Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P46531 (NOTC1_HUMAN)

Last modified November 3, 2009. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Neurogenic locus notch homolog protein 1
      Short name=Notch 1
      Short name=hN1
Alternative name(s):
    Translocation-associated notch protein TAN-1
Cleaved into the following 2 chains:
    1- Recommended name:
            Notch 1 extracellular truncation
    2- Recommended name:
            Notch 1 intracellular domain
Gene names
Name: NOTCH1
Synonyms: TAN1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length2555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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 RBP-J kappa and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May be important for normal lymphocyte function. In altered form, may contribute to transformation or progression in some T-cell neoplasms. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. May be important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, may function as a receptor for neuronal DNER and may be involved in the differentiation of Bergmann glia By similarity.

Subunit structure

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Notch 1 intracellular domain: Nucleus By similarity. Note: Following proteolytical processing NICD is translocated to the nucleus By similarity.

Tissue specificity

In fetal tissues most abundant in spleen, brain stem and lung. Also present in most adult tissues where it is found mainly in lymphoid tissues.

Post-translational modification

Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane By similarity.

Phosphorylated By similarity.

Involvement in disease

Defects in NOTCH1 are a cause of aortic valve disease [MIM:109730]. The disorder consists of an early developmental defect in the aortic valve and a later de-repression of calcium deposition that causes progressive aortic valve disease. Calcification of the aortic valve is the third leading cause of heart disease in adults. The incidence increases with age, and it is often associated with a bicuspid aortic valve present in 1-2% of the population. Ref.13

Sequence similarities

Belongs to the NOTCH family.

Contains 5 ANK repeats.

Contains 36 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RBPJQ063301EBI-636374,EBI-632552
SNW1Q135732EBI-636374,EBI-632715

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 25552537Neurogenic locus notch homolog protein 1
PRO_0000007674
Chain1721 – 2555835Notch 1 extracellular truncation By similarity
PRO_0000007675
Chain1754 – 2555802Notch 1 intracellular domain By similarity
PRO_0000007676

Regions

Topological domain19 – 17351717Extracellular Potential
Transmembrane1736 – 175621 Potential
Topological domain1757 – 2555799Cytoplasmic Potential
Domain20 – 5839EGF-like 1
Domain59 – 9941EGF-like 2
Domain102 – 13938EGF-like 3
Domain140 – 17637EGF-like 4
Domain178 – 21639EGF-like 5; calcium-binding Potential
Domain218 – 25538EGF-like 6
Domain257 – 29337EGF-like 7; calcium-binding Potential
Domain295 – 33339EGF-like 8; calcium-binding Potential
Domain335 – 37137EGF-like 9; calcium-binding Potential
Domain372 – 41039EGF-like 10
Domain412 – 45039EGF-like 11; calcium-binding Potential
Domain452 – 48837EGF-like 12; calcium-binding Potential
Domain490 – 52637EGF-like 13; calcium-binding Potential
Domain528 – 56437EGF-like 14; calcium-binding Potential
Domain566 – 60136EGF-like 15; calcium-binding Potential
Domain603 – 63937EGF-like 16; calcium-binding Potential
Domain641 – 67636EGF-like 17; calcium-binding Potential
Domain678 – 71437EGF-like 18; calcium-binding Potential
Domain716 – 75136EGF-like 19; calcium-binding Potential
Domain753 – 78937EGF-like 20
Domain791 – 82737EGF-like 21; calcium-binding Potential
Domain829 – 86739EGF-like 22
Domain869 – 90537EGF-like 23; calcium-binding Potential
Domain907 – 94337EGF-like 24
Domain945 – 98137EGF-like 25; calcium-binding Potential
Domain983 – 101937EGF-like 26
Domain1021 – 105737EGF-like 27
Domain1059 – 109537EGF-like 28
Domain1097 – 114347EGF-like 29
Domain1145 – 118137EGF-like 30
Domain1183 – 121937EGF-like 31; calcium-binding Potential
Domain1221 – 126545EGF-like 32; calcium-binding Potential
Domain1267 – 130539EGF-like 33
Domain1307 – 134640EGF-like 34
Domain1348 – 138437EGF-like 35
Domain1387 – 142640EGF-like 36
Repeat1449 – 148941LNR 1
Repeat1490 – 153142LNR 2
Repeat1532 – 157140LNR 3
Repeat1927 – 195630ANK 1
Repeat1960 – 199031ANK 2
Repeat1994 – 202330ANK 3
Repeat2027 – 205630ANK 4
Repeat2060 – 208930ANK 5
Compositional bias1575 – 15784Poly-Val
Compositional bias1661 – 16644Poly-Arg
Compositional bias1728 – 17314Poly-Pro
Compositional bias1740 – 17434Poly-Ala
Compositional bias1901 – 19044Poly-Glu
Compositional bias2259 – 22624Poly-Gly
Compositional bias2403 – 24064Poly-Gln
Compositional bias2410 – 24178Poly-Pro
Compositional bias2521 – 25244Poly-Ser

Sites

Metal binding14571Calcium; via carbonyl oxygen
Metal binding14601Calcium
Metal binding14751Calcium
Metal binding14781Calcium
Site1664 – 16652Cleavage; by furin-like protease By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation11791N-linked (GlcNAc...) Potential
Glycosylation12411N-linked (GlcNAc...) Potential
Glycosylation14891N-linked (GlcNAc...) Potential
Glycosylation15871N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 37 By similarity
Disulfide bond31 ↔ 46 By similarity
Disulfide bond48 ↔ 57 By similarity
Disulfide bond63 ↔ 74 By similarity
Disulfide bond68 ↔ 87 By similarity
Disulfide bond89 ↔ 98 By similarity
Disulfide bond106 ↔ 117 By similarity
Disulfide bond111 ↔ 127 By similarity
Disulfide bond129 ↔ 138 By similarity
Disulfide bond144 ↔ 155 By similarity
Disulfide bond149 ↔ 164 By similarity
Disulfide bond166 ↔ 175 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond189 ↔ 204 By similarity
Disulfide bond206 ↔ 215 By similarity
Disulfide bond222 ↔ 233 By similarity
Disulfide bond227 ↔ 243 By similarity
Disulfide bond245 ↔ 254 By similarity
Disulfide bond261 ↔ 272 By similarity
Disulfide bond266 ↔ 281 By similarity
Disulfide bond283 ↔ 292 By similarity
Disulfide bond299 ↔ 312 By similarity
Disulfide bond306 ↔ 321 By similarity
Disulfide bond323 ↔ 332 By similarity
Disulfide bond339 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond361 ↔ 370 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 398 By similarity
Disulfide bond400 ↔ 409 By similarity
Disulfide bond416 ↔ 429 By similarity
Disulfide bond423 ↔ 438 By similarity
Disulfide bond440 ↔ 449 By similarity
Disulfide bond456 ↔ 467 By similarity
Disulfide bond461 ↔ 476 By similarity
Disulfide bond478 ↔ 487 By similarity
Disulfide bond494 ↔ 505 By similarity
Disulfide bond499 ↔ 514 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond532 ↔ 543 By similarity
Disulfide bond537 ↔ 552 By similarity
Disulfide bond554 ↔ 563 By similarity
Disulfide bond570 ↔ 580 By similarity
Disulfide bond575 ↔ 589 By similarity
Disulfide bond591 ↔ 600 By similarity
Disulfide bond607 ↔ 618 By similarity
Disulfide bond612 ↔ 627 By similarity
Disulfide bond629 ↔ 638 By similarity
Disulfide bond645 ↔ 655 By similarity
Disulfide bond650 ↔ 664 By similarity
Disulfide bond666 ↔ 675 By similarity
Disulfide bond682 ↔ 693 By similarity
Disulfide bond687 ↔ 702 By similarity
Disulfide bond704 ↔ 713 By similarity
Disulfide bond720 ↔ 730 By similarity
Disulfide bond725 ↔ 739 By similarity
Disulfide bond741 ↔ 750 By similarity
Disulfide bond757 ↔ 768 By similarity
Disulfide bond762 ↔ 777 By similarity
Disulfide bond779 ↔ 788 By similarity
Disulfide bond795 ↔ 806 By similarity
Disulfide bond800 ↔ 815 By similarity
Disulfide bond817 ↔ 826 By similarity
Disulfide bond833 ↔ 844 By similarity
Disulfide bond838 ↔ 855 By similarity
Disulfide bond857 ↔ 866 By similarity
Disulfide bond873 ↔ 884 By similarity
Disulfide bond878 ↔ 893 By similarity
Disulfide bond895 ↔ 904 By similarity
Disulfide bond911 ↔ 922 By similarity
Disulfide bond916 ↔ 931 By similarity
Disulfide bond933 ↔ 942 By similarity
Disulfide bond949 ↔ 960 By similarity
Disulfide bond954 ↔ 969 By similarity
Disulfide bond971 ↔ 980 By similarity
Disulfide bond987 ↔ 998 By similarity
Disulfide bond992 ↔ 1007 By similarity
Disulfide bond1009 ↔ 1018 By similarity
Disulfide bond1025 ↔ 1036 By similarity
Disulfide bond1030 ↔ 1045 By similarity
Disulfide bond1047 ↔ 1056 By similarity
Disulfide bond1063 ↔ 1074 By similarity
Disulfide bond1068 ↔ 1083 By similarity
Disulfide bond1085 ↔ 1094 By similarity
Disulfide bond1101 ↔ 1122 By similarity
Disulfide bond1116 ↔ 1131 By similarity
Disulfide bond1133 ↔ 1142 By similarity
Disulfide bond1149 ↔ 1160 By similarity
Disulfide bond1154 ↔ 1169 By similarity
Disulfide bond1171 ↔ 1180 By similarity
Disulfide bond1187 ↔ 1198 By similarity
Disulfide bond1192 ↔ 1207 By similarity
Disulfide bond1209 ↔ 1218 By similarity
Disulfide bond1225 ↔ 1244 By similarity
Disulfide bond1238 ↔ 1253 By similarity
Disulfide bond1255 ↔ 1264 By similarity
Disulfide bond1271 ↔ 1284 By similarity
Disulfide bond1276 ↔ 1293 By similarity
Disulfide bond1295 ↔ 1304 By similarity
Disulfide bond1311 ↔ 1322 By similarity
Disulfide bond1316 ↔ 1334 By similarity
Disulfide bond1336 ↔ 1345 By similarity
Disulfide bond1352 ↔ 1363 By similarity
Disulfide bond1357 ↔ 1372 By similarity
Disulfide bond1374 ↔ 1383 By similarity
Disulfide bond1391 ↔ 1403 By similarity
Disulfide bond1397 ↔ 1414 By similarity
Disulfide bond1416 ↔ 1425 By similarity
Disulfide bond1449 ↔ 1472 Ref.9
Disulfide bond1454 ↔ 1467 Ref.9
Disulfide bond1463 ↔ 1479 Ref.9
Disulfide bond1490 ↔ 1514 By similarity
Disulfide bond1496 ↔ 1509 By similarity
Disulfide bond1505 ↔ 1521 By similarity
Disulfide bond1536 ↔ 1549 By similarity
Disulfide bond1545 ↔ 1561 By similarity

Natural variations

Natural variant3001Q → R: dbSNP rs11574885.
VAR_034898
Natural variant8791R → W: dbSNP rs11574895.
VAR_048990
Natural variant16711V → I: dbSNP rs2229968.
VAR_046618

Experimental info

Sequence conflict1871G → R in AAG33848. Ref.1
Sequence conflict1871G → R in AAA60614. Ref.3
Sequence conflict2821R → P in AAG33848. Ref.1
Sequence conflict2821R → P in AAA60614. Ref.3
Sequence conflict4771I → M in AAG33848. Ref.1
Sequence conflict4771I → M in AAA60614. Ref.3
Sequence conflict614 – 6152HG → LR in AAG33848. Ref.1
Sequence conflict614 – 6152HG → LR in AAA60614. Ref.3
Sequence conflict6211R → P in AAG33848. Ref.1
Sequence conflict6211R → P in AAA60614. Ref.3
Sequence conflict6771I → S in AAG33848. Ref.1
Sequence conflict6771I → S in AAA60614. Ref.3
Sequence conflict7751Y → I in AAG33848. Ref.1
Sequence conflict7751Y → I in AAA60614. Ref.3
Sequence conflict8031Q → K in AAG33848. Ref.1
Sequence conflict8031Q → K in AAA60614. Ref.3
Sequence conflict860 – 8623GWQ → AGAK in AAG33848. Ref.1
Sequence conflict860 – 8623GWQ → AGAK in AAA60614. Ref.3
Sequence conflict10211D → V in AAG33848. Ref.1
Sequence conflict10211D → V in AAA60614. Ref.3
Sequence conflict10281Q → R in AAG33848. Ref.1
Sequence conflict10281Q → R in AAA60614. Ref.3
Sequence conflict10321H → L in AAG33848. Ref.1
Sequence conflict10321H → L in AAA60614. Ref.3
Sequence conflict1040 – 10434CGSY → RGLH in AAG33848. Ref.1
Sequence conflict1040 – 10434CGSY → RGLH in AAA60614. Ref.3

Secondary structure

1 ............................................... 2555
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P46531-1 [UniParc].

Last modified September 23, 2008. Version 4.
Checksum: E173C872D195F028

FASTA2,555272,505
        10         20         30         40         50         60 
MPPLLAPLLC LALLPALAAR GPRCSQPGET CLNGGKCEAA NGTEACVCGG AFVGPRCQDP 

        70         80         90        100        110        120 
NPCLSTPCKN AGTCHVVDRR GVADYACSCA LGFSGPLCLT PLDNACLTNP CRNGGTCDLL 

       130        140        150        160        170        180 
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFEA SYICHCPPSF HGPTCRQDVN 

       190        200        210        220        230        240 
ECGQKPGLCR HGGTCHNEVG SYRCVCRATH TGPNCERPYV PCSPSPCQNG GTCRPTGDVT 

       250        260        270        280        290        300 
HECACLPGFT GQNCEENIDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 

       310        320        330        340        350        360 
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFHGATC HDRVASFYCE 

       370        380        390        400        410        420 
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECSLGA 

       430        440        450        460        470        480 
NPCEHAGKCI NTLGSFECQC LQGYTGPRCE IDVNECVSNP CQNDATCLDQ IGEFQCICMP 

       490        500        510        520        530        540 
GYEGVHCEVN TDECASSPCL HNGRCLDKIN EFQCECPTGF TGHLCQYDVD ECASTPCKNG 

       550        560        570        580        590        600 
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CRPGYTGHHC 

       610        620        630        640        650        660 
ETNINECSSQ PCRHGGTCQD RDNAYLCFCL KGTTGPNCEI NLDDCASSPC DSGTCLDKID 

       670        680        690        700        710        720 
GYECACEPGY TGSMCNINID ECAGNPCHNG GTCEDGINGF TCRCPEGYHD PTCLSEVNEC 

       730        740        750        760        770        780 
NSNPCVHGAC RDSLNGYKCD CDPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR 

       790        800        810        820        830        840 
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCLLP YTGATCEVVL APCAPSPCRN 

       850        860        870        880        890        900 
GGECRQSEDY ESFSCVCPTG WQGQTCEVDI NECVLSPCRH GASCQNTHGG YRCHCQAGYS 

       910        920        930        940        950        960 
GRNCETDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFRGT FCEEDINECA SDPCRNGANC 

       970        980        990       1000       1010       1020 
TDCVDSYTCT CPAGFSGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQH 

      1030       1040       1050       1060       1070       1080 
DVNECDSQPC LHGGTCQDGC GSYRCTCPQG YTGPNCQNLV HWCDSSPCKN GGKCWQTHTQ 

      1090       1100       1110       1120       1130       1140 
YRCECPSGWT GLYCDVPSVS CEVAAQRQGV DVARLCQHGG LCVDAGNTHH CRCQAGYTGS 

      1150       1160       1170       1180       1190       1200 
YCEDLVDECS PSPCQNGATC TDYLGGYSCK CVAGYHGVNC SEEIDECLSH PCQNGGTCLD 

      1210       1220       1230       1240       1250       1260 
LPNTYKCSCP RGTQGVHCEI NVDDCNPPVD PVSRSPKCFN NGTCVDQVGG YSCTCPPGFV 

      1270       1280       1290       1300       1310       1320 
GERCEGDVNE CLSNPCDARG TQNCVQRVND FHCECRAGHT GRRCESVING CKGKPCKNGG 

      1330       1340       1350       1360       1370       1380 
TCAVASNTAR GFICKCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGPFTG 

      1390       1400       1410       1420       1430       1440 
PECQFPASSP CLGGNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFGGGAGRDI 

      1450       1460       1470       1480       1490       1500 
PPPLIEEACE LPECQEDAGN KVCSLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 

      1510       1520       1530       1540       1550       1560 
SDGHCDSQCN SAGCLFDGFD CQRAEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD 

      1570       1580       1590       1600       1610       1620 
CAEHVPERLA AGTLVVVVLM PPEQLRNSSF HFLRELSRVL HTNVVFKRDA HGQQMIFPYY 

      1630       1640       1650       1660       1670       1680 
GREEELRKHP IKRAAEGWAA PDALLGQVKA SLLPGGSEGG RRRRELDPMD VRGSIVYLEI 

      1690       1700       1710       1720       1730       1740 
DNRQCVQASS QCFQSATDVA AFLGALASLG SLNIPYKIEA VQSETVEPPP PAQLHFMYVA 

      1750       1760       1770       1780       1790       1800 
AAAFVLLFFV GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA 

      1810       1820       1830       1840       1850       1860 
SDGALMDDNQ NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRMSAMAP 

      1870       1880       1890       1900       1910       1920 
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL 

      1930       1940       1950       1960       1970       1980 
HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL 

      1990       2000       2010       2020       2030       2040 
IRNRATDLDA RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN 

      2050       2060       2070       2080       2090       2100 
VDAAVVLLKN GANKDMQNNR EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI 

      2110       2120       2130       2140       2150       2160 
AQERMHHDIV RLLDEYNLVR SPQLHGAPLG GTPTLSPPLC SPNGYLGSLK PGVQGKKVRK 

      2170       2180       2190       2200       2210       2220 
PSSKGLACGS KEAKDLKARR KKSQDGKGCL LDSSGMLSPV DSLESPHGYL SDVASPPLLP 

      2230       2240       2250       2260       2270       2280 
SPFQQSPSVP LNHLPGMPDT HLGIGHLNVA AKPEMAALGG GGRLAFETGP PRLSHLPVAS 

      2290       2300       2310       2320       2330       2340 
GTSTVLGSSS GGALNFTVGG STSLNGQCEW LSRLQSGMVP NQYNPLRGSV APGPLSTQAP 

      2350       2360       2370       2380       2390       2400 
SLQHGMVGPL HSSLAASALS QMMSYQGLPS TRLATQPHLV QTQQVQPQNL QMQQQNLQPA 

      2410       2420       2430       2440       2450       2460 
NIQQQQSLQP PPPPPQPHLG VSSAASGHLG RSFLSGEPSQ ADVQPLGPSS LAVHTILPQE 

      2470       2480       2490       2500       2510       2520 
SPALPTSLPS SLVPPVTAAQ FLTPPSQHSY SSPVDNTPSH QLQVPEHPFL TPSPESPDQW 

      2530       2540       2550 
SSSSPHSNVS DWSEGVSSPP TSMQSQIARI PEAFK

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Complete human notch 1 (hN1) cDNA sequence."
Mann R.S., Blaumueller C.M., Zagouras P.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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. expand/collapse author list , 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: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms."
Ellisen L.W., Bird J., West D.C., Soreng A.L., Reynolds T.C., Smith S.D., Sklar J.
Cell 66:649-661(1991) [PubMed: 1831692] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2443.
[4]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] OF 489-2555.
Tissue: Aortic endothelium.
[5]"Human ligands of the Notch receptor."
Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L., Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.
Am. J. Pathol. 154:785-794(1999) [PubMed: 10079256] [Abstract]
Cited for: IDENTIFICATION OF LIGANDS.
[6]"Human deltex is a conserved regulator of Notch signalling."
Matsuno K., Eastman D., Mitsiades T., Quinn A.M., Carcanciu M.L., Ordentlich P., Kadesch T., Artavanis-Tsakonas S.
Nat. Genet. 19:74-78(1998) [PubMed: 9590294] [Abstract]
Cited for: INTERACTION WITH DTX1.
[7]"MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors."
Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S., Griffin J.D.
Nat. Genet. 26:484-489(2000) [PubMed: 11101851] [Abstract]
Cited for: INTERACTION WITH MAML1.
[8]"Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors."
Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.
Mol. Cell. Biol. 22:7688-7700(2002) [PubMed: 12370315] [Abstract]
Cited for: INTERACTION WITH MAML2 AND MAML3.
[9]"Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1."
Vardar D., North C.L., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.
Biochemistry 42:7061-7067(2003) [PubMed: 12795601] [Abstract]
Cited for: STRUCTURE BY NMR OF 1446-1480 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
[10]"Structural and functional properties of the human notch-1 ligand binding region."
Hambleton S., Valeyev N.V., Muranyi A., Knott V., Werner J.M., McMichael A.J., Handford P.A., Downing A.K.
Structure 12:2173-2183(2004) [PubMed: 15576031] [Abstract]
Cited for: STRUCTURE BY NMR OF 411-526.
[11]"High-resolution crystal structure of the human Notch 1 ankyrin domain."
Ehebauer M.T., Chirgadze D.Y., Hayward P., Martinez Arias A., Blundell T.L.
Biochem. J. 392:13-20(2005) [PubMed: 16011479] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1872-2114.
[12]"Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes."
Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.
Cell 124:973-983(2006) [PubMed: 16530044] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1872-2126 IN COMPLEX WITH RBPSUH AND MAML1.
[13]"Mutations in NOTCH1 cause aortic valve disease."
Garg V., Muth A.N., Ransom J.F., Schluterman M.K., Barnes R., King I.N., Grossfeld P.D., Srivastava D.
Nature 437:270-274(2005) [PubMed: 16025100] [Abstract]
Cited for: INVOLVEMENT IN AORTIC VALVE DISEASE.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AF308602 mRNA. Translation: AAG33848.1.
AL592301, AL354671 Genomic DNA. Translation: CAI13934.1.
AL354671, AL592301 Genomic DNA. Translation: CAI16149.1.
M73980 mRNA. Translation: AAA60614.1.
AB209873 mRNA. Translation: BAD93110.1.
IPIIPI00412982.
PIRA40043.
RefSeqNP_060087.3.
UniGeneHs.495473

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PB5NMR-A1446-1480[»]
1TOZNMR-A411-526[»]
1YYHX-ray1.90A/B1872-2114[»]
2F8XX-ray3.25K1872-2126[»]
2F8YX-ray1.55A/B1905-2126[»]
2HE0X-ray1.90A/B1873-2114[»]
2VJ3X-ray2.60A411-526[»]
3ETOX-ray2.00A/B1447-1733[»]
3I08X-ray3.20A/C1446-1664[»]
B/D1666-1733[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP46531. 7 interactions.
STRINGP46531.

PTM databases

PhosphoSiteP46531.

Proteomic databases

PRIDEP46531.

Genome annotation databases

EnsemblENST00000277541; ENSP00000277541; ENSG00000148400; Homo sapiens. [Genome view]
GeneID4851.
KEGGhsa:4851.
UCSCuc004chz.1. human.

Organism-specific databases

CTD4851.
GeneCardsGC09M138508.
H-InvDBHIX0008549.
HGNCHGNC:7881. NOTCH1.
MIM109730. phenotype.
190198. gene.
Orphanet1244. Bicuspid aortic valve.
86871. Leukemia, T-cell prolymphocytic.
PharmGKBPA31683.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP46531.

Enzyme and pathway databases

Pathway_Interaction_DBps1pathway. Presenilin action in Notch and Wnt signaling.
ReactomeREACT_299. Signaling by Notch.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP46531.
BgeeP46531.
CleanExHS_NOTCH1.
GenevestigatorP46531.
GermOnlineENSG00000148400. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR010660. Notch_NOD.
IPR011656. Notch_NODP.
IPR000800. Notch_region.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 6 hits.
PF00008. EGF. 30 hits.
PF07645. EGF_CA. 4 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSPR01452. NOTCH.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 24 hits.
SM00004. NL. 3 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 35 hits.
PS01186. EGF_2. 27 hits.
PS50026. EGF_3. 36 hits.
PS01187. EGF_CA. 20 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio18684.
SOURCESearch...

Hide | Top

Entry information

Entry nameNOTC1_HUMAN
AccessionPrimary (citable) accession number: P46531
Secondary accession number(s): Q59ED8, Q5SXM3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Hide | Top

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents