Q63604 (NTRK2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BDNF/NT-3 growth factors receptor
EC=2.7.10.1

Alternative name(s):
Neurotrophic tyrosine kinase receptor type 2
TrkB tyrosine kinase
Short name=Trk-B

Gene names

Name:	Ntrk2
Synonyms:	Trkb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	821 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. May also play a role in neutrophin-dependent calcium signaling in glial cells. Ref.2 Ref.6 Ref.9 Ref.10
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	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. 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. Ref.13
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. Interacts (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2. Interacts with SQSTM1 and KIDINS220. Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein By similarity. Note: Internalized to endosomes upon ligand-binding By similarity. Ref.2
Tissue specificity	Widely expressed in the central and peripheral nervous system. The different forms are differentially expressed in various cell types. Isoform T2 is primarily expressed in neurons.
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. Ref.2 Ref.3 Ref.4 Ref.6 Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 2 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 LRRNT domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern PubMed 21951697. Source: RGD calcium-mediated signaling using intracellular calcium source Inferred from electronic annotation. Source: Compara central nervous system neuron development Inferred from sequence or structural similarity. Source: UniProtKB cerebral cortex development Inferred from sequence or structural similarity. Source: UniProtKB feeding behavior Inferred from electronic annotation. Source: Compara glutamate secretion Inferred from electronic annotation. Source: Compara learning Inferred from sequence or structural similarity. Source: UniProtKB long-term memory Inferred from direct assay PubMed 21136519. Source: RGD long-term synaptic potentiation Inferred from electronic annotation. Source: Compara mechanoreceptor differentiation Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from mutant phenotype Ref.10. Source: UniProtKB neuron migration Inferred from sequence or structural similarity. Source: UniProtKB oligodendrocyte differentiation Inferred from electronic annotation. Source: Compara peripheral nervous system neuron development Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of axonogenesis Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of cell proliferation Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 16983663. Source: RGD protein autophosphorylation Inferred from direct assay Ref.6. Source: UniProtKB regulation of Rac GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of dendrite development Inferred from mutant phenotype PubMed 15654844. Source: RGD regulation of neurotransmitter secretion Inferred from direct assay PubMed 16477614. Source: RGD regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara response to auditory stimulus Inferred from expression pattern PubMed 21034795. Source: RGD retinal rod cell development Inferred from electronic annotation. Source: Compara vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome axon terminus Inferred from direct assay PubMed 18582438. Source: RGD cell surface Inferred from direct assay PubMed 17079678. Source: RGD cytosol Inferred from electronic annotation. Source: Compara endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell excitatory synapse Inferred from direct assay PubMed 17079678. Source: RGD growth cone Inferred from direct assay PubMed 17079678. Source: RGD integral to plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 17079678. Source: RGD postsynaptic density Inferred from direct assay PubMed 11226670PubMed 16477614. Source: RGD presynaptic active zone Inferred from direct assay PubMed 16477614. Source: RGD terminal bouton Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW brain-derived neurotrophic factor binding Inferred from direct assay Ref.2. Source: UniProtKB brain-derived neurotrophic factor-activated receptor activity Inferred from direct assay Ref.2Ref.4. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform GP145-TrkB (identifier: Q63604-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform T1 (identifier: Q63604-2)

Also known as: GP95-TrkB;

The sequence of this isoform differs from the canonical sequence as follows:
     466-476: PASVISNDDDS → FVLFHKIPLDG
     477-821: Missing.

Note: Non-catalytic isoform.

Isoform T2 (identifier: Q63604-3)

The sequence of this isoform differs from the canonical sequence as follows:
     466-474: PASVISNDD → KQKCAYFAS
     475-821: Missing.

Note: Non-catalytic isoform.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	By similarity
	Chain	32 – 821	790	BDNF/NT-3 growth factors receptor		PRO_0000016729
Regions
	Topological domain	32 – 429	398	Extracellular Potential
	Transmembrane	430 – 453	24	Helical; Potential
	Topological domain	454 – 821	368	Cytoplasmic Potential
	Domain	32 – 61	30	LRRNT
	Repeat	92 – 113	22	LRR 1
	Repeat	116 – 137	22	LRR 2
	Domain	148 – 196	49	LRRCT
	Domain	197 – 282	86	Ig-like C2-type 1
	Domain	295 – 365	71	Ig-like C2-type 2
	Domain	537 – 806	270	Protein kinase
	Nucleotide binding	543 – 551	9	ATP By similarity
Sites
	Active site	675	1	Proton acceptor By similarity
	Binding site	571	1	ATP By similarity
	Site	515	1	Interaction with SHC1
	Site	705	1	Interaction with SH2D1A
	Site	816	1	Interaction with PLCG1 By similarity
Amino acid modifications
	Modified residue	515	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	701	1	Phosphotyrosine; by autocatalysis Ref.3
	Modified residue	705	1	Phosphotyrosine; by autocatalysis Ref.3
	Modified residue	706	1	Phosphotyrosine; by autocatalysis Ref.3
	Modified residue	816	1	Phosphotyrosine; by autocatalysis Ref.3
	Glycosylation	67	1	N-linked (GlcNAc...) By similarity
	Glycosylation	95	1	N-linked (GlcNAc...) By similarity
	Glycosylation	121	1	N-linked (GlcNAc...) By similarity
	Glycosylation	178	1	N-linked (GlcNAc...) By similarity
	Glycosylation	205	1	N-linked (GlcNAc...) By similarity
	Glycosylation	241	1	N-linked (GlcNAc...) By similarity
	Glycosylation	254	1	N-linked (GlcNAc...) By similarity
	Glycosylation	280	1	N-linked (GlcNAc...) By similarity
	Glycosylation	325	1	N-linked (GlcNAc...) Potential
	Glycosylation	338	1	N-linked (GlcNAc...) By similarity
	Glycosylation	411	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	32 ↔ 38		By similarity
	Disulfide bond	36 ↔ 45		By similarity
	Disulfide bond	152 ↔ 176		By similarity
	Disulfide bond	154 ↔ 194		By similarity
	Disulfide bond	218 ↔ 266		By similarity
	Disulfide bond	302 ↔ 345		By similarity
Natural variations
	Alternative sequence	466 – 476	11	PASVISNDDDS → FVLFHKIPLDG in isoform T1.		VSP_002910
	Alternative sequence	466 – 474	9	PASVISNDD → KQKCAYFAS in isoform T2.		VSP_002912
	Alternative sequence	475 – 821	347	Missing in isoform T2.		VSP_002913
	Alternative sequence	477 – 821	345	Missing in isoform T1.		VSP_002911
Experimental info
	Mutagenesis	515	1	Y → F: Loss of interaction with SHC1. Ref.9
	Mutagenesis	571	1	K → A: Loss of kinase activity. Ref.6
	Mutagenesis	701	1	Y → F: Loss of autophosphorylation and altered interaction with SHC1 and PLCG1; when associated with F-705 and F-706. Ref.6
	Mutagenesis	705	1	Y → F: Loss of autophosphorylation; when associated with F-701 and F-706. Ref.6 Ref.13
	Mutagenesis	706	1	Y → F: Loss of autophosphorylation; when associated with F-701 and F-705. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform GP145-TrkB [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0DDACDA212CDAA0E	FASTA	821	92,186
	10 20 30 40 50 60 MSPWPRWHGP AMARLWGLCL LVLGFWRASL ACPMSCKCST TRIWCTEPSP GIVAFPRLEP 70 80 90 100 110 120 NSIDPENITE ILIANQKRLE IINEDDVEAY VGLKNLTIVD SGLKFVAYKA FLKNGNLRHI 130 140 150 160 170 180 NFTRNKLTSL SRRHFRHLDL SDLILTGNPF TCSCDIMWLK TLQETKSSPD TQDLYCLNES 190 200 210 220 230 240 SKNTPLANLQ IPNCGLPSAR LAAPNLTVEE GKSVTISCSV 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 VADQTNREHL 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 NIHTLLQNLA KASPVYLDIL G
	Isoform T1 (GP95-TrkB) [UniParc]. Checksum: 79AFCD9CA0AB13A8	FASTA	476	53,212
	10 20 30 40 50 60 MSPWPRWHGP AMARLWGLCL LVLGFWRASL ACPMSCKCST TRIWCTEPSP GIVAFPRLEP 70 80 90 100 110 120 NSIDPENITE ILIANQKRLE IINEDDVEAY VGLKNLTIVD SGLKFVAYKA FLKNGNLRHI 130 140 150 160 170 180 NFTRNKLTSL SRRHFRHLDL SDLILTGNPF TCSCDIMWLK TLQETKSSPD TQDLYCLNES 190 200 210 220 230 240 SKNTPLANLQ IPNCGLPSAR LAAPNLTVEE GKSVTISCSV 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 VADQTNREHL SVYAVVVIAS VVGFCLLVML LLLKLARHSK FGMKGFVLFH KIPLDG
	Isoform T2 [UniParc]. Checksum: 2A6F19237F9F692A	FASTA	474	52,971
	10 20 30 40 50 60 MSPWPRWHGP AMARLWGLCL LVLGFWRASL ACPMSCKCST TRIWCTEPSP GIVAFPRLEP 70 80 90 100 110 120 NSIDPENITE ILIANQKRLE IINEDDVEAY VGLKNLTIVD SGLKFVAYKA FLKNGNLRHI 130 140 150 160 170 180 NFTRNKLTSL SRRHFRHLDL SDLILTGNPF TCSCDIMWLK TLQETKSSPD TQDLYCLNES 190 200 210 220 230 240 SKNTPLANLQ IPNCGLPSAR LAAPNLTVEE GKSVTISCSV 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 VADQTNREHL SVYAVVVIAS VVGFCLLVML LLLKLARHSK FGMKGKQKCA YFAS

References

[1]	"trkB, a neural receptor protein-tyrosine kinase: evidence for a full-length and two truncated receptors." Middlemas D.S., Lindberg R.A., Hunter T. Mol. Cell. Biol. 11:143-153(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Cerebellum.
[2]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN BDNF AND NTF3 SIGNALING, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[3]	"Identification of TrkB autophosphorylation sites and evidence that phospholipase C-gamma 1 is a substrate of the TrkB receptor." Middlemas D.S., Meisenhelder J., Hunter T. J. Biol. Chem. 269:5458-5466(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-701; TYR-705; TYR-706 AND TYR-816.
[4]	"Naturally occurring truncated trkB receptors have dominant inhibitory effects on brain-derived neurotrophic factor signaling." Eide F.F., Vining E.R., Eide B.L., Zang K., Wang X.Y., Reichardt L.F. J. Neurosci. 16:3123-3129(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, HOMODIMERIZATION, AUTOPHOSPHORYLATION.
[5]	"Identification and characterization of novel substrates of Trk receptors in developing neurons." Qian X., Riccio A., Zhang Y., Ginty D.D. Neuron 21:1017-1029(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SH2B1 AND SH2B2.
[6]	"Activation loop tyrosines contribute varying roles to TrkB autophosphorylation and signal transduction." McCarty J.H., Feinstein S.C. Oncogene 16:1691-1700(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF SHC1 AND PLCG1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1; PLCG1 AND PLCG2, MUTAGENESIS OF LYS-571; TYR-701; TYR-705 AND TYR-706.
[7]	"Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR." Bibel M., Hoppe E., Barde Y.A. EMBO J. 18:616-622(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NGFR.
[8]	"The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation." Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M. J. Biol. Chem. 274:9861-9870(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FRS2.
[9]	"Brain-derived neurotrophic factor induces phosphorylation of fibroblast growth factor receptor substrate 2." Easton J.B., Moody N.M., Zhu X., Middlemas D.S. J. Biol. Chem. 274:11321-11327(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-515.
[10]	"The TrkB-Shc site signals neuronal survival and local axon growth via MEK and P13-kinase." Atwal J.K., Massie B., Miller F.D., Kaplan D.R. Neuron 27:265-277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN AXONOGENESIS AND NEURON SURVIVAL.
[11]	"Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling." Geetha T., Wooten M.W. J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SQSTM1.
[12]	"A unique pathway for sustained neurotrophin signaling through an ankyrin-rich membrane-spanning protein." Arevalo J.C., Yano H., Teng K.K., Chao M.V. EMBO J. 23:2358-2368(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIDINS220.
[13]	"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, MUTAGENESIS OF TYR-705.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55291 mRNA. Translation: AAA42279.1. M55292 mRNA. Translation: AAA42280.1. M55293 mRNA. Translation: AAA42281.1.
IPI	IPI00210944. IPI00231143. IPI00231144.
PIR	A39667. B39667. C39667.
RefSeq	NP_001156640.1. NM_001163168.2. NP_036863.1. NM_012731.2.
UniGene	Rn.11246.
3D structure databases
ProteinModelPortal	Q63604.
SMR	Q63604. Positions 283-385.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5717N.
MINT	MINT-1204365.
PTM databases
PhosphoSite	Q63604.
Proteomic databases
PaxDb	Q63604.
PRIDE	Q63604.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000042145; ENSRNOP00000045635; ENSRNOG00000018839.
GeneID	25054.
KEGG	rno:25054.
UCSC	RGD:3213. rat.
Organism-specific databases
CTD	4915.
RGD	3213. Ntrk2.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104172.
HOGENOM	HOG000264255.
HOVERGEN	HBG056735.
InParanoid	Q63604.
KO	K04360.
OMA	YGKDERQ.
OrthoDB	EOG4255S6.
Enzyme and pathway databases
BRENDA	2.7.10.1. 5301.
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
ArrayExpress	Q63604.
Genevestigator	Q63604.
GermOnline	ENSRNOG00000018839. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.40.10. 2 hits.
InterPro	IPR000483. Cys-rich_flank_reg_C. IPR007110. Ig-like_dom. 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_cat_dom. 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]
Pfam	PF07679. I-set. 2 hits. PF01462. LRRNT. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR01939. NTKRECEPTOR. PR01941. NTKRECEPTOR2. PR00109. TYRKINASE.
SMART	SM00408. IGc2. 1 hit. SM00082. LRRCT. 1 hit. SM00013. LRRNT. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1795111.
NextBio	605258.

Entry information

Entry name

NTRK2_RAT

Accession

Primary (citable) accession number: Q63604
Secondary accession number(s): Q63605, Q63606

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program