High affinity nerve growth factor receptor precursor

Preferred order of sections

Names and origin

Protein names

Recommended name:
High affinity nerve growth factor receptor
EC=2.7.10.1

Alternative name(s):
Neurotrophic tyrosine kinase receptor type 1
TRK1-transforming tyrosine kinase protein
Tropomyosin-related kinase A
Tyrosine kinase receptor
Tyrosine kinase receptor A
Short name=Trk-A
gp140trk
p140-TrkA

Gene names

Name:	NTRK1
Synonyms:	MTC, TRK, TRKA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Isoform TrkA-III is resistant to NGF, constitutively activates AKT1 and NF-kappa-B and is unable to activate the Ras-MAPK signaling cascade. Antagonizes the anti-proliferative NGF-NTRK1 signaling that promotes neuronal precursors differentiation. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
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 By similarity. Regulated by NGFR By similarity. Ref.19
Subunit structure	Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Homodimerization is induced by binding of a NGF dimer. 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 By similarity. Interacts with SH2D1A; regulates NTRK1 By similarity. 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. Interacts with RAB7A By similarity. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.23
Subcellular location	Cell membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein By similarity. Note: Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport By similarity. Ref.18
Tissue specificity	Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by pluripotent neural stem and neural crest progenitors. Ref.14 Ref.18
Induction	Isoform TrkA-III is up-regulated upon hypoxia in cells normally expressing it. Ref.18 Ref.19
Domain	The transmembrane domain mediates interaction with KIDINS220 By similarity. The extracellular domain mediates interaction with NGFR By similarity.
Post-translational modification	Ligand-mediated autophosphorylation. Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-496 mediates interaction and phosphorylation of SHC1. N-glycosylated Probable. Isoform TrkA-I is N-glycosylated. Ref.18 Ref.23 Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor By similarity.
Involvement in disease	Congenital insensitivity to pain with anhidrosis (CIPA) [MIM:256800]: Characterized by a congenital insensitivity to pain, anhidrosis (absence of sweating), absence of reaction to noxious stimuli, self-mutilating behavior, and mental retardation. This rare autosomal recessive disorder is also known as congenital sensory neuropathy with anhidrosis or hereditary sensory and autonomic neuropathy type IV or familial dysautonomia type II. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.26 Ref.28 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells. Note: The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving NTRK1 are found in thyroid papillary carcinomas. Translocation t(1;3)(q21;q11) with TFG generates the TRKT3 (TRK-T3) transcript by fusing TFG to the 3'-end of NTRK1; a rearrangement with TPM3 generates the TRK transcript by fusing TPM3 to the 3'-end of NTRK1; an intrachromosomal rearrangement that links the protein kinase domain of NTRK1 to the 5'-end of the TPR gene forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting with antibodies against the C-terminus of the NTRK1 protein.
Miscellaneous	Trk also stands for tropomyosin-related kinase since it was first isolated as an oncogenic protein which was the result of a fusion between the tropomyosin gene TPM3 and NTRK1.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 2 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 protein kinase domain.
Sequence caution	The sequence CAA27243.1 differs from that shown. Reason: Erroneous termination at position 786. Translated as Gln. The sequence CAA27243.1 differs from that shown. Reason: Frameshift at position 769. The sequence CAA27243.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence CAA29888.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence CAA44719.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence CAA59936.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Proto-oncogene
Domain	Immunoglobulin domain Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara Ras protein signal transduction Traceable author statement. Source: Reactome Sertoli cell development Inferred from electronic annotation. Source: Compara activation of MAPKK activity Traceable author statement. Source: Reactome activation of adenylate cyclase activity Traceable author statement. Source: Reactome activation of phospholipase C activity Traceable author statement. Source: Reactome aging Inferred from electronic annotation. Source: Compara axon guidance Inferred from electronic annotation. Source: Compara axonogenesis involved in innervation Inferred from sequence or structural similarity. Source: UniProtKB cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to nicotine Inferred from electronic annotation. Source: Compara detection of mechanical stimulus involved in sensory perception of pain Inferred from electronic annotation. Source: Compara detection of temperature stimulus involved in sensory perception of pain Inferred from electronic annotation. Source: Compara developmental programmed cell death Inferred from sequence or structural similarity. Source: UniProtKB learning or memory Inferred from electronic annotation. Source: Compara mechanoreceptor differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from direct assay Ref.18. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB olfactory nerve development Inferred from electronic annotation. Source: Compara phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of ERK1 and ERK2 cascade Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of Ras GTPase activity Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of Ras protein signal transduction Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of neuron projection development Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of programmed cell death Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from direct assay Ref.18. Source: UniProtKB response to activity Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to hydrostatic pressure Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to radiation Inferred from electronic annotation. Source: Compara sympathetic nervous system development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara cytoplasmic vesicle Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Traceable author statement. Source: Reactome integral to plasma membrane Inferred from direct assay Ref.18. Source: UniProtKB neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nerve growth factor binding Inferred from direct assay Ref.18 Ref.23. Source: UniProtKB nerve growth factor receptor activity Inferred from direct assay Ref.18. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.23. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from direct assay Ref.18. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] Note: TrkA-I and TrkA-II isoforms have similar biological properties but are differentially expressed.

Isoform TrkA-II (identifier: P04629-1) Also known as: TrkAII; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.

Isoform TrkA-I (identifier: P04629-2) Also known as: TrkAI; The sequence of this isoform differs from the canonical sequence as follows: 393-398: Missing.
Note: Has enhanced responsiveness to NTF3 neurotrophin.

Isoform 3 (identifier: P04629-3) The sequence of this isoform differs from the canonical sequence as follows: 1-71: MLRGGRRGQL...LPGAENLTEL → MKEAALICLA...SRCTNLLAAS 393-398: Missing.

Isoform TrkA-III (identifier: P04629-4) Also known as: TrkAIII; The sequence of this isoform differs from the canonical sequence as follows: 192-284: GVPTLKVQVP...EVSVQVNVSF → V 393-398: Missing.
Note: Constitutively active. Does not bind NGF and does not interact with GRB2 and FRS2.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Potential

Chain

33 – 796

764

High affinity nerve growth factor receptor

PRO_0000016724

Regions

Topological domain

33 – 423

391

Extracellular Potential

Transmembrane

424 – 439

16

Helical; Potential

Topological domain

440 – 796

357

Cytoplasmic Potential

Repeat

90 – 113

24

LRR 1

Repeat

116 – 137

22

LRR 2

Domain

148 – 193

46

LRRCT

Domain

194 – 283

90

Ig-like C2-type 1

Domain

299 – 365

67

Ig-like C2-type 2

Domain

510 – 781

272

Protein kinase

Nucleotide binding

516 – 524

9

ATP By similarity

Region

469 – 490

22

Interaction with SQSTM1 By similarity

Sites

Active site

650

1

Proton acceptor By similarity

Binding site

544

1

ATP By similarity

Site

398 – 399

2

Breakpoint for translocation to form TRK and TRK-T3

Site

486

1

Breakpoint for translocation to form TRK-T1

Site

496

1

Interaction with SHC1

Site

791

1

Interaction with PLCG1

Amino acid modifications

Modified residue

496

1

Phosphotyrosine; by autocatalysis Ref.16 Ref.18

Modified residue

676

1

Phosphotyrosine; by autocatalysis

Modified residue

680

1

Phosphotyrosine; by autocatalysis Ref.18

Modified residue

681

1

Phosphotyrosine; by autocatalysis Ref.18

Modified residue

791

1

Phosphotyrosine; by autocatalysis Ref.15 Ref.16 Ref.18

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

95

1

N-linked (GlcNAc...) Ref.23

Glycosylation

121

1

N-linked (GlcNAc...) Ref.23

Glycosylation

188

1

N-linked (GlcNAc...) Ref.23

Glycosylation

202

1

N-linked (GlcNAc...) Potential

Glycosylation

253

1

N-linked (GlcNAc...) Potential

Glycosylation

262

1

N-linked (GlcNAc...) Ref.23

Glycosylation

281

1

N-linked (GlcNAc...) Ref.23

Glycosylation

318

1

N-linked (GlcNAc...) Potential

Glycosylation

323

1

N-linked (GlcNAc...) Potential

Glycosylation

338

1

N-linked (GlcNAc...) Potential

Glycosylation

358

1

N-linked (GlcNAc...) Ref.23

Glycosylation

401

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Natural variations

Alternative sequence

1 – 71

71

MLRGG…NLTEL → MKEAALICLAPSVPPILTVK SWDTMQLRAARSRCTNLLAA S in isoform 3.

VSP_041905

Alternative sequence

192 – 284

93

GVPTL…VNVSF → V in isoform TrkA-III.

VSP_042152

Alternative sequence

393 – 398

6

Missing in isoform TrkA-I, isoform 3 and isoform TrkA-III.

VSP_002899

Natural variant

6

1

R → W. Ref.37

VAR_068480

Natural variant

18

1

G → E.
Corresponds to variant rs1007211 [ dbSNP | Ensembl ].

VAR_049714

Natural variant

80

1

Q → R. Ref.36
Corresponds to variant rs55891455 [ dbSNP | Ensembl ].

VAR_041461

Natural variant

85

1

R → S. Ref.26 Ref.35

VAR_009623

Natural variant

93

1

L → P in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells. Ref.32 Ref.35

VAR_009624

Natural variant

107

1

A → V in an ovarian serous carcinoma sample; somatic mutation. Ref.36

VAR_041462

Natural variant

213

1

L → P in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells. Ref.26 Ref.35

VAR_009625

Natural variant

237

1

T → M. Ref.36
Corresponds to variant rs55909005 [ dbSNP | Ensembl ].

VAR_041463

Natural variant

238

1

V → G. Ref.36
Corresponds to variant rs56000394 [ dbSNP | Ensembl ].

VAR_041464

Natural variant

260

1

R → G. Ref.36
Corresponds to variant rs35116695 [ dbSNP | Ensembl ].

VAR_041465

Natural variant

359

1

Y → C in CIPA. Ref.34

VAR_068481

Natural variant

444

1

R → Q. Ref.36
Corresponds to variant rs56320207 [ dbSNP | Ensembl ].

VAR_041466

Natural variant

452

1

R → C. Ref.36
Corresponds to variant rs34900547 [ dbSNP | Ensembl ].

VAR_041467

Natural variant

492

1

E → K in CIPA. Ref.37

VAR_068482

Natural variant

522

1

G → R in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells. Ref.32 Ref.35

VAR_009626

Natural variant

566

1

M → T. Ref.36
Corresponds to variant rs55892037 [ dbSNP | Ensembl ].

VAR_041468

Natural variant

577

1

G → R in CIPA; loss of function; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells. Ref.24 Ref.32 Ref.33 Ref.35

VAR_004103

Natural variant

587

1

M → V in CIPA. Ref.28

VAR_009627

Natural variant

604

1

H → Y. Ref.26 Ref.27 Ref.29 Ref.34 Ref.35 Ref.36
Corresponds to variant rs6336 [ dbSNP | Ensembl ].

VAR_009628

Natural variant

613

1

G → V. Ref.26 Ref.27 Ref.29 Ref.31 Ref.34 Ref.35 Ref.36
Corresponds to variant rs6339 [ dbSNP | Ensembl ].

VAR_009629

Natural variant

649

1

R → W in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells. Ref.26 Ref.35

VAR_009630

Natural variant

654

1

R → C in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells. Ref.32 Ref.35 Ref.37

VAR_009631

Natural variant

674

1

D → Y in CIPA; unknown pathological significance; might impair the function of the enzyme without compromising autophosphorylation. Ref.32 Ref.35

VAR_009632

Natural variant

695

1

P → L in CIPA. Ref.31

VAR_009633

Natural variant

714

1

G → S in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells. Ref.26 Ref.35

VAR_009634

Natural variant

780

1

R → P in CIPA; loss of function. Ref.25

VAR_009635

Natural variant

780

1

R → Q. Ref.27 Ref.36
Corresponds to variant rs35669708 [ dbSNP | Ensembl ].

VAR_009636

Natural variant

790

1

V → I. Ref.36
Corresponds to variant rs55948542 [ dbSNP | Ensembl ].

VAR_041469

Experimental info

Mutagenesis

496

1

Y → F: Loss of interaction with SHC1 and altered phosphorylation of SHC1. Altered neurite outgrowth and altered activation of the MAPK pathway; when associated with F-791. Ref.16

Mutagenesis

544

1

K → N: Loss of kinase activity. Ref.16

Mutagenesis

791

1

Y → F: Loss of interaction with PLCG1 and altered phosphorylation of PLCG1. Altered neurite outgrowth and altered activation of the MAPK pathway; when associated with F-496. Ref.15 Ref.16

Sequence conflict

263

1

V → L in AAA36770. Ref.1

Sequence conflict

300

1

C → S in AAA36770. Ref.1

Sequence conflict

529

1

C → S in CAA59936. Ref.10

Secondary structure

1

.

796

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform TrkA-II (TrkAII) [UniParc]. Last modified May 2, 2006. Version 4. Checksum: 6C15C721E336B601 Show »	FASTA	796	87,497
10 20 30 40 50 60 MLRGGRRGQL GWHSWAAGPG SLLAWLILAS AGAAPCPDAC CPHGSSGLRC TRDGALDSLH 70 80 90 100 110 120 HLPGAENLTE LYIENQQHLQ HLELRDLRGL GELRNLTIVK SGLRFVAPDA FHFTPRLSRL 130 140 150 160 170 180 NLSFNALESL SWKTVQGLSL QELVLSGNPL HCSCALRWLQ RWEEEGLGGV PEQKLQCHGQ 190 200 210 220 230 240 GPLAHMPNAS CGVPTLKVQV PNASVDVGDD VLLRCQVEGR GLEQAGWILT ELEQSATVMK 250 260 270 280 290 300 SGGLPSLGLT LANVTSDLNR KNVTCWAEND VGRAEVSVQV NVSFPASVQL HTAVEMHHWC 310 320 330 340 350 360 IPFSVDGQPA PSLRWLFNGS VLNETSFIFT EFLEPAANET VRHGCLRLNQ PTHVNNGNYT 370 380 390 400 410 420 LLAANPFGQA SASIMAAFMD NPFEFNPEDP IPVSFSPVDT NSTSGDPVEK KDETPFGVSV 430 440 450 460 470 480 AVGLAVFACL FLSTLLLVLN KCGRRNKFGI NRPAVLAPED GLAMSLHFMT LGGSSLSPTE 490 500 510 520 530 540 GKGSGLQGHI IENPQYFSDA CVHHIKRRDI VLKWELGEGA FGKVFLAECH NLLPEQDKML 550 560 570 580 590 600 VAVKALKEAS ESARQDFQRE AELLTMLQHQ HIVRFFGVCT EGRPLLMVFE YMRHGDLNRF 610 620 630 640 650 660 LRSHGPDAKL LAGGEDVAPG PLGLGQLLAV ASQVAAGMVY LAGLHFVHRD LATRNCLVGQ 670 680 690 700 710 720 GLVVKIGDFG MSRDIYSTDY YRVGGRTMLP IRWMPPESIL YRKFTTESDV WSFGVVLWEI 730 740 750 760 770 780 FTYGKQPWYQ LSNTEAIDCI TQGRELERPR ACPPEVYAIM RGCWQREPQQ RHSIKDVHAR 790 LQALAQAPPV YLDVLG « Hide
Isoform TrkA-I (TrkAI) [UniParc]. Checksum: 25F05BADA8A2A50C Show »	FASTA	790	86,880
10 20 30 40 50 60 MLRGGRRGQL GWHSWAAGPG SLLAWLILAS AGAAPCPDAC CPHGSSGLRC TRDGALDSLH 70 80 90 100 110 120 HLPGAENLTE LYIENQQHLQ HLELRDLRGL GELRNLTIVK SGLRFVAPDA FHFTPRLSRL 130 140 150 160 170 180 NLSFNALESL SWKTVQGLSL QELVLSGNPL HCSCALRWLQ RWEEEGLGGV PEQKLQCHGQ 190 200 210 220 230 240 GPLAHMPNAS CGVPTLKVQV PNASVDVGDD VLLRCQVEGR GLEQAGWILT ELEQSATVMK 250 260 270 280 290 300 SGGLPSLGLT LANVTSDLNR KNVTCWAEND VGRAEVSVQV NVSFPASVQL HTAVEMHHWC 310 320 330 340 350 360 IPFSVDGQPA PSLRWLFNGS VLNETSFIFT EFLEPAANET VRHGCLRLNQ PTHVNNGNYT 370 380 390 400 410 420 LLAANPFGQA SASIMAAFMD NPFEFNPEDP IPDTNSTSGD PVEKKDETPF GVSVAVGLAV 430 440 450 460 470 480 FACLFLSTLL LVLNKCGRRN KFGINRPAVL APEDGLAMSL HFMTLGGSSL SPTEGKGSGL 490 500 510 520 530 540 QGHIIENPQY FSDACVHHIK RRDIVLKWEL GEGAFGKVFL AECHNLLPEQ DKMLVAVKAL 550 560 570 580 590 600 KEASESARQD FQREAELLTM LQHQHIVRFF GVCTEGRPLL MVFEYMRHGD LNRFLRSHGP 610 620 630 640 650 660 DAKLLAGGED VAPGPLGLGQ LLAVASQVAA GMVYLAGLHF VHRDLATRNC LVGQGLVVKI 670 680 690 700 710 720 GDFGMSRDIY STDYYRVGGR TMLPIRWMPP ESILYRKFTT ESDVWSFGVV LWEIFTYGKQ 730 740 750 760 770 780 PWYQLSNTEA IDCITQGREL ERPRACPPEV YAIMRGCWQR EPQQRHSIKD VHARLQALAQ 790 APPVYLDVLG « Hide
Isoform 3 [UniParc]. Checksum: 2452CA9C211243C9 Show »	FASTA	760	83,993
10 20 30 40 50 60 MKEAALICLA PSVPPILTVK SWDTMQLRAA RSRCTNLLAA SYIENQQHLQ HLELRDLRGL 70 80 90 100 110 120 GELRNLTIVK SGLRFVAPDA FHFTPRLSRL NLSFNALESL SWKTVQGLSL QELVLSGNPL 130 140 150 160 170 180 HCSCALRWLQ RWEEEGLGGV PEQKLQCHGQ GPLAHMPNAS CGVPTLKVQV PNASVDVGDD 190 200 210 220 230 240 VLLRCQVEGR GLEQAGWILT ELEQSATVMK SGGLPSLGLT LANVTSDLNR KNVTCWAEND 250 260 270 280 290 300 VGRAEVSVQV NVSFPASVQL HTAVEMHHWC IPFSVDGQPA PSLRWLFNGS VLNETSFIFT 310 320 330 340 350 360 EFLEPAANET VRHGCLRLNQ PTHVNNGNYT LLAANPFGQA SASIMAAFMD NPFEFNPEDP 370 380 390 400 410 420 IPDTNSTSGD PVEKKDETPF GVSVAVGLAV FACLFLSTLL LVLNKCGRRN KFGINRPAVL 430 440 450 460 470 480 APEDGLAMSL HFMTLGGSSL SPTEGKGSGL QGHIIENPQY FSDACVHHIK RRDIVLKWEL 490 500 510 520 530 540 GEGAFGKVFL AECHNLLPEQ DKMLVAVKAL KEASESARQD FQREAELLTM LQHQHIVRFF 550 560 570 580 590 600 GVCTEGRPLL MVFEYMRHGD LNRFLRSHGP DAKLLAGGED VAPGPLGLGQ LLAVASQVAA 610 620 630 640 650 660 GMVYLAGLHF VHRDLATRNC LVGQGLVVKI GDFGMSRDIY STDYYRVGGR TMLPIRWMPP 670 680 690 700 710 720 ESILYRKFTT ESDVWSFGVV LWEIFTYGKQ PWYQLSNTEA IDCITQGREL ERPRACPPEV 730 740 750 760 YAIMRGCWQR EPQQRHSIKD VHARLQALAQ APPVYLDVLG « Hide
Isoform TrkA-III (TrkAIII) [UniParc]. Checksum: 580555F90386A5A7 Show »	FASTA	698	77,145
10 20 30 40 50 60 MLRGGRRGQL GWHSWAAGPG SLLAWLILAS AGAAPCPDAC CPHGSSGLRC TRDGALDSLH 70 80 90 100 110 120 HLPGAENLTE LYIENQQHLQ HLELRDLRGL GELRNLTIVK SGLRFVAPDA FHFTPRLSRL 130 140 150 160 170 180 NLSFNALESL SWKTVQGLSL QELVLSGNPL HCSCALRWLQ RWEEEGLGGV PEQKLQCHGQ 190 200 210 220 230 240 GPLAHMPNAS CVPASVQLHT AVEMHHWCIP FSVDGQPAPS LRWLFNGSVL NETSFIFTEF 250 260 270 280 290 300 LEPAANETVR HGCLRLNQPT HVNNGNYTLL AANPFGQASA SIMAAFMDNP FEFNPEDPIP 310 320 330 340 350 360 DTNSTSGDPV EKKDETPFGV SVAVGLAVFA CLFLSTLLLV LNKCGRRNKF GINRPAVLAP 370 380 390 400 410 420 EDGLAMSLHF MTLGGSSLSP TEGKGSGLQG HIIENPQYFS DACVHHIKRR DIVLKWELGE 430 440 450 460 470 480 GAFGKVFLAE CHNLLPEQDK MLVAVKALKE ASESARQDFQ REAELLTMLQ HQHIVRFFGV 490 500 510 520 530 540 CTEGRPLLMV FEYMRHGDLN RFLRSHGPDA KLLAGGEDVA PGPLGLGQLL AVASQVAAGM 550 560 570 580 590 600 VYLAGLHFVH RDLATRNCLV GQGLVVKIGD FGMSRDIYST DYYRVGGRTM LPIRWMPPES 610 620 630 640 650 660 ILYRKFTTES DVWSFGVVLW EIFTYGKQPW YQLSNTEAID CITQGRELER PRACPPEVYA 670 680 690 IMRGCWQREP QQRHSIKDVH ARLQALAQAP PVYLDVLG « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of the human trk proto-oncogene." Martin-Zanca D., Oskam R., Mitra G., Copeland T.D., Barbacid M. Mol. Cell. Biol. 9:24-33(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKA-I). Tissue: Colon.
[2]	"Human trks: molecular cloning, tissue distribution, and expression of extracellular domain immunoadhesins." Shelton D.L., Sutherland J., Gripp J., Camerato T., Armanini M.P., Phillips H.S., Carroll K., Spencer S.D., Levinson A.D. J. Neurosci. 15:477-491(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Structure and organization of the human TRKA gene encoding a high affinity receptor for nerve growth factor." Indo Y., Mardy S., Tsuruta M., Karim M.A., Matsuda I. Jpn. J. Hum. Genet. 42:343-351(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKA-II), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175 (ISOFORM 3). Tissue: Uterus.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS TRKA-I AND TRKA-II). Tissue: Brain.
[7]	"Methylation adjacent to negatively regulating AP-1 site reactivates TrkA gene expression during cancer progression." Fujimoto M., Kitazawa R., Maeda S., Kitazawa S. Oncogene 24:5108-5118(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
[8]	"A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences." Martin-Zanca D., Hughes S.H., Barbacid M. Nature 319:743-748(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 399-796, CHROMOSOMAL TRANSLOCATION WITH TPM3.
[9]	"Activation of the receptor kinase domain of the trk oncogene by recombination with two different cellular sequences." Kozma S.C., Redmond S.M.S., Saurer S.M., Groner B., Hynes N.E. EMBO J. 7:147-154(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 399-796.
[10]	"The DNA rearrangement that generates the TRK-T3 oncogene involves a novel gene on chromosome 3 whose product has a potential coiled-coil domain." Greco A., Mariani C., Miranda C., Lupas A., Pagliardini S., Pomati M., Pierotti M.A. Mol. Cell. Biol. 15:6118-6127(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 399-796, CHROMOSOMAL TRANSLOCATION WITH TFG.
[11]	"TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in human papillary thyroid carcinomas." Greco A., Pierotti M.A., Bongarzone I., Pagliardini S., Lanzi C., Della Porta G. Oncogene 7:237-242(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 486-796, CHROMOSOMAL REARRANGEMENT WITH TPR.
[12]	"High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor." Hempstead B.L., Martin-Zanca D., Kaplan D.R., Parada L.F., Chao M.V. Nature 350:678-683(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS RECEPTOR FOR NGF.
[13]	"The trk proto-oncogene encodes a receptor for nerve growth factor." Klein R., Jing S., Nanduri V., O'Rourke E., Barbacid M. Cell 65:189-197(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NGF SIGNALING, IDENTIFICATION AS THE HIGH AFFINITY NGF RECEPTOR.
[14]	"Tissue-specific alternative splicing generates two isoforms of the trkA receptor." Barker P.A., Lomen-Hoerth C., Gensch E.M., Meakin S.O., Glass D.J., Shooter E.M. J. Biol. Chem. 268:15150-15157(1993) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS TRKA-I AND TRKA-II), FUNCTION IN CELL SURVIVAL, NGF-BINDING, PHOSPHORYLATION, TISSUE SPECIFICITY.
