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Q16620

- NTRK2_HUMAN

UniProt

Q16620 - NTRK2_HUMAN

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Protein

BDNF/NT-3 growth factors receptor

Gene

NTRK2

Organism
Homo sapiens (Human)
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 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 and mediate communication between neurons and glia.1 Publication

Catalytic activityi

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

Enzyme regulationi

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei516 – 5161Interaction with SHC1By similarity
Binding sitei572 – 5721ATPPROSITE-ProRule annotation
Active sitei676 – 6761Proton acceptorPROSITE-ProRule annotation
Sitei706 – 7061Interaction with SH2D1ABy similarity
Sitei817 – 8171Interaction with PLCG1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi544 – 5529ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. brain-derived neurotrophic factor-activated receptor activity Source: UniProtKB
  3. brain-derived neurotrophic factor binding Source: UniProtKB
  4. neurotrophin binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. activation of adenylate cyclase activity Source: Reactome
  2. aging Source: Ensembl
  3. brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  4. calcium-mediated signaling using intracellular calcium source Source: Ensembl
  5. central nervous system neuron development Source: UniProtKB
  6. cerebral cortex development Source: UniProtKB
  7. circadian rhythm Source: Ensembl
  8. feeding behavior Source: Ensembl
  9. glutamate secretion Source: Ensembl
  10. learning Source: UniProtKB
  11. long-term memory Source: Ensembl
  12. long-term synaptic potentiation Source: Ensembl
  13. mechanoreceptor differentiation Source: Ensembl
  14. negative regulation of anoikis Source: Ensembl
  15. negative regulation of neuron apoptotic process Source: UniProtKB
  16. neuromuscular junction development Source: Ensembl
  17. neuron differentiation Source: UniProtKB
  18. neuron migration Source: UniProtKB
  19. neurotrophin TRK receptor signaling pathway Source: Reactome
  20. oligodendrocyte differentiation Source: Ensembl
  21. peripheral nervous system neuron development Source: Ensembl
  22. positive regulation of axonogenesis Source: UniProtKB
  23. positive regulation of cell proliferation Source: UniProtKB
  24. positive regulation of gene expression Source: UniProtKB
  25. positive regulation of MAPK cascade Source: UniProtKB
  26. positive regulation of neuron projection development Source: UniProtKB
  27. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  28. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  29. protein autophosphorylation Source: UniProtKB
  30. regulation of dendrite development Source: Ensembl
  31. regulation of neurotransmitter secretion Source: Ensembl
  32. regulation of protein kinase B signaling Source: Ensembl
  33. regulation of Rac GTPase activity Source: UniProtKB
  34. response to auditory stimulus Source: Ensembl
  35. retinal rod cell development Source: Ensembl
  36. transmembrane receptor protein tyrosine kinase signaling pathway Source: Reactome
  37. vasculogenesis Source: Ensembl
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

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_11046. NGF-independant TRKA activation.
SignaLinkiQ16620.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
BDNF/NT-3 growth factors receptor (EC:2.7.10.1)
Alternative name(s):
GP145-TrkB
Short name:
Trk-B
Neurotrophic tyrosine kinase receptor type 2
TrkB tyrosine kinase
Tropomyosin-related kinase B
Gene namesi
Name:NTRK2
Synonyms:TRKB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:8032. NTRK2.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytosol Source: Ensembl
  3. dendritic spine Source: Ensembl
  4. endosome Source: UniProtKB-KW
  5. excitatory synapse Source: Ensembl
  6. growth cone Source: Ensembl
  7. integral component of plasma membrane Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. neuronal postsynaptic density Source: Ensembl
  10. postsynaptic membrane Source: Ensembl
  11. presynaptic active zone Source: Ensembl
  12. receptor complex Source: MGI
  13. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Obesity hyperphagia and developmental delay (OHPDD) [MIM:613886]: A disorder characterized by early-onset obesity, hyperphagia, and severe developmental delay in motor function, speech, and language.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti706 – 7061Y → C in OHPDD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation. 1 Publication
VAR_065890

Keywords - Diseasei

Disease mutation, Obesity

Organism-specific databases

MIMi613886. phenotype.
Orphaneti251612. Pilocytic astrocytoma.
PharmGKBiPA31818.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 822791BDNF/NT-3 growth factors receptorPRO_0000016727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 381 PublicationPROSITE-ProRule annotation
Disulfide bondi36 ↔ 451 PublicationPROSITE-ProRule annotation
Glycosylationi67 – 671N-linked (GlcNAc...)2 Publications
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
Glycosylationi121 – 1211N-linked (GlcNAc...)2 Publications
Disulfide bondi152 ↔ 1761 PublicationPROSITE-ProRule annotation
Disulfide bondi154 ↔ 1941 PublicationPROSITE-ProRule annotation
Glycosylationi178 – 1781N-linked (GlcNAc...)1 Publication
Glycosylationi205 – 2051N-linked (GlcNAc...)1 Publication
Disulfide bondi218 ↔ 2661 PublicationPROSITE-ProRule annotation
Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
Glycosylationi254 – 2541N-linked (GlcNAc...)2 Publications
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
Disulfide bondi302 ↔ 3451 PublicationPROSITE-ProRule annotation
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)1 Publication
Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
Modified residuei516 – 5161Phosphotyrosine; by autocatalysisBy similarity
Modified residuei702 – 7021Phosphotyrosine; by autocatalysisBy similarity
Modified residuei706 – 7061Phosphotyrosine; by autocatalysisBy similarity
Modified residuei707 – 7071Phosphotyrosine; by autocatalysisBy similarity
Modified residuei817 – 8171Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Isoform TrkB-T-Shc is not phosphorylated.1 Publication
Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ16620.
PRIDEiQ16620.

PTM databases

PhosphoSiteiQ16620.

Expressioni

Tissue specificityi

Isoform TrkB is expressed in the central and peripheral nervous system. In the central nervous system (CNS), expression is observed in the cerebral cortex, hippocampus, thalamus, choroid plexus, granular layer of the cerebellum, brain stem, and spinal cord. In the peripheral nervous system, it is expressed in many cranial ganglia, the ophthalmic nerve, the vestibular system, multiple facial structures, the submaxillary glands, and dorsal root ganglia. Isoform TrkB-T1 is mainly expressed in the brain but also detected in other tissues including pancreas, kidney and heart. Isoform TrkB-T-Shc is predominantly expressed in the brain.2 Publications

Developmental stagei

Widely expressed in fetal brain.1 Publication

Gene expression databases

BgeeiQ16620.
CleanExiHS_NTRK2.
ExpressionAtlasiQ16620. baseline and differential.
GenevestigatoriQ16620.

Organism-specific databases

HPAiCAB010346.
HPA007637.

Interactioni

Subunit structurei

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 (By similarity). Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway.By similarity2 Publications

Protein-protein interaction databases

BioGridi110970. 24 interactions.
DIPiDIP-5720N.
IntActiQ16620. 7 interactions.
MINTiMINT-156841.
STRINGi9606.ENSP00000277120.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi286 – 2927
Beta strandi300 – 3089
Beta strandi314 – 3196
Beta strandi322 – 3243
Beta strandi328 – 33710
Beta strandi339 – 35012
Helixi353 – 3553
Beta strandi357 – 3648
Beta strandi369 – 3768
Beta strandi500 – 5034
Beta strandi506 – 5127
Turni515 – 5173
Helixi535 – 5373
Beta strandi538 – 5458
Beta strandi552 – 5576
Beta strandi567 – 5748
Helixi579 – 59214
Beta strandi603 – 6075
Beta strandi609 – 61810
Helixi625 – 6317
Helixi634 – 6385
Beta strandi641 – 6433
Helixi650 – 66920
Helixi679 – 6813
Beta strandi682 – 6843
Helixi686 – 6883
Beta strandi690 – 6923
Helixi698 – 7014
Helixi703 – 7053
Beta strandi707 – 7093
Turni710 – 7123
Beta strandi713 – 7153
Helixi717 – 7193
Helixi722 – 7276
Helixi732 – 74716
Turni748 – 7503
Turni753 – 7564
Helixi759 – 76810
Helixi780 – 78910
Helixi794 – 7963
Helixi800 – 81314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HCFX-ray2.70X/Y286-383[»]
1WWBX-ray2.10X283-385[»]
2MFQNMR-B497-519[»]
4ASZX-ray1.70A527-822[»]
4AT3X-ray1.77A527-822[»]
4AT4X-ray2.36A527-822[»]
4AT5X-ray1.71A527-822[»]
ProteinModelPortaliQ16620.
SMRiQ16620. Positions 31-385, 527-822.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16620.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 430399ExtracellularSequence AnalysisAdd
BLAST
Topological domaini455 – 822368CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei431 – 45424HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 6130LRRNTAdd
BLAST
Repeati92 – 11322LRR 1Add
BLAST
Repeati116 – 13722LRR 2Add
BLAST
Domaini148 – 19649LRRCTAdd
BLAST
Domaini197 – 28286Ig-like C2-type 1Add
BLAST
Domaini295 – 36571Ig-like C2-type 2Add
BLAST
Domaini538 – 807270Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 2 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000264255.
HOVERGENiHBG056735.
InParanoidiQ16620.
KOiK04360.
OMAiCEIMWIK.
OrthoDBiEOG7QG43C.
PhylomeDBiQ16620.
TreeFamiTF106465.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
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.
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]
PfamiPF07679. I-set. 2 hits.
PF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTiSM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 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]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform TrkB (identifier: Q16620-1) [UniParc]FASTAAdd to Basket

Also known as: gp145-TrkB

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.

« Hide

        10         20         30         40         50
MSSWIRWHGP AMARLWGFCW LVVGFWRAAF ACPTSCKCSA SRIWCSDPSP
60 70 80 90 100
GIVAFPRLEP NSVDPENITE IFIANQKRLE IINEDDVEAY VGLRNLTIVD
110 120 130 140 150
SGLKFVAHKA FLKNSNLQHI NFTRNKLTSL SRKHFRHLDL SELILVGNPF
160 170 180 190 200
TCSCDIMWIK TLQEAKSSPD TQDLYCLNES SKNIPLANLQ IPNCGLPSAN
210 220 230 240 250
LAAPNLTVEE GKSITLSCSV AGDPVPNMYW DVGNLVSKHM NETSHTQGSL
260 270 280 290 300
RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH
310 320 330 340 350
WCIPFTVKGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN
360 370 380 390 400
PTHMNNGDYT LIAKNEYGKD EKQISAHFMG WPGIDDGANP NYPDVIYEDY
410 420 430 440 450
GTAANDIGDT TNRSNEIPST DVTDKTGREH LSVYAVVVIA SVVGFCLLVM
460 470 480 490 500
LFLLKLARHS KFGMKGPASV ISNDDDSASP LHHISNGSNT PSSSEGGPDA
510 520 530 540 550
VIIGMTKIPV IENPQYFGIT NSQLKPDTFV QHIKRHNIVL KRELGEGAFG
560 570 580 590 600
KVFLAECYNL CPEQDKILVA VKTLKDASDN ARKDFHREAE LLTNLQHEHI
610 620 630 640 650
VKFYGVCVEG DPLIMVFEYM KHGDLNKFLR AHGPDAVLMA EGNPPTELTQ
660 670 680 690 700
SQMLHIAQQI AAGMVYLASQ HFVHRDLATR NCLVGENLLV KIGDFGMSRD
710 720 730 740 750
VYSTDYYRVG GHTMLPIRWM PPESIMYRKF TTESDVWSLG VVLWEIFTYG
760 770 780 790 800
KQPWYQLSNN EVIECITQGR VLQRPRTCPQ EVYELMLGCW QREPHMRKNI
810 820
KGIHTLLQNL AKASPVYLDI LG
Length:822
Mass (Da):91,999
Last modified:November 1, 1996 - v1
Checksum:i2FEB9159948F0D13
GO
Isoform TrkB-T1 (identifier: Q16620-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     467-477: PASVISNDDDS → FVLFHKIPLDG
     478-822: Missing.

Note: Non-catalytic isoform.

Show »
Length:477
Mass (Da):53,051
Checksum:iC4A7F565BC88372F
GO
Isoform TrkB-T-Shc (identifier: Q16620-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     529-537: FVQHIKRHN → WPRGSPKTA
     538-822: Missing.

Show »
Length:537
Mass (Da):59,167
Checksum:i5A8FA252A3871CC1
GO
Isoform 4 (identifier: Q16620-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     465-465: K → KDFSWFGFGKVKSRQGV

Show »
Length:838
Mass (Da):93,826
Checksum:i130C95A9D8895432
GO
Isoform 5 (identifier: Q16620-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     465-465: K → KDFSWFGFGKVKSRQGV
     529-537: FVQHIKRHN → WPRGSPKTA
     538-822: Missing.

Show »
Length:553
Mass (Da):60,994
Checksum:iBD98221B9EE1A6C1
GO
Isoform TrkB-T-TK (identifier: Q16620-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     710-735: GGHTMLPIRWMPPESIMYRKFTTESD → SSCADQRPQGPLSLRDPCCICLLRLS
     736-822: Missing.

Show »
Length:735
Mass (Da):81,569
Checksum:i5E0746BCCA281069
GO
Isoform TrkB-N-T1 (identifier: Q16620-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-156: Missing.
     467-477: PASVISNDDDS → FVLFHKIPLDG
     478-822: Missing.

Show »
Length:321
Mass (Da):35,332
Checksum:i64C146AAB494744E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381L → F in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041470
Natural varianti309 – 3091G → R.1 Publication
VAR_016320
Natural varianti338 – 3381N → Y.
Corresponds to variant rs1047856 [ dbSNP | Ensembl ].
VAR_011973
Natural varianti545 – 5451G → V.
Corresponds to variant rs1075108 [ dbSNP | Ensembl ].
VAR_049715
Natural varianti697 – 6971M → I in a lung carcinoma sample; somatic mutation. 1 Publication
VAR_046518
Natural varianti699 – 6991R → G in a lung carcinoma sample; somatic mutation. 1 Publication
VAR_046519
Natural varianti706 – 7061Y → C in OHPDD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation. 1 Publication
VAR_065890
Natural varianti718 – 7181R → C in a lung carcinoma sample; somatic mutation. 1 Publication
VAR_046520

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 156156Missing in isoform TrkB-N-T1. 1 PublicationVSP_042177Add
BLAST
Alternative sequencei465 – 4651K → KDFSWFGFGKVKSRQGV in isoform 4 and isoform 5. 1 PublicationVSP_041942
Alternative sequencei467 – 47711PASVISNDDDS → FVLFHKIPLDG in isoform TrkB-T1 and isoform TrkB-N-T1. 6 PublicationsVSP_002901Add
BLAST
Alternative sequencei478 – 822345Missing in isoform TrkB-T1 and isoform TrkB-N-T1. 6 PublicationsVSP_002902Add
BLAST
Alternative sequencei529 – 5379FVQHIKRHN → WPRGSPKTA in isoform TrkB-T-Shc and isoform 5. 1 PublicationVSP_002903
Alternative sequencei538 – 822285Missing in isoform TrkB-T-Shc and isoform 5. 1 PublicationVSP_002904Add
BLAST
Alternative sequencei710 – 73526GGHTM…TTESD → SSCADQRPQGPLSLRDPCCI CLLRLS in isoform TrkB-T-TK. 1 PublicationVSP_042178Add
BLAST
Alternative sequencei736 – 82287Missing in isoform TrkB-T-TK. 1 PublicationVSP_042179Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12140 mRNA. Translation: AAC51371.1.
S76473 mRNA. Translation: AAB33109.1.
S76474 mRNA. Translation: AAB33110.1.
X75958 mRNA. Translation: CAA53571.1.
AF410899 mRNA. Translation: AAL67965.1.
AF410900 mRNA. Translation: AAL67966.1.
AF410901 mRNA. Translation: AAL67967.1.
AF508964 mRNA. Translation: AAM77876.1.
AB209118 mRNA. Translation: BAD92355.1.
AK294285 mRNA. Translation: BAG57570.1.
AL445532, AL390777, AL596132 Genomic DNA. Translation: CAH71816.1.
AL390777, AL596132 Genomic DNA. Translation: CAH72193.1.
AL390777, AL596132 Genomic DNA. Translation: CAH72194.1.
AL390777, AL445532, AL596132 Genomic DNA. Translation: CAH72195.1.
AL596132, AL390777 Genomic DNA. Translation: CAH72313.1.
AL596132, AL390777 Genomic DNA. Translation: CAH72314.1.
AL596132, AL390777, AL445532 Genomic DNA. Translation: CAH72316.1.
CH471089 Genomic DNA. Translation: EAW62688.1.
BC031835 mRNA. Translation: AAH31835.1.
CCDSiCCDS35050.1. [Q16620-1]
CCDS35051.1. [Q16620-5]
CCDS35052.1. [Q16620-3]
CCDS35053.1. [Q16620-2]
CCDS6671.1. [Q16620-4]
PIRiA56853.
I73631.
RefSeqiNP_001007098.1. NM_001007097.2. [Q16620-2]
NP_001018074.1. NM_001018064.2. [Q16620-1]
NP_001018075.1. NM_001018065.2. [Q16620-5]
NP_001018076.1. NM_001018066.2. [Q16620-3]
NP_006171.2. NM_006180.4. [Q16620-4]
XP_005252058.1. XM_005252001.1. [Q16620-4]
XP_005252060.1. XM_005252003.1. [Q16620-4]
XP_005252061.1. XM_005252004.1. [Q16620-4]
XP_005252063.1. XM_005252006.2. [Q16620-5]
XP_005252064.1. XM_005252007.1. [Q16620-2]
UniGeneiHs.494312.
Hs.712776.

Genome annotation databases

EnsembliENST00000277120; ENSP00000277120; ENSG00000148053. [Q16620-4]
ENST00000304053; ENSP00000306167; ENSG00000148053. [Q16620-5]
ENST00000323115; ENSP00000314586; ENSG00000148053. [Q16620-1]
ENST00000359847; ENSP00000352906; ENSG00000148053. [Q16620-2]
ENST00000376208; ENSP00000365381; ENSG00000148053. [Q16620-3]
ENST00000376213; ENSP00000365386; ENSG00000148053. [Q16620-1]
ENST00000376214; ENSP00000365387; ENSG00000148053. [Q16620-4]
ENST00000395882; ENSP00000379221; ENSG00000148053. [Q16620-2]
GeneIDi4915.
KEGGihsa:4915.
UCSCiuc004any.1. human. [Q16620-6]
uc004anz.1. human. [Q16620-4]
uc004aoa.1. human. [Q16620-1]
uc011lsz.2. human. [Q16620-5]
uc011lta.2. human. [Q16620-3]
uc011ltb.1. human. [Q16620-7]

Polymorphism databases

DMDMi2497560.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12140 mRNA. Translation: AAC51371.1 .
S76473 mRNA. Translation: AAB33109.1 .
S76474 mRNA. Translation: AAB33110.1 .
X75958 mRNA. Translation: CAA53571.1 .
AF410899 mRNA. Translation: AAL67965.1 .
AF410900 mRNA. Translation: AAL67966.1 .
AF410901 mRNA. Translation: AAL67967.1 .
AF508964 mRNA. Translation: AAM77876.1 .
AB209118 mRNA. Translation: BAD92355.1 .
AK294285 mRNA. Translation: BAG57570.1 .
AL445532 , AL390777 , AL596132 Genomic DNA. Translation: CAH71816.1 .
AL390777 , AL596132 Genomic DNA. Translation: CAH72193.1 .
AL390777 , AL596132 Genomic DNA. Translation: CAH72194.1 .
AL390777 , AL445532 , AL596132 Genomic DNA. Translation: CAH72195.1 .
AL596132 , AL390777 Genomic DNA. Translation: CAH72313.1 .
AL596132 , AL390777 Genomic DNA. Translation: CAH72314.1 .
AL596132 , AL390777 , AL445532 Genomic DNA. Translation: CAH72316.1 .
CH471089 Genomic DNA. Translation: EAW62688.1 .
BC031835 mRNA. Translation: AAH31835.1 .
CCDSi CCDS35050.1. [Q16620-1 ]
CCDS35051.1. [Q16620-5 ]
CCDS35052.1. [Q16620-3 ]
CCDS35053.1. [Q16620-2 ]
CCDS6671.1. [Q16620-4 ]
PIRi A56853.
I73631.
RefSeqi NP_001007098.1. NM_001007097.2. [Q16620-2 ]
NP_001018074.1. NM_001018064.2. [Q16620-1 ]
NP_001018075.1. NM_001018065.2. [Q16620-5 ]
NP_001018076.1. NM_001018066.2. [Q16620-3 ]
NP_006171.2. NM_006180.4. [Q16620-4 ]
XP_005252058.1. XM_005252001.1. [Q16620-4 ]
XP_005252060.1. XM_005252003.1. [Q16620-4 ]
XP_005252061.1. XM_005252004.1. [Q16620-4 ]
XP_005252063.1. XM_005252006.2. [Q16620-5 ]
XP_005252064.1. XM_005252007.1. [Q16620-2 ]
UniGenei Hs.494312.
Hs.712776.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HCF X-ray 2.70 X/Y 286-383 [» ]
1WWB X-ray 2.10 X 283-385 [» ]
2MFQ NMR - B 497-519 [» ]
4ASZ X-ray 1.70 A 527-822 [» ]
4AT3 X-ray 1.77 A 527-822 [» ]
4AT4 X-ray 2.36 A 527-822 [» ]
4AT5 X-ray 1.71 A 527-822 [» ]
ProteinModelPortali Q16620.
SMRi Q16620. Positions 31-385, 527-822.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110970. 24 interactions.
DIPi DIP-5720N.
IntActi Q16620. 7 interactions.
MINTi MINT-156841.
STRINGi 9606.ENSP00000277120.

Chemistry

BindingDBi Q16620.
ChEMBLi CHEMBL4898.
DrugBanki DB00321. Amitriptyline.
GuidetoPHARMACOLOGYi 1818.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q16620.

Polymorphism databases

DMDMi 2497560.

Proteomic databases

PaxDbi Q16620.
PRIDEi Q16620.

Protocols and materials databases

DNASUi 4915.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000277120 ; ENSP00000277120 ; ENSG00000148053 . [Q16620-4 ]
ENST00000304053 ; ENSP00000306167 ; ENSG00000148053 . [Q16620-5 ]
ENST00000323115 ; ENSP00000314586 ; ENSG00000148053 . [Q16620-1 ]
ENST00000359847 ; ENSP00000352906 ; ENSG00000148053 . [Q16620-2 ]
ENST00000376208 ; ENSP00000365381 ; ENSG00000148053 . [Q16620-3 ]
ENST00000376213 ; ENSP00000365386 ; ENSG00000148053 . [Q16620-1 ]
ENST00000376214 ; ENSP00000365387 ; ENSG00000148053 . [Q16620-4 ]
ENST00000395882 ; ENSP00000379221 ; ENSG00000148053 . [Q16620-2 ]
GeneIDi 4915.
KEGGi hsa:4915.
UCSCi uc004any.1. human. [Q16620-6 ]
uc004anz.1. human. [Q16620-4 ]
uc004aoa.1. human. [Q16620-1 ]
uc011lsz.2. human. [Q16620-5 ]
uc011lta.2. human. [Q16620-3 ]
uc011ltb.1. human. [Q16620-7 ]

Organism-specific databases

CTDi 4915.
GeneCardsi GC09P087283.
HGNCi HGNC:8032. NTRK2.
HPAi CAB010346.
HPA007637.
MIMi 600456. gene.
613886. phenotype.
neXtProti NX_Q16620.
Orphaneti 251612. Pilocytic astrocytoma.
PharmGKBi PA31818.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000264255.
HOVERGENi HBG056735.
InParanoidi Q16620.
KOi K04360.
OMAi CEIMWIK.
OrthoDBi EOG7QG43C.
PhylomeDBi Q16620.
TreeFami TF106465.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_11046. NGF-independant TRKA activation.
SignaLinki Q16620.

Miscellaneous databases

EvolutionaryTracei Q16620.
GeneWikii TrkB_receptor.
GenomeRNAii 4915.
NextBioi 18915.
PROi Q16620.
SOURCEi Search...

Gene expression databases

Bgeei Q16620.
CleanExi HS_NTRK2.
ExpressionAtlasi Q16620. baseline and differential.
Genevestigatori Q16620.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi 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.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR000719. Prot_kinase_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 ]
Pfami PF07679. I-set. 2 hits.
PF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTi SM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 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. "Cloning and chromosomal localization of the human TRK-B tyrosine kinase receptor gene (NTRK2)."
    Nakagawara A., Liu X.-G., Ikegaki N., White P.S., Yamashiro D.J., Nycum L.M., Biegel J.A., Brodeur G.M.
    Genomics 25:538-546(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB).
    Tissue: Hippocampus.
  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 TRKB AND TRKB-T1).
    Tissue: Brain.
  3. "Cloning of a non-catalytic form of human trkB and distribution of messenger RNA for trkB in human brain."
    Allen S.J., Dawbarn D., Eckford S.D., Wilcock G.K., Ashcroft M., Colebrook S.M., Feeney R., Macgowan S.H.
    Neuroscience 60:825-834(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB-T1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Hippocampus.
  4. "Analysis of the human TrkB gene genomic organization reveals novel TrkB isoforms, unusual gene length, and splicing mechanism."
    Stoilov P., Castren E., Stamm S.
    Biochem. Biophys. Res. Commun. 290:1054-1065(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TRKB; TRKB-T1; TRKB-T-SHC; 4 AND 5), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "Full length truncated TrkB sequence identified in a screen for genes regulated by ischemic preconditioning."
    Steinbeck J.A., Thomsen S., Wessig J., Leypoldt F., Lewerenz J., Methner A.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB-T1), VARIANT ARG-309.
  6. "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.
    , 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 TRKB-N-T1).
    Tissue: Amygdala.
  7. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKB-T-TK).
    Tissue: Brain.
  8. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKB-T1).
    Tissue: Brain.
  11. "Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding."
    Haniu M., Talvenheimo J., Le J., Katta V., Welcher A., Rohde M.F.
    Arch. Biochem. Biophys. 322:256-264(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-95; ASN-121; ASN-178; ASN-205; ASN-241; ASN-254; ASN-280; ASN-338 AND ASN-412.
  12. "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.
  13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67; ASN-121 AND ASN-254.
    Tissue: Plasma.
  14. "Human TrkB gene: novel alternative transcripts, protein isoforms and expression pattern in the prefrontal cerebral cortex during postnatal development."
    Luberg K., Wong J., Weickert C.S., Timmusk T.
    J. Neurochem. 113:952-964(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS TRKB-T-TK AND TRKB-N-T1).
  15. "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 (2.1 ANGSTROMS) OF 283-385.
  16. "Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5."
    Banfield M.J., Naylor R.L., Robertson A.G., Allen S.J., Dawbarn D., Brady R.L.
    Structure 9:1191-1199(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 284-383 IN COMPLEX WITH NTF4.
  17. "A de novo mutation affecting human TrkB associated with severe obesity and developmental delay."
    Yeo G.S., Connie Hung C.C., Rochford J., Keogh J., Gray J., Sivaramakrishnan S., O'Rahilly S., Farooqi I.S.
    Nat. Neurosci. 7:1187-1189(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OHPDD CYS-706, CHARACTERIZATION OF VARIANT OHPDD CYS-706, FUNCTION AS A BDNF-ACTIVATED RECEPTOR, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  18. "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.
    , 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: VARIANT [LARGE SCALE ANALYSIS] PHE-138.
  19. "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 ILE-697; GLY-699 AND CYS-718.

Entry informationi

Entry nameiNTRK2_HUMAN
AccessioniPrimary (citable) accession number: Q16620
Secondary accession number(s): B1ANZ4
, B4DFV9, Q16675, Q59GJ1, Q8WXJ5, Q8WXJ6, Q8WXJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Trk also stands for tropomyosin-related kinase since the first Trk was isolated as an oncogenic protein which was the result of a fusion between the tropomyosin gene TPM3 and NTRK1.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3