UniProt ID | NOTC3_HUMAN | |
---|---|---|
UniProt AC | Q9UM47 | |
Protein Name | Neurogenic locus notch homolog protein 3 | |
Gene Name | NOTCH3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 2321 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein. Notch 3 intracellular domain: Nucleus. Following proteolytical processing NICD is translocated to the nucleus. |
|
Protein Description | Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. [PubMed: 15350543 Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity] | |
Protein Sequence | MGPGARGRRRRRRPMSPPPPPPPVRALPLLLLLAGPGAAAPPCLDGSPCANGGRCTQLPSREAACLCPPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCPRGFRGPDCSLPDPCLSSPCAHGARCSVGPDGRFLCSCPPGYQGRSCRSDVDECRVGEPCRHGGTCLNTPGSFRCQCPAGYTGPLCENPAVPCAPSPCRNGGTCRQSGDLTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNTLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVNGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSTCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCDRNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGTRCESQVDECRSQPCRHGGKCLDLVDKYLCRCPSGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFRCLCPPGSLPPLCLPPSHPCAHEPCSHGICYDAPGGFRCVCEPGWSGPRCSQSLARDACESQPCRAGGTCSSDGMGFHCTCPPGVQGRQCELLSPCTPNPCEHGGRCESAPGQLPVCSCPQGWQGPRCQQDVDECAGPAPCGPHGICTNLAGSFSCTCHGGYTGPSCDQDINDCDPNPCLNGGSCQDGVGSFSCSCLPGFAGPRCARDVDECLSNPCGPGTCTDHVASFTCTCPPGYGGFHCEQDLPDCSPSSCFNGGTCVDGVNSFSCLCRPGYTGAHCQHEADPCLSRPCLHGGVCSAAHPGFRCTCLESFTGPQCQTLVDWCSRQPCQNGGRCVQTGAYCLCPPGWSGRLCDIRSLPCREAAAQIGVRLEQLCQAGGQCVDEDSSHYCVCPEGRTGSHCEQEVDPCLAQPCQHGGTCRGYMGGYMCECLPGYNGDNCEDDVDECASQPCQHGGSCIDLVARYLCSCPPGTLGVLCEINEDDCGPGPPLDSGPRCLHNGTCVDLVGGFRCTCPPGYTGLRCEADINECRSGACHAAHTRDCLQDPGGGFRCLCHAGFSGPRCQTVLSPCESQPCQHGGQCRPSPGPGGGLTFTCHCAQPFWGPRCERVARSCRELQCPVGVPCQQTPRGPRCACPPGLSGPSCRSFPGSPPGASNASCAAAPCLHGGSCRPAPLAPFFRCACAQGWTGPRCEAPAAAPEVSEEPRCPRAACQAKRGDQRCDRECNSPGCGWDGGDCSLSVGDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCHAGGRERTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDAHGQAMVFPYHRPSPGSEPRARRELAPEVIGSVVMLEIDNRLCLQSPENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEPPEPSVPLLPLLVAGAVLLLVILVLGVMVARRKREHSTLWFPEGFSLHKDVASGHKGRREPVGQDALGMKNMAKGESLMGEVATDWMDTECPEAKRLKVEEPGMGAEEAVDCRQWTQHHLVAADIRVAPAMALTPPQGDADADGMDVNVRGPDGFTPLMLASFCGGALEPMPTEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHFANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPPGPHGLGPLLCPPGAFLPGLKAAQSGSKKSRRPPGKAGLGPQGPRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFGGPPASPGGFPLEGPYAAATATAVSLAQLGGPGRAGLGRQPPGGCVLSLGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGTPVSPQERPPPYLAVPGHGEEYPAAGAHSSPPKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSESTPSPATATGAMATTTGALPAQPLPLSVPSSLAQAQTQLGPQPEVTPKRQVLA | |
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 |
---|---|---|---|---|---|
84 | Phosphorylation | QLEDPCHSGPCAGRG CCCCCCCCCCCCCCC | 51.66 | - | |
118 | Phosphorylation | GFRGPDCSLPDPCLS CCCCCCCCCCCCCCC | 50.76 | - | |
125 | Phosphorylation | SLPDPCLSSPCAHGA CCCCCCCCCCCCCCC | 38.66 | - | |
126 | Phosphorylation | LPDPCLSSPCAHGAR CCCCCCCCCCCCCCC | 15.85 | - | |
135 | Phosphorylation | CAHGARCSVGPDGRF CCCCCCCEECCCCCE | 25.26 | - | |
211 | Phosphorylation | SPCRNGGTCRQSGDL CCCCCCCCCCCCCCC | 13.10 | - | |
529 | Phosphorylation | CVDQPDGYECRCAEG CCCCCCCCEECCCCC | 21.16 | - | |
725 | O-linked_Glycosylation | CVCEPGWSGPRCSQS EEECCCCCCCCCCHH | 44.85 | 28657654 | |
1179 | N-linked_Glycosylation | SGPRCLHNGTCVDLV CCCCEEECCEEEECC | 34.22 | UniProtKB CARBOHYD | |
1197 | Phosphorylation | RCTCPPGYTGLRCEA EEECCCCCCCEEEEE | 11.92 | - | |
