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P15209 (NTRK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 141. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BDNF/NT-3 growth factors receptor
EC=2.7.10.1
Alternative name(s):
GP145-TrkB/GP95-TrkB
Short name=Trk-B
Neurotrophic tyrosine kinase receptor type 2
TrkB tyrosine kinase
Gene names
Name:Ntrk2
Synonyms:Trkb
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length821 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 the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon 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. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. Isoform GP95-TRKB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19

Catalytic activity

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

Enzyme regulation

The formation of active receptors dimers able to fully transduce the ligand-mediated signal, may be negatively regulated by the formation of inactive heterodimers with the non-catalytic isoforms By similarity. The neuronal activity and the influx of calcium positively regulate the kinase activity and the internalization of the receptor which are both important for active signaling. Regulated by NGFR that may control the internalization of the receptor. NGFR may also stimulate the activation by BDNF compared to NTF3 and NTF4. SH2D1A inhibits the autophosphorylation of the receptor, and alters the recruitment and activation of downstream effectors and signaling cascades. Ref.11 Ref.15 Ref.16

Subunit structure

Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Interacts (phosphorylated upon activation by BDNF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by BDNF) with PLCG1 and/or PLCG2; mediates PLCG1 phosphorylation and activation. Interacts with SH2B1 and SH2B2. Interacts with NGFR; may regulate the ligand specificity of the receptor By similarity. Interacts (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2. Interacts with SQSTM1 and KIDINS220 By similarity. Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway By similarity. Ref.10 Ref.16 Ref.17

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Note: Internalized to endosomes upon ligand-binding. Ref.11

Tissue specificity

Widely expressed in the central and peripheral nervous system. The different forms are differentially expressed in various cell types. Isoform GP95-TRKB is specifically expressed in glial cells.

Post-translational modification

Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Some isoforms are not phosphorylated By similarity. Ref.17 Ref.18

Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor. Ref.15

Disruption phenotype

Mice lacking isoform GP145-TRKB, the catalytic isoform, do not display feeding activity and die at P1. This is associated neuronal deficiencies in the central and the peripheral nervous systems. Ref.7

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 LRRNT domain.

Contains 1 protein kinase domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform GP145-TRKB (identifier: P15209-1)

Also known as: L3; TrkBTK+; TRKB-FL;

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 GP95-TRKB (identifier: P15209-2)

Also known as: TRKB-T1; TrkBTK-;

The sequence of this isoform differs from the canonical sequence as follows:
     466-476: PASVISNDDDS → FVLFHKIPLDG
     477-821: Missing.
Note: Non-catalytic isoform.
Isoform L1 (identifier: P15209-3)

The sequence of this isoform differs from the canonical sequence as follows:
     72-120: Missing.
Isoform L10 (identifier: P15209-4)

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → M
     72-143: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 821790BDNF/NT-3 growth factors receptor
PRO_0000016728

Regions

Topological domain32 – 429398Extracellular Potential
Transmembrane430 – 45324Helical; Potential
Topological domain454 – 821368Cytoplasmic Potential
Domain32 – 6130LRRNT
Repeat92 – 11322LRR 1
Repeat116 – 13722LRR 2
Domain148 – 19649LRRCT
Domain197 – 28286Ig-like C2-type 1
Domain301 – 36565Ig-like C2-type 2
Domain537 – 806270Protein kinase
Nucleotide binding543 – 5519ATP By similarity

Sites

Active site6751Proton acceptor By similarity
Binding site5711ATP By similarity
Site5151Interaction with SHC1
Site7051Interaction with SH2D1A By similarity
Site8161Interaction with PLCG1

Amino acid modifications

Modified residue5151Phosphotyrosine; by autocatalysis By similarity
Modified residue7011Phosphotyrosine; by autocatalysis By similarity
Modified residue7051Phosphotyrosine; by autocatalysis By similarity
Modified residue7061Phosphotyrosine; by autocatalysis By similarity
Modified residue8161Phosphotyrosine; by autocatalysis By similarity
Glycosylation671N-linked (GlcNAc...) By similarity
Glycosylation951N-linked (GlcNAc...) By similarity
Glycosylation1211N-linked (GlcNAc...) By similarity
Glycosylation1781N-linked (GlcNAc...) By similarity
Glycosylation2051N-linked (GlcNAc...) By similarity
Glycosylation2411N-linked (GlcNAc...) By similarity
Glycosylation2541N-linked (GlcNAc...) By similarity
Glycosylation2801N-linked (GlcNAc...) By similarity
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) By similarity
Glycosylation4111N-linked (GlcNAc...) By similarity
Disulfide bond32 ↔ 38 By similarity
Disulfide bond36 ↔ 45 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond154 ↔ 194 By similarity
Disulfide bond218 ↔ 266 By similarity
Disulfide bond302 ↔ 345 By similarity

Natural variations

Alternative sequence711I → M in isoform L10.
VSP_002905
Alternative sequence72 – 14372Missing in isoform L10.
VSP_002906
Alternative sequence72 – 12049Missing in isoform L1.
VSP_002907
Alternative sequence466 – 47611PASVISNDDDS → FVLFHKIPLDG in isoform GP95-TRKB.
VSP_002908
Alternative sequence477 – 821345Missing in isoform GP95-TRKB.
VSP_002909

Experimental info

Mutagenesis5151Y → F: Loss of interaction with SHC1. Ref.10
Mutagenesis8161Y → F: Loss of interaction with PLCG1. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform GP145-TRKB (L3) (TrkBTK+) (TRKB-FL) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 50E08D5FF86D8F30

FASTA82192,133
        10         20         30         40         50         60 
MSPWLKWHGP AMARLWGLCL LVLGFWRASL ACPTSCKCSS ARIWCTEPSP GIVAFPRLEP 

        70         80         90        100        110        120 
NSVDPENITE ILIANQKRLE IINEDDVEAY VGLRNLTIVD SGLKFVAYKA FLKNSNLRHI 

       130        140        150        160        170        180 
NFTRNKLTSL SRRHFRHLDL SDLILTGNPF TCSCDIMWLK TLQETKSSPD TQDLYCLNES 

       190        200        210        220        230        240 
SKNMPLANLQ IPNCGLPSAR LAAPNLTVEE GKSVTLSCSV GGDPLPTLYW DVGNLVSKHM 

       250        260        270        280        290        300 
NETSHTQGSL RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH 

       310        320        330        340        350        360 
WCIPFTVRGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN PTHMNNGDYT 

       370        380        390        400        410        420 
LMAKNEYGKD ERQISAHFMG RPGVDYETNP NYPEVLYEDW TTPTDIGDTT NKSNEIPSTD 

       430        440        450        460        470        480 
VADQSNREHL SVYAVVVIAS VVGFCLLVML LLLKLARHSK FGMKGPASVI SNDDDSASPL 

       490        500        510        520        530        540 
HHISNGSNTP SSSEGGPDAV IIGMTKIPVI ENPQYFGITN SQLKPDTFVQ HIKRHNIVLK 

       550        560        570        580        590        600 
RELGEGAFGK VFLAECYNLC PEQDKILVAV KTLKDASDNA RKDFHREAEL LTNLQHEHIV 

       610        620        630        640        650        660 
KFYGVCVEGD PLIMVFEYMK HGDLNKFLRA HGPDAVLMAE GNPPTELTQS QMLHIAQQIA 

       670        680        690        700        710        720 
AGMVYLASQH FVHRDLATRN CLVGENLLVK IGDFGMSRDV YSTDYYRVGG HTMLPIRWMP 

       730        740        750        760        770        780 
PESIMYRKFT TESDVWSLGV VLWEIFTYGK QPWYQLSNNE VIECITQGRV LQRPRTCPQE 

       790        800        810        820 
VYELMLGCWQ REPHTRKNIK SIHTLLQNLA KASPVYLDIL G

« Hide

Isoform GP95-TRKB (TRKB-T1) (TrkBTK-) [UniParc].

Checksum: 20A8B375ED397ACE
Show »

FASTA47653,186
Isoform L1 [UniParc].

Checksum: E3E800582F9D3FB6
Show »

FASTA77286,535
Isoform L10 [UniParc].

Checksum: 791E6861C97AA53F
Show »

FASTA74983,744

References

« Hide 'large scale' references
[1]"trkB, a novel tyrosine protein kinase receptor expressed during mouse neural development."
Klein R., Parada L.F., Coulier F., Barbacid M.
EMBO J. 8:3701-3709(1989) [PubMed: 2555172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GP145-TRKB).
Tissue: Brain.
[2]"The trkB tyrosine protein kinase gene codes for a second neurogenic receptor that lacks the catalytic kinase domain."
Klein R., Conway D., Parada L.F., Barbacid M.
Cell 61:647-656(1990) [PubMed: 2160854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GP145-TRKB AND GP95-TRKB).
Tissue: Brain.
[3]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GP145-TRKB AND GP95-TRKB).
Strain: C57BL/6J and NOD.
Tissue: Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GP95-TRKB).
Strain: C57BL/6.
Tissue: Brain.
[5]"TrkB variants with deletions in the leucine-rich motifs of the extracellular domain."
Ninkina N., Grashchuck M., Buchman V.L., Davies A.M.
J. Biol. Chem. 272:13019-13025(1997) [PubMed: 9148911] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS L1 AND L10).
Tissue: Trigeminal ganglion.
[6]"The neurotrophic factors brain-derived neurotrophic factor and neurotrophin-3 are ligands for the trkB tyrosine kinase receptor."
Soppet D., Escandon E., Maragos J., Middlemas D.S., Reid S.W., Blair J., Burton L.E., Stanton B.R., Kaplan D.R., Hunter T., Nicolics K., Parada L.F.
Cell 65:895-903(1991) [PubMed: 1645620] [Abstract]
Cited for: FUNCTION IN BDNF AND NTF3 SIGNALING.
[7]"Targeted disruption of the trkB neurotrophin receptor gene results in nervous system lesions and neonatal death."
Klein R., Smeyne R.J., Wurst W., Long L.K., Auerbach B.A., Joyner A.L., Barbacid M.
Cell 75:113-122(1993) [PubMed: 8402890] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]"Characterization of neurotrophin and Trk receptor functions in developing sensory ganglia: direct NT-3 activation of TrkB neurons in vivo."
Farinas I., Wilkinson G.A., Backus C., Reichardt L.F., Patapoutian A.
Neuron 21:325-334(1998) [PubMed: 9728914] [Abstract]
Cited for: FUNCTION IN NTF3-MEDIATED NEURON SURVIVAL.
[9]"Essential role for TrkB receptors in hippocampus-mediated learning."
Minichiello L., Korte M., Wolfer D., Kuehn R., Unsicker K., Cestari V., Rossi-Arnaud C., Lipp H.P., Bonhoeffer T., Klein R.
Neuron 24:401-414(1999) [PubMed: 10571233] [Abstract]
Cited for: FUNCTION IN LONG-TERM POTENTIATION AND LEARNING.
[10]"Mechanism of TrkB-mediated hippocampal long-term potentiation."
Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M.
Neuron 36:121-137(2002) [PubMed: 12367511] [Abstract]
Cited for: FUNCTION IN LONG-TERM POTENTIATION AND LEARNING, INTERACTION WITH SHC1 AND PLCG1, MUTAGENESIS OF TYR-515 AND TYR-816.
[11]"Regulation of TrkB receptor tyrosine kinase and its internalization by neuronal activity and Ca2+ influx."
Du J., Feng L., Zaitsev E., Je H.S., Liu X.W., Lu B.
J. Cell Biol. 163:385-395(2003) [PubMed: 14581459] [Abstract]
Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION.
[12]"Truncated TrkB-T1 mediates neurotrophin-evoked calcium signalling in glia cells."
Rose C.R., Blum R., Pichler B., Lepier A., Kafitz K.W., Konnerth A.
Nature 426:74-78(2003) [PubMed: 14603320] [Abstract]
Cited for: FUNCTION IN CALCIUM SIGNALING (ISOFORM GP95-TRKB).
[13]"TrkB regulates neocortex formation through the Shc/PLCgamma-mediated control of neuronal migration."
Medina D.L., Sciarretta C., Calella A.M., Von Bohlen Und Halbach O., Unsicker K., Minichiello L.
EMBO J. 23:3803-3814(2004) [PubMed: 15372074] [Abstract]
Cited for: FUNCTION IN NEURONAL MIGRATION AND DIFFERENTIATION.
[14]"Suppression of anoikis and induction of metastasis by the neurotrophic receptor TrkB."
Douma S., Van Laar T., Zevenhoven J., Meuwissen R., Van Garderen E., Peeper D.S.
Nature 430:1034-1039(2004) [PubMed: 15329723] [Abstract]
Cited for: FUNCTION AS A SUPPRESSOR OF ANOIKIS.
[15]"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: 16113645] [Abstract]
Cited for: UBIQUITINATION, ENZYME REGULATION.
[16]"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: 16223723] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH SH2D1A.
[17]"TrkB binds and tyrosine-phosphorylates Tiam1, leading to activation of Rac1 and induction of changes in cellular morphology."
Miyamoto Y., Yamauchi J., Tanoue A., Wu C., Mobley W.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10444-10449(2006) [PubMed: 16801538] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TIAM1, FUNCTION IN CELL DIFFERENTIATION, INTERACTION WITH TIAM1.
[18]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-515, MASS SPECTROMETRY.
Tissue: Brain.
[19]"TrkB (tropomyosin-related kinase B) controls the assembly and maintenance of GABAergic synapses in the cerebellar cortex."
Chen A.I., Nguyen C.N., Copenhagen D.R., Badurek S., Minichiello L., Ranscht B., Reichardt L.F.
J. Neurosci. 31:2769-2780(2011) [PubMed: 21414899] [Abstract]
Cited for: FUNCTION IN SYNAPSE FORMATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M33385 mRNA. Translation: AAA40482.1.
X17647 mRNA. Translation: CAA35636.1.
AK018789 mRNA. Translation: BAB31412.1.
AK147391 mRNA. Translation: BAE27880.1.
AK160789 mRNA. Translation: BAE36012.1.
BC052014 mRNA. Translation: AAH52014.2.
IPIIPI00128360.
IPI00229333.
IPI00229334.
IPI00270098.
PIRA35104.
S06943.
RefSeqNP_001020245.1. NM_001025074.1.
NP_032771.1. NM_008745.2.
UniGeneMm.130054.

3D structure databases

ProteinModelPortalP15209.
SMRP15209. Positions 32-385, 529-811.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5722N.
IntActP15209. 1 interaction.
STRINGP15209.

PTM databases

PhosphoSiteP15209.

Proteomic databases

PRIDEP15209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079828; ENSMUSP00000078757; ENSMUSG00000055254.
ENSMUST00000109838; ENSMUSP00000105464; ENSMUSG00000055254.
ENSMUST00000109839; ENSMUSP00000105465; ENSMUSG00000055254.
ENSMUST00000109840; ENSMUSP00000105466; ENSMUSG00000055254.
GeneID18212.
KEGGmmu:18212.
UCSCuc007qui.1. mouse.

Organism-specific databases

CTD4915.
MGIMGI:97384. Ntrk2.

Phylogenomic databases

eggNOGroNOG12558.
GeneTreeENSGT00590000082855.
HOGENOMHBG402948.
HOVERGENHBG056735.
InParanoidP15209.
OMAKFVAYKA.
OrthoDBEOG4255S6.
PhylomeDBP15209.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressP15209.
BgeeP15209.
CleanExMM_NTRK2.
GenevestigatorP15209.
GermOnlineENSMUSG00000055254. Mus musculus.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000372. LRR-contain_N.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR020455. Tyr_kin_neurotrophic_rcpt_2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR020777. Tyr_kinase_NGF_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
KOK04360.
PfamPF07679. I-set. 2 hits.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTSM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 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

NextBio293608.
SOURCESearch...

Entry information

Entry nameNTRK2_MOUSE
AccessionPrimary (citable) accession number: P15209
Secondary accession number(s): Q3TUF9, Q80WU0, Q91XJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 25, 2012
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents