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Q07008

- NOTC1_RAT

UniProt

Q07008 - NOTC1_RAT

Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (16 Oct 2013)
      Previous versions | rss
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    Functioni

    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) By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1457 – 14571Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi1460 – 14601CalciumPROSITE-ProRule annotation
    Metal bindingi1475 – 14751CalciumPROSITE-ProRule annotation
    Metal bindingi1478 – 14781CalciumPROSITE-ProRule annotation
    Sitei1654 – 16552Cleavage; by furin-like proteaseBy similarity
    Sitei1710 – 17112Cleavage; by ADAM17By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. core promoter binding Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. enzyme inhibitor activity Source: UniProtKB
    5. receptor activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. astrocyte differentiation Source: RGD
    3. brain development Source: RGD
    4. cell differentiation in spinal cord Source: RGD
    5. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    6. cilium morphogenesis Source: UniProtKB
    7. negative regulation of catalytic activity Source: UniProtKB
    8. negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
    9. negative regulation of cell proliferation Source: UniProtKB
    10. negative regulation of endothelial cell chemotaxis Source: UniProtKB
    11. negative regulation of glial cell proliferation Source: UniProtKB
    12. negative regulation of myotube differentiation Source: UniProtKB
    13. negative regulation of neurogenesis Source: UniProtKB
    14. negative regulation of neuron differentiation Source: RGD
    15. negative regulation of oligodendrocyte differentiation Source: UniProtKB
    16. negative regulation of pro-B cell differentiation Source: UniProtKB
    17. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    18. Notch signaling involved in heart development Source: UniProtKB
    19. Notch signaling pathway Source: RGD
    20. oligodendrocyte differentiation Source: RGD
    21. organ regeneration Source: RGD
    22. positive regulation of astrocyte differentiation Source: UniProtKB
    23. positive regulation of BMP signaling pathway Source: UniProtKB
    24. positive regulation of endothelial cell differentiation Source: RGD
    25. positive regulation of glial cell differentiation Source: RGD
    26. positive regulation of JAK-STAT cascade Source: UniProtKB
    27. positive regulation of neuroblast proliferation Source: RGD
    28. positive regulation of transcription, DNA-templated Source: UniProtKB
    29. positive regulation of transcription from RNA polymerase II promoter Source: RGD
    30. positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
    31. positive regulation of transcription of Notch receptor target Source: RGD
    32. regulation of cardioblast proliferation Source: RGD
    33. regulation of cell proliferation Source: RGD
    34. response to corticosteroid Source: RGD
    35. response to lipopolysaccharide Source: RGD
    36. spermatogenesis Source: RGD
    37. tissue regeneration Source: RGD
    38. transcription, DNA-templated Source: UniProtKB-KW
    39. tube formation Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Developmental protein, Receptor

    Keywords - Biological processi

    Angiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_194345. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_198299. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_198304. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_198659. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_198750. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_198752. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_198754. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_198789. Pre-NOTCH Processing in Golgi.
    REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurogenic locus notch homolog protein 1
    Short name:
    Notch 1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Notch1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi3187. Notch1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. acrosomal vesicle Source: RGD
    2. cytoskeleton Source: UniProtKB
    3. Golgi apparatus Source: RGD
    4. integral component of membrane Source: UniProtKB-KW
    5. lamellipodium Source: UniProtKB
    6. nucleus Source: RGD
    7. plasma membrane Source: RGD
    8. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 25312513Neurogenic locus notch homolog protein 1PRO_0000007680Add
    BLAST
    Chaini1711 – 2531821Notch 1 extracellular truncationBy similarityPRO_0000007681Add
    BLAST
    Chaini1744 – 2531788Notch 1 intracellular domainBy similarityPRO_0000007682Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 37By similarity
    Disulfide bondi31 ↔ 46By similarity
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi48 ↔ 57By similarity
    Disulfide bondi63 ↔ 74By similarity
    Glycosylationi65 – 651O-linked (Glc...)By similarity
    Disulfide bondi68 ↔ 87By similarity
    Glycosylationi73 – 731O-linked (Fuc...)By similarity
    Disulfide bondi89 ↔ 98By similarity
    Disulfide bondi106 ↔ 117By similarity
    Disulfide bondi111 ↔ 127By similarity
    Glycosylationi116 – 1161O-linked (Fuc...)By similarity
    Disulfide bondi129 ↔ 138By similarity
    Disulfide bondi144 ↔ 155By similarity
    Glycosylationi146 – 1461O-linked (Glc...)By similarity
    Disulfide bondi149 ↔ 164By similarity
    Disulfide bondi166 ↔ 175By similarity
    Disulfide bondi182 ↔ 195By similarity
    Disulfide bondi189 ↔ 204By similarity
    Glycosylationi194 – 1941O-linked (Fuc...)By similarity
    Disulfide bondi206 ↔ 215By similarity
    Disulfide bondi222 ↔ 233By similarity
    Disulfide bondi227 ↔ 243By similarity
    Glycosylationi232 – 2321O-linked (Fuc...); alternateBy similarity
    Glycosylationi232 – 2321O-linked (GalNAc...); alternateBy similarity
    Disulfide bondi245 ↔ 254By similarity
    Disulfide bondi261 ↔ 272By similarity
    Disulfide bondi266 ↔ 281By similarity
    Disulfide bondi283 ↔ 292By similarity
    Disulfide bondi299 ↔ 312By similarity
    Disulfide bondi306 ↔ 321By similarity
    Disulfide bondi323 ↔ 332By similarity
    Disulfide bondi339 ↔ 350By similarity
    Glycosylationi341 – 3411O-linked (Glc...)By similarity
    Disulfide bondi344 ↔ 359By similarity
    Disulfide bondi361 ↔ 370By similarity
    Disulfide bondi376 ↔ 387By similarity
    Glycosylationi378 – 3781O-linked (Glc...)By similarity
    Disulfide bondi381 ↔ 398By similarity
    Disulfide bondi400 ↔ 409By similarity
    Disulfide bondi416 ↔ 429By similarity
    Disulfide bondi423 ↔ 438By similarity
    Disulfide bondi440 ↔ 449By similarity
    Disulfide bondi456 ↔ 467By similarity
    Glycosylationi458 – 4581O-linked (Glc...)By similarity
    Disulfide bondi461 ↔ 476By similarity
    Glycosylationi466 – 4661O-linked (Fuc...)By similarity
    Disulfide bondi478 ↔ 487By similarity
    Disulfide bondi494 ↔ 505By similarity
    Glycosylationi496 – 4961O-linked (Glc...)By similarity
    Disulfide bondi499 ↔ 514By similarity
    Disulfide bondi516 ↔ 525By similarity
    Disulfide bondi532 ↔ 543By similarity
    Glycosylationi534 – 5341O-linked (Glc...)By similarity
    Disulfide bondi537 ↔ 552By similarity
    Disulfide bondi554 ↔ 563By similarity
    Disulfide bondi570 ↔ 580By similarity
    Disulfide bondi575 ↔ 589By similarity
    Disulfide bondi591 ↔ 600By similarity
    Disulfide bondi607 ↔ 618By similarity
    Glycosylationi609 – 6091O-linked (Glc...)By similarity
    Disulfide bondi612 ↔ 627By similarity
    Disulfide bondi629 ↔ 638By similarity
    Disulfide bondi645 ↔ 655By similarity
    Glycosylationi647 – 6471O-linked (Glc...)By similarity
    Disulfide bondi650 ↔ 664By similarity
    Disulfide bondi666 ↔ 675By similarity
    Disulfide bondi682 ↔ 693By similarity
    Disulfide bondi687 ↔ 702By similarity
    Disulfide bondi704 ↔ 713By similarity
    Disulfide bondi720 ↔ 730By similarity
    Glycosylationi722 – 7221O-linked (Glc...)By similarity
    Disulfide bondi725 ↔ 739By similarity
    Disulfide bondi741 ↔ 750By similarity
    Disulfide bondi757 ↔ 768By similarity
    Glycosylationi759 – 7591O-linked (Glc...)By similarity
    Disulfide bondi762 ↔ 777By similarity
    Glycosylationi767 – 7671O-linked (Fuc...)By similarity
    Disulfide bondi779 ↔ 788By similarity
    Disulfide bondi795 ↔ 806By similarity
    Glycosylationi797 – 7971O-linked (Glc...)By similarity
    Disulfide bondi800 ↔ 815By similarity
    Glycosylationi805 – 8051O-linked (Fuc...)By similarity
    Disulfide bondi817 ↔ 826By similarity
    Disulfide bondi833 ↔ 844By similarity
    Disulfide bondi838 ↔ 855By similarity
    Disulfide bondi857 ↔ 866By similarity
    Disulfide bondi873 ↔ 884By similarity
    Disulfide bondi878 ↔ 893By similarity
    Glycosylationi888 – 8881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi895 ↔ 904By similarity
    Disulfide bondi911 ↔ 922By similarity
    Disulfide bondi916 ↔ 931By similarity
    Disulfide bondi933 ↔ 942By similarity
    Disulfide bondi949 ↔ 960By similarity
    Glycosylationi951 – 9511O-linked (Glc...)By similarity
    Disulfide bondi954 ↔ 969By similarity
    Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi971 ↔ 980By similarity
    Disulfide bondi987 ↔ 998By similarity
    Disulfide bondi992 ↔ 1007By similarity
    Disulfide bondi1009 ↔ 1018By similarity
    Disulfide bondi1025 ↔ 1036By similarity
    Glycosylationi1027 – 10271O-linked (Glc...)By similarity
    Disulfide bondi1030 ↔ 1045By similarity
    Glycosylationi1035 – 10351O-linked (Fuc...)By similarity
    Disulfide bondi1047 ↔ 1056By similarity
    Disulfide bondi1063 ↔ 1074By similarity
    Glycosylationi1065 – 10651O-linked (Glc...)By similarity
    Disulfide bondi1068 ↔ 1083By similarity
    Disulfide bondi1085 ↔ 1094By similarity
    Disulfide bondi1101 ↔ 1122By similarity
    Disulfide bondi1116 ↔ 1131By similarity
    Disulfide bondi1133 ↔ 1142By similarity
    Disulfide bondi1149 ↔ 1160By similarity
    Disulfide bondi1154 ↔ 1169By similarity
    Disulfide bondi1171 ↔ 1180By similarity
    Glycosylationi1179 – 11791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1187 ↔ 1198By similarity
    Glycosylationi1189 – 11891O-linked (Glc...)By similarity
    Disulfide bondi1192 ↔ 1207By similarity
    Glycosylationi1197 – 11971O-linked (Fuc...)By similarity
    Disulfide bondi1209 ↔ 1218By similarity
    Disulfide bondi1225 ↔ 1244By similarity
    Disulfide bondi1238 ↔ 1253By similarity
    Glycosylationi1241 – 12411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1255 ↔ 1264By similarity
    Disulfide bondi1271 ↔ 1284By similarity
    Glycosylationi1273 – 12731O-linked (Glc...)By similarity
    Disulfide bondi1276 ↔ 1293By similarity
    Disulfide bondi1295 ↔ 1304By similarity
    Disulfide bondi1311 ↔ 1322By similarity
    Disulfide bondi1316 ↔ 1334By similarity
    Disulfide bondi1336 ↔ 1345By similarity
    Disulfide bondi1352 ↔ 1363By similarity
    Disulfide bondi1357 ↔ 1372By similarity
    Glycosylationi1362 – 13621O-linked (Fuc...)By similarity
    Disulfide bondi1374 ↔ 1383By similarity
    Disulfide bondi1391 ↔ 1403By similarity
    Disulfide bondi1397 ↔ 1414By similarity
    Glycosylationi1402 – 14021O-linked (Fuc...); alternateBy similarity
    Glycosylationi1402 – 14021O-linked (GalNAc...); alternateBy similarity
    Disulfide bondi1416 ↔ 1425By similarity
    Disulfide bondi1449 ↔ 1472By similarity
    Disulfide bondi1454 ↔ 1467By similarity
    Disulfide bondi1463 ↔ 1479By similarity
    Glycosylationi1489 – 14891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1490 ↔ 1514By similarity
    Disulfide bondi1496 ↔ 1509By similarity
    Disulfide bondi1505 ↔ 1521By similarity
    Disulfide bondi1536 ↔ 1549By similarity
    Disulfide bondi1545 ↔ 1561By similarity
    Glycosylationi1587 – 15871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1715 – 17151O-linked (GalNAc...)By similarity
    Cross-linki1749 – 1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei1945 – 19451(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
    Modified residuei2012 – 20121(3S)-3-hydroxyasparagine; by HIF1ANBy similarity

    Post-translational modificationi

    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 By similarity.By similarity
    Phosphorylated.By similarity
    O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. 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) By similarity.By similarity
    Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination catalyzed by ITCH. Monoubiquitination at Lys-1749 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 By similarity.By similarity
    Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ07008.
    PRIDEiQ07008.

    Expressioni

    Tissue specificityi

    Expressed in the brain, kidney and spleen. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. Found in both subventricular and ventricular germinal zones.2 Publications

    Developmental stagei

    In the embryo, highest levels occur between days 12 and 14 and decrease rapidly to much lower levels in the adult.

    Gene expression databases

    GenevestigatoriQ07008.

    Interactioni

    Subunit structurei

    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. 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. 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. 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 By similarity. Interacts with THBS4 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000026212.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07008.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 17231705ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1747 – 2531785CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1724 – 174623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 5839EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini59 – 9941EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini102 – 13938EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 17637EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini178 – 21639EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini218 – 25538EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini257 – 29337EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 33339EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 37137EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini372 – 41039EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini412 – 45039EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini452 – 48837EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini490 – 52637EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 56437EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini566 – 60136EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini603 – 63937EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini641 – 67636EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini678 – 71437EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini716 – 75136EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini753 – 78937EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 82737EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini829 – 86739EGF-like 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini869 – 90537EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 94337EGF-like 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini945 – 98137EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini983 – 101937EGF-like 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini1021 – 105737EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1059 – 109537EGF-like 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini1097 – 114347EGF-like 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini1145 – 118137EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1183 – 121937EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1221 – 126545EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1267 – 130539EGF-like 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini1307 – 134640EGF-like 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini1348 – 138437EGF-like 35PROSITE-ProRule annotationAdd
    BLAST
    Domaini1387 – 142640EGF-like 36PROSITE-ProRule annotationAdd
    BLAST
    Repeati1449 – 148941LNR 1Add
    BLAST
    Repeati1490 – 153142LNR 2Add
    BLAST
    Repeati1532 – 157140LNR 3Add
    BLAST
    Repeati1917 – 194630ANK 1Add
    BLAST
    Repeati1950 – 198031ANK 2Add
    BLAST
    Repeati1984 – 201330ANK 3Add
    BLAST
    Repeati2017 – 204630ANK 4Add
    BLAST
    Repeati2050 – 207930ANK 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1937 – 19459HIF1AN-bindingBy similarity
    Regioni2004 – 20129HIF1AN-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1730 – 17334Poly-Ala
    Compositional biasi1891 – 18944Poly-Glu
    Compositional biasi2258 – 22614Poly-Pro
    Compositional biasi2497 – 25004Poly-Ser

    Sequence similaritiesi

    Belongs to the NOTCH family.Curated
    Contains 5 ANK repeats.PROSITE-ProRule annotation
    Contains 36 EGF-like domains.PROSITE-ProRule annotation
    Contains 3 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00730000110611.
    HOGENOMiHOG000234369.
    HOVERGENiHBG052650.
    InParanoidiQ07008.
    KOiK02599.
    OMAiGASCQNT.
    OrthoDBiEOG7992RD.
    TreeFamiTF351641.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR024600. DUF3454_notch.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR008297. Notch.
    IPR022362. Notch_1.
    IPR000800. Notch_dom.
    IPR010660. Notch_NOD_dom.
    IPR011656. Notch_NODP_dom.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 21 hits.
    PF07645. EGF_CA. 5 hits.
    PF12661. hEGF. 2 hits.
    PF06816. NOD. 1 hit.
    PF07684. NODP. 1 hit.
    PF00066. Notch. 3 hits.
    [Graphical view]
    PIRSFiPIRSF002279. Notch. 1 hit.
    PRINTSiPR01452. LNOTCHREPEAT.
    PR01984. NOTCH1.
    SMARTiSM00248. ANK. 6 hits.
    SM00181. EGF. 11 hits.
    SM00179. EGF_CA. 25 hits.
    SM00004. NL. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF57184. SSF57184. 5 hits.
    SSF90193. SSF90193. 3 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS00010. ASX_HYDROXYL. 22 hits.
    PS00022. EGF_1. 35 hits.
    PS01186. EGF_2. 27 hits.
    PS50026. EGF_3. 36 hits.
    PS01187. EGF_CA. 21 hits.
    PS50258. LNR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q07008-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG     50
    AFVGQRCQDP SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT 100
    PLANACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA 150
    NGGQCLPFES SYICGCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG 200
    SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA 250
    GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 300
    LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC 350
    HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC 400
    PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE 450
    IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL 500
    HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG AKCLDGPNTY 550
    TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC 600
    ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC 650
    DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF 700
    TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC 750
    DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC 800
    LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY 850
    ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 900
    GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA 950
    SNPCQNGANC TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD 1000
    GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG 1050
    YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ YHCECRSGWT GFNCDVLSVS 1100
    CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS YCEDEVDECS 1150
    PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 1200
    LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG 1250
    YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT 1300
    GRRCESVING CRGKPCRNGG VCAVASNTAR GFICRCPAGF EGATCENDAR 1350
    TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ 1400
    GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE 1450
    LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 1500
    SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN 1550
    SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL 1600
    HTNVVFKRDA QGQQMIFPYY GREEELRKHP IKRSAVGWAT TSLLPGTNGG 1650
    RQRRELDPMD IHGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG 1700
    SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR 1750
    RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 1800
    NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP 1850
    TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI 1900
    SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM 1950
    GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM 2000
    LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK 2050
    EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 2100
    RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK 2150
    PSTKGLACSS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL 2200
    SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG 2250
    GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW 2300
    LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI HSSLSTNTLS 2350
    PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA 2400
    NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP 2450
    MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS 2500
    PHSNISDWSE GISSPPTSMP SQITHIPEAF K 2531
    Length:2,531
    Mass (Da):270,822
    Last modified:October 16, 2013 - v3
    Checksum:i3E61AE863AA237F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091G → A in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti334 – 3341E → D in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti402 – 4021S → R in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti577 – 5771Y → I in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti951 – 9511S → T in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti1339 – 13391G → R in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti1435 – 14351G → A in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti1595 – 15962EL → DV in CAA40667. (PubMed:1764995)Curated
    Sequence conflicti2501 – 25011P → R in CAA40667. (PubMed:1764995)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57405 mRNA. Translation: CAA40667.1.
    AABR06021907 Genomic DNA. No translation available.
    AABR06021908 Genomic DNA. No translation available.
    CH474001 Genomic DNA. Translation: EDL93491.1.
    PIRiS18188.
    RefSeqiNP_001099191.1. NM_001105721.1.
    UniGeneiRn.25046.

    Genome annotation databases

    EnsembliENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322.
    GeneIDi25496.
    KEGGirno:25496.
    UCSCiRGD:3187. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57405 mRNA. Translation: CAA40667.1 .
    AABR06021907 Genomic DNA. No translation available.
    AABR06021908 Genomic DNA. No translation available.
    CH474001 Genomic DNA. Translation: EDL93491.1 .
    PIRi S18188.
    RefSeqi NP_001099191.1. NM_001105721.1.
    UniGenei Rn.25046.

    3D structure databases

    ProteinModelPortali Q07008.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000026212.

    Proteomic databases

    PaxDbi Q07008.
    PRIDEi Q07008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026212 ; ENSRNOP00000026212 ; ENSRNOG00000019322 .
    GeneIDi 25496.
    KEGGi rno:25496.
    UCSCi RGD:3187. rat.

    Organism-specific databases

    CTDi 4851.
    RGDi 3187. Notch1.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00730000110611.
    HOGENOMi HOG000234369.
    HOVERGENi HBG052650.
    InParanoidi Q07008.
    KOi K02599.
    OMAi GASCQNT.
    OrthoDBi EOG7992RD.
    TreeFami TF351641.

    Enzyme and pathway databases

    Reactomei REACT_194345. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_198299. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_198304. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_198659. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_198750. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_198752. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_198754. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_198789. Pre-NOTCH Processing in Golgi.
    REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

    Miscellaneous databases

    NextBioi 35582897.
    PROi Q07008.

    Gene expression databases

    Genevestigatori Q07008.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR024600. DUF3454_notch.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR008297. Notch.
    IPR022362. Notch_1.
    IPR000800. Notch_dom.
    IPR010660. Notch_NOD_dom.
    IPR011656. Notch_NODP_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 21 hits.
    PF07645. EGF_CA. 5 hits.
    PF12661. hEGF. 2 hits.
    PF06816. NOD. 1 hit.
    PF07684. NODP. 1 hit.
    PF00066. Notch. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002279. Notch. 1 hit.
    PRINTSi PR01452. LNOTCHREPEAT.
    PR01984. NOTCH1.
    SMARTi SM00248. ANK. 6 hits.
    SM00181. EGF. 11 hits.
    SM00179. EGF_CA. 25 hits.
    SM00004. NL. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF57184. SSF57184. 5 hits.
    SSF90193. SSF90193. 3 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS00010. ASX_HYDROXYL. 22 hits.
    PS00022. EGF_1. 35 hits.
    PS01186. EGF_2. 27 hits.
    PS50026. EGF_3. 36 hits.
    PS01187. EGF_CA. 21 hits.
    PS50258. LNR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A homolog of Drosophila Notch expressed during mammalian development."
      Weinmaster G., Roberts V.J., Lemke G.
      Development 113:199-205(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Schwann cell.
    2. Weinmaster G.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 1652-1653.
    3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Notch1 and Notch3 instructively restrict bFGF-responsive multipotent neural progenitor cells to an astroglial fate."
      Tanigaki K., Nogaki F., Takahashi J., Tashiro K., Kurooka H., Honjo T.
      Neuron 29:45-55(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Notch2: a second mammalian Notch gene."
      Weinmaster G., Roberts V.J., Lemke G.
      Development 116:931-941(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Expression patterns of Notch1, Notch2, and Notch3 suggest multiple functional roles for the Notch-DSL signaling system during brain development."
      Irvin D.K., Zurcher S.D., Nguyen T., Weinmaster G., Kornblum H.I.
      J. Comp. Neurol. 436:167-181(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiNOTC1_RAT
    AccessioniPrimary (citable) accession number: Q07008
    Secondary accession number(s): F1M9E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 16, 2013
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3