UniProt ID | NOTC1_HUMAN | |
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UniProt AC | P46531 | |
Protein Name | Neurogenic locus notch homolog protein 1 | |
Gene Name | NOTCH1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 2555 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Notch 1 intracellular domain: Nucleus . Following proteolytical processing NICD is translocated to the nucleus. Nuclear location may require MEGF10. |
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Protein Description | Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. 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. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO).. | |
Protein Sequence | MPPLLAPLLCLALLPALAARGPRCSQPGETCLNGGKCEAANGTEACVCGGAFVGPRCQDPNPCLSTPCKNAGTCHVVDRRGVADYACSCALGFSGPLCLTPLDNACLTNPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGQKPGLCRHGGTCHNEVGSYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFHGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCEIDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVNTDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCRPGYTGHHCETNINECSSQPCRHGGTCQDRDNAYLCFCLKGTTGPNCEINLDDCASSPCDSGTCLDKIDGYECACEPGYTGSMCNINIDECAGNPCHNGGTCEDGINGFTCRCPEGYHDPTCLSEVNECNSNPCVHGACRDSLNGYKCDCDPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINECVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFRGTFCEEDINECASDPCRNGANCTDCVDSYTCTCPAGFSGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQHDVNECDSQPCLHGGTCQDGCGSYRCTCPQGYTGPNCQNLVHWCDSSPCKNGGKCWQTHTQYRCECPSGWTGLYCDVPSVSCEVAAQRQGVDVARLCQHGGLCVDAGNTHHCRCQAGYTGSYCEDLVDECSPSPCQNGATCTDYLGGYSCKCVAGYHGVNCSEEIDECLSHPCQNGGTCLDLPNTYKCSCPRGTQGVHCEINVDDCNPPVDPVSRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDVNECLSNPCDARGTQNCVQRVNDFHCECRAGHTGRRCESVINGCKGKPCKNGGTCAVASNTARGFICKCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGPFTGPECQFPASSPCLGGNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFGGGAGRDIPPPLIEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGREEELRKHPIKRAAEGWAAPDALLGQVKASLLPGGSEGGRRRRELDPMDVRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPLGGTPTLSPPLCSPNGYLGSLKPGVQGKKVRKPSSKGLACGSKEAKDLKARRKKSQDGKGCLLDSSGMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSVPLNHLPGMPDTHLGIGHLNVAAKPEMAALGGGGRLAFETGPPRLSHLPVASGTSTVLGSSSGGALNFTVGGSTSLNGQCEWLSRLQSGMVPNQYNPLRGSVAPGPLSTQAPSLQHGMVGPLHSSLAASALSQMMSYQGLPSTRLATQPHLVQTQQVQPQNLQMQQQNLQPANIQQQQSLQPPPPPPQPHLGVSSAASGHLGRSFLSGEPSQADVQPLGPSSLAVHTILPQESPALPTSLPSSLVPPVTAAQFLTPPSQHSYSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNVSDWSEGVSSPPTSMQSQIARIPEAFK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
41 | N-linked_Glycosylation | GGKCEAANGTEACVC CCCCCCCCCCEEEEE | 66.04 | UniProtKB CARBOHYD | |
65 | O-linked_Glycosylation | QDPNPCLSTPCKNAG CCCCCCCCCCCCCCC | 36.70 | UniProtKB CARBOHYD | |