[15]	"A Trk nerve growth factor (NGF) receptor point mutation affecting interaction with phospholipase C-gamma 1 abolishes NGF-promoted peripherin induction but not neurite outgrowth." Loeb D.M., Stephens R.M., Copeland T.D., Kaplan D.R., Greene L.A. J. Biol. Chem. 269:8901-8910(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-791, INTERACTION WITH PLCG1, MUTAGENESIS OF TYR-791.
[16]	"Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses." Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., Kaplan D.R. Neuron 12:691-705(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEURONAL DIFFERENTIATION, FUNCTION IN PHOSPHORYLATION OF SHC1 AND PLCG1, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-496; LYS-544 AND TYR-791, PHOSPHORYLATION AT TYR-496 AND TYR-791.
[17]	"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor." Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J. J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, INTERACTION WITH SQSTM1.
[18]	"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma." Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R. Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEURONAL CELL PROLIFERATION AND DIFFERENTIATION, FUNCTION IN SIGNALING CASCADE ACTIVATION, NGF-BINDING, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM TRKA-III), CHARACTERIZATION OF ISOFORM TRKA-III, PHOSPHORYLATION AT TYR-496; TYR-680; TYR-681 AND TYR-791, INTERACTION WITH FRS2; GRB2; PIK3R1; PLCG1; SHC1, GLYCOSYLATION, TISSUE SPECIFICITY, INDUCTION BY HYPOXIA.
[19]	"Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling." Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S., Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L., Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A. Nat. Neurosci. 14:54-61(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SORT1, ENZYME REGULATION.
[20]	"Structure and ligand recognition of the phosphotyrosine binding domain of Shc." Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M., Meadows R.P., Sattler M., Harlan J.E., Wade W.S., Burakoff S.J., Fesik S.W. Nature 378:584-592(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 489-500.
[21]	"Crystal structures of the neurotrophin-binding domain of TrkA, TrkB and TrkC." Ultsch M.H., Wiesmann C., Simmons L.C., Henrich J., Yang M., Reilly D., Bass S.H., de Vos A.M. J. Mol. Biol. 290:149-159(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 278-386.
[22]	"Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor." Wiesmann C., Ultsch M.H., Bass S.H., de Vos A.M. Nature 401:184-188(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 282-382.
[23]	"Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors." Wehrman T., He X., Raab B., Dukipatti A., Blau H., Garcia K.C. Neuron 53:25-38(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 36-382 IN COMPLEX WITH NGF, HOMODIMERIZATION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-95; ASN-121; ASN-188; ASN-262; ASN-281 AND ASN-358.
[24]	"Mutations in the TRKA/NGF receptor gene in patients with congenital insensitivity to pain with anhidrosis." Indo Y., Tsuruta M., Hayashida Y., Karim M.A., Ohta K., Kawano T., Mitsubuchi H., Tonoki H., Awaya Y., Matsuda I. Nat. Genet. 13:485-488(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA ARG-577.
[25]	"A novel NTRK1 mutation associated with congenital insensitivity to pain with anhidrosis." Greco A., Villa R., Tubino B., Romano L., Penso D., Pierotti M.A. Am. J. Hum. Genet. 64:1207-1210(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA PRO-780.
[26]	"Congenital insensitivity to pain with anhidrosis: novel mutations in the TRKA (NTRK1) gene encoding a high-affinity receptor for nerve growth factor." Mardy S., Miura Y., Endo F., Matsuda I., Sztriha L., Frossard P., Moosa A., Ismail E.A.R., Macaya A., Andria G., Toscano E., Gibson W., Graham G.E., Indo Y. Am. J. Hum. Genet. 64:1570-1579(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CIPA PRO-213; TRP-649 AND SER-714, VARIANTS SER-85; TYR-604 AND VAL-613.
[27]	"Mutation analysis reveals novel sequence variants in NTRK1 in sporadic human medullary thyroid carcinoma." Gimm O., Greco A., Hoang-Vu C., Dralle H., Pierotti M.A., Eng C. J. Clin. Endocrinol. Metab. 84:2784-2787(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TYR-604; VAL-613 AND GLN-780.
[28]	"A novel point mutation affecting the tyrosine kinase domain of the TRKA gene in a family with congenital insensitivity to pain with anhidrosis." Yotsumoto S., Setoyama M., Hozumi H., Mizoguchi S., Fukumaru S., Kobayashi K., Saheki T., Kanzaki T. J. Invest. Dermatol. 112:810-814(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA VAL-587.
[29]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TYR-604 AND VAL-613.
[30]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[31]	"Congenital insensitivity to pain with anhidrosis (CIPA) in Israeli-Bedouins: genetic heterogeneity, novel mutations in the TRKA/NGF receptor gene, clinical findings, and results of nerve conduction studies." Shatzky S., Moses S., Levy J., Pinsk V., Hershkovitz E., Herzog L., Shorer Z., Luder A., Parvari R. Am. J. Med. Genet. 92:353-360(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA LEU-695, VARIANT VAL-613. Tissue: Peripheral blood.
[32]	"Mutation and polymorphism analysis of the TRKA (NTRK1) gene encoding a high-affinity receptor for nerve growth factor in congenital insensitivity to pain with anhidrosis (CIPA) families." Miura Y., Mardy S., Awaya Y., Nihei K., Endo F., Matsuda I., Indo Y. Hum. Genet. 106:116-124(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CIPA PRO-93; ARG-522; ARG-577; CYS-654 AND TYR-674.
[33]	"The Gly571Arg mutation, associated with the autonomic and sensory disorder congenital insensitivity to pain with anhidrosis, causes the inactivation of the NTRK1/nerve growth factor receptor." Greco A., Villa R., Fusetti L., Orlandi R., Pierotti M.A. J. Cell. Physiol. 182:127-133(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA ARG-577.
[34]	"A novel TRK A (NTRK1) mutation associated with hereditary sensory and autonomic neuropathy type V." Houlden H., King R.H., Hashemi-Nejad A., Wood N.W., Mathias C.J., Reilly M., Thomas P.K. Ann. Neurol. 49:521-525(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIPA CYS-359, VARIANTS TYR-604 AND VAL-613.
[35]	"Congenital insensitivity to pain with anhidrosis (CIPA): effect of TRKA (NTRK1) missense mutations on autophosphorylation of the receptor tyrosine kinase for nerve growth factor." Mardy S., Miura Y., Endo F., Matsuda I., Indo Y. Hum. Mol. Genet. 10:179-188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS CIPA PRO-93; PRO-213; ARG-522; ARG-577; TRP-649; CYS-654 AND SER-714, CHARACTERIZATION OF VARIANTS SER-85; TYR-604; VAL-613 AND TYR-674.
[36]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-80; VAL-107; MET-237; GLY-238; GLY-260; GLN-444; CYS-452; THR-566; TYR-604; VAL-613; GLN-780 AND ILE-790.
[37]	"Frequency of mutations in the genes associated with hereditary sensory and autonomic neuropathy in a UK cohort." Davidson G.L., Murphy S.M., Polke J.M., Laura M., Salih M.A., Muntoni F., Blake J., Brandner S., Davies N., Horvath R., Price S., Donaghy M., Roberts M., Foulds N., Ramdharry G., Soler D., Lunn M.P., Manji H. , Davis M.B., Houlden H., Reilly M.M. J. Neurol. 259:1673-1685(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CIPA LYS-492 AND CYS-654, VARIANT TRP-6.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23102 mRNA. Translation: AAA36770.1.
AB019488 Genomic DNA. Translation: BAA34355.1.
AK312704 mRNA. Translation: BAG35582.1.
DB265639 mRNA. No translation available.
AL158169 Genomic DNA. Translation: CAH70010.1.
BC062580 mRNA. Translation: AAH62580.1.
BC136554 mRNA. Translation: AAI36555.1.
BC144239 mRNA. Translation: AAI44240.1.
AY321513 Genomic DNA. Translation: AAP88292.1.
X03541 mRNA. Translation: CAA27243.1. Sequence problems.
X06704 mRNA. Translation: CAA29888.1. Sequence problems.
X85960 mRNA. Translation: CAA59936.1. Sequence problems.
X62947 mRNA. Translation: CAA44719.1. Sequence problems.

IPI

IPI00025076.
IPI00514519.

PIR

TVHUTT. A30124.
S23741.

RefSeq

NP_001007793.1. NM_001007792.1.
NP_001012331.1. NM_001012331.1.
NP_002520.2. NM_002529.3.

UniGene

Hs.406293.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HE7	X-ray	2.00	A	285-413	[»]
1SHC	NMR	-	B	489-500	[»]
1WWA	X-ray	2.50	X/Y	278-386	[»]
1WWW	X-ray	2.20	X/Y	282-382	[»]
2IFG	X-ray	3.40	A/B	36-382	[»]
4AOJ	X-ray	2.75	A/B/C	473-796	[»]
4F0I	X-ray	2.30	A/B	498-796	[»]
4GT5	X-ray	2.40	A	498-796	[»]

ProteinModelPortal

P04629.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1060N.
DIP-5714N.

IntAct

P04629. 9 interactions.

MINT

MINT-124106.

PTM databases

PhosphoSite

P04629.

Polymorphism databases

DMDM

94730402.

Proteomic databases

PaxDb

P04629.

PRIDE

P04629.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368196; ENSP00000357179; ENSG00000198400.
ENST00000392302; ENSP00000376120; ENSG00000198400.
ENST00000524377; ENSP00000431418; ENSG00000198400.

GeneID

4914.

KEGG

hsa:4914.

UCSC

uc001fqh.1. human.
uc001fqi.1. human.

Organism-specific databases

CTD

4914.

GeneCards

GC01P156786.

HGNC

HGNC:8031. NTRK1.

HPA

CAB004606.

MIM

164970. gene.
188550. phenotype.
191315. gene.
256800. phenotype.

neXtProt

NX_P04629.

Orphanet

99361. Familial medullary thyroid carcinoma.
642. Hereditary sensory and autonomic neuropathy type 4.
64752. Hereditary sensory and autonomic neuropathy type 5.

PharmGKB

PA31817.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG056735.

InParanoid

P04629.

KO

K03176.

OMA

CPDACCP.

PhylomeDB

P04629.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P04629.

Bgee

P04629.

Genevestigator

P04629.

GermOnline

ENSG00000198400. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR020461. Tyr_kinase_neurotrophic_rcpt_1.
IPR020777. Tyr_kinase_NGF_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR01939. NTKRECEPTOR.
PR01940. NTKRECEPTOR1.
PR00109. TYRKINASE.

SMART

SM00409. IG. 1 hit.
SM00082. LRRCT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04629.

ChEMBL

CHEMBL2815.

ChiTaRS

NTRK1. human.

DrugBank

DB00619. Imatinib.

EvolutionaryTrace

P04629.

GenomeRNAi

4914.

NextBio

18907.

SOURCE

Search...

Entry information

Entry name

NTRK1_HUMAN

Accession

Primary (citable) accession number: P04629
Secondary accession number(s): B2R6T5

Q9UIU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 181 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.