SRC8_RAT
ID SRC8_RAT Reviewed; 509 AA.
AC Q66HL2; D3ZRB0;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Src substrate cortactin;
GN Name=Cttn {ECO:0000312|RGD:619839};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAH81802.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12612086; DOI=10.1128/mcb.23.6.2162-2170.2003;
RA Cao H., Orth J.D., Chen J., Weller S.G., Heuser J.E., McNiven M.A.;
RT "Cortactin is a component of clathrin-coated pits and participates in
RT receptor-mediated endocytosis.";
RL Mol. Cell. Biol. 23:2162-2170(2003).
RN [5]
RP INTERACTION WITH KCNA2.
RX PubMed=12151401; DOI=10.1074/jbc.m205005200;
RA Hattan D., Nesti E., Cachero T.G., Morielli A.D.;
RT "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the
RT actin-binding protein cortactin.";
RL J. Biol. Chem. 277:38596-38606(2002).
RN [6]
RP INTERACTION WITH KCNA2.
RX PubMed=17959782; DOI=10.1073/pnas.0703865104;
RA Williams M.R., Markey J.C., Doczi M.A., Morielli A.D.;
RT "An essential role for cortactin in the modulation of the potassium channel
RT Kv1.2.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:17412-17417(2007).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF SER-368; SER-381; TYR-384; TYR-429 AND
RP TYR-445.
RX PubMed=18768925; DOI=10.1152/ajpcell.00238.2008;
RA Kruchten A.E., Krueger E.W., Wang Y., McNiven M.A.;
RT "Distinct phospho-forms of cortactin differentially regulate actin
RT polymerization and focal adhesions.";
RL Am. J. Physiol. 295:C1113-C1122(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP TYR-384; TYR-429 AND TYR-445.
RX PubMed=19995918; DOI=10.1128/mcb.00330-09;
RA Cao H., Chen J., Krueger E.W., McNiven M.A.;
RT "SRC-mediated phosphorylation of dynamin and cortactin regulates the
RT 'constitutive' endocytosis of transferrin.";
RL Mol. Cell. Biol. 30:781-792(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNM2 AND ACTN1.
RX PubMed=21210813; DOI=10.1111/j.1471-4159.2011.07169.x;
RA Kurklinsky S., Chen J., McNiven M.A.;
RT "Growth cone morphology and spreading are regulated by a dynamin-cortactin
RT complex at point contacts in hippocampal neurons.";
RL J. Neurochem. 117:48-60(2011).
RN [10]
RP INTERACTION WITH KCNH1.
RX PubMed=23144454; DOI=10.1074/jbc.m112.372540;
RA Herrmann S., Ninkovic M., Kohl T., Lorinczi E., Pardo L.A.;
RT "Cortactin controls surface expression of the voltage-gated potassium
RT channel K(V)10.1.";
RL J. Biol. Chem. 287:44151-44163(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-364; SER-368 AND SER-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP FUNCTION, INTERACTION WITH PTK2, PHOSPHORYLATION AT TYR-384; TYR-429 AND
RP TYR-445, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF TYR-384; TYR-429 AND TYR-445.
RX PubMed=22952866; DOI=10.1371/journal.pone.0044041;
RA Tomar A., Lawson C., Ghassemian M., Schlaepfer D.D.;
RT "Cortactin as a target for FAK in the regulation of focal adhesion
RT dynamics.";
RL PLoS ONE 7:E44041-E44041(2012).
CC -!- FUNCTION: Contributes to the organization of the actin cytoskeleton and
CC cell shape (PubMed:18768925). Plays a role in the formation of
CC lamellipodia and in cell migration (PubMed:18768925). Plays a role in
CC the regulation of neuron morphology, axon growth and formation of
CC neuronal growth cones (PubMed:21210813). Through its interaction with
CC CTTNBP2, involved in the regulation of neuronal spine density (By
CC similarity). Plays a role in the invasiveness of cancer cells, and the
CC formation of metastases (By similarity). Plays a role in focal adhesion
CC assembly and turnover (PubMed:18768925, PubMed:22952866). In complex
CC with ABL1 and MYLK regulates cortical actin-based cytoskeletal
CC rearrangement critical to sphingosine 1-phosphate (S1P)-mediated
CC endothelial cell (EC) barrier enhancement (By similarity). Plays a role
CC in intracellular protein transport and endocytosis, and in modulating
CC the levels of potassium channels present at the cell membrane (By
CC similarity). Plays a role in receptor-mediated endocytosis via
CC clathrin-coated pits (PubMed:12612086, PubMed:19995918). Required for
CC stabilization of KCNH1 channels at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q14247, ECO:0000269|PubMed:12612086,
CC ECO:0000269|PubMed:18768925, ECO:0000269|PubMed:19995918,
CC ECO:0000269|PubMed:21210813, ECO:0000269|PubMed:22952866}.
CC -!- SUBUNIT: Interacts with SHANK2 and SHANK3 (via its SH3 domain).
CC Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3
CC domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region).
CC Interacts with FER. Forms a complex with ABL1 and MYLK (By similarity).
CC Interacts with FGD1. Identified in a complex containing FGFR4, NCAM1,
CC CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2.
CC Interacts with CTTNBP2NL; this interaction may target CTTN to stress
CC fibers. Interacts with CTTNBP2; this interaction may target CTTN at the
CC cell cortex or dendritic spines (By similarity). Interacts (via SH3
CC domain) with DNM2 (PubMed:21210813). Interacts with ACTN1
CC (PubMed:21210813). Interacts with KCNA2 (via non-phosphorylated C-
CC terminus) (PubMed:12151401, PubMed:17959782). Interacts with PTK2/FAK1
CC (PubMed:22952866). Interacts with KCNH1 (PubMed:23144454). Interacts
CC (via SH3 domain) with DIP2A (via N-terminus); the interaction enhances
CC CTTN acetylation and is required for proper synaptic transmission (By
CC similarity). {ECO:0000250|UniProtKB:Q14247,
CC ECO:0000250|UniProtKB:Q60598, ECO:0000269|PubMed:12151401,
CC ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:21210813,
CC ECO:0000269|PubMed:22952866, ECO:0000269|PubMed:23144454}.
CC -!- INTERACTION:
CC Q66HL2; P45592: Cfl1; NbExp=4; IntAct=EBI-6273816, EBI-917556;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Cell projection, ruffle
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12612086}.
CC Cell projection {ECO:0000269|PubMed:22952866}. Cell projection,
CC podosome {ECO:0000250|UniProtKB:Q01406}. Cell junction
CC {ECO:0000269|PubMed:21210813}. Cell projection, dendritic spine
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Membrane,
CC clathrin-coated pit {ECO:0000269|PubMed:12612086,
CC ECO:0000269|PubMed:19995918}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:18768925, ECO:0000269|PubMed:22952866}. Cell
CC membrane {ECO:0000269|PubMed:12612086, ECO:0000269|PubMed:19995918,
CC ECO:0000269|PubMed:21210813}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Colocalizes
CC transiently with PTK2/FAK1 at focal adhesions (PubMed:22952866).
CC Associated with membrane ruffles and lamellipodia. In the presence of
CC CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2,
CC localizes at the cell cortex. In response to neuronal activation by
CC glutamate, redistributes from dendritic spines to the dendritic shaft
CC (By similarity). Colocalizes with DNM2 at the basis of filopodia in
CC hippocampus neuron growth zones (PubMed:21210813). {ECO:0000250,
CC ECO:0000269|PubMed:21210813, ECO:0000269|PubMed:22952866}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:12612086}.
CC -!- DOMAIN: The SH3 motif may mediate binding to the cytoskeleton.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated by FER. Phosphorylated in response to FGR
CC activation. Phosphorylation by SRC promotes MYLK binding (By
CC similarity). Tyrosine phosphorylation in transformed cells may
CC contribute to cellular growth regulation and transformation.
CC Phosphorylated by PKN2 at both serine and threonine residues in a GTP-
CC bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence
CC down-regulated CTTN ability to associate with filamentous actin (By
CC similarity). Phosphorylated on tyrosine residues in response to CHRM1
CC activation (PubMed:12151401). Phosphorylated by PTK2/FAK1 in response
CC to cell adhesion (PubMed:22952866). {ECO:0000250|UniProtKB:Q14247,
CC ECO:0000250|UniProtKB:Q60598, ECO:0000269|PubMed:12151401,
CC ECO:0000269|PubMed:19995918, ECO:0000269|PubMed:22952866}.
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DR EMBL; AABR06009380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06009448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473953; EDM12238.1; -; Genomic_DNA.
DR EMBL; BC081802; AAH81802.1; -; mRNA.
DR RefSeq; NP_068640.2; NM_021868.2.
DR RefSeq; XP_017445759.1; XM_017590270.1.
DR AlphaFoldDB; Q66HL2; -.
DR SMR; Q66HL2; -.
DR IntAct; Q66HL2; 7.
DR MINT; Q66HL2; -.
DR STRING; 10116.ENSRNOP00000028283; -.
DR iPTMnet; Q66HL2; -.
DR jPOST; Q66HL2; -.
DR PaxDb; Q66HL2; -.
DR PRIDE; Q66HL2; -.
DR GeneID; 60465; -.
DR KEGG; rno:60465; -.
DR UCSC; RGD:619839; rat.
DR CTD; 2017; -.
DR RGD; 619839; Cttn.
DR VEuPathDB; HostDB:ENSRNOG00000050994; -.
DR eggNOG; ENOG502QS6C; Eukaryota.
DR HOGENOM; CLU_019379_1_0_1; -.
DR InParanoid; Q66HL2; -.
DR PhylomeDB; Q66HL2; -.
DR TreeFam; TF318935; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q66HL2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000047280; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q66HL2; baseline and differential.
DR Genevisible; Q66HL2; RN.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0071933; F:Arp2/3 complex binding; IPI:RGD.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0070064; F:proline-rich region binding; IPI:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0097581; P:lamellipodium organization; IMP:UniProtKB.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:RGD.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0030516; P:regulation of axon extension; IMP:UniProtKB.
DR GO; GO:0060491; P:regulation of cell projection assembly; IMP:RGD.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISO:RGD.
DR CDD; cd11959; SH3_Cortactin; 1.
DR InterPro; IPR015503; Cortactin.
DR InterPro; IPR035716; Cortactin_SH3.
DR InterPro; IPR003134; Hs1_Cortactin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829:SF15; PTHR10829:SF15; 3.
DR Pfam; PF02218; HS1_rep; 6.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51090; CORTACTIN; 6.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cell membrane; Cell projection; Coated pit;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis; Isopeptide bond;
KW Membrane; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Synapse; Ubl conjugation.
FT CHAIN 1..509
FT /note="Src substrate cortactin"
FT /id="PRO_0000431700"
FT REPEAT 80..116
FT /note="Cortactin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT REPEAT 117..153
FT /note="Cortactin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT REPEAT 154..190
FT /note="Cortactin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT REPEAT 191..227
FT /note="Cortactin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT REPEAT 228..264
FT /note="Cortactin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT REPEAT 265..287
FT /note="Cortactin 6; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00413"
FT DOMAIN 451..509
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..364
FT /evidence="ECO:0000255"
FT COMPBIAS 318..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 119
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 181
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 277
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 384
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000269|PubMed:22952866"
FT MOD_RES 405
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MOD_RES 429
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000269|PubMed:22952866"
FT MOD_RES 445
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000269|PubMed:22952866"
FT MOD_RES 445
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 448
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q14247"
FT MUTAGEN 368
FT /note="S->A: Inhibits actin polymerization; when associated
FT with A-381."
FT /evidence="ECO:0000269|PubMed:18768925"
FT MUTAGEN 381
FT /note="S->A: Inhibits actin polymerization; when associated
FT with A-368."
FT /evidence="ECO:0000269|PubMed:18768925"
FT MUTAGEN 384
FT /note="Y->E: Promotes reorganization of the actin
FT cytoskeleton and cell motility; when associated with E-429
FT and E-445."
FT /evidence="ECO:0000269|PubMed:18768925"
FT MUTAGEN 384
FT /note="Y->F: Impairs receptor-mediated endocytosis.
FT Increases the stability of focal adhesion and decreases
FT their turnover; when associated with F-429 and F-445."
FT /evidence="ECO:0000269|PubMed:19995918,
FT ECO:0000269|PubMed:22952866"
FT MUTAGEN 429
FT /note="Y->E: Promotes reorganization of the actin
FT cytoskeleton and cell motility; when associated with E-384
FT and E-445."
FT /evidence="ECO:0000269|PubMed:18768925"
FT MUTAGEN 429
FT /note="Y->F: Impairs receptor-mediated endocytosis.
FT Increases the stability of focal adhesion and decreases
FT their turnover; when associated with F-384 and F-445."
FT /evidence="ECO:0000269|PubMed:19995918,
FT ECO:0000269|PubMed:22952866"
FT MUTAGEN 445
FT /note="Y->E: Promotes reorganization of the actin
FT cytoskeleton and cell motility; when associated with E-384
FT and E-429."
FT /evidence="ECO:0000269|PubMed:18768925"
FT MUTAGEN 445
FT /note="Y->F: Impairs receptor-mediated endocytosis.
FT Increases the stability of focal adhesion and decreases
FT their turnover; when associated with F-384 and F-429."
FT /evidence="ECO:0000269|PubMed:19995918,
FT ECO:0000269|PubMed:22952866"
SQ SEQUENCE 509 AA; 56942 MW; 059CDB52681E2592 CRC64;
MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE
NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV GHEYQSKLSK HCSQVDSVRG
FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG
KTEKHESQKD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT
DRQDKCALGW DHQEKLQLHE SQKDYAKGFG GKYGVQKDRM DKNASTFEEV VQVPSAYQKT
VPIEAVTSKT SNIRANFENL AKEREQEDRR KAEAERAQRM AQERQEQEEA RRKLEEQARA
KKQTPPASPS PQPAEDRPPS SPIYEDAAPL KAEPSYGSSE PEPEYSTEAA GLPEASNQQG
LAYTSEPVYE TTEVPGHYQA EDDTYDGYES DLGITAIALY DYQAAGDDEI SFDPDDVITN
IEMIDDGWWR GVCKGRYGLF PANYVELRQ
