UniProt ID | NTRK1_HUMAN | |
---|---|---|
UniProt AC | P04629 | |
Protein Name | High affinity nerve growth factor receptor | |
Gene Name | NTRK1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 796 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Early endosome membrane Single-pass type I membrane protein . Late endosome membrane Single-pass type I membrane protein . Rapidly internalized after NGF binding (PubMed:1281417). Internalized |
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Protein Description | Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand. [PubMed: 1850821] | |
Protein Sequence | MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACCPHGSSGLRCTRDGALDSLHHLPGAENLTELYIENQQHLQHLELRDLRGLGELRNLTIVKSGLRFVAPDAFHFTPRLSRLNLSFNALESLSWKTVQGLSLQELVLSGNPLHCSCALRWLQRWEEEGLGGVPEQKLQCHGQGPLAHMPNASCGVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTELEQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGRAEVSVQVNVSFPASVQLHTAVEMHHWCIPFSVDGQPAPSLRWLFNGSVLNETSFIFTEFLEPAANETVRHGCLRLNQPTHVNNGNYTLLAANPFGQASASIMAAFMDNPFEFNPEDPIPVSFSPVDTNSTSGDPVEKKDETPFGVSVAVGLAVFACLFLSTLLLVLNKCGRRNKFGINRPAVLAPEDGLAMSLHFMTLGGSSLSPTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
67 | N-linked_Glycosylation | HHLPGAENLTELYIE CCCCCCCCHHHHHHH | 52.29 | UniProtKB CARBOHYD | |
95 | N-linked_Glycosylation | RGLGELRNLTIVKSG CCCHHHCCEEEEECC | 54.91 | 17196528 | |
121 | N-linked_Glycosylation | TPRLSRLNLSFNALE CCCHHHCCCCHHHHH | 32.31 | 17196528 | |
123 | Phosphorylation | RLSRLNLSFNALESL CHHHCCCCHHHHHCC | 18.51 | - | |
188 | N-linked_Glycosylation | GPLAHMPNASCGVPT CCCCCCCCCCCCCCE | 36.59 | 17196528 | |
202 | N-linked_Glycosylation | TLKVQVPNASVDVGD EEEEECCCCEEECCC | 46.09 | UniProtKB CARBOHYD | |
253 | N-linked_Glycosylation | SLGLTLANVTSDLNR CCCEEEEECCCCCCC | 40.49 | UniProtKB CARBOHYD | |
262 | N-linked_Glycosylation | TSDLNRKNVTCWAEN CCCCCCCCCEEEEEC | 30.97 | 17196528 | |
281 | N-linked_Glycosylation | AEVSVQVNVSFPASV EEEEEEEEEEECCEE | 13.46 | 17196528 | |
318 | N-linked_Glycosylation | PSLRWLFNGSVLNET CCCHHHHCCCCCCCC | 39.39 | UniProtKB CARBOHYD | |
323 | N-linked_Glycosylation | LFNGSVLNETSFIFT HHCCCCCCCCEEEEH | 48.63 | UniProtKB CARBOHYD | |
338 | N-linked_Glycosylation | EFLEPAANETVRHGC HHCHHHCCCHHHCCE | 47.80 | UniProtKB CARBOHYD | |
358 | N-linked_Glycosylation | PTHVNNGNYTLLAAN CCEECCCCEEEEEEC | 28.83 | 17196528 | |
401 | N-linked_Glycosylation | SFSPVDTNSTSGDPV CCCCCCCCCCCCCCC | 38.53 | UniProtKB CARBOHYD | |
482 | Ubiquitination | SLSPTEGKGSGLQGH CCCCCCCCCCCCCCC | 43.61 | 1624673 | |
496 | Phosphorylation | HIIENPQYFSDACVH CCCCCCHHCCHHHHH | 13.30 | 10629055 | |
591 | Phosphorylation | PLLMVFEYMRHGDLN EEEEEEEEHHHCCHH | 6.49 | 25884760 | |
640 | Phosphorylation | QVAAGMVYLAGLHFV HHHHHHHHHHHHHHH | 5.07 | 11159935 | |
672 | Phosphorylation | KIGDFGMSRDIYSTD EECCCCCCCCCEECC | 27.47 | - | |
676 | Phosphorylation | FGMSRDIYSTDYYRV CCCCCCCEECCCEEE | 15.14 | 25884760 | |
677 | Phosphorylation | GMSRDIYSTDYYRVG CCCCCCEECCCEEEC | 18.35 | 25921289 | |
680 | Phosphorylation | RDIYSTDYYRVGGRT CCCEECCCEEECCEE | 8.02 | 15488758 | |
681 | Phosphorylation | DIYSTDYYRVGGRTM CCEECCCEEECCEEE | 11.13 | 25884760 | |
701 | Phosphorylation | MPPESILYRKFTTES CCHHHEEEEEECCHH | 15.30 | 18173729 | |
729 | Phosphorylation | TYGKQPWYQLSNTEA HCCCCCCEECCCCCH | 13.27 | 25884760 | |
757 | Phosphorylation | RACPPEVYAIMRGCW CCCCHHHHHHHCCHH | 6.69 | 16319926 | |
791 | Phosphorylation | LAQAPPVYLDVLG-- HHHCCCEEEECCC-- | 11.71 | 10861667 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
496 | Y | Phosphorylation | Kinase | NTRK1 | P04629 | PhosphoELM |
676 | Y | Phosphorylation | Kinase | NTRK1 | P04629 | PhosphoELM |
680 | Y | Phosphorylation | Kinase | NTRK1 | P04629 | PhosphoELM |
681 | Y | Phosphorylation | Kinase | NTRK1 | P04629 | PhosphoELM |
791 | Y | Phosphorylation | Kinase | NTRK1 | P04629 | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRAF6 | Q9Y4K3 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | NEDD4L | Q96PU5 | PMID:16701206 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NTRK1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of NTRK1_HUMAN !! |
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N-linked Glycosylation | |
Reference | PubMed |
"Structural and mechanistic insights into nerve growth factorinteractions with the TrkA and p75 receptors."; Wehrman T., He X., Raab B., Dukipatti A., Blau H., Garcia K.C.; Neuron 53:25-38(2007). Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 36-382 IN COMPLEX WITH NGF,HOMODIMERIZATION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-95;ASN-121; ASN-188; ASN-262; ASN-281 AND ASN-358. | |
Phosphorylation | |
Reference | PubMed |
"TrkA alternative splicing: a regulated tumor-promoting switch inhuman neuroblastoma."; Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,Mackay A.R.; Cancer Cell 6:347-360(2004). Cited for: FUNCTION IN NEURONAL CELL PROLIFERATION AND DIFFERENTIATION, FUNCTIONIN SIGNALING CASCADE ACTIVATION, NGF-BINDING, SUBCELLULAR LOCATION,ALTERNATIVE SPLICING (ISOFORM TRKA-III), CHARACTERIZATION OF ISOFORMTRKA-III, PHOSPHORYLATION AT TYR-496; TYR-680; TYR-681 AND TYR-791,INTERACTION WITH FRS2; GRB2; PIK3R1; PLCG1; SHC1, GLYCOSYLATION,TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIA. | |
"Trk receptors use redundant signal transduction pathways involvingSHC and PLC-gamma 1 to mediate NGF responses."; Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A.,Kaplan D.R.; Neuron 12:691-705(1994). Cited for: FUNCTION IN NEURONAL DIFFERENTIATION, FUNCTION IN PHOSPHORYLATION OFSHC1 AND PLCG1, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-496; LYS-544AND TYR-791, AND PHOSPHORYLATION AT TYR-496 AND TYR-791. | |
"A Trk nerve growth factor (NGF) receptor point mutation affectinginteraction with phospholipase C-gamma 1 abolishes NGF-promotedperipherin induction but not neurite outgrowth."; Loeb D.M., Stephens R.M., Copeland T.D., Kaplan D.R., Greene L.A.; J. Biol. Chem. 269:8901-8910(1994). Cited for: PHOSPHORYLATION AT TYR-791, INTERACTION WITH PLCG1, AND MUTAGENESIS OFTYR-791. |