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P78504 (JAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein jagged-1

Short name=Jagged1
Short name=hJ1
Alternative name(s):
CD_antigen=CD339
Gene names
Name:JAG1
Synonyms:JAGL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation By similarity. Enhances fibroblast growth factor-induced angiogenesis (in vitro). Ref.3 Ref.12

Subunit structure

Interacts with NOTCH2 and NOTCH3 By similarity. Interacts with NOTCH1 (in the presence of calcium ions). Ref.12

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Widely expressed in adult and fetal tissues. In cervix epithelium expressed in undifferentiated subcolumnar reserve cells and squamous metaplasia. Expression is up-regulated in cervical squamous cell carcinoma. Expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells.

Developmental stage

Expressed in 32-52 days embryos in the distal cardiac outflow tract and pulmonary artery, major arteries, portal vein, optic vesicle, otocyst, branchial arches, metanephros, pancreas, mesocardium, around the major bronchial branches, and in the neural tube. Ref.10

Domain

The second EGF-like domain is atypical. Ref.12 Ref.13

Involvement in disease

Alagille syndrome 1 (ALGS1) [MIM:118450]: A form of Alagille syndrome, an autosomal dominant multisystem disorder. It is clinically defined by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. There are characteristic facial features and less frequent clinical involvement of the renal and vascular systems.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.28

Tetralogy of Fallot (TOF) [MIM:187500]: A congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. In this condition, blood from both ventricles (oxygen-rich and oxygen-poor) is pumped into the body often causing cyanosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.18

Sequence similarities

Contains 1 DSL domain.

Contains 16 EGF-like domains.

Sequence caution

The sequence AAC51323.1 differs from that shown. Reason: Frameshift at position 1187.

Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch receptor processing

Traceable author statement. Source: Reactome

Notch signaling involved in heart development

Inferred from mutant phenotype PubMed 20437614. Source: BHF-UCL

Notch signaling pathway

Inferred from mutant phenotype PubMed 19682396. Source: UniProtKB

T cell mediated immunity

Inferred from mutant phenotype PubMed 23086448. Source: UniProt

angiogenesis

Non-traceable author statement Ref.8. Source: UniProtKB

aorta morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

auditory receptor cell differentiation

Inferred from electronic annotation. Source: Ensembl

cardiac neural crest cell development involved in outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cardiac right ventricle morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cardiac septum morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell fate determination

Non-traceable author statement Ref.2. Source: UniProtKB

distal tubule development

Inferred from electronic annotation. Source: Ensembl

endocardial cushion cell development

Inferred from sequence or structural similarity. Source: BHF-UCL

endothelial cell differentiation

Non-traceable author statement Ref.4. Source: UniProtKB

hemopoiesis

Non-traceable author statement Ref.4. Source: UniProtKB

keratinocyte differentiation

Non-traceable author statement PubMed 12107827. Source: UniProtKB

loop of Henle development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial sheet

Inferred from electronic annotation. Source: Ensembl

myoblast differentiation

Non-traceable author statement Ref.4. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of stem cell differentiation

Inferred from mutant phenotype PubMed 19682396. Source: UniProtKB

nervous system development

Non-traceable author statement PubMed 8923452. Source: UniProtKB

neuronal stem cell maintenance

Inferred from expression pattern PubMed 19682396. Source: UniProtKB

positive regulation of Notch signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of myeloid cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20437614. Source: BHF-UCL

pulmonary artery morphogenesis

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

pulmonary valve morphogenesis

Inferred from mutant phenotype PubMed 20437614Ref.9. Source: BHF-UCL

regulation of cell migration

Non-traceable author statement PubMed 11549580. Source: UniProtKB

regulation of cell proliferation

Non-traceable author statement Ref.4. Source: UniProtKB

response to muramyl dipeptide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

extracellular region

Non-traceable author statement PubMed 11427524. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement PubMed 11427524. Source: UniProtKB

membrane

Traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 20437614. Source: BHF-UCL

   Molecular_functionNotch binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

growth factor activity

Non-traceable author statement PubMed 11067884. Source: UniProtKB

structural molecule activity

Non-traceable author statement PubMed 10679295. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CD46P155295EBI-2847071,EBI-2623451

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 12181185Protein jagged-1
PRO_0000007625

