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High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1)

 NTRK1_MOUSE             Reviewed;         799 AA.
Q3UFB7;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
22-NOV-2017, entry version 120.
RecName: Full=High affinity nerve growth factor receptor;
EC=2.7.10.1;
AltName: Full=Neurotrophic tyrosine kinase receptor type 1;
Flags: Precursor;
Name=Ntrk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Sympathetic ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
DISRUPTION PHENOTYPE, AND FUNCTION IN DEVELOPMENT OF THE NERVOUS
SYSTEM.
PubMed=8145823; DOI=10.1038/368246a0;
Smeyne R.J., Klein R., Schnapp A., Long L.K., Bryant S., Lewin A.,
Lira S.A., Barbacid M.;
"Severe sensory and sympathetic neuropathies in mice carrying a
disrupted Trk/NGF receptor gene.";
Nature 368:246-249(1994).
[3]
FUNCTION IN SYMPATHETIC NEURONS SURVIVAL, AND DEVELOPMENTAL STAGE.
PubMed=8815902;
Fagan A.M., Zhang H., Landis S., Smeyne R.J., Silos-Santiago I.,
Barbacid M.;
"TrkA, but not TrkC, receptors are essential for survival of
sympathetic neurons in vivo.";
J. Neurosci. 16:6208-6218(1996).
[4]
UBIQUITINATION, AND ENZYME REGULATION.
PubMed=16113645; DOI=10.1038/sj.embor.7400503;
Makkerh J.P., Ceni C., Auld D.S., Vaillancourt F., Dorval G.,
Barker P.A.;
"p75 neurotrophin receptor reduces ligand-induced Trk receptor
ubiquitination and delays Trk receptor internalization and
degradation.";
EMBO Rep. 6:936-941(2005).
[5]
ENZYME REGULATION, AND INTERACTION WITH SH2D1A.
PubMed=16223723; DOI=10.1074/jbc.M506554200;
Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.;
"SLAM-associated protein as a potential negative regulator in Trk
signaling.";
J. Biol. Chem. 280:41744-41752(2005).
[6]
FUNCTION IN NGF AND NTF3 SIGNALING, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=21816277; DOI=10.1016/j.cell.2011.07.008;
Harrington A.W., St Hillaire C., Zweifel L.S., Glebova N.O.,
Philippidou P., Halegoua S., Ginty D.D.;
"Recruitment of actin modifiers to TrkA endosomes governs retrograde
NGF signaling and survival.";
Cell 146:421-434(2011).
[7]
INDUCTION.
PubMed=23785138; DOI=10.1523/JNEUROSCI.2757-12.2013;
Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
"p75 neurotrophin receptor is a clock gene that regulates oscillatory
components of circadian and metabolic networks.";
J. Neurosci. 33:10221-10234(2013).
-!- FUNCTION: Receptor tyrosine kinase involved in the development and
the maturation of the central and peripheral nervous systems
through regulation of proliferation, differentiation and survival
of sympathetic and nervous neurons. High affinity receptor for NGF
which is its primary ligand, it can also bind and be activated by
NTF3/neurotrophin-3. However, NTF3 only supports axonal extension
through NTRK1 but has no effect on neuron survival. Upon dimeric
NGF ligand-binding, undergoes homodimerization,
autophosphorylation and activation. Recruits, phosphorylates
and/or activates several downstream effectors including SHC1,
FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping
signaling cascades driving cell survival and differentiation.
Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that
regulates cell differentiation and survival. Through PLCG1
controls NF-Kappa-B activation and the transcription of genes
involved in cell survival. Through SHC1 and SH2B1 controls a Ras-
PI3 kinase-AKT1 signaling cascade that is also regulating
survival. In absence of ligand and activation, may promote cell
death, making the survival of neurons dependent on trophic
factors. {ECO:0000269|PubMed:21816277, ECO:0000269|PubMed:8145823,
ECO:0000269|PubMed:8815902}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: The pro-survival signaling effect of NTRK1 in
neurons requires its endocytosis into signaling early endosomes
and its retrograde axonal transport. This is regulated by
different proteins including CFL1, RAC1 and SORT1. NTF3 is unable
to induce this signaling probably due to the lability of the NTF3-
NTRK1 complex in endosomes. SH2D1A inhibits the
autophosphorylation of the receptor, and alters the recruitment
and activation of downstream effectors and signaling cascades.
Regulated by NGFR. {ECO:0000269|PubMed:16113645,
ECO:0000269|PubMed:16223723, ECO:0000269|PubMed:21816277}.
-!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
affinity) and dimeric (high affinity) structures. Homodimerization
is induced by binding of a NGF dimer (By similarity). Found in a
complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2;
the complex is mainly formed at late endosomes in a nerve growth
factor (NGF)-dependent manner. Interacts with RAPGEF2; the
interaction is strengthened after NGF stimulation. Interacts with
SQSTM1; bridges NTRK1 to NGFR. Forms a ternary complex with NGFR
and KIDINS220; this complex is affected by the expression levels
of KIDINS220 and an increase in KIDINS220 expression leads to a
decreased association of NGFR and NTRK1. Interacts (phosphorylated
upon activation by NGF) with SHC1; mediates SHC1 phosphorylation
and activation. Interacts (phosphorylated upon activation by NGF)
with PLCG1; mediates PLCG1 phosphorylation and activation.
Interacts (phosphorylated) with SH2B1 and SH2B2. Interacts with
GRB2. Interacts with PIK3R1. Interacts with FRS2. Interacts with
SORT1; may regulate NTRK1 anterograde axonal transport (By
similarity). Interacts with SH2D1A; regulates NTRK1
(PubMed:16223723). Interacts with NRADD. Interacts with RAB7A.
Interacts with PTPRS (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P35739, ECO:0000269|PubMed:16223723}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P35739}. Early endosome membrane
{ECO:0000269|PubMed:21816277}; Single-pass type I membrane protein
{ECO:0000269|PubMed:21816277}. Late endosome membrane
{ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P35739}. Note=Internalized to
endosomes upon binding of NGF or NTF3 and further transported to
the cell body via a retrograde axonal transport. Localized at cell
membrane and early endosomes before nerve growth factor (NGF)
stimulation. Recruited to late endosomes after NGF stimulation.
Colocalized with RAPGEF2 at late endosomes.
{ECO:0000250|UniProtKB:P35739}.
-!- DEVELOPMENTAL STAGE: First detected at E13.5, a time coinciding
with the requirement of sympathetic neurons for NGF.
{ECO:0000269|PubMed:8815902}.
-!- INDUCTION: Expression oscillates in a circadian manner in the
suprachiasmatic nucleus (SCN) of the brain.
{ECO:0000269|PubMed:23785138}.
-!- DOMAIN: The transmembrane domain mediates interaction with
KIDINS220. {ECO:0000250}.
-!- DOMAIN: The extracellular domain mediates interaction with NGFR.
{ECO:0000250}.
-!- PTM: Ligand-mediated autophosphorylation. Interaction with SQSTM1
is phosphotyrosine-dependent. Autophosphorylation at Tyr-499
mediates interaction and phosphorylation of SHC1.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P04629}.
-!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation;
regulated by NGFR. Ubiquitination regulates the internalization of
the receptor. {ECO:0000269|PubMed:16113645}.
-!- DISRUPTION PHENOTYPE: Mice die early after birth due to severe
sensory and sympathetic neuropathies characterized by extensive
neuronal cell loss in trigeminal, sympathetic and dorsal root
ganglia, as well as a decrease in the cholinergic basal forebrain
projections to the hippocampus and cortex. There are for instance
35% fewer cells by E17.5 in the superior cervical ganglion, a
major component of the sympathetic system.
{ECO:0000269|PubMed:8145823}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAE28644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK081588; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK148691; BAE28644.1; ALT_INIT; mRNA.
CCDS; CCDS50947.1; -.
RefSeq; NP_001028296.1; NM_001033124.1.
UniGene; Mm.80682; -.
ProteinModelPortal; Q3UFB7; -.
SMR; Q3UFB7; -.
BioGrid; 201868; 9.
DIP; DIP-60900N; -.
IntAct; Q3UFB7; 6.
STRING; 10090.ENSMUSP00000029712; -.
iPTMnet; Q3UFB7; -.
PhosphoSitePlus; Q3UFB7; -.
PaxDb; Q3UFB7; -.
PeptideAtlas; Q3UFB7; -.
PRIDE; Q3UFB7; -.
Ensembl; ENSMUST00000029712; ENSMUSP00000029712; ENSMUSG00000028072.
GeneID; 18211; -.
KEGG; mmu:18211; -.
UCSC; uc008psw.1; mouse.
CTD; 4914; -.
MGI; MGI:97383; Ntrk1.
eggNOG; KOG1026; Eukaryota.
eggNOG; ENOG410YGKQ; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000264255; -.
HOVERGEN; HBG056735; -.
InParanoid; Q3UFB7; -.
KO; K03176; -.
OMA; PEVYAIM; -.
OrthoDB; EOG091G01JY; -.
PhylomeDB; Q3UFB7; -.
TreeFam; TF106465; -.
Reactome; R-MMU-170968; Frs2-mediated activation.
Reactome; R-MMU-170984; ARMS-mediated activation.
Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
Reactome; R-MMU-187042; TRKA activation by NGF.
Reactome; R-MMU-198203; PI3K/AKT activation.
PRO; PR:Q3UFB7; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028072; -.
CleanEx; MM_NTRK1; -.
Genevisible; Q3UFB7; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0048406; F:nerve growth factor binding; ISS:UniProtKB.
GO; GO:0010465; F:nerve growth factor receptor activity; ISS:UniProtKB.
GO; GO:0005166; F:neurotrophin p75 receptor binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0060385; P:axonogenesis involved in innervation; IMP:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0061368; P:behavioral response to formalin induced pain; IMP:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:MGI.
GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0060384; P:innervation; IMP:MGI.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:MGI.
GO; GO:0007399; P:nervous system development; IDA:MGI.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
GO; GO:0021553; P:olfactory nerve development; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; ISS:UniProtKB.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0010623; P:programmed cell death involved in cell development; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
GO; GO:0048485; P:sympathetic nervous system development; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR031635; NTRK_C2.
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; IPR020461; Tyr_kinase_neurotrophic_rcpt_1.
InterPro; IPR020777; Tyr_kinase_NGF_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF13855; LRR_8; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF16920; TPKR_C2; 1.
PRINTS; PR01939; NTKRECEPTOR.
PRINTS; PR01940; NTKRECEPTOR1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; Endosome; Glycoprotein;
Immunoglobulin domain; Kinase; Leucine-rich repeat; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 799 High affinity nerve growth factor
receptor.
/FTId=PRO_0000278537.
TOPO_DOM 34 420 Extracellular. {ECO:0000255}.
TRANSMEM 421 441 Helical. {ECO:0000255}.
TOPO_DOM 442 799 Cytoplasmic. {ECO:0000255}.
REPEAT 90 113 LRR 1.
REPEAT 116 137 LRR 2.
DOMAIN 148 219 LRRCT.
DOMAIN 196 285 Ig-like C2-type 1.
DOMAIN 205 368 Ig-like C2-type 2.
DOMAIN 513 784 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 519 527 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 472 493 Interaction with SQSTM1. {ECO:0000250}.
ACT_SITE 653 653 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 547 547 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 499 499 Interaction with SHC1. {ECO:0000250}.
SITE 794 794 Interaction with PLCG1. {ECO:0000250}.
MOD_RES 499 499 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 679 679 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 683 683 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 684 684 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 794 794 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 41 {ECO:0000250|UniProtKB:P04629}.
DISULFID 40 50 {ECO:0000250|UniProtKB:P04629}.
DISULFID 154 193 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 217 267 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 302 348 {ECO:0000250|UniProtKB:P04629}.
SEQUENCE 799 AA; 87738 MW; 1A37F76A63564603 CRC64;
MLRGQRLGQL GWHRPAAGLG SLMTSLMLAC ASAASCREVC CPVGPSGLRC TRAGSLDTLR
GLRGAGNLTE LYVENQQHLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FRFTPRLSHL
NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALFWLQ RWEQEGLCGV HTQTLHDSGP
GDQFLPLGHN TSCGVPTVKI QMPNDSVEVG DDVFLQCQVE GLALQQADWI LTELEGAATV
KKFGDLPSLG LILVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGLAVEQHH
WCIPFSVDGQ PAPSLRWLFN GSVLNETSFI FTQFLESALT NETMRHGCLR LNQPTHVNNG
NYTLLAANPY GQAAASVMAA FMDNPFEFNP EDPIPVSFSP VDGNSTSRDP VEKKDETPFG
VSVAVGLAVS AALFLSALLL VLNKCGQRSK FGINRPAVLA PEDGLAMSLH FMTLGGSSLS
PTEGKGSGLQ GHIMENPQYF SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD
KMLVAVKALK EASENARQDF QREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL
NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV HRDLATRNCL
VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE SILYRKFSTE SDVWSFGVVL
WEIFTYGKQP WYQLSNTEAI ECITQGRELE RPRACPPDVY AIMRGCWQRE PQQRLSMKDV
HARLQALAQA PPSYLDVLG


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