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Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)

 FAK1_RAT                Reviewed;        1055 AA.
O35346; Q62900;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
27-SEP-2017, entry version 172.
RecName: Full=Focal adhesion kinase 1;
Short=FADK 1;
EC=2.7.10.2;
AltName: Full=Focal adhesion kinase-related nonkinase;
Short=FRNK;
AltName: Full=Protein-tyrosine kinase 2;
AltName: Full=p125FAK;
AltName: Full=pp125FAK;
Name=Ptk2; Synonyms=Fak, Fak1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Corpus striatum;
PubMed=8738136; DOI=10.1016/0169-328X(95)00273-U;
Burgaya F., Girault J.A.;
"Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals
multiple transcripts with different patterns of expression.";
Brain Res. Mol. Brain Res. 37:63-73(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 350-528 (ISOFORM 1).
STRAIN=Wistar;
Sasaki T., Nagura K., Sasaki H.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH TGFB1I1.
PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T.,
Ishino M., Takahashi S., Suzuki R., Sasaki T.;
"Cell adhesion kinase beta forms a complex with a new member, Hic-5,
of proteins localized at focal adhesions.";
J. Biol. Chem. 273:1003-1014(1998).
[4]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-722 AND SER-913, AND
CHARACTERIZATION OF ISOFORM 2.
PubMed=12732587; DOI=10.1161/01.HYP.0000072772.74183.5F;
Yi X.P., Wang X., Gerdes A.M., Li F.;
"Subcellular redistribution of focal adhesion kinase and its related
nonkinase in hypertrophic myocardium.";
Hypertension 41:1317-1323(2003).
[5]
INTERACTION WITH ARHGEF28.
PubMed=12702722; DOI=10.1074/jbc.M302381200;
Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W.,
Schlaepfer D.D.;
"Direct interaction of focal adhesion kinase with p190RhoGEF.";
J. Biol. Chem. 278:24865-24873(2003).
[6]
SUMOYLATION AT LYS-152, MUTAGENESIS OF LYS-152, INTERACTION WITH
PIAS1, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-397, AND
SUBCELLULAR LOCATION.
PubMed=14500712; DOI=10.1074/jbc.M308562200;
Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M.,
Boutterin M.C., Girault J.A.;
"PIAS1-mediated sumoylation of focal adhesion kinase activates its
autophosphorylation.";
J. Biol. Chem. 278:47434-47440(2003).
[7]
FUNCTION, AND INTERACTION WITH DCC.
PubMed=15494733; DOI=10.1038/nn1330;
Ren X.R., Ming G.L., Xie Y., Hong Y., Sun D.M., Zhao Z.Q., Feng Z.,
Wang Q., Shim S., Chen Z.F., Song H.J., Mei L., Xiong W.C.;
"Focal adhesion kinase in netrin-1 signaling.";
Nat. Neurosci. 7:1204-1212(2004).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CHARACTERIZATION OF ISOFORM
2.
PubMed=16373587; DOI=10.1152/ajpheart.00659.2005;
Yi X.P., Zhou J., Huber L., Qu J., Wang X., Gerdes A.M., Li F.;
"Nuclear compartmentalization of FAK and FRNK in cardiac myocytes.";
Am. J. Physiol. 290:H2509-H2515(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576; SER-913 AND
TYR-928, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Non-receptor protein-tyrosine kinase that plays an
essential role in regulating cell migration, adhesion, spreading,
reorganization of the actin cytoskeleton, formation and
disassembly of focal adhesions and cell protrusions, cell cycle
progression, cell proliferation and apoptosis. Required for early
embryonic development and placenta development. Required for
embryonic angiogenesis, normal cardiomyocyte migration and
proliferation, and normal heart development. Regulates axon growth
and neuronal cell migration, axon branching and synapse formation;
required for normal development of the nervous system. Plays a
role in osteogenesis and differentiation of osteoblasts. Functions
in integrin signal transduction, but also in signaling downstream
of numerous growth factor receptors, G-protein coupled receptors
(GPCR), EPHA2, netrin receptors and LDL receptors. Forms
multisubunit signaling complexes with SRC and SRC family members
upon activation; this leads to the phosphorylation of additional
tyrosine residues, creating binding sites for scaffold proteins,
effectors and substrates. Regulates numerous signaling pathways.
Promotes activation of phosphatidylinositol 3-kinase and the AKT1
signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1
and the MAP kinase signaling cascade. Promotes localized and
transient activation of guanine nucleotide exchange factors (GEFs)
and GTPase-activating proteins (GAPs), and thereby modulates the
activity of Rho family GTPases. Signaling via CAS family members
mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to
P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity,
P53/TP53 ubiquitination and proteasomal degradation.
Phosphorylates SRC; this increases SRC kinase activity.
Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes
phosphorylation of PXN and STAT1; most likely PXN and STAT1 are
phosphorylated by a SRC family kinase that is recruited to
autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself.
Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires
both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and
PIK3R1. Isoform 2 (FRNK) does not contain a kinase domain and
inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced
expression can attenuate the nuclear accumulation of LPXN and
limit its ability to enhance serum response factor (SRF)-dependent
gene transcription (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15494733}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Subject to autoinhibition, mediated by
interactions between the FERM domain and the kinase domain.
Activated by autophosphorylation at Tyr-397. This promotes
interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in
the kinase activation loop by SRC. Phosphorylation at Tyr-397,
Tyr-576 and Tyr-577 is required for maximal kinase activity.
-!- SUBUNIT: Interacts with GIT1. Component of a complex that contains
at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts
with STEAP4. Interacts with ZFYVE21. Interacts with ESR1.
Interacts with PIK3R1 or PIK3R2. Interacts with FGR, FLT4 and RET.
Interacts with EPHA2 in resting cells; activation of EPHA2
recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and
dissociation of the complex. Interacts with EPHA1 (kinase
activity-dependent). Interacts with P53/TP53. Interacts (via first
Pro-rich region) with CAS family members (via SH3 domain),
including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with TGFB1I1.
Interacts with SRC, GRB2 and GRB7. Interacts with ARHGEF28.
Interacts with SHB. Interacts with PXN and TLN1. Interacts with
SORBS1. Interacts with STAT1. Interacts with WASL. Interacts with
ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1
activity and activation of downstream signaling pathways.
Interacts with ARHGEF7. Interacts with MDM2 (By similarity).
Interacts with PIAS1. Interacts with DCC. Interacts with LPXN (via
LD motif 3) (By similarity). Interacts with MISP (By similarity).
Interacts with EMP2; regulates PTK2 activation and localization
(By similarity). {ECO:0000250|UniProtKB:P34152,
ECO:0000250|UniProtKB:Q05397}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-6252940, EBI-6252940;
Q5XI86:Ptrh2; NbExp=3; IntAct=EBI-6252940, EBI-6252926;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
membrane; Peripheral membrane protein; Cytoplasmic side.
Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000250}. Nucleus. Note=Constituent of
focal adhesions. Detected at microtubules (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=O35346-1; Sequence=Displayed;
Name=2; Synonyms=FRNK;
IsoId=O35346-2; Sequence=VSP_042172;
-!- DOMAIN: The first Pro-rich domain interacts with the SH3 domain of
CAS family members, such as BCAR1 and NEDD9. {ECO:0000250}.
-!- DOMAIN: The carboxy-terminal region is the site of focal adhesion
targeting (FAT) sequence which mediates the localization of FAK1
to focal adhesions.
-!- PTM: Phosphorylated on tyrosine residues upon activation, e.g.
upon integrin signaling. Tyr-397 is the major autophosphorylation
site, but other kinases can also phosphorylate this residue.
Phosphorylation at Tyr-397 promotes interaction with SRC and SRC
family members, leading to phosphorylation at Tyr-576, Tyr-577 and
at additional tyrosine residues. FGR promotes phosphorylation at
Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-
861 and Tyr-928, even when cells are not adherent. Tyr-397, Tyr-
576 and Ser-722 are phosphorylated only when cells are adherent.
Phosphorylation at Tyr-397 is important for interaction with BMX,
PIK3R1 and SHC1. Phosphorylation at Tyr-928 is important for
interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is
recruited to PTK2 via EPHA2 (tyrosine phosphorylated).
Microtubule-induced dephosphorylation at Tyr-397 is crucial for
the induction of focal adhesion disassembly; this
dephosphorylation could be catalyzed by PTPN11 and regulated by
ZFYVE21 (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated; this enhances autophosphorylation.
{ECO:0000269|PubMed:12732587, ECO:0000269|PubMed:14500712,
ECO:0000269|PubMed:16373587}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF020777; AAB72203.1; -; mRNA.
EMBL; U43942; AAA86280.1; -; mRNA.
RefSeq; NP_037213.1; NM_013081.2. [O35346-1]
UniGene; Rn.2809; -.
ProteinModelPortal; O35346; -.
SMR; O35346; -.
BioGrid; 247643; 5.
CORUM; O35346; -.
DIP; DIP-41330N; -.
IntAct; O35346; 6.
MINT; MINT-208164; -.
STRING; 10116.ENSRNOP00000011219; -.
ChEMBL; CHEMBL5773; -.
iPTMnet; O35346; -.
PhosphoSitePlus; O35346; -.
PaxDb; O35346; -.
PeptideAtlas; O35346; -.
PRIDE; O35346; -.
Ensembl; ENSRNOT00000011219; ENSRNOP00000011219; ENSRNOG00000007916. [O35346-1]
GeneID; 25614; -.
KEGG; rno:25614; -.
UCSC; RGD:3443; rat. [O35346-1]
CTD; 5747; -.
RGD; 3443; Ptk2.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; O35346; -.
KO; K05725; -.
PhylomeDB; O35346; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
Reactome; R-RNO-391160; Signal regulatory protein family interactions.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
Reactome; R-RNO-418885; DCC mediated attractive signaling.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-8874081; MET activates PTK2 signaling.
PRO; PR:O35346; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000007916; -.
ExpressionAtlas; O35346; baseline and differential.
Genevisible; O35346; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IDA:RGD.
GO; GO:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:RGD.
GO; GO:0005730; C:nucleolus; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005178; F:integrin binding; IPI:RGD.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IDA:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:RGD.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:RGD.
GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0045444; P:fat cell differentiation; IEP:RGD.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007254; P:JNK cascade; IMP:RGD.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IMP:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR005189; Focal_adhesion_kin_target_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
Pfam; PF00373; FERM_M; 1.
Pfam; PF03623; Focal_AT; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
ProDom; PD006413; Focal_adhesion_target_reg; 1.
SMART; SM00295; B41; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF68993; SSF68993; 1.
PROSITE; PS00661; FERM_2; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Acetylation; Alternative promoter usage; Angiogenesis; ATP-binding;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Isopeptide bond; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Tyrosine-protein kinase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q05397}.
CHAIN 2 1055 Focal adhesion kinase 1.
/FTId=PRO_0000088079.
DOMAIN 35 355 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 422 680 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 428 434 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 500 502 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 707 1055 Interaction with TGFB1I1. {ECO:0000250}.
REGION 915 1055 Interaction with ARHGEF28. {ECO:0000250}.
COMPBIAS 712 733 Pro-rich.
COMPBIAS 863 916 Pro-rich.
ACT_SITE 546 546 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 454 454 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 5 5 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P34152}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14500712}.
MOD_RES 407 407 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 570 570 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 576 576 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 577 577 Phosphotyrosine; by RET and SRC.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 722 722 Phosphoserine.
{ECO:0000269|PubMed:12732587}.
MOD_RES 732 732 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P34152}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 861 861 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 913 913 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:12732587}.
MOD_RES 917 917 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 928 928 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:14500712}.
VAR_SEQ 1 692 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_042172.
MUTAGEN 152 152 K->R: Abolishes sumoylation.
{ECO:0000269|PubMed:14500712}.
SEQUENCE 1055 AA; 119717 MW; 3AFB4ED682D14A33 CRC64;
MAAAYLDPNL NHTPSSSTKT HLGTGTERSP GAMERVLKVF HYFESSNEPT TWASIIRHGD
ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA DQVDQDIALK LGCLEIRRSY
WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII
RPQKEGERAL PSIPKLANNE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE
RIELGRCIGE GQFGDVHQGV YLSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK
RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA
YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY
PSPRSSEGFY PSPQHMVQTN HYQISGYPGS HGIPAMAGSI YPGQASLLDQ TELWNHRPQE
MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS
RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPAESYNE
GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP EEYVPMVKEV
GLALRTLLAT VDETIPILPA STHREIEMAQ KLLNSDLGEL ISKMKLAQQY VMTSLQQEYK
KQMLTAAHAL AVDAKNLLDV IDQARLKMLG QTRPH


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