Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3UFB7 (NTRK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:Ntrk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.2 Ref.3 Ref.6

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. Regulated by NGFR. Ref.4 Ref.5 Ref.6

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. 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 NRADD By similarity. Interacts with SH2D1A; regulates NTRK1. 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.5

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 By similarity. Note: 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. Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport. Ref.6

Developmental stage

First detected at E13.5, a time coinciding with the requirement of sympathetic neurons for NGF. Ref.3

Induction

Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain. Ref.4 Ref.5 Ref.6 Ref.7

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-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. Ref.4

Disruption phenotype

Mice die early after birth due to severe sensory and sympathetic neuropathies characterized by extensive neuronal cell loss in trigeminal, sympathetic and dorsal root ganglia, as well as a decrease in the cholinergic basal forebrain projections to the hippocampus and cortex. There are for instance 35% fewer cells by E17.5 in the superior cervical ganglion, a major component of the sympathetic system. Ref.2

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 BAE28644.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Endosome
Membrane
   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 mutant phenotype PubMed 15459109. Source: MGI

Sertoli cell development

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from electronic annotation. Source: Ensembl

axonogenesis involved in innervation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from sequence orthology PubMed 19029245. Source: MGI

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

circadian rhythm

Inferred from expression pattern Ref.7. Source: UniProtKB

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 mutant phenotype PubMed 15376326. Source: MGI

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from mutant phenotype Ref.3. Source: UniProtKB

nerve growth factor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Inferred from direct assay PubMed 12810599. Source: MGI

neurotrophin TRK receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

olfactory nerve development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from sequence orthology 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 sequence or structural similarity. Source: UniProtKB

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 11877420. Source: MGI

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

sympathetic nervous system development

Inferred from mutant phenotype Ref.3. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from sequence orthology PubMed 19029245. Source: MGI

cytoplasm

Inferred from direct assay PubMed 10207144PubMed 11551509. Source: MGI

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

integral component of plasma membrane

Inferred from sequence or structural similarity. 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 sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

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

protein binding

Inferred from physical interaction PubMed 19755105. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from sequence orthology PubMed 19029245. Source: MGI

transmembrane receptor protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 799766High affinity nerve growth factor receptor
PRO_0000278537

Regions

Topological domain34 – 420387Extracellular Potential
Transmembrane421 – 44121Helical; Potential
Topological domain442 – 799358Cytoplasmic Potential
Repeat90 – 11324LRR 1
Repeat116 – 13722LRR 2
Domain148 – 21972LRRCT
Domain196 – 28590Ig-like C2-type 1
Domain205 – 368164Ig-like C2-type 2
Domain513 – 784272Protein kinase
Nucleotide binding519 – 5279ATP By similarity
Region472 – 49322Interaction with SQSTM1 By similarity

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

Sequences

Sequence LengthMass (Da)Tools
Q3UFB7 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 1A37F76A63564603

FASTA79987,738
        10         20         30         40         50         60 
MLRGQRLGQL GWHRPAAGLG SLMTSLMLAC ASAASCREVC CPVGPSGLRC TRAGSLDTLR 

        70         80         90        100        110        120 
GLRGAGNLTE LYVENQQHLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FRFTPRLSHL 

       130        140        150        160        170        180 
NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALFWLQ RWEQEGLCGV HTQTLHDSGP 

       190        200        210        220        230        240 
GDQFLPLGHN TSCGVPTVKI QMPNDSVEVG DDVFLQCQVE GLALQQADWI LTELEGAATV 

       250        260        270        280        290        300 
KKFGDLPSLG LILVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGLAVEQHH 

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

       370        380        390        400        410        420 
NYTLLAANPY GQAAASVMAA FMDNPFEFNP EDPIPVSFSP VDGNSTSRDP 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 EASENARQDF QREAELLTML 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

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Sympathetic ganglion.
[2]"Severe sensory and sympathetic neuropathies in mice carrying a disrupted Trk/NGF receptor gene."
Smeyne R.J., Klein R., Schnapp A., Long L.K., Bryant S., Lewin A., Lira S.A., Barbacid M.
Nature 368:246-249(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN DEVELOPMENT OF THE NERVOUS SYSTEM.
[3]"TrkA, but not TrkC, receptors are essential for survival of sympathetic neurons in vivo."
Fagan A.M., Zhang H., Landis S., Smeyne R.J., Silos-Santiago I., Barbacid M.
J. Neurosci. 16:6208-6218(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYMPATHETIC NEURONS SURVIVAL, DEVELOPMENTAL STAGE.
[4]"p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation."
Makkerh J.P., Ceni C., Auld D.S., Vaillancourt F., Dorval G., Barker P.A.
EMBO Rep. 6:936-941(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, ENZYME REGULATION.
[5]"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.
[6]"Recruitment of actin modifiers to TrkA endosomes governs retrograde NGF signaling and survival."
Harrington A.W., St Hillaire C., Zweifel L.S., Glebova N.O., Philippidou P., Halegoua S., Ginty D.D.
Cell 146:421-434(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NGF AND NTF3 SIGNALING, ENZYME REGULATION, SUBCELLULAR LOCATION.
[7]"p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK081588 mRNA. No translation available.
AK148691 mRNA. Translation: BAE28644.1. Different initiation.
CCDSCCDS50947.1.
RefSeqNP_001028296.1. NM_001033124.1.
UniGeneMm.80682.

3D structure databases

ProteinModelPortalQ3UFB7.
SMRQ3UFB7. Positions 36-391, 504-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201868. 7 interactions.
STRING10090.ENSMUSP00000029712.

PTM databases

PhosphoSiteQ3UFB7.

Proteomic databases

PaxDbQ3UFB7.
PRIDEQ3UFB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029712; ENSMUSP00000029712; ENSMUSG00000028072.
GeneID18211.
KEGGmmu:18211.
UCSCuc008psw.1. mouse.

Organism-specific databases

CTD4914.
MGIMGI:97383. Ntrk1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110657.
HOGENOMHOG000264255.
HOVERGENHBG056735.
InParanoidQ3UFB7.
KOK03176.
OMAKNVTCWA.
OrthoDBEOG7GTT32.
PhylomeDBQ3UFB7.
TreeFamTF106465.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeQ3UFB7.
CleanExMM_NTRK1.
GenevestigatorQ3UFB7.

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.
IPR001611. Leu-rich_rpt.
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]
PfamPF13855. LRR_8. 1 hit.
PF07714. 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

NextBio293598.
PROQ3UFB7.
SOURCESearch...

Entry information

Entry nameNTRK1_MOUSE
AccessionPrimary (citable) accession number: Q3UFB7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 92 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot