GenomeNet

Database: UniProt
Entry: Q9QYE5
LinkDB: Q9QYE5
Original site: Q9QYE5 
ID   JAG2_MOUSE              Reviewed;        1247 AA.
AC   Q9QYE5; F8VPV5; O55139; O70219;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   13-FEB-2019, entry version 167.
DE   RecName: Full=Protein jagged-2;
DE            Short=Jagged2;
DE   Flags: Precursor;
GN   Name=Jag2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RA   Tsai S.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 302-819.
RC   TISSUE=Brain;
RX   PubMed=9341252; DOI=10.1007/s003359900642;
RA   Lan Y., Jiang R., Shawber C., Weinmaster G., Gridley T.;
RT   "The Jagged2 gene maps to chromosome 12 and is a candidate for the lgl
RT   and sm mutations.";
RL   Mamm. Genome 8:875-876(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 325-759.
RC   TISSUE=Brain;
RX   PubMed=9486542; DOI=10.1016/S0925-4773(97)00146-9;
RA   Valsecchi C., Ghezzi C., Ballabio A., Rugarli E.I.;
RT   "JAGGED2: a putative Notch ligand expressed in the apical ectodermal
RT   ridge and in sites of epithelial-mesenchymal interactions.";
RL   Mech. Dev. 69:203-207(1997).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9315665; DOI=10.1128/MCB.17.10.6057;
RA   Luo B., Aster J.C., Hasserjian R.P., Kuo F., Sklar J.;
RT   "Isolation and functional analysis of a cDNA for human Jagged2, a gene
RT   encoding a ligand for the Notch1 receptor.";
RL   Mol. Cell. Biol. 17:6057-6067(1997).
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. Plays an essential role during limb, craniofacial and
CC       thymic development. May be involved in myogenesis and in the
CC       development of peripheral and central nervous systems.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Found to be highest in fetal thymus,
CC       epidermis, foregut dorsal root ganglia and inner ear. In 2-weeK-
CC       old mice, abundant in heart, lung, thymus, skeletal muscle, brain
CC       and testis. Expression overlaps partially with Notch1 expression.
CC       {ECO:0000269|PubMed:9315665}.
CC   -!- DEVELOPMENTAL STAGE: At 13 dpc, found in paravertebral vessels and
CC       dorsal root ganglia. At 14 dpc, in oropharyngeal epithelium,
CC       developing thymus and in the muscles of the tongue. By 15 dpc, in
CC       many tissues.
DR   EMBL; AF038572; AAF16411.1; -; mRNA.
DR   EMBL; AC160929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF010137; AAC14010.1; -; mRNA.
DR   EMBL; Y14495; CAA74835.1; -; mRNA.
DR   CCDS; CCDS26200.1; -.
DR   RefSeq; NP_034718.2; NM_010588.2.
DR   UniGene; Mm.186146; -.
DR   ProteinModelPortal; Q9QYE5; -.
DR   SMR; Q9QYE5; -.
DR   BioGrid; 200855; 1.
DR   STRING; 10090.ENSMUSP00000075224; -.
DR   iPTMnet; Q9QYE5; -.
DR   PhosphoSitePlus; Q9QYE5; -.
DR   MaxQB; Q9QYE5; -.
DR   PaxDb; Q9QYE5; -.
DR   PeptideAtlas; Q9QYE5; -.
DR   PRIDE; Q9QYE5; -.
DR   DNASU; 16450; -.
DR   Ensembl; ENSMUST00000075827; ENSMUSP00000075224; ENSMUSG00000002799.
DR   GeneID; 16450; -.
DR   KEGG; mmu:16450; -.
DR   UCSC; uc007pfl.1; mouse.
DR   CTD; 3714; -.
DR   MGI; MGI:1098270; Jag2.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000160944; -.
DR   HOGENOM; HOG000113124; -.
DR   HOVERGEN; HBG031645; -.
DR   InParanoid; Q9QYE5; -.
DR   KO; K21635; -.
DR   OrthoDB; 72177at2759; -.
DR   TreeFam; TF351835; -.
DR   Reactome; R-MMU-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   PRO; PR:Q9QYE5; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000002799; Expressed in 265 organ(s), highest expression level in primary oocyte.
DR   ExpressionAtlas; Q9QYE5; baseline and differential.
DR   Genevisible; Q9QYE5; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; ISO:MGI.
DR   GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR   GO; GO:1990134; P:epithelial cell apoptotic process involved in palatal shelf morphogenesis; IMP:MGI.
DR   GO; GO:0042492; P:gamma-delta T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; NAS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; ISO:MGI.
DR   GO; GO:0030217; P:T cell differentiation; ISO:MGI.
DR   GO; GO:0045061; P:thymic T cell selection; ISS:UniProtKB.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR033108; Jag2.
DR   InterPro; IPR026219; Jagged/Serrate.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR44097:SF1; PTHR44097:SF1; 1.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR02059; JAGGEDFAMILY.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 16.
DR   SMART; SM00179; EGF_CA; 14.
DR   SMART; SM00215; VWC_out; 1.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 16.
DR   PROSITE; PS01186; EGF_2; 11.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 7.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   1247       Protein jagged-2.
FT                                /FTId=PRO_0000007630.
FT   TOPO_DOM     24   1082       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1083   1103       Helical. {ECO:0000255}.
FT   TOPO_DOM   1104   1247       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      196    240       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      241    274       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      275    305       EGF-like 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      307    345       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      347    383       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      385    421       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      423    459       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      461    496       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      498    534       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      536    572       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      574    634       EGF-like 10; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      636    672       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      674    710       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      712    748       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      751    787       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      789    825       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      827    863       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MOD_RES    1125   1125       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y219}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    570    570       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    619    619       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1060   1060       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    198    207       {ECO:0000250}.
FT   DISULFID    211    223       {ECO:0000250}.
FT   DISULFID    231    240       {ECO:0000250}.
FT   DISULFID    245    256       {ECO:0000250}.
FT   DISULFID    249    262       {ECO:0000250}.
FT   DISULFID    264    273       {ECO:0000250}.
FT   DISULFID    276    287       {ECO:0000250}.
FT   DISULFID    282    293       {ECO:0000250}.
FT   DISULFID    295    304       {ECO:0000250}.
FT   DISULFID    311    323       {ECO:0000250}.
FT   DISULFID    317    333       {ECO:0000250}.
FT   DISULFID    335    344       {ECO:0000250}.
FT   DISULFID    351    362       {ECO:0000250}.
FT   DISULFID    356    371       {ECO:0000250}.
FT   DISULFID    373    382       {ECO:0000250}.
FT   DISULFID    389    400       {ECO:0000250}.
FT   DISULFID    394    409       {ECO:0000250}.
FT   DISULFID    411    420       {ECO:0000250}.
FT   DISULFID    427    438       {ECO:0000250}.
FT   DISULFID    432    447       {ECO:0000250}.
FT   DISULFID    449    458       {ECO:0000250}.
FT   DISULFID    465    475       {ECO:0000250}.
FT   DISULFID    469    484       {ECO:0000250}.
FT   DISULFID    486    495       {ECO:0000250}.
FT   DISULFID    502    513       {ECO:0000250}.
FT   DISULFID    507    522       {ECO:0000250}.
FT   DISULFID    524    533       {ECO:0000250}.
FT   DISULFID    540    551       {ECO:0000250}.
FT   DISULFID    545    560       {ECO:0000250}.
FT   DISULFID    562    571       {ECO:0000250}.
FT   DISULFID    589    612       {ECO:0000255}.
FT   DISULFID    606    622       {ECO:0000255}.
FT   DISULFID    624    633       {ECO:0000250}.
FT   DISULFID    640    651       {ECO:0000250}.
FT   DISULFID    645    660       {ECO:0000250}.
FT   DISULFID    662    671       {ECO:0000250}.
FT   DISULFID    678    689       {ECO:0000250}.
FT   DISULFID    683    698       {ECO:0000250}.
FT   DISULFID    700    709       {ECO:0000250}.
FT   DISULFID    716    727       {ECO:0000250}.
FT   DISULFID    721    736       {ECO:0000250}.
FT   DISULFID    738    747       {ECO:0000250}.
FT   DISULFID    755    766       {ECO:0000250}.
FT   DISULFID    760    775       {ECO:0000250}.
FT   DISULFID    777    786       {ECO:0000250}.
FT   DISULFID    793    804       {ECO:0000250}.
FT   DISULFID    798    813       {ECO:0000250}.
FT   DISULFID    815    824       {ECO:0000250}.
FT   DISULFID    831    842       {ECO:0000250}.
FT   DISULFID    836    851       {ECO:0000250}.
FT   DISULFID    853    862       {ECO:0000250}.
FT   CONFLICT    302    302       L -> M (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    378    378       N -> S (in Ref. 1; AAF16411, 3; AAC14010
FT                                and 4; CAA74835). {ECO:0000305}.
FT   CONFLICT    461    461       N -> T (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    469    478       CQHGGTCKDL -> VSAWGHLQGP (in Ref. 3;
FT                                AAC14010). {ECO:0000305}.
FT   CONFLICT    492    492       G -> V (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    546    546       L -> F (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    549    549       A -> V (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    735    738       RCAC -> PAR (in Ref. 4; CAA74835).
FT                                {ECO:0000305}.
FT   CONFLICT    809    809       N -> H (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT    812    812       R -> A (in Ref. 3; AAC14010).
FT                                {ECO:0000305}.
FT   CONFLICT   1030   1030       V -> M (in Ref. 1; AAF16411).
FT                                {ECO:0000305}.
FT   CONFLICT   1126   1126       A -> T (in Ref. 1; AAF16411).
FT                                {ECO:0000305}.
FT   CONFLICT   1223   1223       R -> C (in Ref. 1; AAF16411).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1247 AA;  134745 MW;  E1352B1856946EA6 CRC64;
     MRARGWGRLP RRLLLLLVLC VQATRPMGYF ELQLSALRNV NGELLSGACC DGDGRTTRAG
     GCGRDECDTY VRVCLKEYQA KVTPTGPCSY GYGATPVLGG NSFYLPPAGA AGDRARARSR
     TGGHQDPGLV VIPFQFAWPR SFTLIVEAWD WDNDTTPDEE LLIERVSHAG MINPEDRWKS
     LHFSGHVAHL ELQIRVRCDE NYYSATCNKF CRPRNDFFGH YTCDQYGNKA CMDGWMGKEC
     KEAVCKQGCN LLHGGCTVPG ECRCSYGWQG KFCDECVPYP GCVHGSCVEP WHCDCETNWG
     GLLCDKDLNY CGSHHPCVNG GTCINAEPDQ YLCACPDGYL GKNCERAEHA CASNPCANGG
     SCHEVPSGFE CHCPSGWNGP TCALDIDECA SNPCAAGGTC VDQVDGFECI CPEQWVGATC
     QLDANECEGK PCLNAFSCKN LIGGYYCDCL PGWKGINCQI NINDCHGQCQ HGGTCKDLVN
     GYQCVCPRGF GGRHCELEYD KCASSPCRRG GICEDLVDGF RCHCPRGLSG LHCEVDMDLC
     EPSPCLNGAR CYNLEGDYYC ACPEDFGGKN CSVPRDTCPG GACRVIDGCG FEAGSRARGV
     APSGICGPHG HCVSLPGGNF SCICDSGFTG TYCHENIDDC MGQPCRNGGT CIDEVDSFRC
     FCPSGWEGEL CDINPNDCLP DPCHSRGRCY DLVNDFYCAC DDGWKGKTCH SREFQCDAYT
     CSNGGTCYDS GDTFRCACPP GWKGSTCTIA KNSSCVPNPC VNGGTCVGSG DSFSCICRDG
     WEGRTCTHNT NDCNPLPCYN GGICVDGVNW FRCECAPGFA GPDCRINIDE CQSSPCAYGA
     TCVDEINGYR CSCPPGRSGP RCQEVVIFTR PCWSRGMSFP HGSSWMEDCN SCRCLDGHRD
     CSKVWCGWKP CLLSGQPSDP SAQCPPGQQC QEKAVGQCLQ PPCENWGECT AEEPLPPSTP
     CQPRSSHLDN NCARLTLRFN RDQVPQGTTV GAICSGIRAL PATRAAAHDR LLLLLCDRAS
     SGASAVEVAV SFSPARDLPD SSLIQSTAHA IVAAITQRGN SSLLLAVTEV KVETVVMGGS
     STGLLVPVLC SVFSVLWLAC VVICVWWTRK RRKERERSRL PRDESANNQW APLNPIRNPI
     ERPGGSGLGT GGHKDILYQC KNFTPPPRRA GEALPGPAGH GAGGEDEEDE ELSRGDGDSP
     EAEKFISHKF TKDPSCSLGR PARWAPGPKV DNRAVRSTKD VRRAGRE
//
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