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Q16288 (NTRK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NT-3 growth factor receptor

EC=2.7.10.1
Alternative name(s):
GP145-TrkC
Short name=Trk-C
Neurotrophic tyrosine kinase receptor type 3
TrkC tyrosine kinase
Gene names
Name:NTRK3
Synonyms:TRKC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length839 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for neurotrophin-3 (NT-3). This is a tyrosine-protein kinase receptor. Known substrates for the trk receptors are SHC1, PI-3 kinase, and PLCG1. The different isoforms do not have identical signaling properties.

Catalytic activity

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

Subunit structure

Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Binds SH2B2. Interacts with SQSTM1 and KIDINS220 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Widely expressed but mainly in nervous tissue. Isoform 2 is expressed at higher levels in adult brain than in fetal brain.

Post-translational modification

Ligand-mediated auto-phosphorylation.

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 componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   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
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

activation of Ras GTPase activity

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

activation of protein kinase B activity

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cochlea development

Inferred from electronic annotation. Source: Ensembl

mechanoreceptor differentiation

Inferred from electronic annotation. Source: Ensembl

modulation by virus of host transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

neuron fate specification

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

neurotrophin signaling pathway

Inferred from direct assay PubMed 23027130. Source: GOC

positive regulation of actin cytoskeleton reorganization

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

positive regulation of axon extension involved in regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

positive regulation of positive chemotaxis

Inferred from direct assay PubMed 23027130. Source: BHF-UCL

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

neurotrophin binding

Traceable author statement Ref.1. Source: ProtInc

neurotrophin receptor activity

Inferred from electronic annotation. Source: InterPro

p53 binding

Inferred from physical interaction PubMed 23027130. Source: BHF-UCL

transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q16288-1)

Also known as: A;

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 2 (identifier: Q16288-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     529-612: YVQHIKRRDI...FYGVCGDGDP → WVFSNIDNHG...VYFSKGRHGF
     613-839: Missing.
Isoform 3 (identifier: Q16288-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     712-725: Missing.
Isoform 4 (identifier: Q16288-4)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     402-410: ESTDNFILF → V
Isoform 5 (identifier: Q16288-5)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     402-410: ESTDNFILF → V
     712-725: Missing.
Note: No experimental confirmation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 839808NT-3 growth factor receptor
PRO_0000016731

Regions

Topological domain32 – 429398Extracellular Potential
Transmembrane430 – 45324Helical; Potential
Topological domain454 – 839386Cytoplasmic Potential
Repeat104 – 12522LRR 1
Repeat128 – 14922LRR 2
Domain160 – 20950LRRCT
Domain210 – 30091Ig-like C2-type 1
Domain309 – 38274Ig-like C2-type 2
Domain538 – 839302Protein kinase
Nucleotide binding544 – 5529ATP By similarity

Sites

Active site6791Proton acceptor By similarity
Binding site5721ATP By similarity
Site5161Interaction with SHC1 By similarity
Site8341Interaction with PLC-gamma-1 By similarity

Amino acid modifications

Modified residue5161Phosphotyrosine; by autocatalysis By similarity
Modified residue7051Phosphotyrosine; by autocatalysis By similarity
Modified residue7091Phosphotyrosine; by autocatalysis By similarity
Modified residue7101Phosphotyrosine; by autocatalysis By similarity
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Disulfide bond320 ↔ 362 Ref.6

Natural variations

Alternative sequence402 – 4109ESTDNFILF → V in isoform 4 and isoform 5.
VSP_002924
Alternative sequence529 – 61284YVQHI…GDGDP → WVFSNIDNHGILNLKDNRDH LVPSTHYIYEEPEVQSGEVS YPRSHGFREIMLNPISLPGH SKPLNHGIYVEDVNVYFSKG RHGF in isoform 2.
VSP_002925
Alternative sequence613 – 839227Missing in isoform 2.
VSP_002926
Alternative sequence712 – 72514Missing in isoform 3 and isoform 5.
VSP_002927
Natural variant1491T → R in a gastric adenocarcinoma sample; somatic mutation. Ref.7
VAR_041471
Natural variant3061R → C. Ref.7
Corresponds to variant rs56386352 [ dbSNP | Ensembl ].
VAR_041472
Natural variant3071V → L in a lung adenocarcinoma sample; somatic mutation. Ref.7
VAR_041473
Natural variant3361L → Q in a lung adenocarcinoma sample; somatic mutation. Ref.7
VAR_041474
Natural variant6641A → S in a lung carcinoma sample; somatic mutation. Ref.8
VAR_046521
Natural variant6771H → Y in a lung adenocarcinoma sample; somatic mutation. Ref.7 Ref.8
VAR_041475
Natural variant6781R → Q. Ref.7
Corresponds to variant rs55890138 [ dbSNP | Ensembl ].
VAR_041476
Natural variant7351R → F in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.
VAR_046770
Natural variant7361W → C in a lung carcinoma sample; somatic mutation. Ref.8
VAR_046522
Natural variant7451R → P in a lung carcinoma sample; somatic mutation. Ref.8
VAR_046523
Natural variant7661Y → F in a lung carcinoma sample; somatic mutation. Ref.8
VAR_046524
Natural variant7681K → R. Ref.7
Corresponds to variant rs55770052 [ dbSNP | Ensembl ].
VAR_046771
Natural variant7811E → K. Ref.7
Corresponds to variant rs56393451 [ dbSNP | Ensembl ].
VAR_046772

