ID   LSB1_YEAST              Reviewed;         241 AA.
AC   P53281;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=LAS seventeen-binding protein 1;
DE            Short=LAS17-binding protein 1;
GN   Name=LSB1; OrderedLocusNames=YGR136W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313265; PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
RP   INTERACTION WITH LAS17.
RX   MEDLINE=99443803; PubMed=10512884;
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
RT   syndrome protein Las17p interacts with the Arp2/3 complex.";
RL   Mol. Biol. Cell 10:3521-3538(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=10407277;
RX   DOI=10.1002/(SICI)1097-0061(199907)15:10B<973::AID-YEA402>3.3.CO;2-C;
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   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND MASS
RP   SPECTROMETRY.
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
RA   Marsischky G., Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND MASS
RP   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
RT   to mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, AND
RP   MASS SPECTROMETRY.
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
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS
RP   SPECTROMETRY.
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Involved in resistance to EDTA.
CC   -!- SUBUNIT: Interacts with LAS17.
CC   -!- INTERACTION:
CC       P38266:-; NbExp=1; IntAct=EBI-23329, EBI-21584;
CC       P43582:-; NbExp=1; IntAct=EBI-23329, EBI-22766;
CC       P53238:-; NbExp=1; IntAct=EBI-23329, EBI-23185;
CC       Q12446:LAS17; NbExp=5; IntAct=EBI-23329, EBI-10022;
CC       P09938:RNR2; NbExp=1; IntAct=EBI-23329, EBI-15240;
CC       P39940:RSP5; NbExp=1; IntAct=EBI-23329, EBI-16219;
CC       Q02821:SRP1; NbExp=1; IntAct=EBI-23329, EBI-1797;
CC   -!- SIMILARITY: Belongs to the LSB1 family.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z72921; CAA97149.1; -; Genomic_DNA.
DR   PIR; S64445; S64445.
DR   RefSeq; NP_011652.1; -.
DR   HSSP; P29355; 1SEM.
DR   SMR; P53281; 56-111.
DR   DIP; DIP:1863N; -.
DR   IntAct; P53281; 14.
DR   PeptideAtlas; P53281; -.
DR   Ensembl; YGR136W; Saccharomyces cerevisiae.
DR   GeneID; 853037; -.
DR   GenomeReviews; Y13135_GR; YGR136W.
DR   KEGG; sce:YGR136W; -.
DR   NMPDR; fig|4932.3.peg.2771; -.
DR   CYGD; YGR136w; -.
DR   SGD; S000003368; LSB1.
DR   HOGENOM; P53281; -.
DR   OMA; P53281; DWWKGYK.
DR   NextBio; 972938; -.
DR   GermOnline; YGR136W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR000108; Neu_cyt_fact_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   ProDom; PD000066; SH3; 1.
DR   SMART; SM00326; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Isopeptide bond; Phosphoprotein; SH3 domain;
KW   Ubl conjugation.
FT   CHAIN         1    241       LAS seventeen-binding protein 1.
FT                                /FTId=PRO_0000202825.
FT   DOMAIN       53    112       SH3.
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine.
FT   CROSSLNK     41     41       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     79     79       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
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
//