Regions

Topological domain34 – 10671034Extracellular Potential
Transmembrane1068 – 109326Helical; Potential
Topological domain1094 – 1218125Cytoplasmic Potential
Domain185 – 22945DSL
Domain230 – 26334EGF-like 1
Domain264 – 29431EGF-like 2; atypical
Domain296 – 33439EGF-like 3
Domain336 – 37237EGF-like 4
Domain374 – 41037EGF-like 5; calcium-binding Potential
Domain412 – 44837EGF-like 6; calcium-binding Potential
Domain450 – 48536EGF-like 7; calcium-binding Potential
Domain487 – 52337EGF-like 8; calcium-binding Potential
Domain525 – 56137EGF-like 9
Domain586 – 62742EGF-like 10
Domain629 – 66537EGF-like 11; calcium-binding Potential
Domain667 – 70337EGF-like 12; calcium-binding Potential
Domain705 – 74137EGF-like 13
Domain744 – 78037EGF-like 14
Domain782 – 81837EGF-like 15; calcium-binding Potential
Domain820 – 85637EGF-like 16; calcium-binding Potential
Region199 – 2079Important for interaction with NOTCH1

Amino acid modifications

Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation5591N-linked (GlcNAc...) Potential
Glycosylation7451N-linked (GlcNAc...) Potential
Glycosylation9601N-linked (GlcNAc...) Potential
Glycosylation9911N-linked (GlcNAc...) Potential
Glycosylation10451N-linked (GlcNAc...) Potential
Glycosylation10641N-linked (GlcNAc...) Potential
Disulfide bond187 ↔ 196 Ref.12 Ref.13
Disulfide bond200 ↔ 212 Ref.12 Ref.13
Disulfide bond220 ↔ 229 Ref.12 Ref.13
Disulfide bond234 ↔ 245 Ref.12 Ref.13
Disulfide bond238 ↔ 251 Ref.12 Ref.13
Disulfide bond253 ↔ 262 Ref.12 Ref.13
Disulfide bond265 ↔ 276 Ref.12 Ref.13
Disulfide bond271 ↔ 282 Ref.12 Ref.13
Disulfide bond284 ↔ 293 Ref.12 Ref.13
Disulfide bond300 ↔ 312 Ref.12 Ref.13
Disulfide bond306 ↔ 322 Ref.12 Ref.13
Disulfide bond324 ↔ 333 Ref.12 Ref.13
Disulfide bond340 ↔ 351 By similarity
Disulfide bond345 ↔ 360 By similarity
Disulfide bond362 ↔ 371 By similarity
Disulfide bond378 ↔ 389 By similarity
Disulfide bond383 ↔ 398 By similarity
Disulfide bond400 ↔ 409 By similarity
Disulfide bond416 ↔ 427 By similarity
Disulfide bond421 ↔ 436 By similarity
Disulfide bond438 ↔ 447 By similarity
Disulfide bond454 ↔ 464 By similarity
Disulfide bond458 ↔ 473 By similarity
Disulfide bond475 ↔ 484 By similarity
Disulfide bond491 ↔ 502 By similarity
Disulfide bond496 ↔ 511 By similarity
Disulfide bond513 ↔ 522 By similarity
Disulfide bond529 ↔ 540 By similarity
Disulfide bond534 ↔ 549 By similarity
Disulfide bond551 ↔ 560 By similarity
Disulfide bond578 ↔ 605 By similarity
Disulfide bond599 ↔ 615 By similarity
Disulfide bond617 ↔ 626 By similarity
Disulfide bond633 ↔ 644 By similarity
Disulfide bond638 ↔ 653 By similarity
Disulfide bond655 ↔ 664 By similarity
Disulfide bond671 ↔ 682 By similarity
Disulfide bond676 ↔ 691 By similarity
Disulfide bond693 ↔ 702 By similarity
Disulfide bond709 ↔ 720 By similarity
Disulfide bond714 ↔ 729 By similarity
Disulfide bond731 ↔ 740 By similarity
Disulfide bond748 ↔ 759 By similarity
Disulfide bond753 ↔ 768 By similarity
Disulfide bond770 ↔ 779 By similarity
Disulfide bond786 ↔ 797 By similarity
Disulfide bond791 ↔ 806 By similarity
Disulfide bond808 ↔ 817 By similarity
Disulfide bond824 ↔ 835 By similarity
Disulfide bond829 ↔ 844 By similarity
Disulfide bond846 ↔ 855 By similarity

Natural variations

Natural variant22 – 254Missing in ALGS1.
VAR_026296
Natural variant311A → V in ALGS1. Ref.26
VAR_026297
Natural variant331G → D in ALGS1. Ref.21
VAR_026298
Natural variant331G → S in ALGS1. Ref.28
VAR_026299
Natural variant331G → V in ALGS1. Ref.28
VAR_026300
Natural variant371L → S in ALGS1. Ref.19 Ref.21
VAR_013186
Natural variant391I → S in ALGS1. Ref.24
VAR_026301
Natural variant401L → P in ALGS1. Ref.26
VAR_026302
Natural variant451V → L in biliary atresia; extrahepatic. Ref.23
Corresponds to variant rs183974372 [ dbSNP | Ensembl ].
VAR_026303
Natural variant531N → D in biliary atresia; extrahepatic. Ref.23
VAR_026304
Natural variant651K → M in biliary atresia; extrahepatic. Ref.23
VAR_026305
Natural variant751F → S in ALGS1. Ref.26
VAR_026306
Natural variant781C → S in ALGS1. Ref.21
VAR_026307
Natural variant791L → H in ALGS1. Ref.15
VAR_013187
Natural variant921C → R in ALGS1. Ref.28
VAR_026308
Natural variant921C → Y in ALGS1. Ref.28
VAR_026309
Natural variant1201I → N in ALGS1. Ref.27
VAR_026310
Natural variant1231P → S in ALGS1. Ref.26
VAR_026311
Natural variant1271A → T in ALGS1. Ref.15
VAR_013188
Natural variant1291P → R in ALGS1. Ref.15
VAR_013189
Natural variant1461V → I.
Corresponds to variant rs6040067 [ dbSNP | Ensembl ].
VAR_048985
Natural variant1521I → T in ALGS1. Ref.16
VAR_013190
Natural variant1551A → P in ALGS1. Ref.28
VAR_026312
Natural variant1631P → L in ALGS1. Ref.15
VAR_013191
Natural variant1631P → R in ALGS1. Ref.26
VAR_026313
Natural variant1811Y → N in ALGS1. Ref.21
VAR_026314
Natural variant1841R → C in ALGS1. Ref.2 Ref.14
VAR_013192
Natural variant1841R → G in ALGS1. Ref.15
VAR_013193
Natural variant1841R → H in ALGS1. Ref.14 Ref.24
VAR_013194
Natural variant1841R → L in ALGS1. Ref.16
VAR_013195
Natural variant1871C → S in ALGS1. Ref.15
VAR_013196
Natural variant1871C → Y in ALGS1. Ref.27
VAR_026315
Natural variant2031R → K in biliary atresia; extrahepatic. Ref.23
VAR_026316
Natural variant2201C → F in ALGS1. Ref.20
VAR_013197
Natural variant2241W → C in ALGS1. Ref.26
VAR_026317
Natural variant2291C → G in ALGS1. Ref.15
VAR_013198
Natural variant2291C → Y in ALGS1. Ref.17
VAR_013199
Natural variant2341C → Y in deafness; with congenital heart defects and posterior embryotoxon. Ref.22
VAR_026318
Natural variant2521R → G in ALGS1. Ref.28
VAR_026319
Natural variant2561G → S in ALGS1. Ref.28
VAR_026320
Natural variant2691P → L in ALGS1. Ref.26
VAR_026321
Natural variant2711C → R in ALGS1. Ref.28
VAR_026322
Natural variant2741G → D in TOF; temperature sensitive mutation; the protein is abnormally glycosylated and retained intracellularly. Ref.18 Ref.25
Corresponds to variant rs28939668 [ dbSNP | Ensembl ].
VAR_013200
Natural variant2841C → F in ALGS1. Ref.15
VAR_013201
Natural variant2881W → C in ALGS1. Ref.15
VAR_013202
Natural variant3861G → R in ALGS1. Ref.17
VAR_013203
Natural variant4381C → F in ALGS1. Ref.15
VAR_013204
Natural variant5041N → S in ALGS1. Ref.28
VAR_026323
Natural variant6901Y → D in biliary atresia; extrahepatic. Ref.23
VAR_026324
Natural variant6931C → Y in ALGS1. Ref.28
VAR_026325
Natural variant7141C → Y in ALGS1. Ref.21
VAR_026326
Natural variant7311C → S in ALGS1. Ref.15
VAR_013205
Natural variant7401C → R in ALGS1. Ref.15
VAR_013206
Natural variant7531C → R in ALGS1. Ref.20
VAR_013207
Natural variant8181R → K. Ref.28
VAR_026327
Natural variant8711P → R in biliary atresia; extrahepatic. Ref.23
Corresponds to variant rs35761929 [ dbSNP | Ensembl ].
VAR_026328
Natural variant8891R → Q in ALGS1. Ref.28
VAR_026329
Natural variant9021C → S in ALGS1. Ref.21
VAR_026330
Natural variant9081H → Q in biliary atresia; extrahepatic. Ref.23
VAR_026331
Natural variant9111C → Y in ALGS1. Ref.28
VAR_026332
Natural variant9131S → R in ALGS1. Ref.24
VAR_026333
Natural variant9211L → P in biliary atresia; extrahepatic. Ref.23
VAR_026334
Natural variant9371R → Q in ALGS1. Ref.26
Corresponds to variant rs145895196 [ dbSNP | Ensembl ].
VAR_026335
Natural variant1055 – 10562VR → G in ALGS1.
VAR_026336
Natural variant12131R → Q in biliary atresia; extrahepatic. Ref.23
VAR_026337

Experimental info

Mutagenesis2071F → A: Strongly reduced NOTCH1 binding. Ref.12
Sequence conflict1171R → P in AAB39007. Ref.5
Sequence conflict2271P → R in AAC51731. Ref.1
Sequence conflict4981N → D in AAC51731. Ref.1

Secondary structure

............................................................ 1218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78504 [UniParc].

Last modified May 2, 2002. Version 3.
Checksum: F36EE9FBF64DF162

FASTA1,218133,799
        10         20         30         40         50         60 
MRSPRTRGRS GRPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGARN 

        70         80         90        100        110        120 
PGDRKCTRDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRGNDRNRI 

       130        140        150        160        170        180 
VLPFSFAWPR SYTLLVEAWD SSNDTVQPDS IIEKASHSGM INPSRQWQTL KQNTGVAHFE 

       190        200        210        220        230        240 
YQIRVTCDDY YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC MEGWMGPECN RAICRQGCSP 

       250        260        270        280        290        300 
KHGSCKLPGD CRCQYGWQGL YCDKCIPHPG CVHGICNEPW QCLCETNWGG QLCDKDLNYC 

       310        320        330        340        350        360 
GTHQPCLNGG TCSNTGPDKY QCSCPEGYSG PNCEIAEHAC LSDPCHNRGS CKETSLGFEC 

       370        380        390        400        410        420 
ECSPGWTGPT CSTNIDDCSP NNCSHGGTCQ DLVNGFKCVC PPQWTGKTCQ LDANECEAKP 

       430        440        450        460        470        480 
CVNAKSCKNL IASYYCDCLP GWMGQNCDIN INDCLGQCQN DASCRDLVNG YRCICPPGYA 

       490        500        510        520        530        540 
GDHCERDIDE CASNPCLNGG HCQNEINRFQ CLCPTGFSGN LCQLDIDYCE PNPCQNGAQC 

       550        560        570        580        590        600 
YNRASDYFCK CPEDYEGKNC SHLKDHCRTT PCEVIDSCTV AMASNDTPEG VRYISSNVCG 

       610        620        630        640        650        660 
PHGKCKSQSG GKFTCDCNKG FTGTYCHENI NDCESNPCRN GGTCIDGVNS YKCICSDGWE 

       670        680        690        700        710        720 
GAYCETNIND CSQNPCHNGG TCRDLVNDFY CDCKNGWKGK TCHSRDSQCD EATCNNGGTC 

       730        740        750        760        770        780 
YDEGDAFKCM CPGGWEGTTC NIARNSSCLP NPCHNGGTCV VNGESFTCVC KEGWEGPICA 

       790        800        810        820        830        840 
QNTNDCSPHP CYNSGTCVDG DNWYRCECAP GFAGPDCRIN INECQSSPCA FGATCVDEIN 

       850        860        870        880        890        900 
GYRCVCPPGH SGAKCQEVSG RPCITMGSVI PDGAKWDDDC NTCQCLNGRI ACSKVWCGPR 

       910        920        930        940        950        960 
PCLLHKGHSE CPSGQSCIPI LDDQCFVHPC TGVGECRSSS LQPVKTKCTS DSYYQDNCAN 

       970        980        990       1000       1010       1020 
ITFTFNKEMM SPGLTTEHIC SELRNLNILK NVSAEYSIYI ACEPSPSANN EIHVAISAED 

      1030       1040       1050       1060       1070       1080 
IRDDGNPIKE ITDKIIDLVS KRDGNSSLIA AVAEVRVQRR PLKNRTDFLV PLLSSVLTVA 

      1090       1100       1110       1120       1130       1140 
WICCLVTAFY WCLRKRRKPG SHTHSASEDN TTNNVREQLN QIKNPIEKHG ANTVPIKDYE 

      1150       1160       1170       1180       1190       1200 
NKNSKMSKIR THNSEVEEDD MDKHQQKARF AKQPAYTLVD REEKPPNGTP TKHPNWTNKQ 

      1210 
DNRDLESAQS LNRMEYIV 

« Hide

References

« Hide 'large scale' references
[1]"Identification and cloning of the human homolog (JAG1) of the rat Jagged1 gene from the Alagille syndrome critical region at 20p12."
Oda T., Elkahloun A.G., Meltzer P.S., Chandrasekharappa S.C.
Genomics 43:376-379(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Alagille syndrome is caused by mutations in human Jagged1, which encodes a ligand for Notch1."
Li L., Krantz I.D., Deng Y., Genin A., Banta A.B., Collins C.C., Qi M., Trask B.J., Kuo W.L., Cochran J., Costa T., Pierpont M.E.M., Rand E.B., Piccoli D.A., Hood L., Spinner N.B.
Nat. Genet. 16:243-251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALGS1 CYS-184.
Tissue: Bone marrow.
[3]"The human homolog of rat Jagged1 expressed by marrow stroma inhibits differentiation of 32D cells through interaction with Notch1."
Li L., Milner L.A., Deng Y., Iwata M., Banta A.B., Graf L., Marcovina S., Friedman C., Trask B.J., Hood L., Torok-Storb B.
Immunity 8:43-55(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]"Rel/NF-kappaB can trigger the Notch signaling pathway by inducing the expression of Jagged1, a ligand for Notch receptors."
Bash J., Zong W.-X., Banga S., Rivera A., Ballard D.W., Ron Y., Gelinas C.
EMBO J. 18:2803-2811(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[5]"Human ligands of the Notch receptor."
Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L., Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.
Am. J. Pathol. 154:785-794(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]"An antisense oligonucleotide to the notch ligand Jagged enhances fibroblast growth factor-induced angiogenesis in vitro."
Zimrin A.B., Pepper M.S., McMahon G.A., Nguyen F., Montesano R., Maciag T.
J. Biol. Chem. 271:32499-32502(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-1218.
Tissue: Umbilical vein endothelial cell.
[9]"Mutations in the human Jagged1 gene are responsible for Alagille syndrome."
Oda T., Elkahloun A.G., Pike B.L., Okajima K., Krantz I.D., Genin A., Piccoli D.A., Meltzer P.S., Spinner N.B., Collins F.S., Chandrasekharappa S.C.
Nat. Genet. 16:235-242(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[10]"JAGGED1 expression in human embryos: correlation with the Alagille syndrome phenotype."
Jones E.A., Clement-Jones M., Wilson D.I.
J. Med. Genet. 37:658-662(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"A conserved face of the Jagged/Serrate DSL domain is involved in Notch trans-activation and cis-inhibition."
Cordle J., Johnson S., Tay J.Z., Roversi P., Wilkin M.B., de Madrid B.H., Shimizu H., Jensen S., Whiteman P., Jin B., Redfield C., Baron M., Lea S.M., Handford P.A.
Nat. Struct. Mol. Biol. 15:849-857(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 185-335, FUNCTION, INTERACTION WITH NOTCH1, DOMAIN, MUTAGENESIS OF PHE-207, DISULFIDE BONDS.
[13]"Exon 6 of human JAG1 encodes a conserved structural unit."
Pintar A., Guarnaccia C., Dhir S., Pongor S.
BMC Struct. Biol. 9:43-43(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 252-295, DOMAIN, DISULFIDE BONDS.
[14]"Spectrum and frequency of Jagged1 (JAG1) mutations in Alagille syndrome patients and their families."
Krantz I.D., Colliton R.P., Genin A., Rand E.B., Li L., Piccoli D.A., Spinner N.B.
Am. J. Hum. Genet. 62:1361-1369(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 CYS-184 AND HIS-184.
[15]"Mutations in JAGGED1 gene are predominantly sporadic in Alagille syndrome."
Crosnier C., Driancourt C., Raynaud N., Dhorne-Pollet S., Pollet N., Bernard O., Hadchouel M., Meunier-Rotival M.
Gastroenterology 116:1141-1148(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 HIS-79; THR-127; ARG-129; LEU-163; GLY-184; SER-187; GLY-229; PHE-284; CYS-288; PHE-438; SER-731 AND ARG-740.
[16]"Jagged-1 mutation analysis in Italian Alagille syndrome patients."
Pilia G., Uda M., Macis D., Frau F., Crisponi L., Balli F., Barbera C., Colombo C., Frediani T., Gatti R., Iorio R., Marazzi M.G., Marcellini M., Musumeci S., Nebbia G., Vajro P., Ruffa G., Zancan L., Cao A., DeVirgilis S.
Hum. Mutat. 14:394-400(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 THR-152 AND LEU-184.
[17]"Jagged1 (JAG1) mutation detection in an Australian Alagille syndrome population."
Heritage M.L., MacMillan J.C., Colliton R.P., Genin A., Spinner N.B., Anderson G.J.
Hum. Mutat. 16:408-416(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 TYR-229 AND ARG-386.
[18]"Familial tetralogy of Fallot caused by mutation in the Jagged1 gene."
Eldadah Z.A., Hamosh A., Biery N.J., Montgomery R.A., Duke M., Elkins R., Dietz H.C.
Hum. Mol. Genet. 10:163-169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TOF ASP-274.
[19]"Defective intracellular transport and processing of JAG1 missense mutations in Alagille syndrome."
Morrissette J.J.D., Colliton R.P., Spinner N.B.
Hum. Mol. Genet. 10:405-413(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALGS1 SER-37.
[20]"Fifteen novel mutations in the JAGGED1 gene of patients with Alagille syndrome."
Crosnier C., Driancourt C., Raynaud N., Hadchouel M., Meunier-Rotival M.
Hum. Mutat. 17:72-73(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 PHE-220 AND ARG-753.
[21]"Mutation analysis of Jagged1 (JAG1) in Alagille syndrome patients."
Colliton R.P., Bason L., Lu F.-M., Piccoli D.A., Krantz I.D., Spinner N.B.
Hum. Mutat. 17:151-152(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 ASP-33; SER-37; SER-78; ASN-181; TYR-714 AND SER-902.
[22]"Familial deafness, congenital heart defects, and posterior embryotoxon caused by cysteine substitution in the first epidermal-growth-factor-like domain of Jagged 1."
Le Caignec C., Lefevre M., Schott J.J., Chaventre A., Gayet M., Calais C., Moisan J.P.
Am. J. Hum. Genet. 71:180-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DEAFNESS TYR-234.
[23]"The significance of human Jagged 1 mutations detected in severe cases of extrahepatic biliary atresia."
Kohsaka T., Yuan Z.-R., Guo S.-X., Tagawa M., Nakamura A., Nakano M., Kawasasaki H., Inomata Y., Tanaka K., Miyauchi J.
Hepatology 36:904-912(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BILIARY ATRESIA LEU-45; ASP-53; MET-65; LYS-203; ASP-690; ARG-871; GLN-908; PRO-921 AND GLN-1213.
[24]"DHPLC mutation analysis of Jagged1 (JAG1) reveals six novel mutations in Australian Alagille syndrome patients."
Heritage M.L., MacMillan J.C., Anderson G.J.
Hum. Mutat. 20:481-481(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 SER-39; HIS-184 AND ARG-913.
[25]"Conditional JAG1 mutation shows the developing heart is more sensitive than developing liver to JAG1 dosage."
Lu F., Morrissette J.J.D., Spinner N.B.
Am. J. Hum. Genet. 72:1065-1070(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ASP-274.
[26]"Identification of 36 novel Jagged1 (JAG1) mutations in patients with Alagille syndrome."
Roepke A., Kujat A., Graeber M., Giannakudis J., Hansmann I.
Hum. Mutat. 21:100-100(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 VAL-31; PRO-40; SER-75; SER-123; ARG-163; CYS-224; LEU-269 AND GLN-937.
[27]"Twelve novel JAG1 gene mutations in Polish Alagille syndrome patients."
Jurkiewicz D., Popowska E., Glaeser C., Hansmann I., Krajewska-Walasek M.
Hum. Mutat. 25:321-321(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 ASN-120 AND TYR-187.
[28]"Jagged1 (JAG1) mutations in Alagille syndrome: increasing the mutation detection rate."
Warthen D.M., Moore E.C., Kamath B.M., Morrissette J.J.D., Sanchez P., Piccoli D.A., Krantz I.D., Spinner N.B.
Hum. Mutat. 27:436-443(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALGS1 22-CYS--ARG-25 DEL; SER-33; VAL-33; ARG-92; TYR-92; PRO-155; GLY-252; SER-256; ARG-271; SER-504; TYR-693; GLN-889; TYR-911 AND 1055-VAL-ARG-1056 GLY DELINS, VARIANT LYS-818.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF003837 mRNA. Translation: AAC51731.1.
U73936 mRNA. Translation: AAC52020.1.
AF028593 mRNA. Translation: AAB84053.1.
U61276 mRNA. Translation: AAB39007.1.
AL035456 Genomic DNA. Translation: CAC07198.1.
BC126205 mRNA. Translation: AAI26206.1.
BC126207 mRNA. Translation: AAI26208.1.
U77720 mRNA. Translation: AAC51323.1. Frameshift.
RefSeqNP_000205.1. NM_000214.2.
UniGeneHs.224012.
Hs.626544.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KB9NMR-A252-295[»]
2VJ2X-ray2.50A/B185-335[»]
4CBZX-ray2.50A/B32-335[»]
4CC0X-ray2.32A/B32-335[»]
4CC1X-ray2.84A/B32-335[»]
DisProtDP00418.
ProteinModelPortalP78504.
SMRP78504. Positions 186-889.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106689. 9 interactions.
DIPDIP-46371N.
IntActP78504. 8 interactions.
MINTMINT-2804836.
STRING9606.ENSP00000254958.

PTM databases

PhosphoSiteP78504.

Polymorphism databases

DMDM20455033.

Proteomic databases

PaxDbP78504.
PeptideAtlasP78504.
PRIDEP78504.

Protocols and materials databases

DNASU182.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254958; ENSP00000254958; ENSG00000101384.
GeneID182.
KEGGhsa:182.
UCSCuc002wnw.2. human.

Organism-specific databases

CTD182.
GeneCardsGC20M010618.
HGNCHGNC:6188. JAG1.
HPACAB010343.
HPA021555.
MIM118450. phenotype.
187500. phenotype.
601920. gene+phenotype.
neXtProtNX_P78504.
Orphanet261600. Alagille syndrome due to 20p12 microdeletion.
261619. Alagille syndrome due to a JAG1 point mutation.
3303. Tetralogy of Fallot.
PharmGKBPA29986.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000113124.
HOVERGENHBG031645.
InParanoidP78504.
KOK06052.
OMAHPNWTNK.
OrthoDBEOG7BKCSS.
PhylomeDBP78504.
TreeFamTF351835.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
SignaLinkP78504.

Gene expression databases

ArrayExpressP78504.
BgeeP78504.
CleanExHS_JAG1.
GenevestigatorP78504.

Family and domain databases

InterProIPR001774. DSL.
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.
IPR026219. Jagged/Serrate.
IPR011651. Notch_ligand_N.
IPR001007. VWF_C.
[Graphical view]
PfamPF01414. DSL. 1 hit.
PF00008. EGF. 10 hits.
PF07645. EGF_CA. 1 hit.
PF07657. MNNL. 1 hit.
[Graphical view]
PRINTSPR02059. JAGGEDFAMILY.
SMARTSM00051. DSL. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 10 hits.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 3 hits.
PROSITEPS00010. ASX_HYDROXYL. 10 hits.
PS51051. DSL. 1 hit.
PS00022. EGF_1. 16 hits.
PS01186. EGF_2. 12 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJAG1. human.
EvolutionaryTraceP78504.
GeneWikiJAG1.
GenomeRNAi182.
NextBio744.
PROP78504.
SOURCESearch...

Entry information

Entry nameJAG1_HUMAN
AccessionPrimary (citable) accession number: P78504
Secondary accession number(s): A0AV43 expand/collapse secondary AC list , O14902, O15122, Q15816
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries