AFAP1_HUMAN
ID AFAP1_HUMAN Reviewed; 730 AA.
AC Q8N556; A8K442; B4DMU2; E9PDT7; Q59EY5; Q9HBY1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Actin filament-associated protein 1;
DE AltName: Full=110 kDa actin filament-associated protein;
DE Short=AFAP-110;
GN Name=AFAP1; Synonyms=AFAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH SRC, PHOSPHORYLATION BY SRC, AND MUTAGENESIS OF PRO-71;
RP PRO-77; TYR-93; TYR-94; TYR-125; TYR-451 AND TYR-453.
RC TISSUE=Lung;
RX PubMed=15485829; DOI=10.1074/jbc.m406880200;
RA Han B., Bai X.H., Lodyga M., Xu J., Yang B.B., Keshavjee S., Post M.,
RA Liu M.;
RT "Conversion of mechanical force into biochemical signaling.";
RL J. Biol. Chem. 279:54793-54801(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP CYS-403.
RC TISSUE=Brain, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-403.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-730 (ISOFORM 1), AND VARIANT
RP MET-518.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP TISSUE SPECIFICITY, AND KNOCKDOWN IN MDA-MB-231 CELLS.
RX PubMed=17520695; DOI=10.1002/jcp.21143;
RA Dorfleutner A., Stehlik C., Zhang J., Gallick G.E., Flynn D.C.;
RT "AFAP-110 is required for actin stress fiber formation and cell adhesion in
RT MDA-MB-231 breast cancer cells.";
RL J. Cell. Physiol. 213:740-749(2007).
RN [8]
RP TISSUE SPECIFICITY, AND POSSIBLE FUNCTION IN PROSTATE CANCER PROGRESSION.
RX PubMed=17885682; DOI=10.1172/jci30710;
RA Zhang J., Park S.I., Artime M.C., Summy J.M., Shah A.N., Bomser J.A.,
RA Dorfleutner A., Flynn D.C., Gallick G.E.;
RT "AFAP-110 is overexpressed in prostate cancer and contributes to
RT tumorigenic growth by regulating focal contacts.";
RL J. Clin. Invest. 117:2962-2973(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-283; SER-664;
RP SER-665; SER-668; SER-679 AND SER-687, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548 AND SER-668, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Can cross-link actin filaments into both network and bundle
CC structures (By similarity). May modulate changes in actin filament
CC integrity and induce lamellipodia formation. May function as an adapter
CC molecule that links other proteins, such as SRC and PKC to the actin
CC cytoskeleton. Seems to play a role in the development and progression
CC of prostate adenocarcinoma by regulating cell-matrix adhesions and
CC migration in the cancer cells. {ECO:0000250,
CC ECO:0000269|PubMed:15485829}.
CC -!- SUBUNIT: Monomer and homomultimer. Interacts via its C-terminus with F-
CC actin; probably involving AFAP1 multimers (By similarity). Interacts
CC with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with
CC PRKCA, PRKCB and PRKCI (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:15485829}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N556-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N556-2; Sequence=VSP_044838;
CC -!- TISSUE SPECIFICITY: Low expression in normal breast epithelial cell
CC line MCF-10A and in tumorigenic breast cancer cell lines MCF-7, T-47D
CC and ZR-75-1. Highly expressed in the invasive breast cancer cell lines
CC MDA-MB-231 and MDA-MB-435. Overexpressed in prostate carcinoma.
CC {ECO:0000269|PubMed:17520695, ECO:0000269|PubMed:17885682}.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC.
CC {ECO:0000269|PubMed:15485829}.
CC -!- MISCELLANEOUS: Knockdown in MDA-MB-231 cells resulted in loss of actin
CC stress fibers, decreased adhesion and spreading on fibronectin.
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DR EMBL; AF188700; AAG17055.1; -; mRNA.
DR EMBL; AK290807; BAF83496.1; -; mRNA.
DR EMBL; AK297631; BAG60004.1; -; mRNA.
DR EMBL; AC004169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032777; AAH32777.1; -; mRNA.
DR EMBL; AB209676; BAD92913.1; -; mRNA.
DR CCDS; CCDS3397.1; -. [Q8N556-1]
DR CCDS; CCDS47010.1; -. [Q8N556-2]
DR RefSeq; NP_001128119.1; NM_001134647.1. [Q8N556-2]
DR RefSeq; NP_940997.1; NM_198595.2. [Q8N556-1]
DR RefSeq; XP_011511846.1; XM_011513544.2. [Q8N556-2]
DR AlphaFoldDB; Q8N556; -.
DR SMR; Q8N556; -.
DR BioGRID; 121895; 64.
DR IntAct; Q8N556; 40.
DR iPTMnet; Q8N556; -.
DR PhosphoSitePlus; Q8N556; -.
DR BioMuta; AFAP1; -.
DR DMDM; 166919564; -.
DR EPD; Q8N556; -.
DR jPOST; Q8N556; -.
DR MassIVE; Q8N556; -.
DR MaxQB; Q8N556; -.
DR PaxDb; Q8N556; -.
DR PeptideAtlas; Q8N556; -.
DR PRIDE; Q8N556; -.
DR ProteomicsDB; 19745; -.
DR ProteomicsDB; 72004; -. [Q8N556-1]
DR Antibodypedia; 2882; 515 antibodies from 32 providers.
DR DNASU; 60312; -.
DR Ensembl; ENST00000358461.6; ENSP00000351245.2; ENSG00000196526.11. [Q8N556-1]
DR Ensembl; ENST00000360265.9; ENSP00000353402.4; ENSG00000196526.11. [Q8N556-1]
DR Ensembl; ENST00000382543.4; ENSP00000371983.3; ENSG00000196526.11. [Q8N556-2]
DR Ensembl; ENST00000420658.6; ENSP00000410689.1; ENSG00000196526.11. [Q8N556-2]
DR GeneID; 60312; -.
DR KEGG; hsa:60312; -.
DR MANE-Select; ENST00000420658.6; ENSP00000410689.1; NM_001134647.2; NP_001128119.1. [Q8N556-2]
DR UCSC; uc003gkg.2; human. [Q8N556-1]
DR CTD; 60312; -.
DR DisGeNET; 60312; -.
DR GeneCards; AFAP1; -.
DR HGNC; HGNC:24017; AFAP1.
DR HPA; ENSG00000196526; Low tissue specificity.
DR MIM; 608252; gene.
DR neXtProt; NX_Q8N556; -.
DR OpenTargets; ENSG00000196526; -.
DR PharmGKB; PA162375733; -.
DR VEuPathDB; HostDB:ENSG00000196526; -.
DR eggNOG; ENOG502QQI1; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_2_0_1; -.
DR InParanoid; Q8N556; -.
DR OMA; NHYKYPV; -.
DR PhylomeDB; Q8N556; -.
DR PathwayCommons; Q8N556; -.
DR SignaLink; Q8N556; -.
DR SIGNOR; Q8N556; -.
DR BioGRID-ORCS; 60312; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; AFAP1; human.
DR GeneWiki; AFAP1; -.
DR GenomeRNAi; 60312; -.
DR Pharos; Q8N556; Tbio.
DR PRO; PR:Q8N556; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N556; protein.
DR Bgee; ENSG00000196526; Expressed in stromal cell of endometrium and 123 other tissues.
DR ExpressionAtlas; Q8N556; baseline and differential.
DR Genevisible; Q8N556; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR030113; AFAP.
DR InterPro; IPR029907; AFAP-110.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14338; PTHR14338; 2.
DR PANTHER; PTHR14338:SF8; PTHR14338:SF8; 2.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..730
FT /note="Actin filament-associated protein 1"
FT /id="PRO_0000317658"
FT DOMAIN 153..249
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 347..441
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 47..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..637
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT COILED 557..648
FT /evidence="ECO:0000255"
FT MOTIF 71..74
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT MOTIF 94..97
FT /note="SH2-binding 1"
FT /evidence="ECO:0000250"
FT MOTIF 451..456
FT /note="SH2-binding 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80YS6"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 510
FT /note="S -> SWEPEDGFPASCSRGLGEEVLYDNAGLYDNLPPPHIFARYSPADRKA
FT SRLSADKLSSNHYKYPASAQSVTNTSSVGRASLGLNSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044838"
FT VARIANT 403
FT /note="S -> C (in dbSNP:rs28406288)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038578"
FT VARIANT 518
FT /note="V -> M (in dbSNP:rs41264705)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_038579"
FT MUTAGEN 71
FT /note="P->A: Decreased tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 77
FT /note="P->A: No effect on tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 93
FT /note="Y->F: Reduces phosphorylation and phosphorylation of
FT SRC at Y-416; when associated with F-94; F-125; F-451 and
FT F-453."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 94
FT /note="Y->F: Reduces phosphorylation and phosphorylation of
FT SRC at Y-416; when associated with F-93; F-125; F-451 and
FT F-453."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 125
FT /note="Y->F: Reduces phosphorylation and phosphorylation of
FT SRC at Y-416; when associated with F-93; F-94; F-451 and F-
FT 453."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 451
FT /note="Y->F: Reduces phosphorylation and phosphorylation of
FT SRC at Y-416; when associated with F-93; F-94; F-125 and F-
FT 453."
FT /evidence="ECO:0000269|PubMed:15485829"
FT MUTAGEN 453
FT /note="Y->F: Reduces phosphorylation and phosphorylation of
FT SRC at Y-416; when associated with F-93; F-94; F-125 and F-
FT 451."
FT /evidence="ECO:0000269|PubMed:15485829"
FT CONFLICT 197
FT /note="P -> L (in Ref. 1; AAG17055)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="G -> D (in Ref. 1; AAG17055)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="E -> G (in Ref. 1; AAG17055)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="T -> A (in Ref. 2; BAF83496)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8N556-2:561
FT /note="A -> V (in Ref. 2; BAG60004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 80725 MW; 4E916BB4F82F5547 CRC64;
MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFDVKDHA QKQETANSLP
APPQMPLPEI PQPWLPPDSG PPPLPTSSLP EGYYEEAVPL SPGKAPEYIT SNYDSDAMSS
SYESYDEEEE DGKGKKTRHQ WPSEEASMDL VKDAKICAFL LRKKRFGQWT KLLCVIKDTK
LLCYKSSKDQ QPQMELPLQG CNITYIPKDS KKKKHELKIT QQGTDPLVLA VQSKEQAEQW
LKVIKEAYSG CSGPVDSECP PPPSSPVHKA ELEKKLSSER PSSDGEGVVE NGITTCNGKE
QVKRKKSSKS EAKGTVSKVT GKKITKIISL GKKKPSTDEQ TSSAEEDVPT CGYLNVLSNS
RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG LDSKHPLTFR LLRNGQEVAV
LEASSSEDMG RWIGILLAET GSSTDPEALH YDYIDVEMSA SVIQTAKQTF CFMNRRVISA
NPYLGGTSNG YAHPSGTALH YDDVPCINGS LKGKKPPVAS NGVTGKGKTL SSQPKKADPA
AVVKRTGSNA AQYKYGKNRV EADAKRLQTK EEELLKRKEA LRNRLAQLRK ERKDLRAAIE
VNAGRKPQAI LEEKLKQLEE ECRQKEAERV SLELELTEVK ESLKKALAGG VTLGLAIEPK
SGTSSPQSPV FRHRTLENSP ISSCDTSDTE GPVPVNSAAV LKKSQAAPGS SPCRGHVLRK
AKEWELKNGT
