DR IntAct; P53281; 29.
DR MINT; P53281; -.
DR STRING; 4932.YGR136W; -.
DR iPTMnet; P53281; -.
DR MaxQB; P53281; -.
DR PaxDb; P53281; -.
DR PRIDE; P53281; -.
DR EnsemblFungi; YGR136W_mRNA; YGR136W; YGR136W.
DR GeneID; 853037; -.
DR KEGG; sce:YGR136W; -.
DR SGD; S000003368; LSB1.
DR VEuPathDB; FungiDB:YGR136W; -.
DR eggNOG; KOG3601; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_064525_2_0_1; -.
DR InParanoid; P53281; -.
DR OMA; WKGRNER; -.
DR BioCyc; YEAST:G3O-30842-MON; -.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR PRO; PR:P53281; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53281; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0033565; C:ESCRT-0 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA: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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..241
FT /note="LAS seventeen-binding protein 1"
FT /id="PRO_0000202825"
FT DOMAIN 53..112
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 118..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..138
FT /note="PY motif"
FT COMPBIAS 118..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..213
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 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 90
FT /note="W->S: Abolishes interaction with LAS17, but not with
FT SUP35. Blocks colocalization with actin."
FT /evidence="ECO:0000269|PubMed:21777813"
SQ SEQUENCE 241 AA; 26139 MW; 5F0B1361AF84AA79 CRC64;
MSASLVNRSL KNIRNELEFL KESNVISGDI FELINSKLPE KWDGNQRSPQ NADTEEYVEA
LYDFEAQQDG DLSLKTGDKI QVLEKISPDW YRGKSNNKIG IFPANYVKPA FTRSASPKSA
EAASSSTVSR PSVPPPSYEP AASQYPSQQV SAPYAPPAGY MQAPPPQQQQ APLPYPPPFT
NYYQQPQQQY APPSQQAPVE AQPQQSSGAS SAFKSFGSKL GNAAIFGAGS AIGSDIVNSI
F
