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 27-MAR-2024, entry version 216. 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}. 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; 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; 178. DR DIP; DIP-534N; -. DR IntAct; P15891; 50. DR MINT; P15891; -. DR STRING; 4932.YCR088W; -. DR iPTMnet; P15891; -. DR MaxQB; P15891; -. DR PaxDb; 4932-YCR088W; -. DR PeptideAtlas; P15891; -. DR EnsemblFungi; YCR088W_mRNA; YCR088W; YCR088W. DR GeneID; 850450; -. DR KEGG; sce:YCR088W; -. DR AGR; SGD:S000000684; -. 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 OrthoDB; 101008at2759; -. DR BioCyc; YEAST:G3O-29382-MONOMER; -. DR BioGRID-ORCS; 850450; 2 hits in 10 CRISPR screens. 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: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; cd11281; ADF_drebrin_like; 1. DR CDD; cd11961; SH3_Abp1_fungi_C2; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1. DR PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1. DR Pfam; PF00241; Cofilin_ADF; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00102; ADF; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1. DR SUPFAM; SSF50044; SH3-domain; 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 FT A-125." FT /evidence="ECO:0000269|PubMed:15872087" FT MUTAGEN 125 FT /note="D->A: In ABP1-4; no effect; when associated with FT A-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 //