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P04629 (NTRK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 192. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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 By similarity. Interacts with RAPGEF2; the interaction is strengthened after NGF stimulation 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. Late 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. 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 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 processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainImmunoglobulin domain
Leucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

Ras protein signal transduction

Traceable author statement. Source: Reactome

Sertoli cell development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

axon guidance

Inferred from electronic annotation. Source: Ensembl

axonogenesis involved in innervation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nerve growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nicotine

Inferred from electronic annotation. Source: Ensembl

detection of mechanical stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

detection of temperature stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

developmental programmed cell death

Inferred from sequence or structural similarity. Source: UniProtKB

learning or memory

Inferred from electronic annotation. Source: Ensembl

mechanoreceptor differentiation

Inferred from electronic annotation. Source: Ensembl

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

neurotrophin TRK receptor signaling pathway

Inferred from direct assay Ref.18. Source: UniProtKB

olfactory nerve development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.18. Source: GOC

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: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.18. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.18. Source: UniProtKB

response to activity

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hydrostatic pressure

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

sympathetic nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Traceable author statement. Source: Reactome

integral component of plasma membrane

Inferred from direct assay Ref.18. Source: UniProtKB

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nerve growth factor binding

Inferred from direct assay Ref.18Ref.23. Source: UniProtKB

nerve growth factor receptor activity

Inferred from direct assay Ref.18. Source: UniProtKB

neurotrophin binding

Traceable author statement Ref.3. Source: ProtInc

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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBLP226812EBI-1028226,EBI-518228
PirbQ8K4V62EBI-1028226,EBI-8602514From a different organism.
PTPN1P180312EBI-1028226,EBI-968788

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 796764High affinity nerve growth factor receptor
PRO_0000016724

Regions

Topological domain33 – 423391Extracellular Potential
Transmembrane424 – 43916Helical; Potential
Topological domain440 – 796357Cytoplasmic Potential
Repeat90 – 11324LRR 1
Repeat116 – 13722LRR 2
Domain148 – 19346LRRCT
Domain194 – 28390Ig-like C2-type 1
Domain299 – 36567Ig-like C2-type 2
Domain510 – 781272Protein kinase
Nucleotide binding516 – 5249ATP By similarity
Region469 – 49022Interaction with SQSTM1 By similarity

Sites

Active site6501Proton acceptor By similarity
Binding site5441ATP By similarity
Site398 – 3992Breakpoint for translocation to form TRK and TRK-T3
Site4861Breakpoint for translocation to form TRK-T1
Site4961Interaction with SHC1
Site7911Interaction with PLCG1

Amino acid modifications

Modified residue4961Phosphotyrosine; by autocatalysis Ref.16 Ref.18
Modified residue6761Phosphotyrosine; by autocatalysis
Modified residue6801Phosphotyrosine; by autocatalysis Ref.18
Modified residue6811Phosphotyrosine; by autocatalysis Ref.18
Modified residue7911Phosphotyrosine; by autocatalysis Ref.15 Ref.16 Ref.18
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Ref.23
Glycosylation1211N-linked (GlcNAc...) Ref.23
Glycosylation1881N-linked (GlcNAc...) Ref.23
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Ref.23
Glycosylation2811N-linked (GlcNAc...) Ref.23
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Ref.23
Glycosylation4011N-linked (GlcNAc...) Potential
Disulfide bond154 ↔ 191 Ref.23
Disulfide bond215 ↔ 265 Ref.23

Natural variations

Alternative sequence1 – 7171MLRGG…NLTEL → MKEAALICLAPSVPPILTVK SWDTMQLRAARSRCTNLLAA S in isoform 3.
VSP_041905
Alternative sequence192 – 28493GVPTL…VNVSF → V in isoform TrkA-III.
VSP_042152
Alternative sequence393 – 3986Missing in isoform TrkA-I, isoform 3 and isoform TrkA-III.
VSP_002899
Natural variant61R → W. Ref.37
VAR_068480
Natural variant181G → E.
Corresponds to variant rs1007211 [ dbSNP | Ensembl ].
VAR_049714
Natural variant801Q → R. Ref.36
Corresponds to variant rs55891455 [ dbSNP | Ensembl ].
VAR_041461
Natural variant851R → S. Ref.26 Ref.35
VAR_009623
Natural variant931L → P in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells. Ref.32 Ref.35
VAR_009624
Natural variant1071A → V in an ovarian serous carcinoma sample; somatic mutation. Ref.36
VAR_041462
Natural variant2131L → P in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells. Ref.26 Ref.35
VAR_009625
Natural variant2371T → M. Ref.36
Corresponds to variant rs55909005 [ dbSNP | Ensembl ].
VAR_041463
Natural variant2381V → G. Ref.36
Corresponds to variant rs56000394 [ dbSNP | Ensembl ].
VAR_041464
Natural variant2601R → G. Ref.36
Corresponds to variant rs35116695 [ dbSNP | Ensembl ].
VAR_041465
Natural variant3591Y → C in CIPA. Ref.34
VAR_068481
Natural variant4441R → Q. Ref.36
Corresponds to variant rs56320207 [ dbSNP | Ensembl ].
VAR_041466
Natural variant4521R → C. Ref.36
Corresponds to variant rs34900547 [ dbSNP | Ensembl ].
VAR_041467
Natural variant4921E → K in CIPA. Ref.37
VAR_068482
Natural variant5221G → 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 variant5661M → T. Ref.36
Corresponds to variant rs55892037 [ dbSNP | Ensembl ].
VAR_041468
Natural variant5771G → 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 variant5871M → V in CIPA. Ref.28
VAR_009627
Natural variant6041H → Y. Ref.26 Ref.27 Ref.29 Ref.34 Ref.35 Ref.36
Corresponds to variant rs6336 [ dbSNP | Ensembl ].
VAR_009628
Natural variant6131G → V. Ref.26 Ref.27 Ref.29 Ref.31 Ref.34 Ref.35 Ref.36
Corresponds to variant rs6339 [ dbSNP | Ensembl ].
VAR_009629
Natural variant6491R → 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 variant6541R → 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 variant6741D → Y in CIPA; unknown pathological significance; might impair the function of the enzyme without compromising autophosphorylation. Ref.32 Ref.35
VAR_009632
Natural variant6951P → L in CIPA. Ref.31
VAR_009633
Natural variant7141G → 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 variant7801R → P in CIPA; loss of function. Ref.25
Corresponds to variant rs35669708 [ dbSNP | Ensembl ].
VAR_009635
Natural variant7801R → Q. Ref.27 Ref.36
Corresponds to variant rs35669708 [ dbSNP | Ensembl ].
VAR_009636
Natural variant7901V → I. Ref.36
Corresponds to variant rs55948542 [ dbSNP | Ensembl ].
VAR_041469

Experimental info

Mutagenesis4961Y → 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
Mutagenesis5441K → N: Loss of kinase activity. Ref.16
Mutagenesis7911Y → 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 conflict2631V → L in AAA36770. Ref.1
Sequence conflict3001C → S in AAA36770. Ref.1
Sequence conflict5291C → S in CAA59936. Ref.10

Secondary structure

...................................................................................................................... 796
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform TrkA-II (TrkAII) [UniParc].

Last modified May 2, 2006. Version 4.
Checksum: 6C15C721E336B601

FASTA79687,497
        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 »

FASTA79086,880
Isoform 3 [UniParc].

Checksum: 2452CA9C211243C9
Show »

FASTA76083,993
Isoform TrkA-III (TrkAIII) [UniParc].

Checksum: 580555F90386A5A7
Show »

FASTA69877,145

References

« Hide '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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., 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. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., 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. expand/collapse author list , 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

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.
PIRTVHUTT. A30124.
S23741.
RefSeqNP_001007793.1. NM_001007792.1.
NP_001012331.1. NM_001012331.1.
NP_002520.2. NM_002529.3.
UniGeneHs.406293.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HE7X-ray2.00A285-413[»]
1SHCNMR-B489-500[»]
1WWAX-ray2.50X/Y278-386[»]
1WWWX-ray2.20X/Y282-382[»]
2IFGX-ray3.40A/B36-382[»]
4AOJX-ray2.75A/B/C473-796[»]
4F0IX-ray2.30A/B498-796[»]
4GT5X-ray2.40A498-796[»]
ProteinModelPortalP04629.
SMRP04629. Positions 36-382, 501-794.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110969. 33 interactions.
DIPDIP-1060N.
DIP-5714N.
IntActP04629. 16 interactions.
MINTMINT-124106.

Chemistry

BindingDBP04629.
ChEMBLCHEMBL2815.
DrugBankDB00619. Imatinib.
GuidetoPHARMACOLOGY1817.

PTM databases

PhosphoSiteP04629.

Polymorphism databases

DMDM94730402.

Proteomic databases

PaxDbP04629.
PRIDEP04629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368196; ENSP00000357179; ENSG00000198400. [P04629-2]
ENST00000392302; ENSP00000376120; ENSG00000198400. [P04629-3]
ENST00000524377; ENSP00000431418; ENSG00000198400. [P04629-1]
GeneID4914.
KEGGhsa:4914.
UCSCuc001fqf.1. human. [P04629-3]
uc001fqh.1. human. [P04629-1]
uc001fqi.1. human. [P04629-2]
uc009wsi.1. human. [P04629-4]

Organism-specific databases

CTD4914.
GeneCardsGC01P156786.
HGNCHGNC:8031. NTRK1.
HPACAB004606.
MIM164970. gene.
188550. phenotype.
191315. gene.
256800. phenotype.
neXtProtNX_P04629.
Orphanet99361. Familial medullary thyroid carcinoma.
642. Hereditary sensory and autonomic neuropathy type 4.
64752. Hereditary sensory and autonomic neuropathy type 5.
146. Papillary or follicular thyroid carcinoma.
PharmGKBPA31817.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG056735.
InParanoidP04629.
KOK03176.
OMAKNVTCWA.
OrthoDBEOG7GTT32.
PhylomeDBP04629.
TreeFamTF106465.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP04629.

Gene expression databases

ArrayExpressP04629.
BgeeP04629.
GenevestigatorP04629.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR01939. NTKRECEPTOR.
PR01940. NTKRECEPTOR1.
PR00109. TYRKINASE.
SMARTSM00409. IG. 1 hit.
SM00082. LRRCT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. 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]
ProtoNetSearch...

Other

ChiTaRSNTRK1. human.
EvolutionaryTraceP04629.
GenomeRNAi4914.
NextBio18907.
PROP04629.
SOURCESearch...

Entry information

Entry nameNTRK1_HUMAN
AccessionPrimary (citable) accession number: P04629
Secondary accession number(s): B2R6T5 expand/collapse secondary AC list , B7ZM34, P08119, Q15655, Q15656, Q5D056, Q5VZS2, Q7Z5C3, Q9UIU7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 192 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM