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Reviewed, UniProtKB/Swiss-Prot Q04721 (NOTC2_HUMAN)

Last modified June 16, 2009. Version 114. 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 · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Neurogenic locus notch homolog protein 2
      Short name=Notch 2
      Short name=hN2
Cleaved into the following 2 chains:
    1- Recommended name:
            Notch 2 extracellular truncation
    2- Recommended name:
            Notch 2 intracellular domain
Gene names
Name: NOTCH2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 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 By similarity. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Notch 2 intracellular domain: Nucleus. Note: Following proteolytical processing NICD is translocated to the nucleus.

Tissue specificity

Expressed in the brain, heart, kidney, lung, skeletal muscle and liver.

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 NOTCH2 are the cause of Alagille syndrome type 2 (ALGS2) [MIM:610205]. Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. There are characteristic facial features and less frequent clinical involvement of the renal and vascular systems. Ref.14

Sequence similarities

Belongs to the NOTCH family.

Contains 6 ANK repeats.

Contains 35 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

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Ontologies

Keywords
   Biological processDifferentiation
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentCell membrane
Membrane
Nucleus
   DiseaseDisease mutation
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
   Molecular functionActivator
Developmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processNotch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

anti-apoptosis

Traceable author statement. Source: UniProtKB

cell cycle arrest

Inferred from direct assay. Source: UniProtKB

cell fate determination Ref.6

Traceable author statement. Source: UniProtKB

cell growth

Inferred from direct assay. Source: UniProtKB

hemopoiesis Ref.5

Traceable author statement. Source: UniProtKB

induction of apoptosis

Traceable author statement. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay. Source: UniProtKB

nervous system development

Non-traceable author statement. Source: UniProtKB

organ morphogenesis

Inferred from expression pattern. Source: UniProtKB

positive regulation of Ras protein signal transduction

Inferred from direct assay. Source: UniProtKB

regulation of transcription, DNA-dependent Ref.6

Traceable author statement. Source: UniProtKB

stem cell maintenance

Traceable author statement. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell surface Ref.6

Inferred from direct assay. Source: UniProtKB

integral to plasma membrane Ref.6

Inferred from direct assay. Source: UniProtKB

nucleus Ref.5

Inferred from direct assay. Source: UniProtKB

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

ligand-regulated transcription factor activity Ref.6

Traceable author statement. Source: UniProtKB

protein heterodimerization activity Ref.6

Non-traceable author statement. Source: UniProtKB

receptor activity Ref.6

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 24712446Neurogenic locus notch homolog protein 2
PRO_0000007683
Chain1666 – 2471806Notch 2 extracellular truncation By similarity
PRO_0000007684
Chain1697 – 2471775Notch 2 intracellular domain By similarity
PRO_0000007685

Regions

Topological domain26 – 16771652Extracellular Potential
Transmembrane1678 – 169821 Potential
Topological domain1699 – 2471773Cytoplasmic Potential
Domain26 – 6338EGF-like 1
Domain64 – 10239EGF-like 2
Domain105 – 14339EGF-like 3
Domain144 – 18037EGF-like 4
Domain182 – 21938EGF-like 5; calcium-binding Potential
Domain221 – 25838EGF-like 6
Domain260 – 29637EGF-like 7; calcium-binding Potential
Domain298 – 33639EGF-like 8; calcium-binding Potential
Domain338 – 37437EGF-like 9; calcium-binding Potential
Domain375 – 41339EGF-like 10
Domain415 – 45440EGF-like 11; calcium-binding Potential
Domain456 – 49237EGF-like 12; calcium-binding Potential
Domain494 – 53037EGF-like 13; calcium-binding Potential
Domain532 – 56837EGF-like 14; calcium-binding Potential
Domain570 – 60536EGF-like 15; calcium-binding Potential
Domain607 – 64337EGF-like 16; calcium-binding Potential
Domain645 – 68036EGF-like 17; calcium-binding Potential
Domain682 – 71837EGF-like 18; calcium-binding Potential
Domain720 – 75536EGF-like 19
Domain757 – 79337EGF-like 20; calcium-binding Potential
Domain795 – 83137EGF-like 21; calcium-binding Potential
Domain833 – 87139EGF-like 22
Domain873 – 90937EGF-like 23; calcium-binding Potential
Domain911 – 94737EGF-like 24; calcium-binding Potential
Domain949 – 98537EGF-like 25; calcium-binding Potential
Domain987 – 102337EGF-like 26; calcium-binding Potential
Domain1025 – 106137EGF-like 27; calcium-binding Potential
Domain1063 – 109937EGF-like 28
Domain1101 – 114747EGF-like 29
Domain1149 – 118537EGF-like 30; calcium-binding Potential
Domain1187 – 122337EGF-like 31; calcium-binding Potential
Domain1225 – 126238EGF-like 32; calcium-binding Potential
Domain1264 – 130239EGF-like 33
Domain1304 – 134340EGF-like 34
Domain1374 – 141239EGF-like 35
Repeat1425 – 146541LNR 1
Repeat1466 – 150237LNR 2
Repeat1503 – 154442LNR 3
Repeat1827 – 187145ANK 1
Repeat1876 – 190530ANK 2
Repeat1909 – 193931ANK 3
Repeat1943 – 197230ANK 4
Repeat1976 – 200530ANK 5
Repeat2009 – 203830ANK 6
Region1425 – 1677253Negative regulatory region (NRR)
Compositional bias1645 – 16484Poly-Ala
Compositional bias1994 – 19974Poly-Leu
Compositional bias2426 – 24294Poly-Ser

Amino acid modifications

Modified residue17161Phosphothreonine Ref.12
Modified residue17781Phosphoserine Ref.12
Modified residue18021Phosphothreonine Ref.12
Modified residue18041Phosphoserine Ref.12
Modified residue18081Phosphothreonine Ref.12 Ref.10
Modified residue18411Phosphoserine Ref.11
Modified residue18421Phosphoserine Ref.11
Modified residue18451Phosphoserine Ref.11
Modified residue20701Phosphoserine Ref.12 Ref.10
Modified residue20741Phosphothreonine Ref.12
Modified residue20781Phosphoserine By similarity
Modified residue20811Phosphoserine Ref.12
Modified residue20971Phosphothreonine Ref.12
Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential
Glycosylation11021N-linked (GlcNAc...) Potential
Glycosylation14651N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 41 By similarity
Disulfide bond35 ↔ 51 By similarity
Disulfide bond53 ↔ 62 By similarity
Disulfide bond68 ↔ 79 By similarity
Disulfide bond73 ↔ 90 By similarity
Disulfide bond92 ↔ 101 By similarity
Disulfide bond109 ↔ 121 By similarity
Disulfide bond115 ↔ 131 By similarity
Disulfide bond133 ↔ 142 By similarity
Disulfide bond148 ↔ 159 By similarity
Disulfide bond153 ↔ 168 By similarity
Disulfide bond170 ↔ 179 By similarity
Disulfide bond186 ↔ 198 By similarity
Disulfide bond192 ↔ 207 By similarity
Disulfide bond209 ↔ 218 By similarity
Disulfide bond225 ↔ 236 By similarity
Disulfide bond230 ↔ 246 By similarity
Disulfide bond248 ↔ 257 By similarity
Disulfide bond264 ↔ 275 By similarity
Disulfide bond269 ↔ 284 By similarity
Disulfide bond286 ↔ 295 By similarity
Disulfide bond302 ↔ 315 By similarity
Disulfide bond309 ↔ 324 By similarity
Disulfide bond326 ↔ 335 By similarity
Disulfide bond342 ↔ 353 By similarity
Disulfide bond347 ↔ 362 By similarity
Disulfide bond364 ↔ 373 By similarity
Disulfide bond379 ↔ 390 By similarity
Disulfide bond384 ↔ 401 By similarity
Disulfide bond403 ↔ 412 By similarity
Disulfide bond419 ↔ 433 By similarity
Disulfide bond427 ↔ 442 By similarity
Disulfide bond444 ↔ 453 By similarity
Disulfide bond460 ↔ 471 By similarity
Disulfide bond465 ↔ 480 By similarity
Disulfide bond482 ↔ 491 By similarity
Disulfide bond498 ↔ 509 By similarity
Disulfide bond503 ↔ 518 By similarity
Disulfide bond520 ↔ 529 By similarity
Disulfide bond536 ↔ 547 By similarity
Disulfide bond541 ↔ 556 By similarity
Disulfide bond558 ↔ 567 By similarity
Disulfide bond574 ↔ 584 By similarity
Disulfide bond579 ↔ 593 By similarity
Disulfide bond595 ↔ 604 By similarity
Disulfide bond611 ↔ 622 By similarity
Disulfide bond616 ↔ 631 By similarity
Disulfide bond633 ↔ 642 By similarity
Disulfide bond649 ↔ 659 By similarity
Disulfide bond654 ↔ 668 By similarity
Disulfide bond670 ↔ 679 By similarity
Disulfide bond686 ↔ 697 By similarity
Disulfide bond691 ↔ 706 By similarity
Disulfide bond708 ↔ 717 By similarity
Disulfide bond724 ↔ 734 By similarity
Disulfide bond729 ↔ 743 By similarity
Disulfide bond745 ↔ 754 By similarity
Disulfide bond761 ↔ 772 By similarity
Disulfide bond766 ↔ 781 By similarity
Disulfide bond783 ↔ 792 By similarity
Disulfide bond799 ↔ 810 By similarity
Disulfide bond804 ↔ 819 By similarity
Disulfide bond821 ↔ 830 By similarity
Disulfide bond837 ↔ 848 By similarity
Disulfide bond842 ↔ 859 By similarity
Disulfide bond861 ↔ 870 By similarity
Disulfide bond877 ↔ 888 By similarity
Disulfide bond882 ↔ 897 By similarity
Disulfide bond899 ↔ 908 By similarity
Disulfide bond915 ↔ 926 By similarity
Disulfide bond920 ↔ 935 By similarity
Disulfide bond937 ↔ 946 By similarity
Disulfide bond953 ↔ 964 By similarity
Disulfide bond958 ↔ 973 By similarity
Disulfide bond975 ↔ 984 By similarity
Disulfide bond991 ↔ 1002 By similarity
Disulfide bond996 ↔ 1011 By similarity
Disulfide bond1013 ↔ 1022 By similarity
Disulfide bond1029 ↔ 1040 By similarity
Disulfide bond1034 ↔ 1049 By similarity
Disulfide bond1051 ↔ 1060 By similarity
Disulfide bond1067 ↔ 1078 By similarity
Disulfide bond1072 ↔ 1087 By similarity
Disulfide bond1089 ↔ 1098 By similarity
Disulfide bond1105 ↔ 1126 By similarity
Disulfide bond1120 ↔ 1135 By similarity
Disulfide bond1137 ↔ 1146 By similarity
Disulfide bond1153 ↔ 1164 By similarity
Disulfide bond1158 ↔ 1173 By similarity
Disulfide bond1175 ↔ 1184 By similarity
Disulfide bond1191 ↔ 1202 By similarity
Disulfide bond1196 ↔ 1211 By similarity
Disulfide bond1213 ↔ 1222 By similarity
Disulfide bond1229 ↔ 1241 By similarity
Disulfide bond1235 ↔ 1250 By similarity
Disulfide bond1252 ↔ 1261 By similarity
Disulfide bond1268 ↔ 1281 By similarity
Disulfide bond1273 ↔ 1290 By similarity
Disulfide bond1292 ↔ 1301 By similarity
Disulfide bond1308 ↔ 1319 By similarity
Disulfide bond1313 ↔ 1331 By similarity
Disulfide bond1333 ↔ 1342 By similarity
Disulfide bond1378 ↔ 1389 By similarity
Disulfide bond1383 ↔ 1400 By similarity
Disulfide bond1402 ↔ 1411 By similarity
Disulfide bond1425 ↔ 1448 Ref.13
Disulfide bond1430 ↔ 1443 Ref.13
Disulfide bond1439 ↔ 1455 Ref.13
Disulfide bond1466 ↔ 1489 Ref.13
Disulfide bond1472 ↔ 1484 Ref.13
Disulfide bond1480 ↔ 1496 Ref.13
Disulfide bond1503 ↔ 1527 Ref.13
Disulfide bond1509 ↔ 1522 Ref.13
Disulfide bond1518 ↔ 1534 Ref.13
Disulfide bond1632 ↔ 1639 Ref.13

Natural variations

Natural variant4441C → Y in ALGS2. Ref.14
VAR_029361
Natural variant16671V → F: dbSNP rs17024517.
VAR_031463

Experimental info

Sequence conflict211A → T in AAG37073. Ref.2
Sequence conflict2101P → L in AAG37073. Ref.2
Sequence conflict10371E → D in AAB19224. Ref.4
Sequence conflict1084 – 10852ES → SP in AAB19224. Ref.4
Sequence conflict10941A → V in AAB19224. Ref.4
Sequence conflict11391L → V in AAB19224. Ref.4
Sequence conflict15191D → N in AAA36377. Ref.1
Sequence conflict20531R → H in AAG37073. Ref.2

Secondary structure

1 .............................................. 2471
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q04721-1 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 605B1B963C812BE1

FASTA2,471265,405
        10         20         30         40         50         60 
MPALRPALLW ALLALWLCCA APAHALQCRD GYEPCVNEGM CVTYHNGTGY CKCPEGFLGE 

        70         80         90        100        110        120 
YCQHRDPCEK NRCQNGGTCV AQAMLGKATC RCASGFTGED CQYSTSHPCF VSRPCLNGGT 

       130        140        150        160        170        180 
CHMLSRDTYE CTCQVGFTGK ECQWTDACLS HPCANGSTCT TVANQFSCKC LTGFTGQKCE 

       190        200        210        220        230        240 
TDVNECDIPG HCQHGGTCLN LPGSYQCQCP QGFTGQYCDS LYVPCAPSPC VNGGTCRQTG 

       250        260        270        280        290        300 
DFTFECNCLP GFEGSTCERN IDDCPNHRCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD 

       310        320        330        340        350        360 
ECLLQPNACQ NGGTCANRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG STCIDRVASF 

       370        380        390        400        410        420 
SCMCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI CTCPQGYKGA DCTEDVDECA 

       430        440        450        460        470        480 
MANSNPCEHA GKCVNTDGAF HCECLKGYAG PRCEMDINEC HSDPCQNDAT CLDKIGGFTC 

       490        500        510        520        530        540 
LCMPGFKGVH CELEINECQS NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP 

       550        560        570        580        590        600 
CLNGAKCIDH PNGYECQCAT GFTGVLCEEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM 

       610        620        630        640        650        660 
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGV NCEINFDDCA SNPCIHGICM 

       670        680        690        700        710        720 
DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCING VNGFRCICPE GPHHPSCYSQ 

       730        740        750        760        770        780 
VNECLSNPCI HGNCTGGLSG YKCLCDAGWV GINCEVDKNE CLSNPCQNGG TCDNLVNGYR 

       790        800        810        820        830        840 
CTCKKGFKGY NCQVNIDECA SNPCLNQGTC FDDISGYTCH CVLPYTGKNC QTVLAPCSPN 

       850        860        870        880        890        900 
PCENAAVCKE SPNFESYTCL CAPGWQGQRC TIDIDECISK PCMNHGLCHN TQGSYMCECP 

       910        920        930        940        950        960 
PGFSGMDCEE DIDDCLANPC QNGGSCMDGV NTFSCLCLPG FTGDKCQTDM NECLSEPCKN 

       970        980        990       1000       1010       1020 
GGTCSDYVNS YTCKCQAGFD GVHCENNINE CTESSCFNGG TCVDGINSFS CLCPVGFTGS 

      1030       1040       1050       1060       1070       1080 
FCLHEINECS SHPCLNEGTC VDGLGTYRCS CPLGYTGKNC QTLVNLCSRS PCKNKGTCVQ 

      1090       1100       1110       1120       1130       1140 
KKAESQCLCP SGWAGAYCDV PNVSCDIAAS RRGVLVEHLC QHSGVCINAG NTHYCQCPLG 

      1150       1160       1170       1180       1190       1200 
YTGSYCEEQL DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG 

      1210       1220       1230       1240       1250       1260 
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA RGPHCLNGGQ CMDRIGGYSC RCLPGFAGER 

      1270       1280       1290       1300       1310       1320 
CEGDINECLS NPCSSEGSLD CIQLTNDYLC VCRSAFTGRH CETFVDVCPQ MPCLNGGTCA 

      1330       1340       1350       1360       1370       1380 
VASNMPDGFI CRCPPGFSGA RCQSSCGQVK CRKGEQCVHT ASGPRCFCPS PRDCESGCAS 

      1390       1400       1410       1420       1430       1440 
SPCQHGGSCH PQRQPPYYSC QCAPPFSGSR CELYTAPPST PPATCLSQYC ADKARDGVCD 

      1450       1460       1470       1480       1490       1500 
EACNSHACQW DGGDCSLTME NPWANCSSPL PCWDYINNQC DELCNTVECL FDNFECQGNS 

      1510       1520       1530       1540       1550       1560 
KTCKYDKYCA DHFKDNHCDQ GCNSEECGWD GLDCAADQPE NLAEGTLVIV VLMPPEQLLQ 

      1570       1580       1590       1600       1610       1620 
DARSFLRALG TLLHTNLRIK RDSQGELMVY PYYGEKSAAM KKQRMTRRSL PGEQEQEVAG 

      1630       1640       1650       1660       1670       1680 
SKVFLEIDNR QCVQDSDHCF KNTDAAAALL ASHAIQGTLS YPLVSVVSES LTPERTQLLY 

      1690       1700       1710       1720       1730       1740 
LLAVAVVIIL FIILLGVIMA KRKRKHGSLW LPEGFTLRRD ASNHKRREPV GQDAVGLKNL 

      1750       1760       1770       1780       1790       1800 
SVQVSEANLI GTGTSEHWVD DEGPQPKKVK AEDEALLSEE DDPIDRRPWT QQHLEAADIR 

      1810       1820       1830       1840       1850       1860 
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED AEDSSANIIT 

      1870       1880       1890       1900       1910       1920 
DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG ADANAQDNMG RCPLHAAVAA 

      1930       1940       1950       1960       1970       1980 
DAQGVFQILI RNRVTDLDAR MNDGTTPLIL AARLAVEGMV AELINCQADV NAVDDHGKSA 

      1990       2000       2010       2020       2030       2040 
LHWAAAVNNV EATLLLLKNG ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD 

      2050       2060       2070       2080       2090       2100 
HMDRLPRDVA RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVICGPNRS FLSLKHTPMG 

      2110       2120       2130       2140       2150       2160 
KKSRRPSAKS TMPTSLPNLA KEAKDAKGSR RKKSLSEKVQ LSESSVTLSP VDSLESPHTY 

      2170       2180       2190       2200       2210       2220 
VSDTTSSPMI TSPGILQASP NPMLATAAPP APVHAQHALS FSNLHEMQPL AHGASTVLPS 

      2230       2240       2250       2260       2270       2280 
VSQLLSHHHI VSPGSGSAGS LSRLHPVPVP ADWMNRMEVN ETQYNEMFGM VLAPAEGTHP 

      2290       2300       2310       2320       2330       2340 
GIAPQSRPPE GKHITTPREP LPPIVTFQLI PKGSIAQPAG APQPQSTCPP AVAGPLPTMY 

      2350       2360       2370       2380       2390       2400 
QIPEMARLPS VAFPTAMMPQ QDGQVAQTIL PAYHPFPASV GKYPTPPSQH SYASSNAAER 

      2410       2420       2430       2440       2450       2460 
TPSHSGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGAGG GQRGPGTHMS 

      2470 
EPPHNNMQVY A

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References

« Hide 'large scale' references
[1]"Complete human notch 2 (hN2) cDNA sequence."
Blaumueller C.M., Mann R.S.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Human Notch2, a novel member of cell-fate determining NOTCH family."
Correa R.G., Camargo A.A., Moreira E.S., Simpson A.J.G.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary tumor.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Partial sequence of EGF-like repeat domain of human Notch2 mRNA."
Lemasson I., Devaux C., Mesnard J.-M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1229.
Tissue: T-cell.
[5]"Human homologs of a Drosophila enhancer of split gene product define a novel family of nuclear proteins."
Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., Artavanis-Tsakonas S.
Nat. Genet. 2:119-127(1992) [PubMed: 1303260] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1810-2447.
Tissue: Brain.
[6]"Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane."
Blaumueller C.M., Qi H., Zagouras P., Artavanis-Tsakonas S.
Cell 90:281-291(1997) [PubMed: 9244302] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[7]"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.
[8]"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.
[9]"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.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1808 AND SER-2070, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1841; SER-1842 AND SER-1845, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1716; SER-1778; THR-1802; SER-1804; THR-1808; SER-2070; THR-2074; SER-2081 AND THR-2097, MASS SPECTROMETRY.
[13]"Structural basis for autoinhibition of Notch."
Gordon W.R., Vardar-Ulu D., Histen G., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.
Nat. Struct. Mol. Biol. 14:295-300(2007) [PubMed: 17401372] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1426-1677, DISULFIDE BONDS.
[14]"NOTCH2 mutations cause Alagille syndrome, a heterogeneous disorder of the notch signaling pathway."
McDaniell R., Warthen D.M., Sanchez-Lara P.A., Pai A., Krantz I.D., Piccoli D.A., Spinner N.B.
Am. J. Hum. Genet. 79:169-173(2006) [PubMed: 16773578] [Abstract]
Cited for: VARIANT ALGS2 TYR-444.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF308601 mRNA. Translation: AAA36377.2.
AF315356 mRNA. Translation: AAG37073.1.
AL359752, AL512503, AL596222 Genomic DNA. Translation: CAI18974.1.
AL512503, AL359752, AL596222 Genomic DNA. Translation: CAH72483.1.
AL596222, AL359752, AL512503 Genomic DNA. Translation: CAH70182.1.
U77493 mRNA. Translation: AAB19224.1.
IPIIPI00297655.
RefSeqNP_077719.2.
UniGeneHs.487360

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2OO4X-ray2.00A/B1423-1677[»]
SMRQ04721. Positions 1858-2071.
ModBaseSearch...

PTM databases

PhosphoSiteQ04721.

Proteomic databases

PRIDEQ04721.

Genome annotation databases

EnsemblENSG00000134250. Homo sapiens. [Contig view]
GeneID4853.
KEGGhsa:4853.

Organism-specific databases

GeneCardsGC01M120256.
H-InvDBHIX0000955.
HGNCHGNC:7882. NOTCH2.
MIM600275. gene.
610205. phenotype.
Orphanet52. Alagille syndrome.
PharmGKBPA31684.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ04721.
HOVERGENQ04721.
OMAQ04721. RYSRADA.

Enzyme and pathway databases

ReactomeREACT_299. Signaling by Notch.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ04721.
BgeeQ04721.
CleanExHS_NOTCH2.
GermOnlineENSG00000134250. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438. EGF_2.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR008297. Notch.
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. 29 hits.
PF07645. EGF_CA. 4 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFPIRSF002279. Notch. 1 hit.
PRINTSPR00010. EGFBLOOD.
PR01452. NOTCH.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 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. 34 hits.
PS01186. EGF_2. 29 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio18692.
SOURCESearch...

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Entry information

Entry nameNOTC2_HUMAN
AccessionPrimary (citable) accession number: Q04721
Secondary accession number(s): Q5T3X7, Q99734, Q9H240
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: April 3, 2007
Last modified: June 16, 2009
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: 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 · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents