ABP1_YEAST
ID ABP1_YEAST Reviewed; 592 AA.
AC P15891; D6VR88;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Actin-binding protein;
GN Name=ABP1; OrderedLocusNames=YCR088W; ORFNames=YCR88W;
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].
RX PubMed=2405279; DOI=10.1038/343288a0;
RA Drubin D.G., Mulholland J., Zhu Z., Botstein D.;
RT "Homology of a yeast actin-binding protein to signal transduction proteins
RT and myosin-I.";
RL Nature 343:288-290(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 PROTEIN SEQUENCE OF 2-13 AND 97-112, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [5]
RP INTERACTION WITH SRV2.
RX PubMed=8552082; DOI=10.1128/mcb.16.2.548;
RA Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R.,
RA Drubin D.G., Field J.;
RT "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-
RT associated protein binds SH3 domains and modulates cytoskeletal
RT localization.";
RL Mol. Cell. Biol. 16:548-556(1996).
RN [6]
RP INTERACTION WITH RVS167.
RX PubMed=10388809; DOI=10.1093/genetics/152.3.881;
RA Colwill K., Field D., Moore L., Friesen J., Andrews B.;
RT "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function
RT is mediated through multiple protein interactions.";
RL Genetics 152:881-893(1999).
RN [7]
RP FUNCTION, INTERACTION WITH ACTIN AND ARP2/3 COMPLEX, AND MUTAGENESIS OF
RP 201-ASP--TRP-203 AND 437-ASP--TRP-439.
RX PubMed=11331312; DOI=10.1083/jcb.153.3.627;
RA Goode B.L., Rodal A.A., Barnes G., Drubin D.G.;
RT "Activation of the Arp2/3 complex by the actin filament binding protein
RT Abp1p.";
RL J. Cell Biol. 153:627-634(2001).
RN [8]
RP INTERACTION WITH SLA1, AND SUBCELLULAR LOCATION.
RX PubMed=11950888; DOI=10.1242/jcs.115.8.1703;
RA Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.;
RT "Sla1p couples the yeast endocytic machinery to proteins regulating actin
RT dynamics.";
RL J. Cell Sci. 115:1703-1715(2002).
RN [9]
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 [10]
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 [11]
RP INTERACTION WITH APP1; PRK1; SCP1 AND YIR003W.
RX PubMed=14737190; DOI=10.1371/journal.pbio.0020014;
RA Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L.,
RA Schneider-Mergener J., Volkmer-Engert R., Cesareni G.;
RT "Protein interaction networks by proteome peptide scanning.";
RL PLoS Biol. 2:94-103(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181; SER-365 AND SER-481, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-181; SER-183 AND
RP SER-389, AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-181; SER-183;
RP SER-313; SER-365; SER-389; SER-458 AND SER-481, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-167; SER-169;
RP THR-181; SER-313 AND SER-365, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-464, AND IDENTIFICATION BY
RP 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).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF SH3 DOMAIN, MUTAGENESIS OF
RP TRP-569, AND INTERACTION WITH ARK1 AND PRK1.
RX PubMed=11668184; DOI=10.1074/jbc.m109848200;
RA Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K.,
RA Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.;
RT "Unusual binding properties of the SH3 domain of the yeast actin-binding
RT protein Abp1: structural and functional analysis.";
RL J. Biol. Chem. 277:5290-5298(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF ADF DOMAIN, MUTAGENESIS OF LYS-21;
RP ARG-24; LYS-80; LYS-94; ARG-96; ASP-122; ASP-125 AND LYS-134, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15872087; DOI=10.1091/mbc.e05-01-0059;
RA Quintero-Monzon O., Rodal A.A., Strokopytov B., Almo S.C., Goode B.L.;
RT "Structural and functional dissection of the Abp1 ADFH actin-binding domain
RT reveals versatile in vivo adapter functions.";
RL Mol. Biol. Cell 16:3128-3139(2005).
CC -!- FUNCTION: Regulates ARP2/3 complex-mediated actin assembly. Recruits
CC ARP2/3 complex to sides of preexisting actin filaments, which may
CC promote nucleation or stabilization of filament branches. Binds to
CC actin filaments, but not actin monomers. Actin binding is required for
CC ARP2/3 complex activation. May also have a role in linking the actin
CC cytoskeleton to endocytosis. recruits components of the endocytotic
CC machinery to cortical actin patches, known sites of endocytosis.
CC {ECO:0000269|PubMed:11331312}.
CC -!- SUBUNIT: Binds F-actin, but not G-actin. Interacts with the ARP2/3
CC complex. Interacts with APP1, ARK1, PRK1, SCP1, SRV2 and YIR003W via
CC its SH3 domain. Interacts with the SH3 domain of RVS167 and with SLA1.
CC {ECO:0000269|PubMed:10388809, ECO:0000269|PubMed:11331312,
CC ECO:0000269|PubMed:11668184, ECO:0000269|PubMed:11950888,
CC ECO:0000269|PubMed:14737190, ECO:0000269|PubMed:8552082}.
CC -!- INTERACTION:
CC P15891; P40563: AIM21; NbExp=10; IntAct=EBI-2036, EBI-25376;
CC P15891; P53933: APP1; NbExp=11; IntAct=EBI-2036, EBI-28798;
CC P15891; P53974: ARK1; NbExp=12; IntAct=EBI-2036, EBI-9817;
CC P15891; Q06604: BSP1; NbExp=2; IntAct=EBI-2036, EBI-37047;
CC P15891; Q12134: HUA2; NbExp=4; IntAct=EBI-2036, EBI-37262;
CC P15891; P50942: INP52; NbExp=2; IntAct=EBI-2036, EBI-28834;
CC P15891; P43603: LSB3; NbExp=6; IntAct=EBI-2036, EBI-22980;
CC P15891; P40494: PRK1; NbExp=11; IntAct=EBI-2036, EBI-9703;
CC P15891; P39743: RVS167; NbExp=6; IntAct=EBI-2036, EBI-14500;
CC P15891; Q08873: SCP1; NbExp=7; IntAct=EBI-2036, EBI-33137;
CC P15891; P32790: SLA1; NbExp=4; IntAct=EBI-2036, EBI-17313;
CC P15891; P17555: SRV2; NbExp=9; IntAct=EBI-2036, EBI-4024;
CC P15891; P32793: YSC84; NbExp=4; IntAct=EBI-2036, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11950888, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15872087}. Note=Cortical actin patches.
CC -!- PTM: The actin depolymerizing factor homology (ADF) domain mediates
CC actin filament binding.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; X51780; CAA36075.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42253.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07557.1; -; Genomic_DNA.
DR PIR; S19503; LLBY.
DR RefSeq; NP_010012.1; NM_001178794.1.
DR PDB; 1HQZ; X-ray; 2.10 A; 1/2/3/4/5/6/7/8/9=1-141.
DR PDB; 1JO8; X-ray; 1.30 A; A=535-592.
DR PDB; 2K3B; NMR; -; A=535-592.
DR PDB; 2RPN; NMR; -; A=535-592.
DR PDBsum; 1HQZ; -.
DR PDBsum; 1JO8; -.
DR PDBsum; 2K3B; -.
DR PDBsum; 2RPN; -.
DR AlphaFoldDB; P15891; -.
DR BMRB; P15891; -.
DR SMR; P15891; -.
DR BioGRID; 31060; 166.
DR DIP; DIP-534N; -.
DR IntAct; P15891; 50.
DR MINT; P15891; -.
DR STRING; 4932.YCR088W; -.
DR iPTMnet; P15891; -.
DR MaxQB; P15891; -.
DR PaxDb; P15891; -.
DR PRIDE; P15891; -.
DR EnsemblFungi; YCR088W_mRNA; YCR088W; YCR088W.
DR GeneID; 850450; -.
DR KEGG; sce:YCR088W; -.
DR SGD; S000000684; ABP1.
DR VEuPathDB; FungiDB:YCR088W; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000168710; -.
DR HOGENOM; CLU_459326_0_0_1; -.
DR InParanoid; P15891; -.
DR OMA; HYASQYD; -.
DR BioCyc; YEAST:G3O-29382-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR EvolutionaryTrace; P15891; -.
DR PRO; PR:P15891; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P15891; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IMP:SGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR GO; GO:0044379; P:protein localization to actin cortical patch; IMP:SGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11961; SH3_Abp1_fungi_C2; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR035718; Abp1_fungi_SH3_C2.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378"
FT CHAIN 2..592
FT /note="Actin-binding protein"
FT /id="PRO_0000064429"
FT DOMAIN 7..136
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REPEAT 200..209
FT /note="1"
FT REPEAT 436..445
FT /note="2"
FT DOMAIN 532..592
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 566..575
FT /note="3"
FT REGION 144..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..575
FT /note="3 X 10 AA approximate repeats (acidic)"
FT COMPBIAS 144..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 21
FT /note="K->A: In ABP1-1; moderately reduces actin binding
FT and partially reduces ARP2/3 complex activation; when
FT associated with A-24."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 24
FT /note="R->A: In ABP1-1; moderately reduces actin binding
FT and partially reduces ARP2/3 complex activation; when
FT associated with A-21."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 80
FT /note="K->A: In ABP1-2; strongly reduces actin binding and
FT abolishes ARP2/3 complex activation."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 94
FT /note="K->A: In ABP1-3; reduces actin binding and abolishes
FT ARP2/3 complex activation; when associated with A-96."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 96
FT /note="R->A: In ABP1-3; reduces actin binding and abolishes
FT ARP2/3 complex activation; when associated with A-94."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 122
FT /note="D->A: In ABP1-4; no effect; when associated with A-
FT 125."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 125
FT /note="D->A: In ABP1-4; no effect; when associated with A-
FT 122."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 134
FT /note="K->A: In ABP1-5; moderately reduces actin binding
FT and abolishes ARP2/3 complex activation."
FT /evidence="ECO:0000269|PubMed:15872087"
FT MUTAGEN 201..203
FT /note="DDW->AAA: Abolishes ARP2/3 complex activation, but
FT not actin binding."
FT /evidence="ECO:0000269|PubMed:11331312"
FT MUTAGEN 437..439
FT /note="DDW->AAA: Abolishes ARP2/3 complex activation, but
FT not actin binding."
FT /evidence="ECO:0000269|PubMed:11331312"
FT MUTAGEN 569
FT /note="W->A: Abolishes protein binding."
FT /evidence="ECO:0000269|PubMed:11668184"
FT CONFLICT 58
FT /note="L -> S (in Ref. 1; CAA36075)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="K -> I (in Ref. 1; CAA36075)"
FT /evidence="ECO:0000305"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1HQZ"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1HQZ"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1HQZ"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1HQZ"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1HQZ"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:1JO8"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:2RPN"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:1JO8"
FT STRAND 566..574
FT /evidence="ECO:0007829|PDB:1JO8"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:1JO8"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:1JO8"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:1JO8"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:1JO8"
SQ SEQUENCE 592 AA; 65576 MW; 39523510704D94AA CRC64;
MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS SFHDFLQLFD
ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA ANFAAVANNL FKGYHVQVTA
RDEDDLDENE LLMKISNAAG ARYSIQTSSK QQGKASTPPV KKSFTPSKSP APVSKKEPVK
TPSPAPAAKI SSRVNDNNDD DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE
KAKEDPRLVQ KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND
DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP DVKDLKSKFE
GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV KAEEAEQPKT DYKKIGNPLP
GMHIEADNEE EPEENDDDWD DDEDEAAQPP LPSRNVASGA PVQKEEPEQE EIAPSLPSRN
SIPAPKQEEA PEQAPEEEIE EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE
YDYDAAEDNE LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN
