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Protein

Neurogenic locus notch homolog protein 2

Gene

Notch2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei614 – 6141Essential for O-xylosylationBy similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • receptor activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-RNO-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 2
Short name:
Notch 2
Cleaved into the following 2 chains:
Gene namesi
Name:Notch2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3188. Notch2.

Subcellular locationi

Notch 2 extracellular truncation :
  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
Notch 2 intracellular domain :
  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by C8orf4/TC1.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 16771652ExtracellularSequence analysisAdd
BLAST
Transmembranei1678 – 169821HelicalSequence analysisAdd
BLAST
Topological domaini1699 – 2471773CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2078 – 20781S → A: Permits Notch2 inhibitory activity upon G-CSF action on myeloid cells. 1 Publication
Mutagenesisi2090 – 20901S → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 24712446Neurogenic locus notch homolog protein 2PRO_0000007689Add
BLAST
Chaini1666 – 2471806Notch 2 extracellular truncationBy similarityPRO_0000007690Add
BLAST
Chaini1697 – 2471775Notch 2 intracellular domainBy similarityPRO_0000007691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 41By similarity
Disulfide bondi35 ↔ 51By similarity
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi53 ↔ 62By similarity
Disulfide bondi68 ↔ 79By similarity
Disulfide bondi73 ↔ 90By similarity
Disulfide bondi92 ↔ 101By similarity
Disulfide bondi109 ↔ 121By similarity
Disulfide bondi115 ↔ 131By similarity
Disulfide bondi133 ↔ 142By similarity
Disulfide bondi148 ↔ 159By similarity
Disulfide bondi153 ↔ 168By similarity
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi170 ↔ 179By similarity
Disulfide bondi186 ↔ 198By similarity
Disulfide bondi192 ↔ 207By similarity
Disulfide bondi209 ↔ 218By similarity
Disulfide bondi225 ↔ 236By similarity
Disulfide bondi230 ↔ 246By similarity
Disulfide bondi248 ↔ 257By similarity
Disulfide bondi264 ↔ 275By similarity
Disulfide bondi269 ↔ 284By similarity
Disulfide bondi286 ↔ 295By similarity
Disulfide bondi302 ↔ 315By similarity
Disulfide bondi309 ↔ 324By similarity
Disulfide bondi326 ↔ 335By similarity
Disulfide bondi342 ↔ 353By similarity
Disulfide bondi347 ↔ 362By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi379 ↔ 390By similarity
Disulfide bondi384 ↔ 401By similarity
Disulfide bondi403 ↔ 412By similarity
Disulfide bondi419 ↔ 433By similarity
Disulfide bondi427 ↔ 442By similarity
Disulfide bondi444 ↔ 453By similarity
Disulfide bondi460 ↔ 471By similarity
Disulfide bondi465 ↔ 480By similarity
Disulfide bondi482 ↔ 491By similarity
Disulfide bondi498 ↔ 509By similarity
Disulfide bondi503 ↔ 518By similarity
Disulfide bondi520 ↔ 529By similarity
Disulfide bondi536 ↔ 547By similarity
Disulfide bondi541 ↔ 556By similarity
Disulfide bondi558 ↔ 567By similarity
Disulfide bondi574 ↔ 584By similarity
Disulfide bondi579 ↔ 593By similarity
Disulfide bondi595 ↔ 604By similarity
Disulfide bondi611 ↔ 622By similarity
Glycosylationi613 – 6131O-linked (Glc...); alternateBy similarity
Glycosylationi613 – 6131O-linked (Xyl...); alternateBy similarity
Disulfide bondi616 ↔ 631By similarity
Disulfide bondi633 ↔ 642By similarity
Disulfide bondi649 ↔ 659By similarity
Disulfide bondi654 ↔ 668By similarity
Disulfide bondi670 ↔ 679By similarity
Disulfide bondi686 ↔ 697By similarity
Disulfide bondi691 ↔ 706By similarity
Disulfide bondi708 ↔ 717By similarity
Disulfide bondi724 ↔ 734By similarity
Disulfide bondi729 ↔ 743By similarity
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi745 ↔ 754By similarity
Disulfide bondi761 ↔ 772By similarity
Disulfide bondi766 ↔ 781By similarity
Disulfide bondi783 ↔ 792By similarity
Disulfide bondi799 ↔ 810By similarity
Disulfide bondi804 ↔ 819By similarity
Disulfide bondi821 ↔ 830By similarity
Disulfide bondi837 ↔ 848By similarity
Disulfide bondi842 ↔ 859By similarity
Disulfide bondi861 ↔ 870By similarity
Disulfide bondi877 ↔ 888By similarity
Disulfide bondi882 ↔ 897By similarity
Disulfide bondi899 ↔ 908By similarity
Disulfide bondi915 ↔ 926By similarity
Disulfide bondi920 ↔ 935By similarity
Disulfide bondi937 ↔ 946By similarity
Disulfide bondi953 ↔ 964By similarity
Disulfide bondi958 ↔ 973By similarity
Disulfide bondi975 ↔ 984By similarity
Disulfide bondi991 ↔ 1002By similarity
Disulfide bondi996 ↔ 1011By similarity
Disulfide bondi1013 ↔ 1022By similarity
Disulfide bondi1029 ↔ 1040By similarity
Disulfide bondi1034 ↔ 1049By similarity
Disulfide bondi1051 ↔ 1060By similarity
Disulfide bondi1067 ↔ 1078By similarity
Disulfide bondi1072 ↔ 1087By similarity
Disulfide bondi1089 ↔ 1098By similarity
Glycosylationi1102 – 11021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1105 ↔ 1126By similarity
Disulfide bondi1120 ↔ 1135By similarity
Disulfide bondi1137 ↔ 1146By similarity
Disulfide bondi1153 ↔ 1164By similarity
Disulfide bondi1158 ↔ 1173By similarity
Disulfide bondi1175 ↔ 1184By similarity
Disulfide bondi1191 ↔ 1202By similarity
Disulfide bondi1196 ↔ 1211By similarity
Disulfide bondi1213 ↔ 1222By similarity
Disulfide bondi1229 ↔ 1241By similarity
Disulfide bondi1235 ↔ 1250By similarity
Disulfide bondi1252 ↔ 1261By similarity
Disulfide bondi1268 ↔ 1281By similarity
Disulfide bondi1273 ↔ 1290By similarity
Disulfide bondi1292 ↔ 1301By similarity
Disulfide bondi1308 ↔ 1319By similarity
Disulfide bondi1313 ↔ 1331By similarity
Disulfide bondi1333 ↔ 1342By similarity
Disulfide bondi1378 ↔ 1389By similarity
Disulfide bondi1383 ↔ 1400By similarity
Disulfide bondi1402 ↔ 1411By similarity
Disulfide bondi1425 ↔ 1448By similarity
Disulfide bondi1430 ↔ 1443By similarity
Disulfide bondi1439 ↔ 1455By similarity
Glycosylationi1465 – 14651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1466 ↔ 1489By similarity
Disulfide bondi1472 ↔ 1484By similarity
Disulfide bondi1480 ↔ 1496By similarity
Disulfide bondi1503 ↔ 1527By similarity
Disulfide bondi1509 ↔ 1522By similarity
Disulfide bondi1518 ↔ 1534By similarity
Disulfide bondi1632 ↔ 1639By similarity
Modified residuei1716 – 17161PhosphothreonineBy similarity
Modified residuei1779 – 17791PhosphoserineBy similarity
Modified residuei1802 – 18021PhosphothreonineBy similarity
Modified residuei1804 – 18041PhosphoserineBy similarity
Modified residuei1808 – 18081PhosphothreonineBy similarity
Modified residuei1842 – 18421PhosphoserineBy similarity
Modified residuei1845 – 18451PhosphoserineCombined sources
Modified residuei2070 – 20701PhosphoserineBy similarity
Modified residuei2078 – 20781Phosphoserine1 Publication
Modified residuei2081 – 20811PhosphoserineBy similarity
Modified residuei2097 – 20971PhosphothreonineBy 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 TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).By similarity
Phosphorylated. G-CSF treatment of myeloid cells specifically promotes Ser-2078 phosphorylation, which inactivates Notch2 and permits differentiation.1 Publication
Hydroxylated by HIF1AN.By similarity
Can be either O-glucosylated or O-xylosylated at Ser-613 by POGLUT1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9QW30.
PRIDEiQ9QW30.

PTM databases

iPTMnetiQ9QW30.
PhosphoSiteiQ9QW30.

Expressioni

Tissue specificityi

Highly expressed in the spleen and choroid plexus in the brain. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. It is more highly localized to ventricular germinal zones. Also found in the heart, liver and kidney.1 Publication

Developmental stagei

Expressed in the brain during E14 and E17.

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 (By similarity). Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65 (By similarity). Interacts with HIF1AN. Interacts (via ANK repeats) with C8orf4/TC1, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025718.

Structurei

3D structure databases

ProteinModelPortaliQ9QW30.
SMRiQ9QW30. Positions 414-533, 1425-1670, 1858-2071.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6338EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini64 – 10239EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 14339EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 18037EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini182 – 21938EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini221 – 25838EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 29637EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini298 – 33639EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini338 – 37437EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini375 – 41339EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini415 – 45440EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini456 – 49237EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini494 – 53037EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini532 – 56837EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini570 – 60536EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini607 – 64337EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini645 – 68036EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini682 – 71837EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini720 – 75536EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini757 – 79337EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini795 – 83137EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini833 – 87139EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini873 – 90937EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini911 – 94737EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini949 – 98537EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini987 – 102337EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1025 – 106137EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1063 – 109937EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1101 – 114747EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Domaini1149 – 118537EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1187 – 122337EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1225 – 126238EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1264 – 130239EGF-like 33PROSITE-ProRule annotationAdd
BLAST
Domaini1304 – 134340EGF-like 34PROSITE-ProRule annotationAdd
BLAST
Domaini1374 – 141239EGF-like 35PROSITE-ProRule annotationAdd
BLAST
Repeati1425 – 146541LNR 1Add
BLAST
Repeati1466 – 150237LNR 2Add
BLAST
Repeati1503 – 154442LNR 3Add
BLAST
Repeati1827 – 187145ANK 1Add
BLAST
Repeati1876 – 190530ANK 2Add
BLAST
Repeati1909 – 193931ANK 3Add
BLAST
Repeati1943 – 197230ANK 4Add
BLAST
Repeati1976 – 200530ANK 5Add
BLAST
Repeati2009 – 203830ANK 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1425 – 1677253Negative regulatory region (NRR)By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1645 – 16484Poly-Ala
Compositional biasi1994 – 19974Poly-Leu
Compositional biasi2426 – 24294Poly-Ser
Compositional biasi2446 – 24516Poly-Gly

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 35 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

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ9QW30.
PhylomeDBiQ9QW30.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 1 hit.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 35 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 26 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9QW30-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGY
60 70 80 90 100
CRCPEGFLGE YCQHRDPCEK NRCQNGGTCV TQAMLGKATC RCAPGFTGED
110 120 130 140 150
CQYSTSHPCF VSRPCQNGGT CHMLSWDTYE CTCQVGFTGK QCQWTDVCLS
160 170 180 190 200
HPCENGSTCS SVANQFSCRC PAGITGQKCD ADINECDIPG RCQHGGTCLN
210 220 230 240 250
LPGSYRCQCP QRFTGQHCDS PYVPCAPSPC VNGGTCRQTG DFTSECHCLP
260 270 280 290 300
GFEGSNCERN IDDCPNHKCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD
310 320 330 340 350
ECLLQPNACQ NGGTCTNRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG
360 370 380 390 400
STCIDRVASF SCLCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI
410 420 430 440 450
CTCPQAYKGA DCTEDVDECA MANSNPCEHA GKCVNTDGAF HCECLKGYAG
460 470 480 490 500
PRCEMDINEC HSDPCQNDAT CLDKIGGFTC LCMPGFKGVH CELEVNECQS
510 520 530 540 550
NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP CLNGAKCIDH
560 570 580 590 600
PNGYECQCAT GFTGTLCDEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM
610 620 630 640 650
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGL NCEINFDDCA
660 670 680 690 700
SNPCLHGACV DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKDATCIND
710 720 730 740 750
VNGFRCMCPE GPHHPSCYSQ VNECLSSPCI HGNCTGGLSG YKCLCDAGWV
760 770 780 790 800
GINCEVDKNE CLSNPCQNGG TCNNLVNGYR CTCKKGFKGY NCQVNIDECA
810 820 830 840 850
SNPCLNQGTC LDDVSGYTCH CMLPYTGKNC QTVLAPCSPN PCENAAVCKE
860 870 880 890 900
APNFESFTCL CAPGWQGQRC TVDVDECVSK PCMNNGICHN TQGSYMCECP
910 920 930 940 950
PGFSGMDCEE DINDCLANPC QNGGSCVDKV NTFSCLCLPG FVGDKCQTDM
960 970 980 990 1000
NECLSEPCKN GGTCSDYVNS YTCTCPAGFH GVHCENNIDE CTESSCFNGG
1010 1020 1030 1040 1050
TCVDGINSFS CLCPVGFTGP FCLHDINECS SNPCLNSGTC VDGLGTYRCT
1060 1070 1080 1090 1100
CPLGYTGKNC QTLVNLCSPS PCKNKGTCAQ EKARPRCLCP PGWDGAYCDV
1110 1120 1130 1140 1150
LNVSCKAAAL QKGVPVEHLC QHSGICINAG NTHHCQCPLG YTGSYCEEQL
1160 1170 1180 1190 1200
DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG
1210 1220 1230 1240 1250
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA GAPHCLNGGQ CVDRIGGYSC
1260 1270 1280 1290 1300
RCLPGFAGER CEGDINECLS NPCSSEGSLD CIQLKNNYQC VCRSAFTGRH
1310 1320 1330 1340 1350
CETFLDVCPQ KPCLNGGTCA VASNVPDGFI CRCPPGFSGA RCQSSCGQVK
1360 1370 1380 1390 1400
CRRGEQCVHT ASGPHCFCPN HKDCESGCAS NPCQHGGTCY PQRQPPYYSC
1410 1420 1430 1440 1450
RCSPPFWGSH CESYTAPTST PPATCLSQYC ADKARDGICD EACNSHACQW
1460 1470 1480 1490 1500
DGGDCSLTME DPWANCTSSL RCWEYINNQC DELCNTAECL FDNFECQRNS
1510 1520 1530 1540 1550
KTCKYDKYCA DHFKDNHCDK GCNNEECGWD GLDCAADQPE NLAEGILVIV
1560 1570 1580 1590 1600
VLLPPEQLLQ DSRSFLRALG TLLHTNLRIK QDSQGALMVY PYYGEKSAAM
1610 1620 1630 1640 1650
KKQKVARRSL PDEQEQEIIG SKVFLEIDNR QCVQDSDQCF KNTDAAAALL
1660 1670 1680 1690 1700
ASHAIQGTLS YPLVSVVSES EDPRNTPLLY LLAVAVVIIL FLILLGVIMA
1710 1720 1730 1740 1750
KRKRKHGFLW LPEGFTLRRD SSNHKRREPV GQDAVGLKNL SVQVSEANLI
1760 1770 1780 1790 1800
GSTTSEHWGD DEGPQPKKAK AEDDEALLSE DDPVDRRPWT QQHLEAADIR
1810 1820 1830 1840 1850
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED
1860 1870 1880 1890 1900
AEDSSANIIT DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG
1910 1920 1930 1940 1950
ADANAQDNMG RCPLHAAVAA DAQGVFQILI RNRVTDLDAR MNDGTTPLIL
1960 1970 1980 1990 2000
AARLAVEGMV AELINCQADV NAVDDHGKSA LHWAAAVNNV EATLLLLKNG
2010 2020 2030 2040 2050
ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD HMDRLPRDVA
2060 2070 2080 2090 2100
RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVLCGPNRS FLSLKHTPMG
2110 2120 2130 2140 2150
KKARRPNTKS TMPTSLPNLA KEAKDVKGSR RKKCLNEKVQ LSESSVTLSP
2160 2170 2180 2190 2200
VDSLESPHTY VSDATSSPMI TSPGILQASP TPLLAAAPAA PVHAQHALSF
2210 2220 2230 2240 2250
SNLHEMQPLR PGASTVLPSV SQLLSHHHIV PPGSGSAGSL GRLHSVPVPS
2260 2270 2280 2290 2300
DWMNRVEMSE TQYSEMFGMV LAPAEGTHPG MAAPQSRAPE GKPIPTQREP
2310 2320 2330 2340 2350
LPPIVTFQLI PKGSLAQAAG APQTQSGCPP AVAGPLPSMY QIPEMARLPS
2360 2370 2380 2390 2400
VAFPPTMMPQ QEGQVAQTIV PTYHPFPASV GKYPTPPSQH SYASSNAAER
2410 2420 2430 2440 2450
TPNHGGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGGGG
2460 2470
GQRGPGTHMS EPPHSNMQVY A
Length:2,471
Mass (Da):265,370
Last modified:May 1, 2000 - v1
Checksum:i7D5C8E18DDE95FE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93661 mRNA. Translation: AAK13558.1.
PIRiA49128.

Genome annotation databases

UCSCiRGD:3188. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93661 mRNA. Translation: AAK13558.1.
PIRiA49128.

3D structure databases

ProteinModelPortaliQ9QW30.
SMRiQ9QW30. Positions 414-533, 1425-1670, 1858-2071.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025718.

PTM databases

iPTMnetiQ9QW30.
PhosphoSiteiQ9QW30.

Proteomic databases

PaxDbiQ9QW30.
PRIDEiQ9QW30.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3188. rat.

Organism-specific databases

RGDi3188. Notch2.

Phylogenomic databases

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ9QW30.
PhylomeDBiQ9QW30.

Enzyme and pathway databases

ReactomeiR-RNO-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.

Miscellaneous databases

PROiQ9QW30.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 1 hit.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 35 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 26 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Notch2: a second mammalian Notch gene."
    Weinmaster G., Roberts V.J., Lemke G.
    Development 116:931-941(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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.
  3. "Phosphorylation of Ser2078 modulates the Notch2 function in 32D cell differentiation."
    Ingles-Esteve J., Espinosa L., Milner L.A., Caelles C., Bigas A.
    J. Biol. Chem. 276:44873-44880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2078, MUTAGENESIS OF SER-2078 AND SER-2090.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1845, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOTC2_RAT
AccessioniPrimary (citable) accession number: Q9QW30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 147 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.