1198 | O-linked_Glycosylation | CTCPPGYTGLRCEAD EECCCCCCCEEEEEC | 35.34 | 28657654 | |
1219 | Phosphorylation | GACHAAHTRDCLQDP CCCCCCCHHHHHHCC | 24.39 | 30631047 | |
1239 | Phosphorylation | CLCHAGFSGPRCQTV EEEECCCCCCCCCEE | 47.14 | 24719451 | |
1272 | O-linked_Glycosylation | PGPGGGLTFTCHCAQ CCCCCCEEEEEEECC | 21.85 | 28657654 | |
1274 | O-linked_Glycosylation | PGGGLTFTCHCAQPF CCCCEEEEEEECCCC | 8.98 | 28657654 | |
1336 | N-linked_Glycosylation | GSPPGASNASCAAAP CCCCCCCCCCCCCCC | 35.03 | UniProtKB CARBOHYD | |
1438 | N-linked_Glycosylation | LQCWRLFNNSRCDPA HHHHHHHCCCCCCCC | 50.59 | UniProtKB CARBOHYD | |
1632 | Ubiquitination | PLRDVRGEPLEPPEP CCCCCCCCCCCCCCC | 35.83 | 21890473 | |
1672 | Phosphorylation | ARRKREHSTLWFPEG HHHHCCCCCEECCCC | 22.05 | 24719451 | |
1673 | Phosphorylation | RRKREHSTLWFPEGF HHHCCCCCEECCCCC | 29.89 | 24719451 | |
1681 | Phosphorylation | LWFPEGFSLHKDVAS EECCCCCCCCHHHHC | 40.18 | 22617229 | |
1684 | Ubiquitination | PEGFSLHKDVASGHK CCCCCCCHHHHCCCC | 60.22 | 22817900 | |
1705 | Ubiquitination | GQDALGMKNMAKGES CCCHHCCCCHHCCCC | 41.60 | 33845483 | |
1712 | Phosphorylation | KNMAKGESLMGEVAT CCHHCCCCHHHHHHH | 32.12 | 28348404 | |
1733 | Ubiquitination | CPEAKRLKVEEPGMG CCHHHCCCCCCCCCC | 52.19 | 33845483 | |
1769 | Phosphorylation | VAPAMALTPPQGDAD EECCHHCCCCCCCCC | 24.31 | 28555341 | |
1849 | Phosphorylation | ALHLAARYARADAAK HHHHHHHHHHHHHHH | 8.84 | - | |
1896 | Phosphorylation | QILIRNRSTDLDARM HHEEECCCCCCHHHC | 29.80 | 27251275 | |
1897 | Phosphorylation | ILIRNRSTDLDARMA HEEECCCCCCHHHCC | 37.03 | 27251275 | |
1908 | Phosphorylation | ARMADGSTALILAAR HHCCCHHHHHHHHHH | 30.89 | - | |
1971 | Ubiquitination | NKDMQDSKEETPLFL CCCCCCCCCCCCHHH | 68.79 | 29967540 | |
1989 | Ubiquitination | EGSYEAAKLLLDHFA CCCHHHHHHHHHHHH | 46.87 | - | |
2028 | Phosphorylation | VRLLDQPSGPRSPPG HHHHHCCCCCCCCCC | 56.66 | 22617229 | |
2032 | Phosphorylation | DQPSGPRSPPGPHGL HCCCCCCCCCCCCCC | 38.28 | 23663014 | |
2069 | Ubiquitination | KSRRPPGKAGLGPQG CCCCCCCCCCCCCCC | 45.08 | 29967540 | |
2085 | Phosphorylation | RGRGKKLTLACPGPL CCCCCCEEEECCCCC | 22.61 | 26074081 | |
2095 | Phosphorylation | CPGPLADSSVTLSPV CCCCCCCCCCEECCC | 22.54 | 26074081 | |
2096 | Phosphorylation | PGPLADSSVTLSPVD CCCCCCCCCEECCCC | 21.48 | 26074081 | |
2098 | Phosphorylation | PLADSSVTLSPVDSL CCCCCCCEECCCCCC | 24.38 | 26074081 | |
2100 | Phosphorylation | ADSSVTLSPVDSLDS CCCCCEECCCCCCCC | 17.32 | 26074081 | |
2104 | Phosphorylation | VTLSPVDSLDSPRPF CEECCCCCCCCCCCC | 34.02 | 26074081 | |
2107 | Phosphorylation | SPVDSLDSPRPFGGP CCCCCCCCCCCCCCC | 28.27 | 26074081 | |
2117 | Phosphorylation | PFGGPPASPGGFPLE CCCCCCCCCCCCCCC | 29.83 | 26074081 | |
2174 | Methylation | AVPLDWARLPPPAPP EEECCHHHCCCCCCC | 43.40 | 24129315 | |
2200 | Phosphorylation | PQLLNPGTPVSPQER CCCCCCCCCCCCCCC | 23.05 | 26074081 | |
2203 | Phosphorylation | LNPGTPVSPQERPPP CCCCCCCCCCCCCCC | 23.28 | 26074081 | |
2211 | Phosphorylation | PQERPPPYLAVPGHG CCCCCCCCEECCCCC | 17.05 | 26074081 | |
2251 | Phosphorylation | YLTPSPESPEHWASP CCCCCCCCCCCCCCC | 38.68 | 22468782 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NOTC3_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 NOTC3_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00536 | Cerebral autosomal dominant arteriopathy with subcortical infarcts and leucoencephalopathy (CADASIL) | |||||
OMIM Disease | ||||||
125310 | Cerebral arteriopathy with subcortical infarcts and leukoencephalopathy, autosomal dominant (CADASIL) | |||||
615293 | Myofibromatosis, infantile 2 (IMF2) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...