Experimental info

Sequence conflict651S → G in BAH12511. Ref.4
Sequence conflict701S → N in AAB33111. Ref.2
Sequence conflict701S → N in AAB33112. Ref.2
Sequence conflict6351D → N in AAA75374. Ref.1

Secondary structure

.......................................................... 839
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 7FE8846830083C08

FASTA83994,428
        10         20         30         40         50         60 
MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD GNLFPLLEGQ 

        70         80         90        100        110        120 
DSGNSNGNAS INITDISRNI TSIHIENWRS LHTLNAVDME LYTGLQKLTI KNSGLRSIQP 

       130        140        150        160        170        180 
RAFAKNPHLR YINLSSNRLT TLSWQLFQTL SLRELQLEQN FFNCSCDIRW MQLWQEQGEA 

       190        200        210        220        230        240 
KLNSQNLYCI NADGSQLPLF RMNISQCDLP EISVSHVNLT VREGDNAVIT CNGSGSPLPD 

       250        260        270        280        290        300 
VDWIVTGLQS INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT 

       310        320        330        340        350        360 
VYYPPRVVSL EEPELRLEHC IEFVVRGNPP PTLHWLHNGQ PLRESKIIHV EYYQEGEISE 

       370        380        390        400        410        420 
GCLLFNKPTH YNNGNYTLIA KNPLGTANQT INGHFLKEPF PESTDNFILF DEVSPTPPIT 

       430        440        450        460        470        480 
VTHKPEEDTF GVSIAVGLAA FACVLLVVLF VMINKYGRRS KFGMKGPVAV ISGEEDSASP 

       490        500        510        520        530        540 
LHHINHGITT PSSLDAGPDT VVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL 

       550        560        570        580        590        600 
KRELGEGAFG KVFLAECYNL SPTKDKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI 

       610        620        630        640        650        660 
VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE LGLSQMLHIA 

       670        680        690        700        710        720 
SQIASGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM SRDVYSTDYY RLFNPSGNDF 

       730        740        750        760        770        780 
CIWCEVGGHT MLPIRWMPPE SIMYRKFTTE SDVWSFGVIL WEIFTYGKQP WFQLSNTEVI 

       790        800        810        820        830 
ECITQGRVLE RPRVCPKEVY DVMLGCWQRE PQQRLNIKEI YKILHALGKA TPIYLDILG 

« Hide

Isoform 2 (B) [UniParc].

Checksum: F2E84DC71B8E4DB3
Show »

FASTA61268,452
Isoform 3 (C) [UniParc].

Checksum: 7ADBE1AF6DB280BF
Show »

FASTA82592,801
Isoform 4 (D) [UniParc].

Checksum: 4823FA200F88433F
Show »

FASTA83193,460
Isoform 5 (E) [UniParc].

Checksum: 674CC49828F86789
Show »

FASTA81791,833

References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNA for human TrkC (NTRK3), chromosomal assignment, and evidence for a splice variant."
McGregor L.M., Baylin S.B., Griffin C.A., Hawkins A.L., Nelkin B.D.
Genomics 22:267-272(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
Tissue: Fetal brain.
[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] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[3]"Genomic characterization of the human trkC gene."
Ichaso N., Rodriguez R.E., Martin-Zanca D., Gonzalez-Sarmiento R.
Oncogene 17:1871-1875(1998) [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 5).
Tissue: Brain.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 (1.9 ANGSTROMS) OF 297-401, DISULFIDE BOND.
[7]"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-149; CYS-306; LEU-307; GLN-336; TYR-677; GLN-678; ARG-768 AND LYS-781.
[8]"Frequent mutations in the neurotrophic tyrosine receptor kinase gene family in large cell neuroendocrine carcinoma of the lung."
Marchetti A., Felicioni L., Pelosi G., Del Grammastro M., Fumagalli C., Sciarrotta M., Malatesta S., Chella A., Barassi F., Mucilli F., Camplese P., D'Antuono T., Sacco R., Buttitta F.
Hum. Mutat. 29:609-616(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-664; TYR-677; CYS-736; PRO-745 AND PHE-766.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05012 mRNA. Translation: AAA75374.1.
S76475 mRNA. Translation: AAB33111.1.
S76476 mRNA. Translation: AAB33112.1.
AJ224521 expand/collapse EMBL AC list , AJ224522, AJ224523, AJ224524, AJ224525, AJ224526, AJ224527, AJ224528, AJ224529, AJ224530, AJ224531, AJ224532, AJ224533, AJ224534, AJ224535 Genomic DNA. Translation: CAA12029.1.
AK297160 mRNA. Translation: BAH12511.1.
AC009711 Genomic DNA. No translation available.
AC011966 Genomic DNA. No translation available.
AC021677 Genomic DNA. No translation available.
PIRA55178.
I73632.
I73633.
RefSeqNP_001012338.1. NM_001012338.2.
NP_001230030.1. NM_001243101.1.
NP_002521.2. NM_002530.3.
UniGeneHs.410969.
Hs.706364.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWCX-ray1.90A297-422[»]
3V5QX-ray2.20A/B530-832[»]
ProteinModelPortalQ16288.
SMRQ16288. Positions 28-401, 529-832.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110971. 9 interactions.
DIPDIP-5723N.
IntActQ16288. 3 interactions.
MINTMINT-188514.
STRING9606.ENSP00000354207.

Chemistry

BindingDBQ16288.
ChEMBLCHEMBL5608.
GuidetoPHARMACOLOGY1819.

PTM databases

PhosphoSiteQ16288.

Polymorphism databases

DMDM134035335.

Proteomic databases

PaxDbQ16288.
PRIDEQ16288.

Protocols and materials databases

DNASU4916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317501; ENSP00000318328; ENSG00000140538. [Q16288-2]
ENST00000355254; ENSP00000347397; ENSG00000140538. [Q16288-3]
ENST00000357724; ENSP00000350356; ENSG00000140538.
ENST00000360948; ENSP00000354207; ENSG00000140538. [Q16288-1]
ENST00000394480; ENSP00000377990; ENSG00000140538. [Q16288-3]
ENST00000540489; ENSP00000444673; ENSG00000140538. [Q16288-2]
ENST00000557856; ENSP00000453959; ENSG00000140538.
GeneID4916.
KEGGhsa:4916.
UCSCuc002bme.2. human. [Q16288-1]
uc002bmf.2. human. [Q16288-3]

Organism-specific databases

CTD4916.
GeneCardsGC15M088402.
HGNCHGNC:8033. NTRK3.
HPACAB009233.
MIM191316. gene.
neXtProtNX_Q16288.
Orphanet2665. Congenital mesoblastic nephroma.
2030. Fibrosarcoma.
PharmGKBPA31819.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000264255.
HOVERGENHBG056735.
InParanoidQ16288.
KOK05101.
OMANFVSIYE.
OrthoDBEOG7GTT32.
PhylomeDBQ16288.
TreeFamTF106465.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkQ16288.

Gene expression databases

ArrayExpressQ16288.
BgeeQ16288.
CleanExHS_NTRK3.
GenevestigatorQ16288.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR020446. Tyr_kin_neurotrophic_rcpt_3.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR020777. Tyr_kinase_NGF_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamPF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR01939. NTKRECEPTOR.
PR01942. NTKRECEPTOR3.
PR00109. TYRKINASE.
SMARTSM00409. IG. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 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]
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Other

ChiTaRSNTRK3. human.
EvolutionaryTraceQ16288.
GeneWikiTrkC_receptor.
GenomeRNAi4916.
NextBio18927.
PROQ16288.
SOURCESearch...

Entry information

Entry nameNTRK3_HUMAN
AccessionPrimary (citable) accession number: Q16288
Secondary accession number(s): B7Z4C5 expand/collapse secondary AC list , E9PG56, H0YND1, O75682, Q12827, Q16289
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 163 of the entry and version 2 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 15

Human chromosome 15: entries, gene names and cross-references to MIM