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Protein

Neurogenic locus notch homolog protein 2

Gene

Notch2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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). May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. 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 similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei612Essential for O-xylosylation1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • enzyme binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • signaling receptor activity Source: InterPro

GO - Biological processi

  • animal organ morphogenesis Source: UniProtKB
  • atrial septum morphogenesis Source: BHF-UCL
  • bone remodeling Source: MGI
  • cell cycle arrest Source: UniProtKB
  • cell fate determination Source: UniProtKB
  • cholangiocyte proliferation Source: MGI
  • ciliary body morphogenesis Source: MGI
  • defense response to bacterium Source: MGI
  • determination of left/right symmetry Source: MGI
  • embryonic limb morphogenesis Source: MGI
  • glomerular capillary formation Source: UniProtKB
  • glomerular visceral epithelial cell development Source: UniProtKB
  • heart looping Source: BHF-UCL
  • hepatocyte proliferation Source: MGI
  • humoral immune response Source: MGI
  • inflammatory response to antigenic stimulus Source: MGI
  • interleukin-4 secretion Source: MGI
  • intrahepatic bile duct development Source: MGI
  • in utero embryonic development Source: MGI
  • left/right axis specification Source: BHF-UCL
  • liver development Source: MGI
  • liver morphogenesis Source: MGI
  • marginal zone B cell differentiation Source: UniProtKB
  • morphogenesis of an epithelial sheet Source: MGI
  • multicellular organism growth Source: MGI
  • myeloid dendritic cell differentiation Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of growth rate Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: MGI
  • Notch signaling pathway Source: UniProtKB
  • placenta blood vessel development Source: MGI
  • placenta development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of BMP signaling pathway Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of osteoclast differentiation Source: UniProtKB
  • positive regulation of Ras protein signal transduction Source: UniProtKB
  • proximal tubule development Source: UniProtKB
  • pulmonary valve morphogenesis Source: MGI
  • regulation of osteoclast development Source: UniProtKB
  • regulation of transcription by RNA polymerase II Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • wound healing Source: UniProtKB

Keywordsi

Molecular functionActivator, Developmental protein, Receptor
Biological processDifferentiation, Notch signaling pathway, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 2
Short name:
Notch 2
Alternative name(s):
Motch B
Cleaved into the following 2 chains:
Gene namesi
Name:Notch2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97364 Notch2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 1677ExtracellularSequence analysisAdd BLAST1652
Transmembranei1678 – 1698HelicalSequence analysisAdd BLAST21
Topological domaini1699 – 2470CytoplasmicSequence analysisAdd BLAST772

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi612S → A: No effect on O-glycosylation by POGLUT1. Loss of O-xylosylation. 1 Publication1
Mutagenesisi1699M → L: No effect on NICD processing. 2 Publications1
Mutagenesisi1699M → V: Decreased NICD processing. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000768626 – 2470Neurogenic locus notch homolog protein 2Add BLAST2445
ChainiPRO_00000076871666 – 2470Notch 2 extracellular truncationAdd BLAST805
ChainiPRO_00000076881697 – 2470Notch 2 intracellular domainAdd BLAST774

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 41By similarity
Disulfide bondi35 ↔ 51By similarity
Glycosylationi46N-linked (GlcNAc...) asparagineSequence 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...) asparagineSequence analysis1
Disulfide bondi170 ↔ 179By similarity
Disulfide bondi186 ↔ 198By similarity
Disulfide bondi192 ↔ 207By similarity
Disulfide bondi209 ↔ 218By similarity
Disulfide bondi228 ↔ 244By similarity
Disulfide bondi246 ↔ 255By similarity
Disulfide bondi262 ↔ 273By similarity
Disulfide bondi267 ↔ 282By similarity
Disulfide bondi284 ↔ 293By similarity
Disulfide bondi300 ↔ 313By similarity
Disulfide bondi307 ↔ 322By similarity
Disulfide bondi324 ↔ 333By similarity
Disulfide bondi340 ↔ 351By similarity
Disulfide bondi345 ↔ 360By similarity
Disulfide bondi362 ↔ 371By similarity
Disulfide bondi377 ↔ 388By similarity
Disulfide bondi382 ↔ 399By similarity
Disulfide bondi401 ↔ 410By similarity
Disulfide bondi417 ↔ 431By similarity
Disulfide bondi425 ↔ 440By similarity
Disulfide bondi442 ↔ 451By similarity
Disulfide bondi458 ↔ 469By similarity
Disulfide bondi463 ↔ 478By similarity
Disulfide bondi480 ↔ 489By similarity
Disulfide bondi496 ↔ 507By similarity
Disulfide bondi501 ↔ 516By similarity
Disulfide bondi518 ↔ 527By similarity
Disulfide bondi534 ↔ 545By similarity
Disulfide bondi539 ↔ 554By similarity
Disulfide bondi556 ↔ 565By similarity
Disulfide bondi572 ↔ 582By similarity
Disulfide bondi577 ↔ 591By similarity
Disulfide bondi593 ↔ 602By similarity
Disulfide bondi609 ↔ 620By similarity
Glycosylationi611O-linked (Glc...) serine; alternate1 Publication1
Glycosylationi611O-linked (Xyl...) serine; alternate1 Publication1
Disulfide bondi614 ↔ 629By similarity
Disulfide bondi631 ↔ 640By similarity
Disulfide bondi647 ↔ 657By similarity
Disulfide bondi652 ↔ 666By similarity
Disulfide bondi668 ↔ 677By similarity
Disulfide bondi684 ↔ 695By similarity
Disulfide bondi689 ↔ 704By similarity
Disulfide bondi706 ↔ 715By similarity
Disulfide bondi722 ↔ 732By similarity
Disulfide bondi727 ↔ 741By similarity
Glycosylationi731N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi743 ↔ 752By similarity
Disulfide bondi759 ↔ 770By similarity
Disulfide bondi764 ↔ 779By similarity
Disulfide bondi781 ↔ 790By similarity
Disulfide bondi797 ↔ 808By similarity
Disulfide bondi802 ↔ 817By similarity
Disulfide bondi819 ↔ 828By similarity
Disulfide bondi835 ↔ 846By similarity
Disulfide bondi840 ↔ 857By similarity
Disulfide bondi859 ↔ 868By similarity
Disulfide bondi875 ↔ 886By similarity
Disulfide bondi880 ↔ 895By similarity
Disulfide bondi897 ↔ 906By similarity
Disulfide bondi913 ↔ 924By similarity
Disulfide bondi918 ↔ 933By similarity
Disulfide bondi935 ↔ 944By similarity
Disulfide bondi951 ↔ 962By similarity
Disulfide bondi956 ↔ 971By similarity
Disulfide bondi973 ↔ 982By similarity
Disulfide bondi989 ↔ 1000By similarity
Disulfide bondi994 ↔ 1009By similarity
Disulfide bondi1011 ↔ 1020By similarity
Disulfide bondi1027 ↔ 1038By similarity
Disulfide bondi1032 ↔ 1047By similarity
Disulfide bondi1049 ↔ 1058By similarity
Disulfide bondi1065 ↔ 1076By similarity
Disulfide bondi1070 ↔ 1085By similarity
Disulfide bondi1087 ↔ 1096By similarity
Glycosylationi1100N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1103 ↔ 1124By similarity
Disulfide bondi1118 ↔ 1133By similarity
Disulfide bondi1135 ↔ 1144By similarity
Disulfide bondi1151 ↔ 1162By similarity
Disulfide bondi1156 ↔ 1171By similarity
Disulfide bondi1173 ↔ 1182By similarity
Disulfide bondi1189 ↔ 1200By similarity
Disulfide bondi1194 ↔ 1209By similarity
Disulfide bondi1211 ↔ 1220By similarity
Disulfide bondi1227 ↔ 1239By similarity
Disulfide bondi1233 ↔ 1248By similarity
Disulfide bondi1250 ↔ 1259By similarity
Disulfide bondi1266 ↔ 1279By similarity
Disulfide bondi1271 ↔ 1288By similarity
Disulfide bondi1290 ↔ 1299By similarity
Disulfide bondi1306 ↔ 1317By similarity
Disulfide bondi1311 ↔ 1329By similarity
Disulfide bondi1331 ↔ 1344By similarity
Disulfide bondi1376 ↔ 1387By similarity
Disulfide bondi1381 ↔ 1398By similarity
Disulfide bondi1400 ↔ 1409By similarity
Disulfide bondi1423 ↔ 1446By similarity
Disulfide bondi1428 ↔ 1441By similarity
Disulfide bondi1437 ↔ 1453By similarity
Glycosylationi1463N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1464 ↔ 1487By similarity
Disulfide bondi1470 ↔ 1482By similarity
Disulfide bondi1478 ↔ 1494By similarity
Disulfide bondi1501 ↔ 1525By similarity
Disulfide bondi1507 ↔ 1520By similarity
Disulfide bondi1516 ↔ 1532By similarity
Disulfide bondi1632 ↔ 1639By similarity
Modified residuei1715PhosphothreonineBy similarity1
Modified residuei1777PhosphoserineCombined sources1
Modified residuei1800PhosphothreonineBy similarity1
Modified residuei1802PhosphoserineBy similarity1
Modified residuei1806PhosphothreonineBy similarity1
Modified residuei1840PhosphoserineCombined sources1
Modified residuei1843PhosphoserineCombined sources1
Modified residuei2068PhosphoserineBy similarity1
Modified residuei2076PhosphoserineBy similarity1
Modified residuei2079PhosphoserineBy similarity1
Modified residuei2095PhosphothreonineBy 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.2 Publications
Hydroxylated by HIF1AN.1 Publication
Can be either O-glucosylated or O-xylosylated at Ser-611 by POGLUT1.
Phosphorylated by GSK3. GSK3-mediated phosphorylation is necessary for NOTCH2 recognition by FBXW7, ubiquitination and degradation via the ubiquitin proteasome pathway.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO35516
PaxDbiO35516
PeptideAtlasiO35516
PRIDEiO35516

PTM databases

iPTMnetiO35516
PhosphoSitePlusiO35516

Expressioni

Tissue specificityi

Expressed in the brain, liver, kidney, neuroepithelia, somites, optic vesicles and branchial arches, but not heart.

Developmental stagei

Expressed in the embryonic ventricular zone, the postnatal ependymal cells, and the choroid plexus throughout embryonic and postnatal development.1 Publication

Gene expression databases

CleanExiMM_NOTCH2

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 MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65. Interacts with HIF1AN. Interacts (via ANK repeats) with TCIM, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity). Interacts with CUL1, RBX1, SKP1 and FBXW7 that are SCF(FBXW7) E3 ubiquitin-protein ligase complex components.By similarity3 Publications

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201809, 6 interactors
CORUMiO35516
DIPiDIP-6008N
IntActiO35516, 2 interactors
STRINGi10090.ENSMUSP00000078741

Structurei

3D structure databases

ProteinModelPortaliO35516
SMRiO35516
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 – 256EGF-like 6; incompletePROSITE-ProRule annotationAdd BLAST36
Domaini258 – 294EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini296 – 334EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini336 – 372EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini373 – 411EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini413 – 452EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini454 – 490EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini492 – 528EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini530 – 566EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini568 – 603EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini605 – 641EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini643 – 678EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini680 – 716EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini718 – 753EGF-like 19PROSITE-ProRule annotationAdd BLAST36
Domaini755 – 791EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini793 – 829EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini831 – 869EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini871 – 907EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini909 – 945EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini947 – 983EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini985 – 1021EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1023 – 1059EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1061 – 1097EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1099 – 1145EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1147 – 1183EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1185 – 1221EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1223 – 1260EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini1262 – 1300EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1302 – 1345EGF-like 34PROSITE-ProRule annotationAdd BLAST44
Domaini1372 – 1410EGF-like 35PROSITE-ProRule annotationAdd BLAST39
Repeati1423 – 1463LNR 1Add BLAST41
Repeati1464 – 1500LNR 2Add BLAST37
Repeati1501 – 1542LNR 3Add BLAST42
Repeati1825 – 1869ANK 1Add BLAST45
Repeati1874 – 1903ANK 2Add BLAST30
Repeati1907 – 1937ANK 3Add BLAST31
Repeati1941 – 1970ANK 4Add BLAST30
Repeati1974 – 2003ANK 5Add BLAST30
Repeati2007 – 2036ANK 6Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1423 – 1677Negative regulatory region (NRR)By similarityAdd BLAST255

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1645 – 1648Poly-Ala4
Compositional biasi1992 – 1995Poly-Leu4
Compositional biasi2183 – 2189Poly-Ala7
Compositional biasi2425 – 2428Poly-Ser4
Compositional biasi2445 – 2450Poly-Gly6

Sequence similaritiesi

Belongs to the NOTCH family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IR7G Eukaryota
COG0666 LUCA
HOGENOMiHOG000234369
HOVERGENiHBG052650
InParanoidiO35516
KOiK20994
PhylomeDBiO35516

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
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_cys_sf
IPR008297 Notch
IPR035993 Notch-like_dom_sf
IPR022336 Notch_2
IPR000800 Notch_dom
IPR010660 Notch_NOD_dom
IPR011656 Notch_NODP_dom
PfamiView protein in Pfam
PF12796 Ank_2, 2 hits
PF11936 DUF3454, 1 hit
PF00008 EGF, 24 hits
PF07645 EGF_CA, 5 hits
PF12661 hEGF, 3 hits
PF06816 NOD, 1 hit
PF07684 NODP, 1 hit
PF00066 Notch, 3 hits
PIRSFiPIRSF002279 Notch, 1 hit
PRINTSiPR01452 LNOTCHREPEAT
PR01985 NOTCH2
SMARTiView protein in SMART
SM00248 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
SUPFAMiSSF48403 SSF48403, 1 hit
SSF57184 SSF57184, 5 hits
SSF90193 SSF90193, 2 hits
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 4 hits
PS00010 ASX_HYDROXYL, 22 hits
PS00022 EGF_1, 33 hits
PS01186 EGF_2, 27 hits
PS50026 EGF_3, 35 hits
PS01187 EGF_CA, 22 hits
PS50258 LNR, 3 hits

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35516-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPDLRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGF
60 70 80 90 100
CRCPEGFLGE YCQHRDPCEK NRCQNGGTCV PQGMLGKATC RCAPGFTGED
110 120 130 140 150
CQYSTSHPCF VSRPCQNGGT CHMLSRDTYE CTCQVGFTGK QCQWTDACLS
160 170 180 190 200
HPCENGSTCT SVASQFSCKC PAGLTGQKCE ADINECDIPG RCQHGGTCLN
210 220 230 240 250
LPGSYRCQCG QGFTGQHCDS PYVRGLPCVN GGTCRQTGDF TLECNCLPGF
260 270 280 290 300
EGSTCERNID DCPNHKCQNG GVCVDGVNTY NCRCPPQWTG QFCTEDVDEC
310 320 330 340 350
LLQPNACQNG GTCTNRNGGY GCVCVNGWSG DDCSENIDDC AYASCTPGST
360 370 380 390 400
CIDRVASFSC LCPEGKAGLL CHLDDACISN PCHKGALCDT NPLNGQYICT
410 420 430 440 450
CPQGYKGADC TEDVDECAMA NSNPCEHAGK CVNTDGAFHC ECLKGYAGPR
460 470 480 490 500
CEMDINECHS DPCQNDATCL DKIGGFTCLC MPGFKGVHCE LEVNECQSNP
510 520 530 540 550
CVNNGQCVDK VNRFQCLCPP GFTGPVCQID IDDCSSTPCL NGAKCIDHPN
560 570 580 590 600
GYECQCATGF TGILCDENID NCDPDPCHHG QCQDGIDSYT CICNPGYMGA
610 620 630 640 650
ICSDQIDECY SSPCLNDGRC IDLVNGYQCN CQPGTSGLNC EINFDDCASN
660 670 680 690 700
PCMHGVCVDG INRYSCVCSP GFTGQRCNID IDECASNPCR KGATCINDVN
710 720 730 740 750
GFRCICPEGP HHPSCYSQVN ECLSNPCIHG NCTGGLSGYK CLCDAGWVGV
760 770 780 790 800
NCEVDKNECL SNPCQNGGTC NNLVNGYRCT CKKGFKGYNC QVNIDECASN
810 820 830 840 850
PCLNQGTCFD DVSGYTCHCM LPYTGKNCQT VLAPCSPNPC ENAAVCKEAP
860 870 880 890 900
NFESFSCLCA PGWQGKRCTV DVDECISKPC MNNGVCHNTQ GSYVCECPPG
910 920 930 940 950
FSGMDCEEDI NDCLANPCQN GGSCVDHVNT FSCQCHPGFI GDKCQTDMNE
960 970 980 990 1000
CLSEPCKNGG TCSDYVNSYT CTCPAGFHGV HCENNIDECT ESSCFNGGTC
1010 1020 1030 1040 1050
VDGINSFSCL CPVGFTGPFC LHDINECSSN PCLNAGTCVD GLGTYRCICP
1060 1070 1080 1090 1100
LGYTGKNCQT LVNLCSRSPC KNKGTCVQEK ARPHCLCPPG WDGAYCDVLN
1110 1120 1130 1140 1150
VSCKAAALQK GVPVEHLCQH SGICINAGNT HHCQCPLGYT GSYCEEQLDE
1160 1170 1180 1190 1200
CASNPCQHGA TCNDFIGGYR CECVPGYQGV NCEYEVDECQ NQPCQNGGTC
1210 1220 1230 1240 1250
IDLVNHFKCS CPPGTRGLLC EENIDECAGG PHCLNGGQCV DRIGGYTCRC
1260 1270 1280 1290 1300
LPGFAGERCE GDINECLSNP CSSEGSLDCV QLKNNYNCIC RSAFTGRHCE
1310 1320 1330 1340 1350
TFLDVCPQKP CLNGGTCAVA SNMPDGFICR CPPGFSGARL QSSCGQVKCR
1360 1370 1380 1390 1400
RGEQCIHTDS GPRCFCLNPK DCESGCASNP CQHGGTCYPQ RQPPHYSCRC
1410 1420 1430 1440 1450
PPSFGGSHCE LYTAPTSTPP ATCQSQYCAD KARDGICDEA CNSHACQWDG
1460 1470 1480 1490 1500
GDCSLTMEDP WANCTSTLRC WEYINNQCDE QCNTAECLFD NFECQRNSKT
1510 1520 1530 1540 1550
CKYDKYCADH FKDNHCDQGC NSEECGWDGL DCASDQPENL AEGTLIIVVL
1560 1570 1580 1590 1600
LPPEQLLQDS RSFLRALGTL LHTNLRIKQD SQGALMVYPY FGEKSAAMKK
1610 1620 1630 1640 1650
QKMTRRSLPE EQEQEQEVIG SKIFLEIDNR QCVQDSDQCF KNTDAAAALL
1660 1670 1680 1690 1700
ASHAIQGTLS YPLVSVFSEL ESPRNAQLLY LLAVAVVIIL FFILLGVIMA
1710 1720 1730 1740 1750
KRKQAWLPLA AGRFTLRRDS SNHKRREPVG QDAVGLKNLS VQVSEANLIG
1760 1770 1780 1790 1800
SGTSEHWVDD EGPQPKKAKA EDEALLSEDD PIDRRPWTQQ HLEAADISHT
1810 1820 1830 1840 1850
PSLALTPPQA EQEVDVLDVN VRGPDGCTPL MLASLRGGSS DLSDEDEDAE
1860 1870 1880 1890 1900
DSSANIITDL VYQGASLQAQ TDRTGEMALH LAARYSRADA AKRLLDAGAD
1910 1920 1930 1940 1950
RNAQDNMGRC PLHAAVAGDA QGVFQILIRN RVTDLDARMN DGTTPLILAA
1960 1970 1980 1990 2000
RLAVEGMVAE LINCQADVNA VDDHGKSALH WAAAVNNVEA TLLLLKNGAN
2010 2020 2030 2040 2050
RDMQDNKEET PLFLAAREGS YEAAKILLDH FANRDITDHM DRLPRDVARD
2060 2070 2080 2090 2100
RMHHDIVRLL DEYNVTPSPP GTVLTSALSP VLCGPNRSFL SLKHTPMGKK
2110 2120 2130 2140 2150
ARRPNTKSTM PTSLPNLAKE AKDAKGSRRK KCLNEKVQLS ESSVTLSPVD
2160 2170 2180 2190 2200
SLESPHTYVS DATSSPMITS PGILQASPTP LLAAAAPAAP VHTQHALSFS
2210 2220 2230 2240 2250
NLHDMQPLAP GASTVLPSVS QLLSHHHIAP PGSSSAGSLG RLHPVPVPAD
2260 2270 2280 2290 2300
WMNRVEMNET QYSEMFGMVL APAEGAHPGI AAPQSRPPEG KHMSTQREPL
2310 2320 2330 2340 2350
PPIVTFQLIP KRSIAQAAGA PQTQSSCPPA VAGPLPSMYQ IPEMPRLPSV
2360 2370 2380 2390 2400
AFPPTMMPQQ EGQVAQTIVP TYHPFPASVG KYPTPPSQHS YASSNAAERT
2410 2420 2430 2440 2450
PSHGGHLQGE HPYLTPSPES PDQWSSSSPH SASDWSDVTT SPTPGGGGGG
2460 2470
QRGPGTHMSE PPHSNMQVYA
Length:2,470
Mass (Da):265,327
Last modified:January 1, 1998 - v1
Checksum:iB55A31B35242716D
GO
Isoform 2 (identifier: O35516-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1302-1508: Missing.

Note: No experimental confirmation available.
Show »
Length:2,263
Mass (Da):242,663
Checksum:i4EF13A99DB3647BC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1340L → C in CAA48340 (PubMed:8440332).Curated1
Sequence conflicti1798S → R in AAC52924 (PubMed:8917536).Curated1
Sequence conflicti1901R → A in AAC52924 (PubMed:8917536).Curated1
Sequence conflicti1918G → A in AAC52924 (PubMed:8917536).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0014051302 – 1508Missing in isoform 2. CuratedAdd BLAST207

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32210 mRNA Translation: BAA22094.1
X68279 mRNA Translation: CAA48340.1
U31881 mRNA Translation: AAC52924.1
PIRiA49175
RefSeqiNP_035058.2, NM_010928.2
UniGeneiMm.485843

Genome annotation databases

GeneIDi18129
KEGGimmu:18129

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiNOTC2_MOUSE
AccessioniPrimary (citable) accession number: O35516
Secondary accession number(s): Q06008, Q60941
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 190 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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