73 | O-linked_Glycosylation | TPCKNAGTCHVVDRR CCCCCCCCEEEECCC | 9.31 | - | |
116 | O-linked_Glycosylation | NPCRNGGTCDLLTLT CCCCCCCCCCEEEEE | 12.30 | - | |
146 | O-linked_Glycosylation | QQADPCASNPCANGG CCCCCCCCCCCCCCC | 48.28 | UniProtKB CARBOHYD | |
174 | O-linked_Glycosylation | PPSFHGPTCRQDVNE CHHHCCCCCCCCHHH | 25.55 | OGP | |
194 | O-linked_Glycosylation | GLCRHGGTCHNEVGS CCCCCCCCCCCCCCC | 18.38 | - | |
232 | O-linked_Glycosylation | SPCQNGGTCRPTGDV CCCCCCCCCCCCCCC | 13.52 | 24226769 | |
311 | O-linked_Glycosylation | NACQNGGTCHNTHGG CHHHCCCCCCCCCCC | 16.40 | - | |
341 | O-linked_Glycosylation | ENIDDCASAACFHGA CCHHHHHHHHHHCCC | 23.80 | UniProtKB CARBOHYD | |
349 | O-linked_Glycosylation | AACFHGATCHDRVAS HHHHCCCCCCHHHHE | 18.24 | - | |
378 | O-linked_Glycosylation | HLNDACISNPCNEGS ECCCHHCCCCCCCCC | 34.30 | UniProtKB CARBOHYD | |
435 | O-linked_Glycosylation | KCINTLGSFECQCLQ HHHHHCCCEECEECC | 22.45 | 30127001 | |
458 | O-linked_Glycosylation | IDVNECVSNPCQNDA ECHHHHHCCCCCCCC | 46.87 | UniProtKB CARBOHYD | |
466 | O-linked_Glycosylation | NPCQNDATCLDQIGE CCCCCCCCHHHHCCC | 19.23 | - | |
496 | O-linked_Glycosylation | VNTDECASSPCLHNG ECCHHHCCCCCCCCC | 46.61 | UniProtKB CARBOHYD | |
518 | Phosphorylation | EFQCECPTGFTGHLC EEECCCCCCCCCCEE | 57.49 | 22210691 | |
534 | O-linked_Glycosylation | YDVDECASTPCKNGA ECHHHHCCCCCCCCC | 44.53 | UniProtKB CARBOHYD | |
535 | Phosphorylation | DVDECASTPCKNGAK CHHHHCCCCCCCCCC | 17.74 | 22210691 | |
609 | O-linked_Glycosylation | TNINECSSQPCRHGG CCHHHCCCCCCCCCC | 50.21 | UniProtKB CARBOHYD | |
617 | O-linked_Glycosylation | QPCRHGGTCQDRDNA CCCCCCCCCCCCCCC | 16.16 | - | |
647 | O-linked_Glycosylation | INLDDCASSPCDSGT ECHHHHCCCCCCCCC | 40.94 | UniProtKB CARBOHYD | |
692 | O-linked_Glycosylation | NPCHNGGTCEDGING CCCCCCCCCCCCCCC | 17.70 | - | |
722 | O-linked_Glycosylation | SEVNECNSNPCVHGA HHHHHHCCCCCCCCH | 54.53 | UniProtKB CARBOHYD | |
759 | O-linked_Glycosylation | INNNECESNPCVNGG CCCCCCCCCCCCCCC | 58.70 | UniProtKB CARBOHYD | |
767 | O-linked_Glycosylation | NPCVNGGTCKDMTSG CCCCCCCCCCCCCCC | 20.13 | - | |
784 | O-linked_Glycosylation | CTCREGFSGPNCQTN EEECCCCCCCCCCCC | 65.28 | - | |
797 | O-linked_Glycosylation | TNINECASNPCLNQG CCHHHHHCCCCCCCC | 53.62 | UniProtKB CARBOHYD | |
805 | O-linked_Glycosylation | NPCLNQGTCIDDVAG CCCCCCCCCHHHCCC | 9.12 | - | |
822 | O-linked_Glycosylation | CNCLLPYTGATCEVV CCEECCCCCCEEEEE | 20.57 | 28314751 | |
825 | O-linked_Glycosylation | LLPYTGATCEVVLAP ECCCCCCEEEEEEEC | 15.56 | OGP | |
859 | O-linked_Glycosylation | SFSCVCPTGWQGQTC CEEEECCCCCCCCEE | 46.02 | OGP | |
900 | Phosphorylation | CHCQAGYSGRNCETD EEECCCCCCCCCCCC | 30.29 | - | |
921 | O-linked_Glycosylation | NPCHNGGSCTDGINT CCCCCCCCCCCCCCH | 18.42 | - | |
923 | O-linked_Glycosylation | CHNGGSCTDGINTAF CCCCCCCCCCCCHHH | 38.67 | OGP | |
951 | O-linked_Glycosylation | EDINECASDPCRNGA HHHHHHCCCCCCCCC | 54.46 | UniProtKB CARBOHYD | |
959 | N-linked_Glycosylation | DPCRNGANCTDCVDS CCCCCCCCCCCCCCE | 30.53 | UniProtKB CARBOHYD | |
997 | O-linked_Glycosylation | SSCFNGGTCVDGINS CCCCCCCEECCCCCC | 15.68 | - | |
1027 | O-linked_Glycosylation | HDVNECDSQPCLHGG CCHHCCCCCCCCCCC | 47.91 | UniProtKB CARBOHYD | |
1035 | O-linked_Glycosylation | QPCLHGGTCQDGCGS CCCCCCCCCCCCCCC | 16.16 | - | |
1065 | O-linked_Glycosylation | NLVHWCDSSPCKNGG CCEEHHCCCCCCCCC | 32.80 | UniProtKB CARBOHYD | |
1159 | O-linked_Glycosylation | SPCQNGATCTDYLGG CCCCCCCCCCHHCCC | 19.82 | - | |
1179 | N-linked_Glycosylation | VAGYHGVNCSEEIDE EEECCCCCCCHHHHH | 28.34 | UniProtKB CARBOHYD | |
1189 | O-linked_Glycosylation | EEIDECLSHPCQNGG HHHHHHHCCCCCCCC | 36.72 | UniProtKB CARBOHYD | |
1197 | O-linked_Glycosylation | HPCQNGGTCLDLPNT CCCCCCCCCCCCCCC | 15.99 | - | |
1241 | N-linked_Glycosylation | RSPKCFNNGTCVDQV CCCCCCCCCCEEEEE | 27.22 | UniProtKB CARBOHYD | |
1273 | O-linked_Glycosylation | GDVNECLSNPCDARG CCHHHHHCCCCCCCC | 50.84 | UniProtKB CARBOHYD | |
1317 | Acetylation | GCKGKPCKNGGTCAV CCCCCCCCCCCEEEE | 68.13 | 19828305 | |
1362 | O-linked_Glycosylation | LRCLNGGTCISGPRS EEECCCCCCCCCCCC | 14.20 | - | |
1379 | O-linked_Glycosylation | CLCLGPFTGPECQFP EEEECCCCCCCCCCC | 55.77 | - | |
1402 | O-linked_Glycosylation | NPCYNQGTCEPTSES CCCCCCCCCCCCCCC | 12.16 | 24226769 | |
1406 | O-linked_Glycosylation | NQGTCEPTSESPFYR CCCCCCCCCCCCCCH | 23.88 | OGP | |
1489 | N-linked_Glycosylation | NFNDPWKNCTQSLQC CCCCCCCCCCHHHHH | 30.14 | UniProtKB CARBOHYD | |
1580 | Ubiquitination | TLVVVVLMPPEQLRN EEEEEEECCHHHHCC | 3.34 | 21963094 | |
1581 | Ubiquitination | LVVVVLMPPEQLRNS EEEEEECCHHHHCCC | 25.72 | 23503661 | |
1587 | N-linked_Glycosylation | MPPEQLRNSSFHFLR CCHHHHCCCCHHHHH | 51.07 | UniProtKB CARBOHYD | |
1589 | O-linked_Glycosylation | PEQLRNSSFHFLREL HHHHCCCCHHHHHHH | 26.70 | 28314751 | |
1708 | O-linked_Glycosylation | AFLGALASLGSLNIP HHHHHHHHHCCCCCC | 33.83 | OGP | |
1725 | O-linked_Glycosylation | IEAVQSETVEPPPPA EEEEECCCCCCCCCH | 35.10 | 24226769 | |
1779 | O-linked_Glycosylation | GFKVSEASKKKRREP CCCCCHHHHHHCCCC | 40.74 | 28314751 | |
1791 | Phosphorylation | REPLGEDSVGLKPLK CCCCCCCCCCCCCCC | 17.49 | 28555341 | |
1795 | Acetylation | GEDSVGLKPLKNASD CCCCCCCCCCCCCCC | 42.23 | 25953088 | |
1795 | Ubiquitination | GEDSVGLKPLKNASD CCCCCCCCCCCCCCC | 42.23 | 29967540 | |
1801 | Phosphorylation | LKPLKNASDGALMDD CCCCCCCCCCCCCCC | 46.07 | 30576142 | |
1821 | Ubiquitination | GDEDLETKKFRFEEP CCCCHHHCCEECCCC | 40.31 | 21963094 | |
1822 | Ubiquitination | DEDLETKKFRFEEPV CCCHHHCCEECCCCE | 49.55 | 21906983 | |
1861 | Phosphorylation | RMSAMAPTPPQGEVD HHHHCCCCCCCCCCC | 37.75 | 18669648 | |
1889 | Phosphorylation | FTPLMIASCSGGGLE CCCEEEEEECCCCCC | 9.63 | 28348404 | |
1891 | Phosphorylation | PLMIASCSGGGLETG CEEEEEECCCCCCCC | 37.67 | 28348404 | |
1897 | Phosphorylation | CSGGGLETGNSEEEE ECCCCCCCCCCCCCC | 46.86 | 21685388 | |
1900 | Phosphorylation | GGLETGNSEEEEDAP CCCCCCCCCCCCCCC | 47.97 | 21685388 | |
1927 | Phosphorylation | LHNQTDRTGETALHL CCCCCCCHHHHHHHH | 42.03 | - | |
1930 | Phosphorylation | QTDRTGETALHLAAR CCCCHHHHHHHHHHH | 35.54 | - | |
1939 | Phosphorylation | LHLAARYSRSDAAKR HHHHHHHCCHHHHHH | 21.54 | 28102081 | |
1941 | Phosphorylation | LAARYSRSDAAKRLL HHHHHCCHHHHHHHH | 26.17 | 28102081 | |
1946 | Methylation | SRSDAAKRLLEASAD CCHHHHHHHHHHHCC | 39.52 | 115385661 | |
1951 | Phosphorylation | AKRLLEASADANIQD HHHHHHHHCCCCCCC | 19.80 | - | |
1955 | Hydroxylation | LEASADANIQDNMGR HHHHCCCCCCCCCCC | 32.76 | 17573339 | |
1986 | Phosphorylation | ILIRNRATDLDARMH HHCCCCCCCCCCCCC | 33.58 | 24719451 | |
1996 | Phosphorylation | DARMHDGTTPLILAA CCCCCCCCHHHHHHH | 31.16 | - | |
1997 | Phosphorylation | ARMHDGTTPLILAAR CCCCCCCHHHHHHHH | 22.94 | - | |
2022 | Hydroxylation | INSHADVNAVDDLGK HHCCCCCCCCCHHHH | 34.49 | - | |
2074 | Phosphorylation | LAAREGSYETAKVLL HHHCCCCHHHHHHHH | 28.31 | 22461510 | |
2090 | Phosphorylation | HFANRDITDHMDRLP HHCCCCCHHHHHHCC | 24.92 | 24719451 | |
2116 | Phosphorylation | IVRLLDEYNLVRSPQ HHHHHHHCCCCCCCC | 17.29 | 27642862 | |
2121 | Phosphorylation | DEYNLVRSPQLHGAP HHCCCCCCCCCCCCC | 14.98 | 30108239 | |
2132 | Phosphorylation | HGAPLGGTPTLSPPL CCCCCCCCCCCCCCC | 15.99 | 27080861 | |
2134 | Phosphorylation | APLGGTPTLSPPLCS CCCCCCCCCCCCCCC | 39.44 | 27080861 | |
2136 | Phosphorylation | LGGTPTLSPPLCSPN CCCCCCCCCCCCCCC | 27.27 | 28450419 | |
2141 | Phosphorylation | TLSPPLCSPNGYLGS CCCCCCCCCCCCCCC | 29.14 | 27080861 | |
2145 | Phosphorylation | PLCSPNGYLGSLKPG CCCCCCCCCCCCCCC | 17.96 | 28450419 | |
2148 | Phosphorylation | SPNGYLGSLKPGVQG CCCCCCCCCCCCCCC | 30.53 | 28450419 | |
2150 | Acetylation | NGYLGSLKPGVQGKK CCCCCCCCCCCCCCC | 41.23 | 26051181 | |
2157 | Acetylation | KPGVQGKKVRKPSSK CCCCCCCCCCCCCCC | 54.84 | 37798817 | |
2160 | Acetylation | VQGKKVRKPSSKGLA CCCCCCCCCCCCCCC | 52.84 | 37798809 | |
2162 | Phosphorylation | GKKVRKPSSKGLACG CCCCCCCCCCCCCCC | 47.95 | 23312004 | |
2163 | Phosphorylation | KKVRKPSSKGLACGS CCCCCCCCCCCCCCC | 38.99 | 23312004 | |
2164 | Acetylation | KVRKPSSKGLACGSK CCCCCCCCCCCCCCH | 63.38 | 37798851 | |
2171 | Acetylation | KGLACGSKEAKDLKA CCCCCCCHHHHHHHH | 47.15 | 23749302 | |
2174 | Acetylation | ACGSKEAKDLKARRK CCCCHHHHHHHHHHH | 65.76 | 37798841 | |
2211 | Phosphorylation | ESPHGYLSDVASPPL CCCCCCCCCCCCCCC | 22.89 | 26074081 | |
2215 | Phosphorylation | GYLSDVASPPLLPSP CCCCCCCCCCCCCCC | 27.22 | 26074081 | |
2221 | Phosphorylation | ASPPLLPSPFQQSPS CCCCCCCCCCCCCCC | 38.01 | 26074081 | |
2274 | O-linked_Glycosylation | ETGPPRLSHLPVASG CCCCCCCCCCCCCCC | 25.02 | 28314751 | |
2280 | O-linked_Glycosylation | LSHLPVASGTSTVLG CCCCCCCCCCEEEEC | 42.72 | 28314751 | |
2282 | O-linked_Glycosylation | HLPVASGTSTVLGSS CCCCCCCCEEEECCC | 20.80 | 28314751 | |
2284 | O-linked_Glycosylation | PVASGTSTVLGSSSG CCCCCCEEEECCCCC | 21.42 | 28314751 | |
2323 | Phosphorylation | SGMVPNQYNPLRGSV CCCCCCCCCCCCCCC | 25.95 | 26356563 | |
2461 | O-linked_Glycosylation | HTILPQESPALPTSL EECCCCCCCCCCCCC | 15.38 | 28314751 | |
2466 | O-linked_Glycosylation | QESPALPTSLPSSLV CCCCCCCCCCCHHCC | 43.69 | 28314751 | |
2511 | Phosphorylation | VPEHPFLTPSPESPD CCCCCCCCCCCCCCC | 23.31 | - | |
2513 | Phosphorylation | EHPFLTPSPESPDQW CCCCCCCCCCCCCCC | 35.74 | - | |
2516 | Phosphorylation | FLTPSPESPDQWSSS CCCCCCCCCCCCCCC | 36.84 | - | |
2521 | Phosphorylation | PESPDQWSSSSPHSN CCCCCCCCCCCCCCC | 18.08 | 16880534 | |
2522 | Phosphorylation | ESPDQWSSSSPHSNV CCCCCCCCCCCCCCH | 31.69 | 16880534 | |
2523 | Phosphorylation | SPDQWSSSSPHSNVS CCCCCCCCCCCCCHH | 42.23 | 16880534 | |
2524 | Phosphorylation | PDQWSSSSPHSNVSD CCCCCCCCCCCCHHH | 28.69 | 16880534 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
1897 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
1900 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
2511 | T | Phosphorylation | Kinase | CDK19 | Q9BWU1 | PSP |
2511 | T | Phosphorylation | Kinase | CDK3 | Q00526 | PSP |
2511 | T | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
2511 | T | Phosphorylation | Kinase | DYRK2 | Q92630 | PSP |
2511 | T | Phosphorylation | Kinase | HIPK2 | Q9H2X6 | PSP |
2511 | T | Phosphorylation | Kinase | MAP3K1 | Q13233 | GPS |
2513 | S | Phosphorylation | Kinase | CDK19 | Q9BWU1 | PSP |
2513 | S | Phosphorylation | Kinase | CDK3 | Q00526 | PSP |
2513 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
2516 | S | Phosphorylation | Kinase | CDK19 | Q9BWU1 | PSP |
2516 | S | Phosphorylation | Kinase | CDK3 | Q00526 | PSP |
2516 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | MDM2 | Q00987 | PMID:23252402 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXW7 | Q969H0 | PMID:17274947 |
- | K | Ubiquitination | E3 ubiquitin ligase | ITCH | Q96J02 | PMID:12682059 |
- | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:15620649 |
* 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 NOTC1_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00002 | Acute lymphoblastic leukemia (ALL) (precursor T lymphoblastic leukemia) | |||||
H00554 | Bicuspid aortic valve | |||||
OMIM Disease | ||||||
109730 | Aortic valve disease 1 (AOVD1) | |||||
616028 | Adams-Oliver syndrome 5 (AOS5) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Hydroxylation | |
Reference | PubMed |
"Asparaginyl hydroxylation of the Notch ankyrin repeat domain byfactor inhibiting hypoxia-inducible factor."; Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,Oldham N.J., Ratcliffe P.J., Schofield C.J.; J. Biol. Chem. 282:24027-24038(2007). Cited for: PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATIONAT ASN-1955, AND MASS SPECTROMETRY. |