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Database: UniProt
Entry: P46531
LinkDB: P46531
Original site: P46531 
ID   NOTC1_HUMAN             Reviewed;        2555 AA.
AC   P46531; Q59ED8; Q5SXM3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 4.
DT   09-JUL-2014, entry version 178.
DE   RecName: Full=Neurogenic locus notch homolog protein 1;
DE            Short=Notch 1;
DE            Short=hN1;
DE   AltName: Full=Translocation-associated notch protein TAN-1;
DE   Contains:
DE     RecName: Full=Notch 1 extracellular truncation;
DE              Short=NEXT;
DE   Contains:
DE     RecName: Full=Notch 1 intracellular domain;
DE              Short=NICD;
DE   Flags: Precursor;
GN   Name=NOTCH1; Synonyms=TAN1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Mann R.S., Blaumueller C.M., Zagouras P.;
RT   "Complete human notch 1 (hN1) cDNA sequence.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-2443.
RX   PubMed=1831692; DOI=10.1016/0092-8674(91)90111-B;
RA   Ellisen L.W., Bird J., West D.C., Soreng A.L., Reynolds T.C.,
RA   Smith S.D., Sklar J.;
RT   "TAN-1, the human homolog of the Drosophila notch gene, is broken by
RT   chromosomal translocations in T lymphoblastic neoplasms.";
RL   Cell 66:649-661(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-2555.
RC   TISSUE=Aortic endothelium;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATION
RP   AT ASN-1955, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17573339; DOI=10.1074/jbc.M704102200;
RA   Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
RA   Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
RA   Oldham N.J., Ratcliffe P.J., Schofield C.J.;
RT   "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
RT   factor inhibiting hypoxia-inducible factor.";
RL   J. Biol. Chem. 282:24027-24038(2007).
RN   [6]
RP   IDENTIFICATION OF LIGANDS.
RX   PubMed=10079256; DOI=10.1016/S0002-9440(10)65325-4;
RA   Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L.,
RA   Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.;
RT   "Human ligands of the Notch receptor.";
RL   Am. J. Pathol. 154:785-794(1999).
RN   [7]
RP   INTERACTION WITH DTX1.
RX   PubMed=9590294; DOI=10.1038/ng0598-74;
RA   Matsuno K., Eastman D., Mitsiades T., Quinn A.M., Carcanciu M.L.,
RA   Ordentlich P., Kadesch T., Artavanis-Tsakonas S.;
RT   "Human deltex is a conserved regulator of Notch signalling.";
RL   Nat. Genet. 19:74-78(1998).
RN   [8]
RP   INTERACTION WITH SNW1.
RX   PubMed=10713164; DOI=10.1128/MCB.20.7.2400-2410.2000;
RA   Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G.,
RA   Hayward S.D.;
RT   "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
RT   domain of NotchIC To facilitate NotchIC function.";
RL   Mol. Cell. Biol. 20:2400-2410(2000).
RN   [9]
RP   INTERACTION WITH MAML1.
RX   PubMed=11101851; DOI=10.1038/82644;
RA   Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S.,
RA   Griffin J.D.;
RT   "MAML1, a human homologue of Drosophila mastermind, is a
RT   transcriptional co-activator for NOTCH receptors.";
RL   Nat. Genet. 26:484-489(2000).
RN   [10]
RP   INTERACTION WITH MAML2 AND MAML3.
RX   PubMed=12370315; DOI=10.1128/MCB.22.21.7688-7700.2002;
RA   Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.;
RT   "Identification of a family of mastermind-like transcriptional
RT   coactivators for mammalian notch receptors.";
RL   Mol. Cell. Biol. 22:7688-7700(2002).
RN   [11]
RP   UBIQUITINATION BY ITCH.
RX   PubMed=18628966; DOI=10.1371/journal.pone.0002735;
RA   Chastagner P., Israel A., Brou C.;
RT   "AIP4/Itch regulates Notch receptor degradation in the absence of
RT   ligand.";
RL   PLoS ONE 3:E2735-E2735(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   FUNCTION.
RX   PubMed=20616313; DOI=10.1161/CIRCRESAHA.110.217257;
RA   Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E.,
RA   Adam M.G., Telzerow A., Augustin H.G., Fischer A.;
RT   "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting
RT   angiogenesis.";
RL   Circ. Res. 107:592-601(2010).
RN   [14]
RP   INTERACTION WITH SNAI1 AND MDM2A.
RX   PubMed=22128911; DOI=10.1186/1741-7007-9-83;
RA   Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K.,
RA   Jung G.;
RT   "Notch1 binds and induces degradation of Snail in hepatocellular
RT   carcinoma.";
RL   BMC Biol. 9:83-83(2011).
RN   [15]
RP   INTERACTION WITH AAK1.
RX   PubMed=21464124; DOI=10.1074/jbc.M110.190769;
RA   Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
RA   Olivo-Marin J.C., Israel A.;
RT   "The adaptor-associated kinase 1, AAK1, is a positive regulator of the
RT   Notch pathway.";
RL   J. Biol. Chem. 286:18720-18730(2011).
RN   [16]
RP   INTERACTION WITH SGK1 AND FBXW7.
RX   PubMed=21147854; DOI=10.1242/jcs.073924;
RA   Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S.,
RA   Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J.,
RA   Park H.S.;
RT   "Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
RT   signaling by downregulation of protein stability through Fbw7
RT   ubiquitin ligase.";
RL   J. Cell Sci. 124:100-112(2011).
RN   [17]
RP   INTERACTION WITH SNW1.
RX   PubMed=21245387; DOI=10.1128/MCB.00360-10;
RA   Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D.,
RA   Alves-Guerra M.C., Robbins D.J., Capobianco A.J.;
RT   "Assembly of a Notch transcriptional activation complex requires
RT   multimerization.";
RL   Mol. Cell. Biol. 31:1396-1408(2011).
RN   [18]
RP   GLYCOSYLATION AT THR-232; THR-1402 AND THR-1725, AND PROTEOLYTIC
RP   PROCESSING.
RX   PubMed=24226769; DOI=10.1038/nature12723;
RA   Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S.,
RA   Clausen H., Brueckner M., Khokha M.K.;
RT   "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
RT   type and laterality.";
RL   Nature 504:456-459(2013).
RN   [19]
RP   STRUCTURE BY NMR OF 1446-1480 IN COMPLEX WITH CALCIUM IONS, AND
RP   DISULFIDE BONDS.
RX   PubMed=12795601; DOI=10.1021/bi034156y;
RA   Vardar D., North C.L., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.;
RT   "Nuclear magnetic resonance structure of a prototype Lin12-Notch
RT   repeat module from human Notch1.";
RL   Biochemistry 42:7061-7067(2003).
RN   [20]
RP   STRUCTURE BY NMR OF 411-526.
RX   PubMed=15576031; DOI=10.1016/j.str.2004.09.012;
RA   Hambleton S., Valeyev N.V., Muranyi A., Knott V., Werner J.M.,
RA   McMichael A.J., Handford P.A., Downing A.K.;
RT   "Structural and functional properties of the human notch-1 ligand
RT   binding region.";
RL   Structure 12:2173-2183(2004).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1872-2114.
RX   PubMed=16011479; DOI=10.1042/BJ20050515;
RA   Ehebauer M.T., Chirgadze D.Y., Hayward P., Martinez Arias A.,
RA   Blundell T.L.;
RT   "High-resolution crystal structure of the human Notch 1 ankyrin
RT   domain.";
RL   Biochem. J. 392:13-20(2005).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1872-2126 IN COMPLEX WITH
RP   RBPSUH AND MAML1.
RX   PubMed=16530044; DOI=10.1016/j.cell.2005.12.037;
RA   Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.;
RT   "Structural basis for cooperativity in recruitment of MAML
RT   coactivators to Notch transcription complexes.";
RL   Cell 124:973-983(2006).
RN   [23]
RP   INVOLVEMENT IN AOVD1.
RX   PubMed=16025100; DOI=10.1038/nature03940;
RA   Garg V., Muth A.N., Ransom J.F., Schluterman M.K., Barnes R.,
RA   King I.N., Grossfeld P.D., Srivastava D.;
RT   "Mutations in NOTCH1 cause aortic valve disease.";
RL   Nature 437:270-274(2005).
CC   -!- FUNCTION: Functions as a receptor for membrane-bound ligands
CC       Jagged1, Jagged2 and Delta1 to regulate cell-fate determination.
CC       Upon ligand activation through the released notch intracellular
CC       domain (NICD) it forms a transcriptional activator complex with
CC       RBPJ/RBPSUH and activates genes of the enhancer of split locus.
CC       Affects the implementation of differentiation, proliferation and
CC       apoptotic programs. Involved in angiogenesis; negatively regulates
CC       endothelial cell proliferation and migration and angiogenic
CC       sprouting. Involved in the maturation of both CD4+ and CD8+ cells
CC       in the thymus. Important for follicular differentiation and
CC       possibly cell fate selection within the follicle. During
CC       cerebellar development, functions as a receptor for neuronal DNER
CC       and is involved in the differentiation of Bergmann glia. Represses
CC       neuronal and myogenic differentiation. May play an essential role
CC       in postimplantation development, probably in some aspect of cell
CC       specification and/or differentiation. May be involved in mesoderm
CC       development, somite formation and neurogenesis. May enhance HIF1A
CC       function by sequestering HIF1AN away from HIF1A. Required for the
CC       THBS4 function in regulating protective astrogenesis from the
CC       subventricular zone (SVZ) niche after injury. Involved in
CC       determination of left/right symmetry by modulating the balance
CC       between motile and immotile (sensory) cilia at the left-right
CC       organiser (LRO).
CC   -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
CC       terminal fragment N(EC) which are probably linked by disulfide
CC       bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also
CC       interacts with MAML1, MAML2 and MAML3 which act as transcriptional
CC       coactivators for NOTCH1. Notch 1 intracellular domain interacts
CC       with SNW1; the interaction involves multimerized NOTCH1 NICD and
CC       is implicated in a formation of an intermediate preactivation
CC       complex which associates with DNA-bound CBF-1/RBPJ. The activated
CC       membrane-bound form interacts with AAK1 which promotes NOTCH1
CC       stabilization. Forms a trimeric complex with FBXW7 and SGK1.
CC       Interacts with HIF1AN. HIF1AN negatively regulates the function of
CC       notch intracellular domain (NICD), accelerating myogenic
CC       differentiation. Interacts (via NICD) with SNAI1 (via zinc
CC       fingers); the interaction induces SNAI1 degradation via MDM2-
CC       mediated ubiquitination and inhibits SNAI1-induced cell invasion.
CC       Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6;
CC       the interaction decreases MAML1 recruitment by NOTCH1 NICD on
CC       target genes DNA and inhibits NOTCH1 transcractivation activity.
CC       Interacts with THBS4 (By similarity).
CC   -!- INTERACTION:
CC       P19838:NFKB1; NbExp=2; IntAct=EBI-636374, EBI-300010;
CC       Q13526:PIN1; NbExp=9; IntAct=EBI-636374, EBI-714158;
CC       Q06330:RBPJ; NbExp=3; IntAct=EBI-636374, EBI-632552;
CC       Q13573:SNW1; NbExp=3; IntAct=EBI-636374, EBI-632715;
CC       P98170:XIAP; NbExp=4; IntAct=EBI-636374, EBI-517127;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus (By
CC       similarity). Note=Following proteolytical processing NICD is
CC       translocated to the nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: In fetal tissues most abundant in spleen,
CC       brain stem and lung. Also present in most adult tissues where it
CC       is found mainly in lymphoid tissues.
CC   -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
CC       which is proteolytically cleaved by a furin-like convertase in the
CC       trans-Golgi network before it reaches the plasma membrane to yield
CC       an active, ligand-accessible form. Cleavage results in a C-
CC       terminal fragment N(TM) and a N-terminal fragment N(EC). Following
CC       ligand binding, it is cleaved by ADAM17 to yield a membrane-
CC       associated intermediate fragment called notch extracellular
CC       truncation (NEXT). Following endocytosis, this fragment is then
CC       cleaved by presenilin dependent gamma-secretase to release a
CC       notch-derived peptide containing the intracellular domain (NICD)
CC       from the membrane (By similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- PTM: O-glycosylated on the EGF-like domains. Contains both O-
CC       linked fucose and O-linked glucose. O-linked glycosylation by
CC       GALNT11 is involved in determination of left/right symmetry:
CC       glycosylation promotes activation of NOTCH1, possibly by promoting
CC       cleavage by ADAM17, modulating the balance between motile and
CC       immotile (sensory) cilia at the left-right organiser (LRO).
CC   -!- PTM: Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination
CC       catalyzed by ITCH. Monoubiquitination at Lys-1759 is required for
CC       activation by gamma-secretase cleavage, it promotes interaction
CC       with AAK1, which stabilizes it. Deubiquitination by EIF3F is
CC       necessary for nuclear import of activated Notch.
CC   -!- PTM: Hydroxylated at Asn-1955 by HIF1AN. Hydroxylated at Asn-2022
CC       by HIF1AN (By similarity). Hydroxylation reduces affinity for
CC       HI1AN and may thus indirectly modulate negative regulation of NICD
CC       (By similarity).
CC   -!- DISEASE: Aortic valve disease 1 (AOVD1) [MIM:109730]: A common
CC       defect in the aortic valve in which two rather than three leaflets
CC       are present. It is often associated with aortic valve
CC       calcification, stenosis and insufficiency. In extreme cases, the
CC       blood flow may be so restricted that the left ventricle fails to
CC       grow, resulting in hypoplastic left heart syndrome. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the NOTCH family.
CC   -!- SIMILARITY: Contains 5 ANK repeats.
CC   -!- SIMILARITY: Contains 36 EGF-like domains.
CC   -!- SIMILARITY: Contains 3 LNR (Lin/Notch) repeats.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/NOTCH1ID30ch9q34.html";
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DR   EMBL; AF308602; AAG33848.1; -; mRNA.
DR   EMBL; AL592301; CAI13934.1; -; Genomic_DNA.
DR   EMBL; AL354671; CAI13934.1; JOINED; Genomic_DNA.
DR   EMBL; AL354671; CAI16149.1; -; Genomic_DNA.
DR   EMBL; AL592301; CAI16149.1; JOINED; Genomic_DNA.
DR   EMBL; M73980; AAA60614.1; -; mRNA.
DR   EMBL; AB209873; BAD93110.1; -; mRNA.
DR   CCDS; CCDS43905.1; -.
DR   PIR; A40043; A40043.
DR   RefSeq; NP_060087.3; NM_017617.3.
DR   UniGene; Hs.495473; -.
DR   PDB; 1PB5; NMR; -; A=1446-1480.
DR   PDB; 1TOZ; NMR; -; A=411-526.
DR   PDB; 1YYH; X-ray; 1.90 A; A/B=1872-2114.
DR   PDB; 2F8X; X-ray; 3.25 A; K=1872-2126.
DR   PDB; 2F8Y; X-ray; 1.55 A; A/B=1905-2126.
DR   PDB; 2HE0; X-ray; 1.90 A; A/B=1872-2114.
DR   PDB; 2VJ3; X-ray; 2.60 A; A=411-526.
DR   PDB; 3ETO; X-ray; 2.00 A; A/B=1446-1733.
DR   PDB; 3I08; X-ray; 3.20 A; A/C=1446-1664, B/D=1665-1733.
DR   PDB; 3L95; X-ray; 2.19 A; X/Y=1448-1728.
DR   PDB; 3NBN; X-ray; 3.45 A; B/E=1872-2126.
DR   PDB; 3V79; X-ray; 3.85 A; K=1872-2126, R=1759-1777.
DR   PDB; 4CUD; X-ray; 1.85 A; A=411-526.
DR   PDB; 4CUE; X-ray; 3.00 A; A=411-526.
DR   PDB; 4CUF; X-ray; 2.29 A; A=411-526.
DR   PDB; 4D0E; X-ray; 1.61 A; A=411-526.
DR   PDB; 4D0F; X-ray; 2.80 A; A=411-526.
DR   PDBsum; 1PB5; -.
DR   PDBsum; 1TOZ; -.
DR   PDBsum; 1YYH; -.
DR   PDBsum; 2F8X; -.
DR   PDBsum; 2F8Y; -.
DR   PDBsum; 2HE0; -.
DR   PDBsum; 2VJ3; -.
DR   PDBsum; 3ETO; -.
DR   PDBsum; 3I08; -.
DR   PDBsum; 3L95; -.
DR   PDBsum; 3NBN; -.
DR   PDBsum; 3V79; -.
DR   PDBsum; 4CUD; -.
DR   PDBsum; 4CUE; -.
DR   PDBsum; 4CUF; -.
DR   PDBsum; 4D0E; -.
DR   PDBsum; 4D0F; -.
DR   ProteinModelPortal; P46531; -.
DR   SMR; P46531; 411-526, 1448-1728, 1883-2122.
DR   BioGrid; 110913; 179.
DR   DIP; DIP-29919N; -.
DR   IntAct; P46531; 21.
DR   MINT; MINT-1417018; -.
DR   STRING; 9606.ENSP00000277541; -.
DR   ChEMBL; CHEMBL2146346; -.
DR   PhosphoSite; P46531; -.
DR   DMDM; 206729936; -.
DR   MaxQB; P46531; -.
DR   PaxDb; P46531; -.
DR   PRIDE; P46531; -.
DR   Ensembl; ENST00000277541; ENSP00000277541; ENSG00000148400.
DR   GeneID; 4851; -.
DR   KEGG; hsa:4851; -.
DR   UCSC; uc004chz.3; human.
DR   CTD; 4851; -.
DR   GeneCards; GC09M139388; -.
DR   H-InvDB; HIX0008549; -.
DR   HGNC; HGNC:7881; NOTCH1.
DR   HPA; CAB008112; -.
DR   HPA; CAB022466; -.
DR   MIM; 109730; phenotype.
DR   MIM; 190198; gene.
DR   neXtProt; NX_P46531; -.
DR   Orphanet; 1244; Bicuspid aortic valve.
DR   PharmGKB; PA31683; -.
DR   eggNOG; COG0666; -.
DR   HOGENOM; HOG000234369; -.
DR   HOVERGEN; HBG052650; -.
DR   KO; K02599; -.
DR   OMA; GASCQNT; -.
DR   OrthoDB; EOG7992RD; -.
DR   PhylomeDB; P46531; -.
DR   TreeFam; TF351641; -.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_116125; Disease.
DR   Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR   Reactome; REACT_2155; NICD traffics to nucleus.
DR   Reactome; REACT_691; A third proteolytic cleavage releases NICD.
DR   Reactome; REACT_71; Gene Expression.
DR   SignaLink; P46531; -.
DR   EvolutionaryTrace; P46531; -.
DR   GeneWiki; Notch-1; -.
DR   GenomeRNAi; 4851; -.
DR   NextBio; 18684; -.
DR   PRO; PR:P46531; -.
DR   ArrayExpress; P46531; -.
DR   Bgee; P46531; -.
DR   CleanEx; HS_NOTCH1; -.
DR   Genevestigator; P46531; -.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0001190; F:RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription; ISS:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0042640; P:anagen; IEA:Ensembl.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0060842; P:arterial endothelial cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0003162; P:atrioventricular node development; IEA:Ensembl.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR   GO; GO:0003209; P:cardiac atrium morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003207; P:cardiac chamber formation; ISS:BHF-UCL.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:BHF-UCL.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003213; P:cardiac right atrium morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003219; P:cardiac right ventricle formation; IEA:Ensembl.
DR   GO; GO:0060411; P:cardiac septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISS:BHF-UCL.
DR   GO; GO:0003208; P:cardiac ventricle morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR   GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISS:BHF-UCL.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:BHF-UCL.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
DR   GO; GO:0060271; P:cilium morphogenesis; ISS:UniProtKB.
DR   GO; GO:0072044; P:collecting duct development; IEA:Ensembl.
DR   GO; GO:0007386; P:compartment pattern specification; IEA:Ensembl.
DR   GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003169; P:coronary vein morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
DR   GO; GO:0072017; P:distal tubule development; IEA:Ensembl.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0060956; P:endocardial cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003157; P:endocardium development; ISS:BHF-UCL.
DR   GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
DR   GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0007440; P:foregut morphogenesis; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR   GO; GO:0003241; P:growth involved in heart morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IMP:DFLAT.
DR   GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR   GO; GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0014031; P:mesenchymal cell development; ISS:BHF-UCL.
DR   GO; GO:0003192; P:mitral valve formation; IMP:BHF-UCL.
DR   GO; GO:2000811; P:negative regulation of anoikis; IMP:BHF-UCL.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:BHF-UCL.
DR   GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; IDA:UniProtKB.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
DR   GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IEA:Ensembl.
DR   GO; GO:2000974; P:negative regulation of pro-B cell differentiation; ISS:UniProtKB.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:0097150; P:neuronal stem cell maintenance; IEP:UniProtKB.
DR   GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
DR   GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
DR   GO; GO:0003344; P:pericardium morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR   GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
DR   GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; ISS:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:1901201; P:regulation of extracellular matrix assembly; ISS:BHF-UCL.
DR   GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
DR   GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR   GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR   GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0035148; P:tube formation; IMP:UniProtKB.
DR   GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060843; P:venous endothelial cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR024600; DUF3454_notch.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_N_dom.
DR   InterPro; IPR008297; Notch.
DR   InterPro; IPR022362; Notch_1.
DR   InterPro; IPR000800; Notch_dom.
DR   InterPro; IPR010660; Notch_NOD_dom.
DR   InterPro; IPR011656; Notch_NODP_dom.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF11936; DUF3454; 1.
DR   Pfam; PF00008; EGF; 23.
DR   Pfam; PF07645; EGF_CA; 5.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF06816; NOD; 1.
DR   Pfam; PF07684; NODP; 1.
DR   Pfam; PF00066; Notch; 3.
DR   PIRSF; PIRSF002279; Notch; 1.
DR   PRINTS; PR01452; LNOTCHREPEAT.
DR   PRINTS; PR01984; NOTCH1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00179; EGF_CA; 24.
DR   SMART; SM00004; NL; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF57184; SSF57184; 6.
DR   SUPFAM; SSF90193; SSF90193; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 22.
DR   PROSITE; PS00022; EGF_1; 35.
DR   PROSITE; PS01186; EGF_2; 27.
DR   PROSITE; PS50026; EGF_3; 36.
DR   PROSITE; PS01187; EGF_CA; 20.
DR   PROSITE; PS50258; LNR; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Angiogenesis; ANK repeat; Calcium;
KW   Cell membrane; Complete proteome; Developmental protein;
KW   Differentiation; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydroxylation; Isopeptide bond;
KW   Membrane; Metal-binding; Notch signaling pathway; Nucleus;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Signal; Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   2555       Neurogenic locus notch homolog protein 1.
FT                                /FTId=PRO_0000007674.
FT   CHAIN      1721   2555       Notch 1 extracellular truncation (By
FT                                similarity).
FT                                /FTId=PRO_0000007675.
FT   CHAIN      1754   2555       Notch 1 intracellular domain (By
FT                                similarity).
FT                                /FTId=PRO_0000007676.
FT   TOPO_DOM     19   1735       Extracellular (Potential).
FT   TRANSMEM   1736   1756       Helical; (Potential).
FT   TOPO_DOM   1757   2555       Cytoplasmic (Potential).
FT   DOMAIN       20     58       EGF-like 1.
FT   DOMAIN       59     99       EGF-like 2.
FT   DOMAIN      102    139       EGF-like 3.
FT   DOMAIN      140    176       EGF-like 4.
FT   DOMAIN      178    216       EGF-like 5; calcium-binding (Potential).
FT   DOMAIN      218    255       EGF-like 6.
FT   DOMAIN      257    293       EGF-like 7; calcium-binding (Potential).
FT   DOMAIN      295    333       EGF-like 8; calcium-binding (Potential).
FT   DOMAIN      335    371       EGF-like 9; calcium-binding (Potential).
FT   DOMAIN      372    410       EGF-like 10.
FT   DOMAIN      412    450       EGF-like 11; calcium-binding (Potential).
FT   DOMAIN      452    488       EGF-like 12; calcium-binding (Potential).
FT   DOMAIN      490    526       EGF-like 13; calcium-binding (Potential).
FT   DOMAIN      528    564       EGF-like 14; calcium-binding (Potential).
FT   DOMAIN      566    601       EGF-like 15; calcium-binding (Potential).
FT   DOMAIN      603    639       EGF-like 16; calcium-binding (Potential).
FT   DOMAIN      641    676       EGF-like 17; calcium-binding (Potential).
FT   DOMAIN      678    714       EGF-like 18; calcium-binding (Potential).
FT   DOMAIN      716    751       EGF-like 19; calcium-binding (Potential).
FT   DOMAIN      753    789       EGF-like 20.
FT   DOMAIN      791    827       EGF-like 21; calcium-binding (Potential).
FT   DOMAIN      829    867       EGF-like 22.
FT   DOMAIN      869    905       EGF-like 23; calcium-binding (Potential).
FT   DOMAIN      907    943       EGF-like 24.
FT   DOMAIN      945    981       EGF-like 25; calcium-binding (Potential).
FT   DOMAIN      983   1019       EGF-like 26.
FT   DOMAIN     1021   1057       EGF-like 27.
FT   DOMAIN     1059   1095       EGF-like 28.
FT   DOMAIN     1097   1143       EGF-like 29.
FT   DOMAIN     1145   1181       EGF-like 30.
FT   DOMAIN     1183   1219       EGF-like 31; calcium-binding (Potential).
FT   DOMAIN     1221   1265       EGF-like 32; calcium-binding (Potential).
FT   DOMAIN     1267   1305       EGF-like 33.
FT   DOMAIN     1307   1346       EGF-like 34.
FT   DOMAIN     1348   1384       EGF-like 35.
FT   DOMAIN     1387   1426       EGF-like 36.
FT   REPEAT     1449   1489       LNR 1.
FT   REPEAT     1490   1531       LNR 2.
FT   REPEAT     1532   1571       LNR 3.
FT   REPEAT     1927   1956       ANK 1.
FT   REPEAT     1960   1990       ANK 2.
FT   REPEAT     1994   2023       ANK 3.
FT   REPEAT     2027   2056       ANK 4.
FT   REPEAT     2060   2089       ANK 5.
FT   REGION     1947   1955       HIF1AN-binding (By similarity).
FT   REGION     2014   2022       HIF1AN-binding (By similarity).
FT   COMPBIAS   1575   1578       Poly-Val.
FT   COMPBIAS   1661   1664       Poly-Arg.
FT   COMPBIAS   1728   1731       Poly-Pro.
FT   COMPBIAS   1740   1743       Poly-Ala.
FT   COMPBIAS   1901   1904       Poly-Glu.
FT   COMPBIAS   2259   2262       Poly-Gly.
FT   COMPBIAS   2403   2406       Poly-Gln.
FT   COMPBIAS   2410   2417       Poly-Pro.
FT   COMPBIAS   2521   2524       Poly-Ser.
FT   METAL      1457   1457       Calcium; via carbonyl oxygen.
FT   METAL      1460   1460       Calcium.
FT   METAL      1475   1475       Calcium.
FT   METAL      1478   1478       Calcium.
FT   SITE       1664   1665       Cleavage; by furin-like protease (By
FT                                similarity).
FT   SITE       1710   1711       Cleavage; by ADAM17 (By similarity).
FT   SITE       1720   1721       Cleavage; by ADAM17.
FT   MOD_RES    1955   1955       (3S)-3-hydroxyasparagine; by HIF1AN;
FT                                partial.
FT   MOD_RES    2022   2022       (3S)-3-hydroxyasparagine; by HIF1AN (By
FT                                similarity).
FT   CARBOHYD     41     41       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     65     65       O-linked (Glc...) (By similarity).
FT   CARBOHYD     73     73       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    116    116       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    146    146       O-linked (Glc...) (By similarity).
FT   CARBOHYD    194    194       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    232    232       O-linked (Fuc...); alternate.
FT   CARBOHYD    232    232       O-linked (GalNAc...); alternate.
FT   CARBOHYD    341    341       O-linked (Glc...) (By similarity).
FT   CARBOHYD    378    378       O-linked (Glc...) (By similarity).
FT   CARBOHYD    458    458       O-linked (Glc...) (By similarity).
FT   CARBOHYD    466    466       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    496    496       O-linked (Glc...) (By similarity).
FT   CARBOHYD    534    534       O-linked (Glc...) (By similarity).
FT   CARBOHYD    609    609       O-linked (Glc...) (By similarity).
FT   CARBOHYD    647    647       O-linked (Glc...) (By similarity).
FT   CARBOHYD    722    722       O-linked (Glc...) (By similarity).
FT   CARBOHYD    759    759       O-linked (Glc...) (By similarity).
FT   CARBOHYD    767    767       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    797    797       O-linked (Glc...) (By similarity).
FT   CARBOHYD    805    805       O-linked (Fuc...) (By similarity).
FT   CARBOHYD    951    951       O-linked (Glc...) (By similarity).
FT   CARBOHYD    959    959       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1027   1027       O-linked (Glc...) (By similarity).
FT   CARBOHYD   1035   1035       O-linked (Fuc...) (By similarity).
FT   CARBOHYD   1065   1065       O-linked (Glc...) (By similarity).
FT   CARBOHYD   1179   1179       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1189   1189       O-linked (Glc...) (By similarity).
FT   CARBOHYD   1197   1197       O-linked (Fuc...) (By similarity).
FT   CARBOHYD   1241   1241       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1273   1273       O-linked (Glc...) (By similarity).
FT   CARBOHYD   1362   1362       O-linked (Fuc...) (By similarity).
FT   CARBOHYD   1402   1402       O-linked (Fuc...); alternate.
FT   CARBOHYD   1402   1402       O-linked (GalNAc...); alternate.
FT   CARBOHYD   1489   1489       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1587   1587       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1725   1725       O-linked (GalNAc...).
FT   DISULFID     24     37       By similarity.
FT   DISULFID     31     46       By similarity.
FT   DISULFID     48     57       By similarity.
FT   DISULFID     63     74       By similarity.
FT   DISULFID     68     87       By similarity.
FT   DISULFID     89     98       By similarity.
FT   DISULFID    106    117       By similarity.
FT   DISULFID    111    127       By similarity.
FT   DISULFID    129    138       By similarity.
FT   DISULFID    144    155       By similarity.
FT   DISULFID    149    164       By similarity.
FT   DISULFID    166    175       By similarity.
FT   DISULFID    182    195       By similarity.
FT   DISULFID    189    204       By similarity.
FT   DISULFID    206    215       By similarity.
FT   DISULFID    222    233       By similarity.
FT   DISULFID    227    243       By similarity.
FT   DISULFID    245    254       By similarity.
FT   DISULFID    261    272       By similarity.
FT   DISULFID    266    281       By similarity.
FT   DISULFID    283    292       By similarity.
FT   DISULFID    299    312       By similarity.
FT   DISULFID    306    321       By similarity.
FT   DISULFID    323    332       By similarity.
FT   DISULFID    339    350       By similarity.
FT   DISULFID    344    359       By similarity.
FT   DISULFID    361    370       By similarity.
FT   DISULFID    376    387       By similarity.
FT   DISULFID    381    398       By similarity.
FT   DISULFID    400    409       By similarity.
FT   DISULFID    416    429       By similarity.
FT   DISULFID    423    438       By similarity.
FT   DISULFID    440    449       By similarity.
FT   DISULFID    456    467       By similarity.
FT   DISULFID    461    476       By similarity.
FT   DISULFID    478    487       By similarity.
FT   DISULFID    494    505       By similarity.
FT   DISULFID    499    514       By similarity.
FT   DISULFID    516    525       By similarity.
FT   DISULFID    532    543       By similarity.
FT   DISULFID    537    552       By similarity.
FT   DISULFID    554    563       By similarity.
FT   DISULFID    570    580       By similarity.
FT   DISULFID    575    589       By similarity.
FT   DISULFID    591    600       By similarity.
FT   DISULFID    607    618       By similarity.
FT   DISULFID    612    627       By similarity.
FT   DISULFID    629    638       By similarity.
FT   DISULFID    645    655       By similarity.
FT   DISULFID    650    664       By similarity.
FT   DISULFID    666    675       By similarity.
FT   DISULFID    682    693       By similarity.
FT   DISULFID    687    702       By similarity.
FT   DISULFID    704    713       By similarity.
FT   DISULFID    720    730       By similarity.
FT   DISULFID    725    739       By similarity.
FT   DISULFID    741    750       By similarity.
FT   DISULFID    757    768       By similarity.
FT   DISULFID    762    777       By similarity.
FT   DISULFID    779    788       By similarity.
FT   DISULFID    795    806       By similarity.
FT   DISULFID    800    815       By similarity.
FT   DISULFID    817    826       By similarity.
FT   DISULFID    833    844       By similarity.
FT   DISULFID    838    855       By similarity.
FT   DISULFID    857    866       By similarity.
FT   DISULFID    873    884       By similarity.
FT   DISULFID    878    893       By similarity.
FT   DISULFID    895    904       By similarity.
FT   DISULFID    911    922       By similarity.
FT   DISULFID    916    931       By similarity.
FT   DISULFID    933    942       By similarity.
FT   DISULFID    949    960       By similarity.
FT   DISULFID    954    969       By similarity.
FT   DISULFID    971    980       By similarity.
FT   DISULFID    987    998       By similarity.
FT   DISULFID    992   1007       By similarity.
FT   DISULFID   1009   1018       By similarity.
FT   DISULFID   1025   1036       By similarity.
FT   DISULFID   1030   1045       By similarity.
FT   DISULFID   1047   1056       By similarity.
FT   DISULFID   1063   1074       By similarity.
FT   DISULFID   1068   1083       By similarity.
FT   DISULFID   1085   1094       By similarity.
FT   DISULFID   1101   1122       By similarity.
FT   DISULFID   1116   1131       By similarity.
FT   DISULFID   1133   1142       By similarity.
FT   DISULFID   1149   1160       By similarity.
FT   DISULFID   1154   1169       By similarity.
FT   DISULFID   1171   1180       By similarity.
FT   DISULFID   1187   1198       By similarity.
FT   DISULFID   1192   1207       By similarity.
FT   DISULFID   1209   1218       By similarity.
FT   DISULFID   1225   1244       By similarity.
FT   DISULFID   1238   1253       By similarity.
FT   DISULFID   1255   1264       By similarity.
FT   DISULFID   1271   1284       By similarity.
FT   DISULFID   1276   1293       By similarity.
FT   DISULFID   1295   1304       By similarity.
FT   DISULFID   1311   1322       By similarity.
FT   DISULFID   1316   1334       By similarity.
FT   DISULFID   1336   1345       By similarity.
FT   DISULFID   1352   1363       By similarity.
FT   DISULFID   1357   1372       By similarity.
FT   DISULFID   1374   1383       By similarity.
FT   DISULFID   1391   1403       By similarity.
FT   DISULFID   1397   1414       By similarity.
FT   DISULFID   1416   1425       By similarity.
FT   DISULFID   1449   1472
FT   DISULFID   1454   1467
FT   DISULFID   1463   1479
FT   DISULFID   1490   1514       By similarity.
FT   DISULFID   1496   1509       By similarity.
FT   DISULFID   1505   1521       By similarity.
FT   DISULFID   1536   1549       By similarity.
FT   DISULFID   1545   1561       By similarity.
FT   CROSSLNK   1759   1759       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VARIANT     300    300       Q -> R (in dbSNP:rs11574885).
FT                                /FTId=VAR_034898.
FT   VARIANT     879    879       R -> W (in dbSNP:rs11574895).
FT                                /FTId=VAR_048990.
FT   VARIANT    1671   1671       V -> I (in dbSNP:rs2229968).
FT                                /FTId=VAR_046618.
FT   CONFLICT    187    187       G -> R (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    282    282       R -> P (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    477    477       I -> M (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    614    615       HG -> LR (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    621    621       R -> P (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    677    677       I -> S (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    775    775       Y -> I (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    803    803       Q -> K (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT    860    862       GWQ -> AGAK (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT   1021   1021       D -> V (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT   1028   1028       Q -> R (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT   1032   1032       H -> L (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   CONFLICT   1040   1043       CGSY -> RGLH (in Ref. 1; AAG33848 and 3;
FT                                AAA60614).
FT   TURN        415    417
FT   STRAND      418    420
FT   STRAND      422    424
FT   STRAND      428    431
FT   STRAND      433    439
FT   STRAND      444    446
FT   TURN        455    458
FT   STRAND      466    469
FT   STRAND      474    477
FT   STRAND      482    487
FT   TURN        493    496
FT   TURN        500    502
FT   STRAND      504    507
FT   STRAND      512    515
FT   STRAND      520    525
FT   HELIX      1448   1450
FT   HELIX      1452   1457
FT   STRAND     1460   1462
FT   HELIX      1465   1467
FT   HELIX      1470   1472
FT   HELIX      1473   1476
FT   TURN       1477   1482
FT   TURN       1486   1489
FT   HELIX      1492   1494
FT   HELIX      1496   1498
FT   TURN       1499   1501
FT   STRAND     1502   1504
FT   HELIX      1507   1509
FT   HELIX      1512   1519
FT   TURN       1530   1532
FT   HELIX      1533   1539
FT   STRAND     1542   1544
FT   HELIX      1547   1549
FT   HELIX      1552   1559
FT   STRAND     1563   1565
FT   STRAND     1571   1580
FT   HELIX      1582   1587
FT   HELIX      1589   1600
FT   STRAND     1602   1606
FT   STRAND     1616   1620
FT   STRAND     1672   1681
FT   HELIX      1685   1688
FT   HELIX      1696   1708
FT   STRAND     1714   1716
FT   STRAND     1718   1724
FT   HELIX      1884   1890
FT   HELIX      1909   1914
FT   TURN       1925   1927
FT   HELIX      1931   1937
FT   HELIX      1941   1949
FT   HELIX      1964   1970
FT   HELIX      1974   1982
FT   STRAND     1983   1985
FT   HELIX      1998   2005
FT   HELIX      2008   2016
FT   HELIX      2031   2037
FT   HELIX      2041   2049
FT   HELIX      2064   2071
FT   HELIX      2074   2082
FT   HELIX      2097   2103
FT   HELIX      2107   2115
SQ   SEQUENCE   2555 AA;  272505 MW;  E173C872D195F028 CRC64;
     MPPLLAPLLC LALLPALAAR GPRCSQPGET CLNGGKCEAA NGTEACVCGG AFVGPRCQDP
     NPCLSTPCKN AGTCHVVDRR GVADYACSCA LGFSGPLCLT PLDNACLTNP CRNGGTCDLL
     TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFEA SYICHCPPSF HGPTCRQDVN
     ECGQKPGLCR HGGTCHNEVG SYRCVCRATH TGPNCERPYV PCSPSPCQNG GTCRPTGDVT
     HECACLPGFT GQNCEENIDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
     LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFHGATC HDRVASFYCE
     CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECSLGA
     NPCEHAGKCI NTLGSFECQC LQGYTGPRCE IDVNECVSNP CQNDATCLDQ IGEFQCICMP
     GYEGVHCEVN TDECASSPCL HNGRCLDKIN EFQCECPTGF TGHLCQYDVD ECASTPCKNG
     AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CRPGYTGHHC
     ETNINECSSQ PCRHGGTCQD RDNAYLCFCL KGTTGPNCEI NLDDCASSPC DSGTCLDKID
     GYECACEPGY TGSMCNINID ECAGNPCHNG GTCEDGINGF TCRCPEGYHD PTCLSEVNEC
     NSNPCVHGAC RDSLNGYKCD CDPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR
     EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCLLP YTGATCEVVL APCAPSPCRN
     GGECRQSEDY ESFSCVCPTG WQGQTCEVDI NECVLSPCRH GASCQNTHGG YRCHCQAGYS
     GRNCETDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFRGT FCEEDINECA SDPCRNGANC
     TDCVDSYTCT CPAGFSGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQH
     DVNECDSQPC LHGGTCQDGC GSYRCTCPQG YTGPNCQNLV HWCDSSPCKN GGKCWQTHTQ
     YRCECPSGWT GLYCDVPSVS CEVAAQRQGV DVARLCQHGG LCVDAGNTHH CRCQAGYTGS
     YCEDLVDECS PSPCQNGATC TDYLGGYSCK CVAGYHGVNC SEEIDECLSH PCQNGGTCLD
     LPNTYKCSCP RGTQGVHCEI NVDDCNPPVD PVSRSPKCFN NGTCVDQVGG YSCTCPPGFV
     GERCEGDVNE CLSNPCDARG TQNCVQRVND FHCECRAGHT GRRCESVING CKGKPCKNGG
     TCAVASNTAR GFICKCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGPFTG
     PECQFPASSP CLGGNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFGGGAGRDI
     PPPLIEEACE LPECQEDAGN KVCSLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
     SDGHCDSQCN SAGCLFDGFD CQRAEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD
     CAEHVPERLA AGTLVVVVLM PPEQLRNSSF HFLRELSRVL HTNVVFKRDA HGQQMIFPYY
     GREEELRKHP IKRAAEGWAA PDALLGQVKA SLLPGGSEGG RRRRELDPMD VRGSIVYLEI
     DNRQCVQASS QCFQSATDVA AFLGALASLG SLNIPYKIEA VQSETVEPPP PAQLHFMYVA
     AAAFVLLFFV GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA
     SDGALMDDNQ NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRMSAMAP
     TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL
     HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL
     IRNRATDLDA RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN
     VDAAVVLLKN GANKDMQNNR EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI
     AQERMHHDIV RLLDEYNLVR SPQLHGAPLG GTPTLSPPLC SPNGYLGSLK PGVQGKKVRK
     PSSKGLACGS KEAKDLKARR KKSQDGKGCL LDSSGMLSPV DSLESPHGYL SDVASPPLLP
     SPFQQSPSVP LNHLPGMPDT HLGIGHLNVA AKPEMAALGG GGRLAFETGP PRLSHLPVAS
     GTSTVLGSSS GGALNFTVGG STSLNGQCEW LSRLQSGMVP NQYNPLRGSV APGPLSTQAP
     SLQHGMVGPL HSSLAASALS QMMSYQGLPS TRLATQPHLV QTQQVQPQNL QMQQQNLQPA
     NIQQQQSLQP PPPPPQPHLG VSSAASGHLG RSFLSGEPSQ ADVQPLGPSS LAVHTILPQE
     SPALPTSLPS SLVPPVTAAQ FLTPPSQHSY SSPVDNTPSH QLQVPEHPFL TPSPESPDQW
     SSSSPHSNVS DWSEGVSSPP TSMQSQIARI PEAFK
//
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