Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei614Essential for O-xylosylationBy similarity1

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)DescriptionActionsGraphical viewLength
Topological domaini26 – 1677ExtracellularSequence analysisAdd BLAST1652
Transmembranei1678 – 1698HelicalSequence analysisAdd BLAST21
Topological domaini1699 – 2471CytoplasmicSequence analysisAdd BLAST773

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2078S → A: Permits Notch2 inhibitory activity upon G-CSF action on myeloid cells. 1 Publication1
Mutagenesisi2090S → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000768926 – 2471Neurogenic locus notch homolog protein 2Add BLAST2446
ChainiPRO_00000076901666 – 2471Notch 2 extracellular truncationBy similarityAdd BLAST806
ChainiPRO_00000076911697 – 2471Notch 2 intracellular domainBy similarityAdd BLAST775

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 41By similarity
Disulfide bondi35 ↔ 51By similarity
Glycosylationi46N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi613O-linked (Glc...); alternateBy similarity1
Glycosylationi613O-linked (Xyl...); alternateBy similarity1
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
Glycosylationi733N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1102N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1465N-linked (GlcNAc...)Sequence analysis1
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 residuei1716PhosphothreonineBy similarity1
Modified residuei1779PhosphoserineBy similarity1
Modified residuei1802PhosphothreonineBy similarity1
Modified residuei1804PhosphoserineBy similarity1
Modified residuei1808PhosphothreonineBy similarity1
Modified residuei1842PhosphoserineBy similarity1
Modified residuei1845PhosphoserineCombined sources1
Modified residuei2070PhosphoserineBy similarity1
Modified residuei2078Phosphoserine1 Publication1
Modified residuei2081PhosphoserineBy similarity1
Modified residuei2097PhosphothreonineBy similarity1

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.
PhosphoSitePlusiQ9QW30.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 63EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini64 – 102EGF-like 2PROSITE-ProRule annotationAdd BLAST39
Domaini105 – 143EGF-like 3PROSITE-ProRule annotationAdd BLAST39
Domaini144 – 180EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini182 – 219EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini221 – 258EGF-like 6PROSITE-ProRule annotationAdd BLAST38
Domaini260 – 296EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini298 – 336EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini338 – 374EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini375 – 413EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini415 – 454EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini456 – 492EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini494 – 530EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini532 – 568EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini570 – 605EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini607 – 643EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini645 – 680EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini682 – 718EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini720 – 755EGF-like 19PROSITE-ProRule annotationAdd BLAST36
Domaini757 – 793EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini795 – 831EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini833 – 871EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini873 – 909EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini911 – 947EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini949 – 985EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini987 – 1023EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1025 – 1061EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1063 – 1099EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1101 – 1147EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1149 – 1185EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1187 – 1223EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1225 – 1262EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini1264 – 1302EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1304 – 1343EGF-like 34PROSITE-ProRule annotationAdd BLAST40
Domaini1374 – 1412EGF-like 35PROSITE-ProRule annotationAdd BLAST39
Repeati1425 – 1465LNR 1Add BLAST41
Repeati1466 – 1502LNR 2Add BLAST37
Repeati1503 – 1544LNR 3Add BLAST42
Repeati1827 – 1871ANK 1Add BLAST45
Repeati1876 – 1905ANK 2Add BLAST30
Repeati1909 – 1939ANK 3Add BLAST31
Repeati1943 – 1972ANK 4Add BLAST30
Repeati1976 – 2005ANK 5Add BLAST30
Repeati2009 – 2038ANK 6Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1425 – 1677Negative regulatory region (NRR)By similarityAdd BLAST253

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1645 – 1648Poly-Ala4
Compositional biasi1994 – 1997Poly-Leu4
Compositional biasi2426 – 2429Poly-Ser4
Compositional biasi2446 – 2451Poly-Gly6

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. 22 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 4 hits.
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.
UniGeneiRn.65930.

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.
UniGeneiRn.65930.

3D structure databases

ProteinModelPortaliQ9QW30.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025718.

PTM databases

iPTMnetiQ9QW30.
PhosphoSitePlusiQ9QW30.

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. 22 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 4 hits.
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...

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: November 30, 2016
This is version 150 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.