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Q3UFB7

- NTRK1_MOUSE

UniProt

Q3UFB7 - NTRK1_MOUSE

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Protein
High affinity nerve growth factor receptor
Gene
Ntrk1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulationi

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei499 – 4991Interaction with SHC1 By similarity
Binding sitei547 – 5471ATP By similarity
Active sitei653 – 6531Proton acceptor By similarity
Sitei794 – 7941Interaction with PLCG1 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi519 – 5279ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nerve growth factor binding Source: UniProtKB
  3. nerve growth factor receptor activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. protein tyrosine kinase activity Source: MGI
  7. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. B cell differentiation Source: MGI
  2. Sertoli cell development Source: Ensembl
  3. aging Source: Ensembl
  4. axon guidance Source: Ensembl
  5. axonogenesis involved in innervation Source: UniProtKB
  6. cellular response to growth factor stimulus Source: MGI
  7. cellular response to nerve growth factor stimulus Source: UniProtKB
  8. cellular response to nicotine Source: Ensembl
  9. circadian rhythm Source: UniProtKB
  10. detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
  11. detection of temperature stimulus involved in sensory perception of pain Source: Ensembl
  12. developmental programmed cell death Source: UniProtKB
  13. learning or memory Source: Ensembl
  14. mechanoreceptor differentiation Source: MGI
  15. negative regulation of cell proliferation Source: UniProtKB
  16. negative regulation of neuron apoptotic process Source: UniProtKB
  17. nerve growth factor signaling pathway Source: UniProtKB
  18. nervous system development Source: MGI
  19. neurotrophin TRK receptor signaling pathway Source: UniProtKB
  20. olfactory nerve development Source: Ensembl
  21. peptidyl-tyrosine phosphorylation Source: GOC
  22. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  24. positive regulation of Ras GTPase activity Source: UniProtKB
  25. positive regulation of Ras protein signal transduction Source: UniProtKB
  26. positive regulation of angiogenesis Source: Ensembl
  27. positive regulation of neuron projection development Source: UniProtKB
  28. positive regulation of programmed cell death Source: UniProtKB
  29. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  30. protein autophosphorylation Source: UniProtKB
  31. protein phosphorylation Source: MGI
  32. response to activity Source: Ensembl
  33. response to axon injury Source: Ensembl
  34. response to drug Source: Ensembl
  35. response to electrical stimulus Source: Ensembl
  36. response to ethanol Source: Ensembl
  37. response to hydrostatic pressure Source: Ensembl
  38. response to nutrient levels Source: Ensembl
  39. response to radiation Source: Ensembl
  40. sympathetic nervous system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_202778. Retrograde neurotrophin signalling.
REACT_205300. PI3K/AKT activation.
REACT_209347. NGF-independant TRKA activation.
REACT_212952. Signalling to STAT3.
REACT_213333. TRKA activation by NGF.

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity nerve growth factor receptor (EC:2.7.10.1)
Alternative name(s):
Neurotrophic tyrosine kinase receptor type 1
Gene namesi
Name:Ntrk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:97383. Ntrk1.

Subcellular locationi

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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 420387Extracellular Reviewed prediction
Add
BLAST
Transmembranei421 – 44121Helical; Reviewed prediction
Add
BLAST
Topological domaini442 – 799358Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cell surface Source: MGI
  3. cytoplasm Source: MGI
  4. cytoplasmic vesicle Source: Ensembl
  5. dendrite Source: Ensembl
  6. early endosome Source: UniProtKB
  7. early endosome membrane Source: UniProtKB-SubCell
  8. integral component of plasma membrane Source: UniProtKB
  9. late endosome Source: UniProtKB
  10. late endosome membrane Source: UniProtKB-SubCell
  11. neuronal cell body Source: Ensembl
  12. plasma membrane Source: UniProtKB
  13. protein complex Source: UniProtKB
  14. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 799766High affinity nerve growth factor receptor
PRO_0000278537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi121 – 1211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi154 ↔ 193 By similarity
Glycosylationi190 – 1901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi204 – 2041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi217 ↔ 267 By similarity
Glycosylationi255 – 2551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi264 – 2641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi320 – 3201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi325 – 3251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi341 – 3411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi361 – 3611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi404 – 4041N-linked (GlcNAc...) Reviewed prediction
Modified residuei499 – 4991Phosphotyrosine; by autocatalysis By similarity
Modified residuei679 – 6791Phosphotyrosine; by autocatalysis By similarity
Modified residuei683 – 6831Phosphotyrosine; by autocatalysis By similarity
Modified residuei684 – 6841Phosphotyrosine; by autocatalysis By similarity
Modified residuei794 – 7941Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3UFB7.
PRIDEiQ3UFB7.

PTM databases

PhosphoSiteiQ3UFB7.

Expressioni

Developmental stagei

First detected at E13.5, a time coinciding with the requirement of sympathetic neurons for NGF.1 Publication

Inductioni

Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain.4 Publications

Gene expression databases

BgeeiQ3UFB7.
CleanExiMM_NTRK1.
GenevestigatoriQ3UFB7.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi201868. 7 interactions.
STRINGi10090.ENSMUSP00000029712.

Structurei

3D structure databases

ProteinModelPortaliQ3UFB7.
SMRiQ3UFB7. Positions 36-391, 504-797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati90 – 11324LRR 1
Add
BLAST
Repeati116 – 13722LRR 2
Add
BLAST
Domaini148 – 21972LRRCT
Add
BLAST
Domaini196 – 28590Ig-like C2-type 1
Add
BLAST
Domaini205 – 368164Ig-like C2-type 2
Add
BLAST
Domaini513 – 784272Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni472 – 49322Interaction with SQSTM1 By similarity
Add
BLAST

Domaini

The transmembrane domain mediates interaction with KIDINS220 By similarity.
The extracellular domain mediates interaction with NGFR By similarity.

Sequence similaritiesi

Contains 1 LRRCT domain.

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00730000110657.
HOGENOMiHOG000264255.
HOVERGENiHBG056735.
InParanoidiQ3UFB7.
KOiK03176.
OMAiKNVTCWA.
OrthoDBiEOG7GTT32.
PhylomeDBiQ3UFB7.
TreeFamiTF106465.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. 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]
PfamiPF13855. LRR_8. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01939. NTKRECEPTOR.
PR01940. NTKRECEPTOR1.
PR00109. TYRKINASE.
SMARTiSM00409. IG. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50835. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3UFB7-1 [UniParc]FASTAAdd to Basket

« Hide

MLRGQRLGQL GWHRPAAGLG SLMTSLMLAC ASAASCREVC CPVGPSGLRC    50
TRAGSLDTLR GLRGAGNLTE LYVENQQHLQ RLEFEDLQGL GELRSLTIVK 100
SGLRFVAPDA FRFTPRLSHL NLSSNALESL SWKTVQGLSL QDLTLSGNPL 150
HCSCALFWLQ RWEQEGLCGV HTQTLHDSGP GDQFLPLGHN TSCGVPTVKI 200
QMPNDSVEVG DDVFLQCQVE GLALQQADWI LTELEGAATV KKFGDLPSLG 250
LILVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGLAVEQHH 300
WCIPFSVDGQ PAPSLRWLFN GSVLNETSFI FTQFLESALT NETMRHGCLR 350
LNQPTHVNNG NYTLLAANPY GQAAASVMAA FMDNPFEFNP EDPIPVSFSP 400
VDGNSTSRDP VEKKDETPFG VSVAVGLAVS AALFLSALLL VLNKCGQRSK 450
FGINRPAVLA PEDGLAMSLH FMTLGGSSLS PTEGKGSGLQ GHIMENPQYF 500
SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD KMLVAVKALK 550
EASENARQDF QREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL 600
NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV 650
HRDLATRNCL VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE 700
SILYRKFSTE SDVWSFGVVL WEIFTYGKQP WYQLSNTEAI ECITQGRELE 750
RPRACPPDVY AIMRGCWQRE PQQRLSMKDV HARLQALAQA PPSYLDVLG 799
Length:799
Mass (Da):87,738
Last modified:February 20, 2007 - v2
Checksum:i1A37F76A63564603
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK081588 mRNA. No translation available.
AK148691 mRNA. Translation: BAE28644.1. Different initiation.
CCDSiCCDS50947.1.
RefSeqiNP_001028296.1. NM_001033124.1.
UniGeneiMm.80682.

Genome annotation databases

EnsembliENSMUST00000029712; ENSMUSP00000029712; ENSMUSG00000028072.
GeneIDi18211.
KEGGimmu:18211.
UCSCiuc008psw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK081588 mRNA. No translation available.
AK148691 mRNA. Translation: BAE28644.1 . Different initiation.
CCDSi CCDS50947.1.
RefSeqi NP_001028296.1. NM_001033124.1.
UniGenei Mm.80682.

3D structure databases

ProteinModelPortali Q3UFB7.
SMRi Q3UFB7. Positions 36-391, 504-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201868. 7 interactions.
STRINGi 10090.ENSMUSP00000029712.

PTM databases

PhosphoSitei Q3UFB7.

Proteomic databases

PaxDbi Q3UFB7.
PRIDEi Q3UFB7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029712 ; ENSMUSP00000029712 ; ENSMUSG00000028072 .
GeneIDi 18211.
KEGGi mmu:18211.
UCSCi uc008psw.1. mouse.

Organism-specific databases

CTDi 4914.
MGIi MGI:97383. Ntrk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00730000110657.
HOGENOMi HOG000264255.
HOVERGENi HBG056735.
InParanoidi Q3UFB7.
KOi K03176.
OMAi KNVTCWA.
OrthoDBi EOG7GTT32.
PhylomeDBi Q3UFB7.
TreeFami TF106465.

Enzyme and pathway databases

Reactomei REACT_202778. Retrograde neurotrophin signalling.
REACT_205300. PI3K/AKT activation.
REACT_209347. NGF-independant TRKA activation.
REACT_212952. Signalling to STAT3.
REACT_213333. TRKA activation by NGF.

Miscellaneous databases

NextBioi 293598.
PROi Q3UFB7.
SOURCEi Search...

Gene expression databases

Bgeei Q3UFB7.
CleanExi MM_NTRK1.
Genevestigatori Q3UFB7.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR007110. 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 ]
Pfami PF13855. LRR_8. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR01939. NTKRECEPTOR.
PR01940. NTKRECEPTOR1.
PR00109. TYRKINASE.
SMARTi SM00409. IG. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiNTRK1_MOUSE
AccessioniPrimary (citable) accession number: Q3UFB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi