P78504 (JAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein jagged-1
Short name=Jagged1
Short name=hJ1

Alternative name(s):
CD_antigen=CD339

Gene names

Name:	JAG1
Synonyms:	JAGL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Notch signaling pathway
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch receptor processing Traceable author statement. Source: Reactome Notch signaling involved in heart development Inferred from mutant phenotype PubMed 20437614. Source: BHF-UCL 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: Compara 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: Compara 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: Compara morphogenesis of an epithelial sheet Inferred from electronic annotation. Source: Compara myoblast differentiation Non-traceable author statement Ref.4. Source: UniProtKB negative regulation of fat cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of myeloid cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara extracellular region Non-traceable author statement PubMed 11427524. Source: UniProtKB integral to plasma membrane Non-traceable author statement PubMed 11427524. Source: UniProtKB
Molecular_function	Notch binding Non-traceable author statement Ref.1. Source: UniProtKB calcium ion binding Non-traceable author statement. Source: UniProtKB 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Potential

Chain

34 – 1218

1185

Protein jagged-1

PRO_0000007625

Regions

Topological domain

34 – 1067

1034

Extracellular Potential

Transmembrane

1068 – 1093

26

Helical; Potential

Topological domain

1094 – 1218

125

Cytoplasmic Potential

Domain

185 – 229

45

DSL

Domain

230 – 263

34

EGF-like 1

Domain

264 – 294

31

EGF-like 2; atypical

Domain

296 – 334

39

EGF-like 3

Domain

336 – 372

37

EGF-like 4

Domain

374 – 410

37

EGF-like 5; calcium-binding Potential

Domain

412 – 448

37

EGF-like 6; calcium-binding Potential

Domain

450 – 485

36

EGF-like 7; calcium-binding Potential

Domain

487 – 523

37

EGF-like 8; calcium-binding Potential

Domain

525 – 561

37

EGF-like 9

Domain

586 – 627

42

EGF-like 10

Domain

629 – 665

37

EGF-like 11; calcium-binding Potential

Domain

667 – 703

37

EGF-like 12; calcium-binding Potential

Domain

705 – 741

37

EGF-like 13

Domain

744 – 780

37

EGF-like 14

Domain

782 – 818

37

EGF-like 15; calcium-binding Potential

Domain

820 – 856

37

EGF-like 16; calcium-binding Potential

Region

199 – 207

9

Important for interaction with NOTCH1

Amino acid modifications

Glycosylation

143

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...) Potential

Glycosylation

382

1

N-linked (GlcNAc...) Potential

Glycosylation

559

1

N-linked (GlcNAc...) Potential

Glycosylation

745

1

N-linked (GlcNAc...) Potential

Glycosylation

960

1

N-linked (GlcNAc...) Potential

Glycosylation

991

1

N-linked (GlcNAc...) Potential

Glycosylation

1045

1

N-linked (GlcNAc...) Potential

Glycosylation

1064

1

N-linked (GlcNAc...) Potential

Disulfide bond

187 ↔ 196

Ref.12 Ref.13

Disulfide bond

200 ↔ 212

Ref.12 Ref.13

Disulfide bond

220 ↔ 229

Ref.12 Ref.13

Disulfide bond

234 ↔ 245

Ref.12 Ref.13

Disulfide bond

238 ↔ 251

Ref.12 Ref.13

Disulfide bond

253 ↔ 262

Ref.12 Ref.13

Disulfide bond

265 ↔ 276

Ref.12 Ref.13

Disulfide bond

271 ↔ 282

Ref.12 Ref.13

Disulfide bond

284 ↔ 293

Ref.12 Ref.13

Disulfide bond

300 ↔ 312

Ref.12 Ref.13

Disulfide bond

306 ↔ 322

Ref.12 Ref.13

Disulfide bond

324 ↔ 333

Ref.12 Ref.13

Disulfide bond

340 ↔ 351

By similarity

Disulfide bond

345 ↔ 360

By similarity

Disulfide bond

362 ↔ 371

By similarity

Disulfide bond

378 ↔ 389

By similarity

Disulfide bond

383 ↔ 398

By similarity

Disulfide bond

400 ↔ 409

By similarity

Disulfide bond

416 ↔ 427

By similarity

Disulfide bond

421 ↔ 436

By similarity

Disulfide bond

438 ↔ 447

By similarity

Disulfide bond

454 ↔ 464

By similarity

Disulfide bond

458 ↔ 473

By similarity

Disulfide bond

475 ↔ 484

By similarity

Disulfide bond

491 ↔ 502

By similarity

Disulfide bond

496 ↔ 511

By similarity

Disulfide bond

513 ↔ 522

By similarity

Disulfide bond

529 ↔ 540

By similarity

Disulfide bond

534 ↔ 549

By similarity

Disulfide bond

551 ↔ 560

By similarity

Disulfide bond

578 ↔ 605

By similarity

Disulfide bond

599 ↔ 615

By similarity

Disulfide bond

617 ↔ 626

By similarity

Disulfide bond

633 ↔ 644

By similarity

Disulfide bond

638 ↔ 653

By similarity

Disulfide bond

655 ↔ 664

By similarity

Disulfide bond

671 ↔ 682

By similarity

Disulfide bond

676 ↔ 691

By similarity

Disulfide bond

693 ↔ 702

By similarity

Disulfide bond

709 ↔ 720

By similarity

Disulfide bond

714 ↔ 729

By similarity

Disulfide bond

731 ↔ 740

By similarity

Disulfide bond

748 ↔ 759

By similarity

Disulfide bond

753 ↔ 768

By similarity

Disulfide bond

770 ↔ 779

By similarity

Disulfide bond

786 ↔ 797

By similarity

Disulfide bond

791 ↔ 806

By similarity

Disulfide bond

808 ↔ 817

By similarity

Disulfide bond

824 ↔ 835

By similarity

Disulfide bond

829 ↔ 844

By similarity

Disulfide bond

846 ↔ 855

By similarity

Natural variations

Natural variant

22 – 25

4

Missing in ALGS1.

VAR_026296

Natural variant

31

1

A → V in ALGS1. Ref.26

VAR_026297

Natural variant

33

1

G → D in ALGS1. Ref.21

VAR_026298

Natural variant

33

1

G → S in ALGS1. Ref.28

VAR_026299

Natural variant

33

1

G → V in ALGS1. Ref.28

VAR_026300

Natural variant

37

1

L → S in ALGS1. Ref.19 Ref.21

VAR_013186

Natural variant

39

1

I → S in ALGS1. Ref.24

VAR_026301

Natural variant

40

1

L → P in ALGS1. Ref.26

VAR_026302

Natural variant

45

1

V → L in biliary atresia; extrahepatic. Ref.23

VAR_026303

Natural variant

53

1

N → D in biliary atresia; extrahepatic. Ref.23

VAR_026304

Natural variant

65

1

K → M in biliary atresia; extrahepatic. Ref.23

VAR_026305

Natural variant

75

1

F → S in ALGS1. Ref.26

VAR_026306

Natural variant

78

1

C → S in ALGS1. Ref.21

VAR_026307

Natural variant

79

1

L → H in ALGS1. Ref.15

VAR_013187

Natural variant

92

1

C → R in ALGS1. Ref.28

VAR_026308

Natural variant

92

1

C → Y in ALGS1. Ref.28

VAR_026309

Natural variant

120

1

I → N in ALGS1. Ref.27

VAR_026310

Natural variant

123

1

P → S in ALGS1. Ref.26

VAR_026311

Natural variant

127

1

A → T in ALGS1. Ref.15

VAR_013188

Natural variant

129

1

P → R in ALGS1. Ref.15

VAR_013189

Natural variant

146

1

V → I.
Corresponds to variant rs6040067 [ dbSNP | Ensembl ].

VAR_048985

Natural variant

152

1

I → T in ALGS1. Ref.16

VAR_013190

Natural variant

155

1

A → P in ALGS1. Ref.28

VAR_026312

Natural variant

163

1

P → L in ALGS1. Ref.15

VAR_013191

Natural variant

163

1

P → R in ALGS1. Ref.26

VAR_026313

Natural variant

181

1

Y → N in ALGS1. Ref.21

VAR_026314

Natural variant

184

1

R → C in ALGS1. Ref.2 Ref.14

VAR_013192

Natural variant

184

1

R → G in ALGS1. Ref.15

VAR_013193

Natural variant

184

1

R → H in ALGS1. Ref.14 Ref.24

VAR_013194

Natural variant

184

1

R → L in ALGS1. Ref.16

VAR_013195

Natural variant

187

1

C → S in ALGS1. Ref.15

VAR_013196

Natural variant

187

1

C → Y in ALGS1. Ref.27

VAR_026315

Natural variant

203

1

R → K in biliary atresia; extrahepatic. Ref.23

VAR_026316

Natural variant

220

1

C → F in ALGS1. Ref.20

VAR_013197

Natural variant

224

1

W → C in ALGS1. Ref.26

VAR_026317

Natural variant

229

1

C → G in ALGS1. Ref.15

VAR_013198

Natural variant

229

1

C → Y in ALGS1. Ref.17

VAR_013199

Natural variant

234

1

C → Y in deafness; with congenital heart defects and posterior embryotoxon. Ref.22

VAR_026318

Natural variant

252

1

R → G in ALGS1. Ref.28

VAR_026319

Natural variant

256

1

G → S in ALGS1. Ref.28

VAR_026320

Natural variant

269

1

P → L in ALGS1. Ref.26

VAR_026321

Natural variant

271

1

C → R in ALGS1. Ref.28

VAR_026322

Natural variant

274

1

G → 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 variant

284

1

C → F in ALGS1. Ref.15

VAR_013201

Natural variant

288

1

W → C in ALGS1. Ref.15

VAR_013202

Natural variant

386

1

G → R in ALGS1. Ref.17

VAR_013203

Natural variant

438

1

C → F in ALGS1. Ref.15

VAR_013204

Natural variant

504

1

N → S in ALGS1. Ref.28

VAR_026323

Natural variant

690

1

Y → D in biliary atresia; extrahepatic. Ref.23

VAR_026324

Natural variant

693

1

C → Y in ALGS1. Ref.28

VAR_026325

Natural variant

714

1

C → Y in ALGS1. Ref.21

VAR_026326

Natural variant

731

1

C → S in ALGS1. Ref.15

VAR_013205

Natural variant

740

1

C → R in ALGS1. Ref.15

VAR_013206

Natural variant

753

1

C → R in ALGS1. Ref.20

VAR_013207

Natural variant

818

1

R → K. Ref.28

VAR_026327

Natural variant

871

1

P → R in biliary atresia; extrahepatic. Ref.23
Corresponds to variant rs35761929 [ dbSNP | Ensembl ].

VAR_026328

Natural variant

889

1

R → Q in ALGS1. Ref.28

VAR_026329

Natural variant

902

1

C → S in ALGS1. Ref.21

VAR_026330

Natural variant

908

1

H → Q in biliary atresia; extrahepatic. Ref.23

VAR_026331

Natural variant

911

1

C → Y in ALGS1. Ref.28

VAR_026332

Natural variant

913

1

S → R in ALGS1. Ref.24

VAR_026333

Natural variant

921

1

L → P in biliary atresia; extrahepatic. Ref.23

VAR_026334

Natural variant

937

1

R → Q in ALGS1. Ref.26

VAR_026335

Natural variant

1055 – 1056

2

VR → G in ALGS1.

VAR_026336

Natural variant

1213

1

R → Q in biliary atresia; extrahepatic. Ref.23

VAR_026337

Experimental info

Mutagenesis

207

1

F → A: Strongly reduced NOTCH1 binding. Ref.12

Sequence conflict

117

1

R → P in AAB39007. Ref.5

Sequence conflict

227

1

P → R in AAC51731. Ref.1

Sequence conflict

498

1

N → D in AAC51731. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1218

Helix Strand Turn

Details...

Turn

193 – 196

4

Beta strand

203 – 205

3

Beta strand

208 – 212

5

Beta strand

218 – 220

3

Beta strand

224 – 226

3

Turn

240 – 242

3

Beta strand

257 – 262

6

Turn

268 – 270

3

Beta strand

272 – 275

4

Beta strand

277 – 280

4

Beta strand

286 – 289

4

Turn

290 – 293

4

Beta strand

295 – 297

3

Helix

299 – 302

4

Beta strand

311 – 314

4

Beta strand

320 – 323

4

Sequences

	Sequence		Length	Mass (Da)
	P78504 [UniParc]. Last modified May 2, 2002. Version 3. Checksum: F36EE9FBF64DF162	FASTA	1,218	133,799
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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.

IPI

IPI00099650.

RefSeq

NP_000205.1. NM_000214.2.

UniGene

Hs.224012.
Hs.626544.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KB9	NMR	-	A	252-295	[»]
2VJ2	X-ray	2.50	A/B	185-335	[»]

DisProt

DP00418.

ProteinModelPortal

P78504.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46371N.

IntAct

P78504. 3 interactions.

MINT

MINT-2804836.

STRING

9606.ENSP00000254958.

PTM databases

PhosphoSite

P78504.

Polymorphism databases

DMDM

20455033.

Proteomic databases

PaxDb

P78504.

PeptideAtlas

P78504.

PRIDE

P78504.

Protocols and materials databases

DNASU

182.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254958; ENSP00000254958; ENSG00000101384.

GeneID

182.

KEGG

hsa:182.

UCSC

uc002wnw.2. human.

Organism-specific databases

CTD

182.

GeneCards

GC20M010618.

HGNC

HGNC:6188. JAG1.

HPA

CAB010343.
HPA021555.

MIM

118450. phenotype.
187500. phenotype.
601920. gene+phenotype.

neXtProt

NX_P78504.

Orphanet

261600. Alagille syndrome due to 20p12 microdeletion.
261619. Alagille syndrome due to a JAG1 point mutation.
3303. Tetralogy of Fallot.

PharmGKB

PA29986.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000113124.

HOVERGEN

HBG031645.

InParanoid

P78504.

KO

K06052.

OMA

IHVAISA.

OrthoDB

EOG4H729Q.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.

SignaLink

P78504.

Gene expression databases

ArrayExpress

P78504.

Bgee

P78504.

CleanEx

HS_JAG1.

Genevestigator

P78504.

GermOnline

ENSG00000101384. Homo sapiens.

Family and domain databases

InterPro

IPR001774. DSL.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR026219. Jagged/Serrate.
IPR011651. Notch_ligand_N.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF01414. DSL. 1 hit.
PF00008. EGF. 10 hits.
PF07645. EGF_CA. 1 hit.
PF07657. MNNL. 1 hit.
[Graphical view]

PRINTS

PR02059. JAGGEDFAMILY.

SMART

SM00051. DSL. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 10 hits.
SM00214. VWC. 1 hit.
[Graphical view]

PROSITE

PS00010. 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]

ProtoNet

Search...

Other

ChiTaRS

JAG1. human.

EvolutionaryTrace

P78504.

GenomeRNAi

182.

NextBio

744.

SOURCE

Search...

Entry information

Entry name

JAG1_HUMAN

Accession

Primary (citable) accession number: P78504
Secondary accession number(s): A0AV43 , O14902, O15122, Q15816

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 2, 2002
Last modified:	May 29, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.