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P35739 (NTRK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
Slow nerve growth factor receptor
p140-TrkA
Short name=Trk-A
Gene names
Name:Ntrk1
Synonyms:Trk, Trka
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length799 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.14

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 By similarity. SH2D1A inhibits the autophosphorylation of the receptor, and alters the recruitment and activation of downstream effectors and signaling cascades. Regulated by NGFR By similarity. Ref.10

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 By similarity. Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a nerve growth factor (NGF)-dependent manner. Interacts with RAPGEF2; the interaction is strengthened after NGF stimulation. Interacts with SQSTM1; bridges NTRK1 to NGFR. Forms a ternary complex with NGFR and KIDINS220; this complex is affected by the expression levels of KIDINS220 and an increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts (phosphorylated upon activation by NGF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by NGF) with PLCG1; mediates PLCG1 phosphorylation and activation. Interacts (phosphorylated) with SH2B1 and SH2B2. Interacts with GRB2. Interacts with PIK3R1. Interacts with FRS2. Interacts with SORT1; may regulate NTRK1 anterograde axonal transport. Interacts with SH2D1A; regulates NTRK1. Interacts with NRADD. Interacts with RAB7A. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Early endosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. 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. Ref.7 Ref.12

Tissue specificity

Isoform Trka-IIis primarily expressed in neuronal cells; isoform Trka-Iis found in non-neuronal tissues.

Domain

The transmembrane domain mediates interaction with KIDINS220. Ref.7 Ref.8 Ref.9

The extracellular domain mediates interaction with NGFR. Ref.7 Ref.8 Ref.9

Post-translational modification

Ligand-mediated autophosphorylation. Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-499 mediates interaction and phosphorylation of SHC1.

N-glycosylated By similarity.

Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor By similarity.

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.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

Sertoli cell development

Inferred from mutant phenotype PubMed 18660385. Source: RGD

aging

Inferred from expression pattern PubMed 21059364. Source: RGD

axon guidance

Inferred from mutant phenotype PubMed 18344912. Source: RGD

axonogenesis involved in innervation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from direct assay PubMed 19029245. Source: MGI

cellular response to nerve growth factor stimulus

Inferred from direct assay Ref.12. Source: UniProtKB

cellular response to nicotine

Inferred from direct assay PubMed 16280603. Source: RGD

detection of mechanical stimulus involved in sensory perception of pain

Inferred from mutant phenotype PubMed 20351485. Source: RGD

detection of temperature stimulus involved in sensory perception of pain

Inferred from mutant phenotype PubMed 20351485. Source: RGD

developmental programmed cell death

Inferred from direct assay Ref.14. Source: UniProtKB

learning or memory

Inferred from mutant phenotype PubMed 18440710. Source: RGD

mechanoreceptor differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 21541365. Source: UniProtKB

negative regulation of neuron death

Inferred from direct assay PubMed 20943663. Source: RGD

nerve growth factor signaling pathway

Inferred from direct assay Ref.12. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

olfactory nerve development

Inferred from expression pattern PubMed 8778281. Source: RGD

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 19029245. Source: GOC

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Ras protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of programmed cell death

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 21550171. Source: RGD

protein autophosphorylation

Inferred from direct assay PubMed 19029245. Source: MGI

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to activity

Inferred from direct assay PubMed 19800940. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 21456016. Source: RGD

response to drug

Inferred from direct assay PubMed 20059802. Source: RGD

response to electrical stimulus

Inferred from direct assay PubMed 19596387. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 17316397. Source: RGD

response to hydrostatic pressure

Inferred from expression pattern PubMed 18817846. Source: RGD

response to nicotine

Inferred from direct assay PubMed 20056136. Source: RGD

response to nutrient levels

Inferred from direct assay PubMed 17582385. Source: RGD

response to radiation

Inferred from expression pattern PubMed 21431457. Source: RGD

sensory perception of pain

Inferred from mutant phenotype PubMed 17667845. Source: RGD

sympathetic nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

axon

Inferred from direct assay PubMed 11134589. Source: RGD

cell surface

Inferred from direct assay PubMed 19029245. Source: MGI

cytoplasmic vesicle

Inferred from direct assay PubMed 17625349. Source: RGD

dendrite

Inferred from direct assay PubMed 11134589. Source: RGD

early endosome

Inferred from direct assay Ref.12. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome

Inferred from direct assay Ref.12. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from direct assay PubMed 18395621. Source: RGD

plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

protein complex

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor binding

Inferred from physical interaction PubMed 19036963. Source: BHF-UCL

nerve growth factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

nerve growth factor receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin p75 receptor binding

Inferred from physical interaction PubMed 9753156. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay PubMed 19029245. Source: MGI

transmembrane receptor protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grb2P629946EBI-976667,EBI-401775

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Both isoforms have similar biological properties.
Isoform TrkA-II (identifier: P35739-1)

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.
Isoform TrkA-I (identifier: P35739-2)

The sequence of this isoform differs from the canonical sequence as follows:
     396-401: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 799767High affinity nerve growth factor receptor
PRO_0000016725

Regions

Topological domain33 – 418386Extracellular Potential
Transmembrane419 – 44224Helical; Potential
Topological domain443 – 799357Cytoplasmic Potential
Repeat90 – 11324LRR 1
Repeat116 – 13722LRR 2
Domain148 – 21972LRRCT
Domain196 – 28590Ig-like C2-type 1
Domain295 – 36874Ig-like C2-type 2
Domain513 – 784272Protein kinase
Nucleotide binding519 – 5279ATP By similarity
Region472 – 49322Interaction with SQSTM1

Sites

Active site6531Proton acceptor By similarity
Binding site5471ATP By similarity
Site4991Interaction with SHC1 By similarity
Site7941Interaction with PLCG1 By similarity

Amino acid modifications

Modified residue4991Phosphotyrosine; by autocatalysis By similarity
Modified residue6791Phosphotyrosine; by autocatalysis By similarity
Modified residue6831Phosphotyrosine; by autocatalysis By similarity
Modified residue6841Phosphotyrosine; by autocatalysis By similarity
Modified residue7941Phosphotyrosine; by autocatalysis By similarity
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Disulfide bond154 ↔ 193 By similarity
Disulfide bond217 ↔ 267 By similarity

Natural variations

Alternative sequence396 – 4016Missing in isoform TrkA-I.
VSP_002900

Experimental info

Mutagenesis5271V → D: Loss of kinase activity. Ref.4

Sequences

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

Last modified June 1, 1994. Version 1.
Checksum: D564E8801E8978F8

FASTA79987,868
        10         20         30         40         50         60 
MLRGQRHGQL GWHRPAAGLG GLVTSLMLAC ACAASCRETC CPVGPSGLRC TRAGTLNTLR 

        70         80         90        100        110        120 
GLRGAGNLTE LYVENQRDLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FHFTPRLSHL 

       130        140        150        160        170        180 
NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALLWLQ RWEQEDLCGV YTQKLQGSGS 

       190        200        210        220        230        240 
GDQFLPLGHN NSCGVPSVKI QMPNDSVEVG DDVFLQCQVE GQALQQADWI LTELEGTATM 

       250        260        270        280        290        300 
KKSGDLPSLG LTLVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGKAVEQHH 

       310        320        330        340        350        360 
WCIPFSVDGQ PAPSLRWFFN GSVLNETSFI FTQFLESALT NETMRHGCLR LNQPTHVNNG 

       370        380        390        400        410        420 
NYTLLAANPY GQAAASIMAA FMDNPFEFNP EDPIPVSFSP VDTNSTSRDP VEKKDETPFG 

       430        440        450        460        470        480 
VSVAVGLAVS AALFLSALLL VLNKCGQRSK FGINRPAVLA PEDGLAMSLH FMTLGGSSLS 

       490        500        510        520        530        540 
PTEGKGSGLQ GHIMENPQYF SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD 

       550        560        570        580        590        600 
KMLVAVKALK ETSENARQDF HREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL 

       610        620        630        640        650        660 
NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV HRDLATRNCL 

       670        680        690        700        710        720 
VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE SILYRKFSTE SDVWSFGVVL 

       730        740        750        760        770        780 
WEIFTYGKQP WYQLSNTEAI ECITQGRELE RPRACPPDVY AIMRGCWQRE PQQRLSMKDV 

       790 
HARLQALAQA PPSYLDVLG 

« Hide

Isoform TrkA-I [UniParc].

Checksum: A4A5D0B76B08655D
Show »

FASTA79387,252

References

[1]"The rat trk protooncogene product exhibits properties characteristic of the slow nerve growth factor receptor."
Meakin S.O., Suter U., Drinkwater C.C., Welcher A.A., Shooter E.M.
Proc. Natl. Acad. Sci. U.S.A. 89:2374-2378(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKA-II).
[2]"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).
[3]"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: INTERACTION WITH SHC1.
[4]"Identification and characterization of novel substrates of Trk receptors in developing neurons."
Qian X., Riccio A., Zhang Y., Ginty D.D.
Neuron 21:1017-1029(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLCG1; SHC1; SH2B1 AND SH2B2, MUTAGENESIS OF VAL-527.
[5]"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: INTERACTION WITH SQSTM1.
[6]"An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors."
Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.
J. Neurosci. 21:176-185(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIDINS220.
[7]"Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling."
Geetha T., Wooten M.W.
J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, DOMAIN.
[8]"A unique pathway for sustained neurotrophin signaling through an ankyrin-rich membrane-spanning protein."
Arevalo J.C., Yano H., Teng K.K., Chao M.V.
EMBO J. 23:2358-2368(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIDINS220, DOMAIN.
[9]"Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning protein."
Chang M.-S., Arevalo J.C., Chao M.V.
J. Neurosci. Res. 78:186-192(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGFR AND KIDINS220, DOMAIN.
[10]"SLAM-associated protein as a potential negative regulator in Trk signaling."
Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.
J. Biol. Chem. 280:41744-41752(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH SH2D1A.
[11]"The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor TrkA."
Saxena S., Bucci C., Weis J., Kruttgen A.
J. Neurosci. 25:10930-10940(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB7A.
[12]"Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes, leading to sustained activation of Rap1 and ERK and neurite outgrowth."
Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.
J. Cell Biol. 178:843-860(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH KIDINS220; MAGI2 AND RAPGEF2, INTERACTION WITH RAPGEF2, SUBCELLULAR LOCATION.
[13]"Neurotrophin receptor homolog-2 regulates nerve growth factor signaling."
Wong A.W., Willingham M., Xiao J., Kilpatrick T.J., Murray S.S.
J. Neurochem. 106:1964-1976(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRADD.
[14]"Neurotrophin receptors TrkA and TrkC cause neuronal death whereas TrkB does not."
Nikoletopoulou V., Lickert H., Frade J.M., Rencurel C., Giallonardo P., Zhang L., Bibel M., Barde Y.A.
Nature 467:59-63(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DEATH.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85214 mRNA. Translation: AAA42286.1.
L12225 Genomic DNA. No translation available.
PIRTVRTTB. A41981.
RefSeqNP_067600.1. NM_021589.1.
XP_006232808.1. XM_006232746.1.
UniGeneRn.39098.

3D structure databases

ProteinModelPortalP35739.
SMRP35739. Positions 36-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248731. 18 interactions.
DIPDIP-5716N.
IntActP35739. 2 interactions.
MINTMINT-191667.

Chemistry

ChEMBLCHEMBL4220.

PTM databases

PhosphoSiteP35739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018961; ENSRNOP00000018961; ENSRNOG00000013953. [P35739-1]
ENSRNOT00000044046; ENSRNOP00000048885; ENSRNOG00000013953. [P35739-2]
GeneID59109.
KEGGrno:59109.
UCSCRGD:620144. rat. [P35739-1]

Organism-specific databases

CTD4914.
RGD620144. Ntrk1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110657.
HOGENOMHOG000264255.
HOVERGENHBG056735.
InParanoidP35739.
KOK03176.
OMAKNVTCWA.
OrthoDBEOG7GTT32.
PhylomeDBP35739.
TreeFamTF106465.

Enzyme and pathway databases

BRENDA2.7.10.1. 5301.

Gene expression databases

GenevestigatorP35739.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. 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.
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

NextBio611747.
PROP35739.

Entry information

Entry nameNTRK1_RAT
AccessionPrimary (citable) accession number: P35739
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families