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Neurogenic locus notch homolog protein 1 (Notch 1) (hN1) (Translocation-associated notch protein TAN-1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]

 NOTC1_HUMAN             Reviewed;        2555 AA.
P46531; Q59ED8; Q5SXM3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 4.
30-AUG-2017, entry version 211.
RecName: Full=Neurogenic locus notch homolog protein 1;
Short=Notch 1;
Short=hN1;
AltName: Full=Translocation-associated notch protein TAN-1;
Contains:
RecName: Full=Notch 1 extracellular truncation;
Short=NEXT;
Contains:
RecName: Full=Notch 1 intracellular domain;
Short=NICD;
Flags: Precursor;
Name=NOTCH1; Synonyms=TAN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Mann R.S., Blaumueller C.M., Zagouras P.;
"Complete human notch 1 (hN1) cDNA sequence.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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., 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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-2443.
PubMed=1831692; DOI=10.1016/0092-8674(91)90111-B;
Ellisen L.W., Bird J., West D.C., Soreng A.L., Reynolds T.C.,
Smith S.D., Sklar J.;
"TAN-1, the human homolog of the Drosophila notch gene, is broken by
chromosomal translocations in T lymphoblastic neoplasms.";
Cell 66:649-661(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-2555.
TISSUE=Aortic endothelium;
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.
[5]
PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATION
AT ASN-1955, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17573339; DOI=10.1074/jbc.M704102200;
Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
Oldham N.J., Ratcliffe P.J., Schofield C.J.;
"Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
factor inhibiting hypoxia-inducible factor.";
J. Biol. Chem. 282:24027-24038(2007).
[6]
IDENTIFICATION OF LIGANDS.
PubMed=10079256; DOI=10.1016/S0002-9440(10)65325-4;
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.;
"Human ligands of the Notch receptor.";
Am. J. Pathol. 154:785-794(1999).
[7]
INTERACTION WITH DTX1.
PubMed=9590294; DOI=10.1038/ng0598-74;
Matsuno K., Eastman D., Mitsiades T., Quinn A.M., Carcanciu M.L.,
Ordentlich P., Kadesch T., Artavanis-Tsakonas S.;
"Human deltex is a conserved regulator of Notch signalling.";
Nat. Genet. 19:74-78(1998).
[8]
INTERACTION WITH SNW1.
PubMed=10713164; DOI=10.1128/MCB.20.7.2400-2410.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G.,
Hayward S.D.;
"SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
domain of NotchIC To facilitate NotchIC function.";
Mol. Cell. Biol. 20:2400-2410(2000).
[9]
INTERACTION WITH MAML1.
PubMed=11101851; DOI=10.1038/82644;
Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S.,
Griffin J.D.;
"MAML1, a human homologue of Drosophila mastermind, is a
transcriptional co-activator for NOTCH receptors.";
Nat. Genet. 26:484-489(2000).
[10]
INTERACTION WITH MAML2 AND MAML3.
PubMed=12370315; DOI=10.1128/MCB.22.21.7688-7700.2002;
Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.;
"Identification of a family of mastermind-like transcriptional
coactivators for mammalian notch receptors.";
Mol. Cell. Biol. 22:7688-7700(2002).
[11]
INTERACTION WITH NOV.
PubMed=12050162; DOI=10.1074/jbc.M203727200;
Sakamoto K., Yamaguchi S., Ando R., Miyawaki A., Kabasawa Y.,
Takagi M., Li C.L., Perbal B., Katsube K.;
"The nephroblastoma overexpressed gene (NOV/ccn3) protein associates
with Notch1 extracellular domain and inhibits myoblast differentiation
via Notch signaling pathway.";
J. Biol. Chem. 277:29399-29405(2002).
[12]
UBIQUITINATION BY ITCH.
PubMed=18628966; DOI=10.1371/journal.pone.0002735;
Chastagner P., Israel A., Brou C.;
"AIP4/Itch regulates Notch receptor degradation in the absence of
ligand.";
PLoS ONE 3:E2735-E2735(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
FUNCTION.
PubMed=20616313; DOI=10.1161/CIRCRESAHA.110.217257;
Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E.,
Adam M.G., Telzerow A., Augustin H.G., Fischer A.;
"Integrin cytoplasmic domain-associated protein-1 attenuates sprouting
angiogenesis.";
Circ. Res. 107:592-601(2010).
[15]
INTERACTION WITH SNAI1 AND MDM2A.
PubMed=22128911; DOI=10.1186/1741-7007-9-83;
Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K.,
Jung G.;
"Notch1 binds and induces degradation of Snail in hepatocellular
carcinoma.";
BMC Biol. 9:83-83(2011).
[16]
INTERACTION WITH AAK1.
PubMed=21464124; DOI=10.1074/jbc.M110.190769;
Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
Olivo-Marin J.C., Israel A.;
"The adaptor-associated kinase 1, AAK1, is a positive regulator of the
Notch pathway.";
J. Biol. Chem. 286:18720-18730(2011).
[17]
INTERACTION WITH SGK1 AND FBXW7.
PubMed=21147854; DOI=10.1242/jcs.073924;
Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S.,
Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J.,
Park H.S.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
signaling by downregulation of protein stability through Fbw7
ubiquitin ligase.";
J. Cell Sci. 124:100-112(2011).
[18]
INTERACTION WITH SNW1.
PubMed=21245387; DOI=10.1128/MCB.00360-10;
Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D.,
Alves-Guerra M.C., Robbins D.J., Capobianco A.J.;
"Assembly of a Notch transcriptional activation complex requires
multimerization.";
Mol. Cell. Biol. 31:1396-1408(2011).
[19]
GLYCOSYLATION AT THR-232; THR-1402 AND THR-1725, AND PROTEOLYTIC
PROCESSING.
PubMed=24226769; DOI=10.1038/nature12723;
Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S.,
Clausen H., Brueckner M., Khokha M.K.;
"The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
type and laterality.";
Nature 504:456-459(2013).
[20]
ANKYRIN REPEATS.
PubMed=25547411; DOI=10.1186/s12859-014-0440-9;
Chakrabarty B., Parekh N.;
"Identifying tandem Ankyrin repeats in protein structures.";
BMC Bioinformatics 15:6599-6599(2014).
[21]
INTERACTION WITH ZMIZ1.
PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y.,
Alarcon A.S., Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S.,
Maillard I., Samuelson L.C., Cierpicki T., Chiang M.Y.;
"The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
Notch1 in T cell development and leukemia.";
Immunity 43:870-883(2015).
[22]
STRUCTURE BY NMR OF 1446-1480 IN COMPLEX WITH CALCIUM IONS, AND
DISULFIDE BONDS.
PubMed=12795601; DOI=10.1021/bi034156y;
Vardar D., North C.L., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.;
"Nuclear magnetic resonance structure of a prototype Lin12-Notch
repeat module from human Notch1.";
Biochemistry 42:7061-7067(2003).
[23]
STRUCTURE BY NMR OF 411-526.
PubMed=15576031; DOI=10.1016/j.str.2004.09.012;
Hambleton S., Valeyev N.V., Muranyi A., Knott V., Werner J.M.,
McMichael A.J., Handford P.A., Downing A.K.;
"Structural and functional properties of the human notch-1 ligand
binding region.";
Structure 12:2173-2183(2004).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1872-2114.
PubMed=16011479; DOI=10.1042/BJ20050515;
Ehebauer M.T., Chirgadze D.Y., Hayward P., Martinez Arias A.,
Blundell T.L.;
"High-resolution crystal structure of the human Notch 1 ankyrin
domain.";
Biochem. J. 392:13-20(2005).
[25]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1872-2126 IN COMPLEX WITH
RBPSUH AND MAML1.
PubMed=16530044; DOI=10.1016/j.cell.2005.12.037;
Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.;
"Structural basis for cooperativity in recruitment of MAML
coactivators to Notch transcription complexes.";
Cell 124:973-983(2006).
[26]
INVOLVEMENT IN AOVD1.
PubMed=16025100; DOI=10.1038/nature03940;
Garg V., Muth A.N., Ransom J.F., Schluterman M.K., Barnes R.,
King I.N., Grossfeld P.D., Srivastava D.;
"Mutations in NOTCH1 cause aortic valve disease.";
Nature 437:270-274(2005).
[27]
INVOLVEMENT IN AOS5, AND VARIANTS AOS5 ARG-429; TYR-1496 AND ASN-1989.
PubMed=25132448; DOI=10.1016/j.ajhg.2014.07.011;
Stittrich A.B., Lehman A., Bodian D.L., Ashworth J., Zong Z., Li H.,
Lam P., Khromykh A., Iyer R.K., Vockley J.G., Baveja R., Silva E.S.,
Dixon J., Leon E.L., Solomon B.D., Glusman G., Niederhuber J.E.,
Roach J.C., Patel M.S.;
"Mutations in NOTCH1 cause Adams-Oliver syndrome.";
Am. J. Hum. Genet. 95:275-284(2014).
-!- 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
RBPJ/RBPSUH and activates genes of the enhancer of split locus.
Affects the implementation of differentiation, proliferation and
apoptotic programs. Involved in angiogenesis; negatively regulates
endothelial cell proliferation and migration and angiogenic
sprouting. Involved in the maturation of both CD4+ and CD8+ cells
in the thymus. Important for follicular differentiation and
possibly cell fate selection within the follicle. During
cerebellar development, functions as a receptor for neuronal DNER
and is involved in the differentiation of Bergmann glia. Represses
neuronal and myogenic differentiation. May play an essential role
in postimplantation development, probably in some aspect of cell
specification and/or differentiation. May be involved in mesoderm
development, somite formation and neurogenesis. May enhance HIF1A
function by sequestering HIF1AN away from HIF1A. Required for the
THBS4 function in regulating protective astrogenesis from the
subventricular zone (SVZ) niche after injury. Involved in
determination of left/right symmetry by modulating the balance
between motile and immotile (sensory) cilia at the left-right
organiser (LRO). {ECO:0000269|PubMed:20616313}.
-!- SUBUNIT: 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 RBPJ/RBPSUH. Also
interacts with MAML1, MAML2 and MAML3 which act as transcriptional
coactivators for NOTCH1 (PubMed:11101851, PubMed:12370315). Notch
1 intracellular domain interacts with SNW1; the interaction
involves multimerized NOTCH1 NICD and is implicated in a formation
of an intermediate preactivation complex which associates with
DNA-bound CBF-1/RBPJ (PubMed:10713164). The activated membrane-
bound form interacts with AAK1 which promotes NOTCH1
stabilization. Forms a trimeric complex with FBXW7 and SGK1.
Interacts with HIF1AN. HIF1AN negatively regulates the function of
notch intracellular domain (NICD), accelerating myogenic
differentiation (PubMed:17573339). Interacts (via NICD) with SNAI1
(via zinc fingers); the interaction induces SNAI1 degradation via
MDM2-mediated ubiquitination and inhibits SNAI1-induced cell
invasion. Interacts (via NICD) with MDM2A. Interacts (via NICD)
with BCL6; the interaction decreases MAML1 recruitment by NOTCH1
NICD on target genes DNA and inhibits NOTCH1 transcractivation
activity. Interacts with THBS4 (By similarity). Interacts (via the
EGF-like repeat region) with NOV (via CTCK domain)
(PubMed:12050162). Interacts (via EGF-like domains) with DLL4 (via
N-terminal DSL and MNNL domains) (By similarity). Interacts with
ZMIZ1. Interacts (via NICD domain) with MEGF10 (via the
cytoplasmic domain) (By similarity).
{ECO:0000250|UniProtKB:Q01705, ECO:0000250|UniProtKB:Q07008,
ECO:0000269|PubMed:10713164, ECO:0000269|PubMed:11101851,
ECO:0000269|PubMed:12050162, ECO:0000269|PubMed:12370315,
ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:26522984,
ECO:0000269|PubMed:9590294}.
-!- INTERACTION:
O60341:KDM1A; NbExp=8; IntAct=EBI-636374, EBI-710124;
Q8N423:LILRB2; NbExp=8; IntAct=EBI-636374, EBI-2816428;
P19838:NFKB1; NbExp=2; IntAct=EBI-636374, EBI-300010;
Q13526:PIN1; NbExp=9; IntAct=EBI-636374, EBI-714158;
Q06330:RBPJ; NbExp=11; IntAct=EBI-636374, EBI-632552;
Q13573:SNW1; NbExp=3; IntAct=EBI-636374, EBI-632715;
P98170:XIAP; NbExp=4; IntAct=EBI-636374, EBI-517127;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q01705}.
-!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
{ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical
processing NICD is translocated to the nucleus. Nuclear location
may require MEGF10. {ECO:0000250|UniProtKB:Q01705}.
-!- 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.
-!- PTM: 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 ADAM17 to yield a membrane-
associated intermediate fragment called notch extracellular
truncation (NEXT). Following endocytosis, this fragment is then
cleaved by presenilin dependent gamma-secretase to release a
notch-derived peptide containing the intracellular domain (NICD)
from the membrane. {ECO:0000250|UniProtKB:Q01705}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- PTM: O-glycosylated on the EGF-like domains (PubMed:24226769).
Contains both O-linked fucose and O-linked glucose in the EGF-like
domains 11, 12 and 13, which are interacting with the residues on
DLL4 (By similarity). O-linked glycosylation by GALNT11 is
involved in determination of left/right symmetry: glycosylation
promotes activation of NOTCH1, possibly by promoting cleavage by
ADAM17, modulating the balance between motile and immotile
(sensory) cilia at the left-right organiser (LRO)
(PubMed:24226769). {ECO:0000250|UniProtKB:Q07008,
ECO:0000269|PubMed:24226769}.
-!- PTM: Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination
catalyzed by ITCH. Monoubiquitination at Lys-1759 is required for
activation by gamma-secretase cleavage, it promotes interaction
with AAK1, which stabilizes it. Deubiquitination by EIF3F is
necessary for nuclear import of activated Notch.
{ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:24226769}.
-!- PTM: Hydroxylated at Asn-1955 by HIF1AN. Hydroxylated at Asn-2022
by HIF1AN (By similarity). Hydroxylation reduces affinity for
HI1AN and may thus indirectly modulate negative regulation of NICD
(By similarity). {ECO:0000250}.
-!- DISEASE: Aortic valve disease 1 (AOVD1) [MIM:109730]: A common
defect in the aortic valve in which two rather than three leaflets
are present. It is often associated with aortic valve
calcification, stenosis and insufficiency. In extreme cases, the
blood flow may be so restricted that the left ventricle fails to
grow, resulting in hypoplastic left heart syndrome.
{ECO:0000269|PubMed:16025100}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Adams-Oliver syndrome 5 (AOS5) [MIM:616028]: A form of
Adams-Oliver syndrome, a disorder characterized by the congenital
absence of skin (aplasia cutis congenita) in combination with
transverse limb defects. Aplasia cutis congenita can be located
anywhere on the body, but in the vast majority of the cases, it is
present on the posterior parietal region where it is often
associated with an underlying defect of the parietal bones. Limb
abnormalities are typically limb truncation defects affecting the
distal phalanges or entire digits (true ectrodactyly). Only
rarely, metatarsals/metacarpals or more proximal limb structures
are also affected. Apart from transverse limb defects, syndactyly,
most commonly of second and third toes, can also be observed. The
clinical features are highly variable and can also include
cardiovascular malformations, brain abnormalities and vascular
defects such as cutis marmorata and dilated scalp veins.
{ECO:0000269|PubMed:25132448}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NOTCH1ID30ch9q34.html";
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EMBL; AF308602; AAG33848.1; -; mRNA.
EMBL; AL592301; CAI13934.1; -; Genomic_DNA.
EMBL; AL354671; CAI13934.1; JOINED; Genomic_DNA.
EMBL; AL354671; CAI16149.1; -; Genomic_DNA.
EMBL; AL592301; CAI16149.1; JOINED; Genomic_DNA.
EMBL; M73980; AAA60614.1; -; mRNA.
EMBL; AB209873; BAD93110.1; -; mRNA.
CCDS; CCDS43905.1; -.
PIR; A40043; A40043.
RefSeq; NP_060087.3; NM_017617.4.
UniGene; Hs.495473; -.
PDB; 1PB5; NMR; -; A=1446-1480.
PDB; 1TOZ; NMR; -; A=411-526.
PDB; 1YYH; X-ray; 1.90 A; A/B=1872-2114.
PDB; 2F8X; X-ray; 3.25 A; K=1872-2126.
PDB; 2F8Y; X-ray; 1.55 A; A/B=1905-2126.
PDB; 2HE0; X-ray; 1.90 A; A/B=1872-2114.
PDB; 2VJ3; X-ray; 2.60 A; A=411-526.
PDB; 3ETO; X-ray; 2.00 A; A/B=1446-1733.
PDB; 3I08; X-ray; 3.20 A; A/C=1446-1664, B/D=1665-1733.
PDB; 3L95; X-ray; 2.19 A; X/Y=1448-1728.
PDB; 3NBN; X-ray; 3.45 A; B/E=1872-2126.
PDB; 3V79; X-ray; 3.85 A; K=1872-2126, R=1759-1777.
PDB; 4CUD; X-ray; 1.85 A; A=411-526.
PDB; 4CUE; X-ray; 3.00 A; A=411-526.
PDB; 4CUF; X-ray; 2.29 A; A=411-526.
PDB; 4D0E; X-ray; 1.61 A; A=411-526.
PDB; 4D0F; X-ray; 2.80 A; A=411-526.
PDB; 5FM9; X-ray; 2.92 A; A=140-294.
PDB; 5FMA; X-ray; 2.46 A; A/B=142-294.
PDB; 5KZO; NMR; -; A=1721-1771.
PDBsum; 1PB5; -.
PDBsum; 1TOZ; -.
PDBsum; 1YYH; -.
PDBsum; 2F8X; -.
PDBsum; 2F8Y; -.
PDBsum; 2HE0; -.
PDBsum; 2VJ3; -.
PDBsum; 3ETO; -.
PDBsum; 3I08; -.
PDBsum; 3L95; -.
PDBsum; 3NBN; -.
PDBsum; 3V79; -.
PDBsum; 4CUD; -.
PDBsum; 4CUE; -.
PDBsum; 4CUF; -.
PDBsum; 4D0E; -.
PDBsum; 4D0F; -.
PDBsum; 5FM9; -.
PDBsum; 5FMA; -.
PDBsum; 5KZO; -.
DisProt; DP01104; -.
ProteinModelPortal; P46531; -.
SMR; P46531; -.
BioGrid; 110913; 195.
DIP; DIP-29919N; -.
IntAct; P46531; 150.
MINT; MINT-1417018; -.
STRING; 9606.ENSP00000277541; -.
BindingDB; P46531; -.
ChEMBL; CHEMBL2146346; -.
iPTMnet; P46531; -.
PhosphoSitePlus; P46531; -.
BioMuta; NOTCH1; -.
DMDM; 206729936; -.
EPD; P46531; -.
MaxQB; P46531; -.
PaxDb; P46531; -.
PeptideAtlas; P46531; -.
PRIDE; P46531; -.
Ensembl; ENST00000277541; ENSP00000277541; ENSG00000148400.
GeneID; 4851; -.
KEGG; hsa:4851; -.
UCSC; uc004chz.4; human.
CTD; 4851; -.
DisGeNET; 4851; -.
GeneCards; NOTCH1; -.
H-InvDB; HIX0008549; -.
HGNC; HGNC:7881; NOTCH1.
HPA; CAB008112; -.
HPA; CAB022466; -.
HPA; HPA067168; -.
MalaCards; NOTCH1; -.
MIM; 109730; phenotype.
MIM; 190198; gene.
MIM; 616028; phenotype.
neXtProt; NX_P46531; -.
OpenTargets; ENSG00000148400; -.
Orphanet; 974; Adams-Oliver syndrome.
Orphanet; 402075; Familial bicuspid aortic valve.
PharmGKB; PA31683; -.
eggNOG; ENOG410IR7G; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00810000125346; -.
HOGENOM; HOG000234369; -.
HOVERGEN; HBG052650; -.
InParanoid; P46531; -.
KO; K02599; -.
OMA; QYVNSYT; -.
OrthoDB; EOG091G01NU; -.
PhylomeDB; P46531; -.
TreeFam; TF351641; -.
Reactome; R-HSA-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-5083630; Defective LFNG causes SCDO3.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
SignaLink; P46531; -.
SIGNOR; P46531; -.
ChiTaRS; NOTCH1; human.
EvolutionaryTrace; P46531; -.
GeneWiki; Notch-1; -.
GenomeRNAi; 4851; -.
PRO; PR:P46531; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148400; -.
CleanEx; HS_NOTCH1; -.
Genevisible; P46531; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
GO; GO:0005112; F:Notch binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISS:BHF-UCL.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0060842; P:arterial endothelial cell differentiation; ISS:BHF-UCL.
GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
GO; GO:0003162; P:atrioventricular node development; IEA:Ensembl.
GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0003209; P:cardiac atrium morphogenesis; ISS:BHF-UCL.
GO; GO:0003207; P:cardiac chamber formation; ISS:BHF-UCL.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0003213; P:cardiac right atrium morphogenesis; ISS:BHF-UCL.
GO; GO:0003219; P:cardiac right ventricle formation; IEA:Ensembl.
GO; GO:0060411; P:cardiac septum morphogenesis; ISS:BHF-UCL.
GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISS:BHF-UCL.
GO; GO:0003208; P:cardiac ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0021515; P:cell differentiation in spinal cord; IEA:Ensembl.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:BHF-UCL.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0072044; P:collecting duct development; IEA:Ensembl.
GO; GO:0007386; P:compartment pattern specification; IEA:Ensembl.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
GO; GO:0003169; P:coronary vein morphogenesis; ISS:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
GO; GO:0072017; P:distal tubule development; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0060956; P:endocardial cell differentiation; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0003157; P:endocardium development; ISS:BHF-UCL.
GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0007492; P:endoderm development; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0007440; P:foregut morphogenesis; IEA:Ensembl.
GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
GO; GO:0003241; P:growth involved in heart morphogenesis; ISS:BHF-UCL.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0007507; P:heart development; IMP:DFLAT.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL.
GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0014031; P:mesenchymal cell development; ISS:BHF-UCL.
GO; GO:0003192; P:mitral valve formation; IMP:BHF-UCL.
GO; GO:2000811; P:negative regulation of anoikis; IMP:BHF-UCL.
GO; GO:0045608; P:negative regulation of auditory receptor cell differentiation; IEA:Ensembl.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:BHF-UCL.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:BHF-UCL.
GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; IDA:UniProtKB.
GO; GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IEA:Ensembl.
GO; GO:2000974; P:negative regulation of pro-B cell differentiation; ISS:UniProtKB.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEP:UniProtKB.
GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0003344; P:pericardium morphogenesis; ISS:BHF-UCL.
GO; GO:1903849; P:positive regulation of aorta morphogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:1901201; P:regulation of extracellular matrix assembly; ISS:BHF-UCL.
GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0035148; P:tube formation; IMP:UniProtKB.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
GO; GO:0060843; P:venous endothelial cell differentiation; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR024600; DUF3454_notch.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR008297; Notch.
InterPro; IPR022362; Notch_1.
InterPro; IPR000800; Notch_dom.
InterPro; IPR010660; Notch_NOD_dom.
InterPro; IPR011656; Notch_NODP_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF11936; DUF3454; 1.
Pfam; PF00008; EGF; 25.
Pfam; PF07645; EGF_CA; 4.
Pfam; PF12661; hEGF; 2.
Pfam; PF06816; NOD; 1.
Pfam; PF07684; NODP; 1.
Pfam; PF00066; Notch; 3.
PIRSF; PIRSF002279; Notch; 1.
PRINTS; PR01452; LNOTCHREPEAT.
PRINTS; PR01984; NOTCH1.
SMART; SM00248; ANK; 6.
SMART; SM01334; DUF3454; 1.
SMART; SM00181; EGF; 36.
SMART; SM00179; EGF_CA; 33.
SMART; SM00004; NL; 3.
SMART; SM01338; NOD; 1.
SMART; SM01339; NODP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57184; SSF57184; 6.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS00010; ASX_HYDROXYL; 22.
PROSITE; PS00022; EGF_1; 35.
PROSITE; PS01186; EGF_2; 27.
PROSITE; PS50026; EGF_3; 36.
PROSITE; PS01187; EGF_CA; 20.
PROSITE; PS50258; LNR; 3.
1: Evidence at protein level;
3D-structure; Activator; Angiogenesis; ANK repeat; Calcium;
Cell membrane; Complete proteome; Developmental protein;
Differentiation; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation;
Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway;
Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transcription; Transcription regulation;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 2555 Neurogenic locus notch homolog protein 1.
/FTId=PRO_0000007674.
CHAIN 1721 2555 Notch 1 extracellular truncation.
{ECO:0000250}.
/FTId=PRO_0000007675.
CHAIN 1754 2555 Notch 1 intracellular domain.
{ECO:0000250}.
/FTId=PRO_0000007676.
TOPO_DOM 19 1735 Extracellular. {ECO:0000255}.
TRANSMEM 1736 1756 Helical. {ECO:0000255}.
TOPO_DOM 1757 2555 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 58 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 59 99 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 102 139 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 140 176 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 178 216 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 218 255 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 257 293 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 295 333 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 335 371 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 372 410 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 412 450 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 452 488 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 490 526 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 528 564 EGF-like 14; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 566 601 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 603 639 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 641 676 EGF-like 17; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 678 714 EGF-like 18; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 716 751 EGF-like 19; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 753 789 EGF-like 20. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 791 827 EGF-like 21; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 829 867 EGF-like 22. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 869 905 EGF-like 23; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 907 943 EGF-like 24. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 945 981 EGF-like 25; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 983 1019 EGF-like 26. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1021 1057 EGF-like 27. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1059 1095 EGF-like 28. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1097 1143 EGF-like 29. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1145 1181 EGF-like 30. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1183 1219 EGF-like 31; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1221 1265 EGF-like 32; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1267 1305 EGF-like 33. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1307 1346 EGF-like 34. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1348 1384 EGF-like 35. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1387 1426 EGF-like 36. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1449 1489 LNR 1.
REPEAT 1490 1531 LNR 2.
REPEAT 1532 1571 LNR 3.
REPEAT 1928 1960 ANK 1.
REPEAT 1961 1994 ANK 2.
REPEAT 1995 2027 ANK 3.
REPEAT 2028 2060 ANK 4.
REPEAT 2061 2094 ANK 5.
REPEAT 2095 2122 ANK 6.
REGION 420 421 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 448 452 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 1947 1955 HIF1AN-binding. {ECO:0000250}.
REGION 2014 2022 HIF1AN-binding. {ECO:0000250}.
COMPBIAS 1575 1578 Poly-Val.
COMPBIAS 1661 1664 Poly-Arg.
COMPBIAS 1728 1731 Poly-Pro.
COMPBIAS 1740 1743 Poly-Ala.
COMPBIAS 1901 1904 Poly-Glu.
COMPBIAS 2259 2262 Poly-Gly.
COMPBIAS 2403 2406 Poly-Gln.
COMPBIAS 2410 2417 Poly-Pro.
COMPBIAS 2521 2524 Poly-Ser.
METAL 432 432 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 435 435 Calcium 1; via amide nitrogen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 452 452 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 453 453 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 455 455 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 469 469 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 470 470 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 490 490 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 491 491 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 493 493 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 507 507 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 508 508 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 1457 1457 Calcium 4; via carbonyl oxygen.
METAL 1460 1460 Calcium 4.
METAL 1475 1475 Calcium 4.
METAL 1478 1478 Calcium 4.
SITE 469 469 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
SITE 1664 1665 Cleavage; by furin-like protease.
{ECO:0000250}.
SITE 1710 1711 Cleavage; by ADAM17. {ECO:0000250}.
SITE 1720 1721 Cleavage; by ADAM17.
MOD_RES 1861 1861 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01705}.
MOD_RES 1955 1955 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17573339}.
MOD_RES 2022 2022 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 73 73 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 116 116 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 146 146 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 194 194 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 232 232 O-linked (Fuc...) threonine; alternate.
{ECO:0000269|PubMed:24226769}.
CARBOHYD 232 232 O-linked (GalNAc...) threonine;
alternate. {ECO:0000269|PubMed:24226769}.
CARBOHYD 341 341 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 378 378 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 435 435 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 458 458 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 466 466 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 496 496 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 534 534 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 609 609 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 647 647 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 722 722 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 759 759 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 767 767 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 797 797 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 805 805 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 951 951 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 959 959 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1027 1027 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1035 1035 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1065 1065 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1179 1179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1189 1189 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1197 1197 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1241 1241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1273 1273 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1362 1362 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1402 1402 O-linked (Fuc...) threonine; alternate.
{ECO:0000269|PubMed:24226769}.
CARBOHYD 1402 1402 O-linked (GalNAc...) threonine;
alternate. {ECO:0000269|PubMed:24226769}.
CARBOHYD 1489 1489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1587 1587 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1725 1725 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:24226769}.
DISULFID 24 37 {ECO:0000250}.
DISULFID 31 46 {ECO:0000250}.
DISULFID 48 57 {ECO:0000250}.
DISULFID 63 74 {ECO:0000250}.
DISULFID 68 87 {ECO:0000250}.
DISULFID 89 98 {ECO:0000250}.
DISULFID 106 117 {ECO:0000250}.
DISULFID 111 127 {ECO:0000250}.
DISULFID 129 138 {ECO:0000250}.
DISULFID 144 155 {ECO:0000250}.
DISULFID 149 164 {ECO:0000250}.
DISULFID 166 175 {ECO:0000250}.
DISULFID 182 195 {ECO:0000250}.
DISULFID 189 204 {ECO:0000250}.
DISULFID 206 215 {ECO:0000250}.
DISULFID 222 233 {ECO:0000250}.
DISULFID 227 243 {ECO:0000250}.
DISULFID 245 254 {ECO:0000250}.
DISULFID 261 272 {ECO:0000250}.
DISULFID 266 281 {ECO:0000250}.
DISULFID 283 292 {ECO:0000250}.
DISULFID 299 312 {ECO:0000250}.
DISULFID 306 321 {ECO:0000250}.
DISULFID 323 332 {ECO:0000250}.
DISULFID 339 350 {ECO:0000250}.
DISULFID 344 359 {ECO:0000250}.
DISULFID 361 370 {ECO:0000250}.
DISULFID 376 387 {ECO:0000250}.
DISULFID 381 398 {ECO:0000250}.
DISULFID 400 409 {ECO:0000250}.
DISULFID 416 429 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 423 438 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 440 449 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 456 467 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 461 476 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 478 487 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 494 505 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 499 514 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 516 525 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 532 543 {ECO:0000250}.
DISULFID 537 552 {ECO:0000250}.
DISULFID 554 563 {ECO:0000250}.
DISULFID 570 580 {ECO:0000250}.
DISULFID 575 589 {ECO:0000250}.
DISULFID 591 600 {ECO:0000250}.
DISULFID 607 618 {ECO:0000250}.
DISULFID 612 627 {ECO:0000250}.
DISULFID 629 638 {ECO:0000250}.
DISULFID 645 655 {ECO:0000250}.
DISULFID 650 664 {ECO:0000250}.
DISULFID 666 675 {ECO:0000250}.
DISULFID 682 693 {ECO:0000250}.
DISULFID 687 702 {ECO:0000250}.
DISULFID 704 713 {ECO:0000250}.
DISULFID 720 730 {ECO:0000250}.
DISULFID 725 739 {ECO:0000250}.
DISULFID 741 750 {ECO:0000250}.
DISULFID 757 768 {ECO:0000250}.
DISULFID 762 777 {ECO:0000250}.
DISULFID 779 788 {ECO:0000250}.
DISULFID 795 806 {ECO:0000250}.
DISULFID 800 815 {ECO:0000250}.
DISULFID 817 826 {ECO:0000250}.
DISULFID 833 844 {ECO:0000250}.
DISULFID 838 855 {ECO:0000250}.
DISULFID 857 866 {ECO:0000250}.
DISULFID 873 884 {ECO:0000250}.
DISULFID 878 893 {ECO:0000250}.
DISULFID 895 904 {ECO:0000250}.
DISULFID 911 922 {ECO:0000250}.
DISULFID 916 931 {ECO:0000250}.
DISULFID 933 942 {ECO:0000250}.
DISULFID 949 960 {ECO:0000250}.
DISULFID 954 969 {ECO:0000250}.
DISULFID 971 980 {ECO:0000250}.
DISULFID 987 998 {ECO:0000250}.
DISULFID 992 1007 {ECO:0000250}.
DISULFID 1009 1018 {ECO:0000250}.
DISULFID 1025 1036 {ECO:0000250}.
DISULFID 1030 1045 {ECO:0000250}.
DISULFID 1047 1056 {ECO:0000250}.
DISULFID 1063 1074 {ECO:0000250}.
DISULFID 1068 1083 {ECO:0000250}.
DISULFID 1085 1094 {ECO:0000250}.
DISULFID 1101 1122 {ECO:0000250}.
DISULFID 1116 1131 {ECO:0000250}.
DISULFID 1133 1142 {ECO:0000250}.
DISULFID 1149 1160 {ECO:0000250}.
DISULFID 1154 1169 {ECO:0000250}.
DISULFID 1171 1180 {ECO:0000250}.
DISULFID 1187 1198 {ECO:0000250}.
DISULFID 1192 1207 {ECO:0000250}.
DISULFID 1209 1218 {ECO:0000250}.
DISULFID 1225 1244 {ECO:0000250}.
DISULFID 1238 1253 {ECO:0000250}.
DISULFID 1255 1264 {ECO:0000250}.
DISULFID 1271 1284 {ECO:0000250}.
DISULFID 1276 1293 {ECO:0000250}.
DISULFID 1295 1304 {ECO:0000250}.
DISULFID 1311 1322 {ECO:0000250}.
DISULFID 1316 1334 {ECO:0000250}.
DISULFID 1336 1345 {ECO:0000250}.
DISULFID 1352 1363 {ECO:0000250}.
DISULFID 1357 1372 {ECO:0000250}.
DISULFID 1374 1383 {ECO:0000250}.
DISULFID 1391 1403 {ECO:0000250}.
DISULFID 1397 1414 {ECO:0000250}.
DISULFID 1416 1425 {ECO:0000250}.
DISULFID 1449 1472 {ECO:0000269|PubMed:12795601}.
DISULFID 1454 1467 {ECO:0000269|PubMed:12795601}.
DISULFID 1463 1479 {ECO:0000269|PubMed:12795601}.
DISULFID 1490 1514 {ECO:0000250}.
DISULFID 1496 1509 {ECO:0000250}.
DISULFID 1505 1521 {ECO:0000250}.
DISULFID 1536 1549 {ECO:0000250}.
DISULFID 1545 1561 {ECO:0000250}.
CROSSLNK 1759 1759 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01705}.
VARIANT 300 300 Q -> R (in dbSNP:rs11574885).
/FTId=VAR_034898.
VARIANT 429 429 C -> R (in AOS5; dbSNP:rs587777736).
{ECO:0000269|PubMed:25132448}.
/FTId=VAR_071960.
VARIANT 879 879 R -> W (in dbSNP:rs11574895).
/FTId=VAR_048990.
VARIANT 1496 1496 C -> Y (in AOS5; dbSNP:rs587781259).
{ECO:0000269|PubMed:25132448}.
/FTId=VAR_071961.
VARIANT 1671 1671 V -> I (in dbSNP:rs2229968).
/FTId=VAR_046618.
VARIANT 1989 1989 D -> N (in AOS5; dbSNP:rs587777734).
{ECO:0000269|PubMed:25132448}.
/FTId=VAR_071962.
CONFLICT 187 187 G -> R (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 282 282 R -> P (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 477 477 I -> M (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 614 615 HG -> LR (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 621 621 R -> P (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 677 677 I -> S (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 775 775 Y -> I (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 803 803 Q -> K (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 860 862 GWQ -> AGAK (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 1021 1021 D -> V (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 1028 1028 Q -> R (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 1032 1032 H -> L (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
CONFLICT 1040 1043 CGSY -> RGLH (in Ref. 1; AAG33848 and 3;
AAA60614). {ECO:0000305}.
HELIX 143 146 {ECO:0000244|PDB:5FMA}.
STRAND 154 157 {ECO:0000244|PDB:5FMA}.
STRAND 162 165 {ECO:0000244|PDB:5FMA}.
STRAND 170 175 {ECO:0000244|PDB:5FMA}.
HELIX 181 184 {ECO:0000244|PDB:5FMA}.
TURN 190 192 {ECO:0000244|PDB:5FMA}.
STRAND 194 198 {ECO:0000244|PDB:5FMA}.
STRAND 201 205 {ECO:0000244|PDB:5FMA}.
STRAND 210 212 {ECO:0000244|PDB:5FMA}.
STRAND 232 235 {ECO:0000244|PDB:5FMA}.
STRAND 237 239 {ECO:0000244|PDB:5FMA}.
STRAND 241 244 {ECO:0000244|PDB:5FMA}.
STRAND 249 254 {ECO:0000244|PDB:5FMA}.
STRAND 271 274 {ECO:0000244|PDB:5FMA}.
STRAND 279 282 {ECO:0000244|PDB:5FMA}.
STRAND 289 292 {ECO:0000244|PDB:5FMA}.
HELIX 415 417 {ECO:0000244|PDB:4D0E}.
STRAND 418 420 {ECO:0000244|PDB:4D0E}.
STRAND 422 424 {ECO:0000244|PDB:4D0E}.
STRAND 428 432 {ECO:0000244|PDB:4D0E}.
STRAND 435 439 {ECO:0000244|PDB:4D0E}.
STRAND 444 446 {ECO:0000244|PDB:4D0E}.
TURN 455 458 {ECO:0000244|PDB:4D0E}.
STRAND 466 470 {ECO:0000244|PDB:4D0E}.
STRAND 473 477 {ECO:0000244|PDB:4D0E}.
STRAND 482 484 {ECO:0000244|PDB:4D0E}.
TURN 493 496 {ECO:0000244|PDB:4D0E}.
TURN 500 502 {ECO:0000244|PDB:2VJ3}.
STRAND 504 507 {ECO:0000244|PDB:4D0E}.
STRAND 512 515 {ECO:0000244|PDB:4D0E}.
STRAND 520 522 {ECO:0000244|PDB:4D0E}.
HELIX 1448 1450 {ECO:0000244|PDB:3L95}.
HELIX 1452 1457 {ECO:0000244|PDB:3ETO}.
STRAND 1460 1462 {ECO:0000244|PDB:3ETO}.
HELIX 1465 1467 {ECO:0000244|PDB:3ETO}.
HELIX 1470 1472 {ECO:0000244|PDB:3ETO}.
HELIX 1473 1476 {ECO:0000244|PDB:3ETO}.
TURN 1477 1482 {ECO:0000244|PDB:3ETO}.
TURN 1486 1489 {ECO:0000244|PDB:3ETO}.
HELIX 1492 1494 {ECO:0000244|PDB:3ETO}.
HELIX 1496 1498 {ECO:0000244|PDB:3ETO}.
TURN 1499 1501 {ECO:0000244|PDB:3ETO}.
STRAND 1502 1504 {ECO:0000244|PDB:3ETO}.
HELIX 1507 1509 {ECO:0000244|PDB:3ETO}.
HELIX 1512 1519 {ECO:0000244|PDB:3ETO}.
TURN 1530 1532 {ECO:0000244|PDB:3ETO}.
HELIX 1533 1539 {ECO:0000244|PDB:3ETO}.
STRAND 1542 1544 {ECO:0000244|PDB:3ETO}.
HELIX 1547 1549 {ECO:0000244|PDB:3ETO}.
HELIX 1552 1559 {ECO:0000244|PDB:3ETO}.
STRAND 1563 1565 {ECO:0000244|PDB:3L95}.
STRAND 1571 1580 {ECO:0000244|PDB:3ETO}.
HELIX 1582 1587 {ECO:0000244|PDB:3ETO}.
HELIX 1589 1600 {ECO:0000244|PDB:3ETO}.
STRAND 1602 1606 {ECO:0000244|PDB:3ETO}.
STRAND 1616 1620 {ECO:0000244|PDB:3ETO}.
STRAND 1672 1681 {ECO:0000244|PDB:3ETO}.
HELIX 1685 1688 {ECO:0000244|PDB:3ETO}.
HELIX 1696 1708 {ECO:0000244|PDB:3ETO}.
STRAND 1714 1716 {ECO:0000244|PDB:3ETO}.
STRAND 1718 1724 {ECO:0000244|PDB:3ETO}.
HELIX 1884 1890 {ECO:0000244|PDB:2F8X}.
HELIX 1909 1914 {ECO:0000244|PDB:2F8X}.
TURN 1925 1927 {ECO:0000244|PDB:2F8Y}.
HELIX 1931 1937 {ECO:0000244|PDB:2F8Y}.
HELIX 1941 1949 {ECO:0000244|PDB:2F8Y}.
HELIX 1964 1970 {ECO:0000244|PDB:2F8Y}.
HELIX 1974 1982 {ECO:0000244|PDB:2F8Y}.
STRAND 1983 1985 {ECO:0000244|PDB:2F8X}.
HELIX 1998 2005 {ECO:0000244|PDB:2F8Y}.
HELIX 2008 2016 {ECO:0000244|PDB:2F8Y}.
HELIX 2031 2037 {ECO:0000244|PDB:2F8Y}.
HELIX 2041 2049 {ECO:0000244|PDB:2F8Y}.
HELIX 2064 2071 {ECO:0000244|PDB:2F8Y}.
HELIX 2074 2082 {ECO:0000244|PDB:2F8Y}.
HELIX 2097 2103 {ECO:0000244|PDB:2F8Y}.
HELIX 2107 2115 {ECO:0000244|PDB:2F8Y}.
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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Genprice Inc, Invoices and accounting
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