P78504 · JAG1_HUMAN
- ProteinProtein jagged-1
- GeneJAG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1218 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in cell-fate decisions during hematopoiesis (PubMed:9462510).
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)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein jagged-1
- Short namesJagged1; hJ1
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP78504
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 34-1067 | Extracellular | ||||
Sequence: QFELEILSMQNVNGELQNGNCCGGARNPGDRKCTRDECDTYFKVCLKEYQSRVTAGGPCSFGSGSTPVIGGNTFNLKASRGNDRNRIVLPFSFAWPRSYTLLVEAWDSSNDTVQPDSIIEKASHSGMINPSRQWQTLKQNTGVAHFEYQIRVTCDDYYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPECNRAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCDKCIPHPGCVHGICNEPWQCLCETNWGGQLCDKDLNYCGTHQPCLNGGTCSNTGPDKYQCSCPEGYSGPNCEIAEHACLSDPCHNRGSCKETSLGFECECSPGWTGPTCSTNIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQLDANECEAKPCVNAKSCKNLIASYYCDCLPGWMGQNCDININDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCERDIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQLDIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCSHLKDHCRTTPCEVIDSCTVAMASNDTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCHENINDCESNPCRNGGTCIDGVNSYKCICSDGWEGAYCETNINDCSQNPCHNGGTCRDLVNDFYCDCKNGWKGKTCHSRDSQCDEATCNNGGTCYDEGDAFKCMCPGGWEGTTCNIARNSSCLPNPCHNGGTCVVNGESFTCVCKEGWEGPICAQNTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCRININECQSSPCAFGATCVDEINGYRCVCPPGHSGAKCQEVSGRPCITMGSVIPDGAKWDDDCNTCQCLNGRIACSKVWCGPRPCLLHKGHSECPSGQSCIPILDDQCFVHPCTGVGECRSSSLQPVKTKCTSDSYYQDNCANITFTFNKEMMSPGLTTEHICSELRNLNILKNVSAEYSIYIACEPSPSANNEIHVAISAEDIRDDGNPIKEITDKIIDLVSKRDGNSSLIAAVAEVRVQRRPLKNRTD | ||||||
Transmembrane | 1068-1093 | Helical | ||||
Sequence: FLVPLLSSVLTVAWICCLVTAFYWCL | ||||||
Topological domain | 1094-1218 | Cytoplasmic | ||||
Sequence: RKRRKPGSHTHSASEDNTTNNVREQLNQIKNPIEKHGANTVPIKDYENKNSKMSKIRTHNSEVEEDDMDKHQQKARFAKQPAYTLVDREEKPPNGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Alagille syndrome 1 (ALGS1)
- Note
- DescriptionA 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.
- See alsoMIM:118450
Natural variants in ALGS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_026296 | 22-25 | missing | in ALGS1 | |
VAR_026297 | 31 | A>V | in ALGS1 | |
VAR_026298 | 33 | G>D | in ALGS1 | |
VAR_026299 | 33 | G>S | in ALGS1; dbSNP:rs876661123 | |
VAR_026300 | 33 | G>V | in ALGS1; dbSNP:rs2122644925 | |
VAR_013186 | 37 | L>S | in ALGS1; the mutant is unable to activate Notch signaling; dbSNP:rs121918352 | |
VAR_026301 | 39 | I>S | in ALGS1 | |
VAR_026302 | 40 | L>P | in ALGS1 | |
VAR_026306 | 75 | F>S | in ALGS1; dbSNP:rs2122644646 | |
VAR_026307 | 78 | C>S | in ALGS1; dbSNP:rs1555830957 | |
VAR_013187 | 79 | L>H | in ALGS1 | |
VAR_026308 | 92 | C>R | in ALGS1 | |
VAR_026309 | 92 | C>Y | in ALGS1 | |
VAR_026310 | 120 | I>N | in ALGS1 | |
VAR_026311 | 123 | P>S | in ALGS1; dbSNP:rs1282498658 | |
VAR_013188 | 127 | A>T | in ALGS1; dbSNP:rs930247415 | |
VAR_013189 | 129 | P>R | in ALGS1; dbSNP:rs1032920906 | |
VAR_013190 | 152 | I>T | in ALGS1 | |
VAR_026312 | 155 | A>P | in ALGS1 | |
VAR_013191 | 163 | P>L | in ALGS1 | |
VAR_026313 | 163 | P>R | in ALGS1; dbSNP:rs1555829676 | |
VAR_026314 | 181 | Y>N | in ALGS1 | |
VAR_013192 | 184 | R>C | in ALGS1; dbSNP:rs121918350 | |
VAR_013193 | 184 | R>G | in ALGS1 | |
VAR_013194 | 184 | R>H | in ALGS1; loss of expression at the cell membrane; dbSNP:rs121918351 | |
VAR_013195 | 184 | R>L | in ALGS1 | |
VAR_013196 | 187 | C>S | in ALGS1 | |
VAR_026315 | 187 | C>Y | in ALGS1 | |
VAR_013197 | 220 | C>F | in ALGS1 | |
VAR_026317 | 224 | W>C | in ALGS1 | |
VAR_013198 | 229 | C>G | in ALGS1 | |
VAR_013199 | 229 | C>Y | in ALGS1 | |
VAR_026319 | 252 | R>G | in ALGS1 | |
VAR_026320 | 256 | G>S | in ALGS1 | |
VAR_026321 | 269 | P>L | in ALGS1; dbSNP:rs797044956 | |
VAR_026322 | 271 | C>R | in ALGS1 | |
VAR_013201 | 284 | C>F | in ALGS1; dbSNP:rs1555829067 | |
VAR_013202 | 288 | W>C | in ALGS1 | |
VAR_013203 | 386 | G>R | in ALGS1; dbSNP:rs863223650 | |
VAR_071513 | 436 | C>W | in ALGS1 | |
VAR_013204 | 438 | C>F | in ALGS1 | |
VAR_026323 | 504 | N>S | in ALGS1; dbSNP:rs527236046 | |
VAR_026325 | 693 | C>Y | in ALGS1; dbSNP:rs566563238 | |
VAR_026326 | 714 | C>Y | in ALGS1; dbSNP:rs2067300040 | |
VAR_013205 | 731 | C>S | in ALGS1 | |
VAR_013206 | 740 | C>R | in ALGS1 | |
VAR_013207 | 753 | C>R | in ALGS1 | |
VAR_026329 | 889 | R>Q | in ALGS1; uncertain significance; dbSNP:rs149419694 | |
VAR_026330 | 902 | C>S | in ALGS1; dbSNP:rs876661122 | |
VAR_026332 | 911 | C>Y | in ALGS1; dbSNP:rs1555827782 | |
VAR_026333 | 913 | S>R | in ALGS1; dbSNP:rs766479402 | |
VAR_026335 | 937 | R>Q | in ALGS1; likely benign; the mutant is able to activate Notch signaling; dbSNP:rs145895196 | |
VAR_026336 | 1055-1056 | VR>G | in ALGS1 |
Tetralogy of Fallot (TOF)
- Note
- DescriptionA 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.
- See alsoMIM:187500
Natural variants in TOF
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_013200 | 274 | G>D | in TOF; temperature sensitive mutation; the protein is abnormally glycosylated and retained intracellularly; unable to activate Notch signaling; dbSNP:rs28939668 | |
VAR_080876 | 810 | P>L | in TOF; the mutant is unable to activate Notch signaling; dbSNP:rs769531968 |
Deafness, congenital heart defects, and posterior embryotoxon (DCHE)
- Note
- DescriptionAn autosomal dominant disease characterized by mild to severe combined hearing loss, congenital heart defects, and posterior embryotoxon, a corneal abnormality consisting of a central collagen core surrounded by a thin layer of Descemets membrane and separated from the anterior chamber by a layer of endothelium. Congenital heart defects include tetralogy of Fallot, ventricular septal defect, or isolated peripheral pulmonic stenosis.
- See alsoMIM:617992
Natural variants in DCHE
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_026318 | 234 | C>Y | in DCHE; the mutant is unable to activate Notch signaling; dbSNP:rs121918353 |
Charcot-Marie-Tooth disease, axonal, 2HH (CMT2HH)
- Note
- DescriptionAn autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2HH is characterized by vocal fold paresis that remains throughout life and may be severe. Additional features include pes cavus, scoliosis, distal sensory impairment with hyporeflexia, mild distal muscle weakness and atrophy primarily affecting the lower limbs, although the upper limbs may also be involved.
- See alsoMIM:619574
Natural variants in CMT2HH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086413 | 577 | S>R | in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum; dbSNP:rs2122606362 | |
VAR_086414 | 650 | S>P | in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum; dbSNP:rs2122604480 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_026296 | 22-25 | in ALGS1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_026297 | 31 | in ALGS1 | |||
Sequence: A → V | ||||||
Natural variant | VAR_026298 | 33 | in ALGS1 | |||
Sequence: G → D | ||||||
Natural variant | VAR_026299 | 33 | in ALGS1; dbSNP:rs876661123 | |||
Sequence: G → S | ||||||
Natural variant | VAR_026300 | 33 | in ALGS1; dbSNP:rs2122644925 | |||
Sequence: G → V | ||||||
Natural variant | VAR_013186 | 37 | in ALGS1; the mutant is unable to activate Notch signaling; dbSNP:rs121918352 | |||
Sequence: L → S | ||||||
Natural variant | VAR_026301 | 39 | in ALGS1 | |||
Sequence: I → S | ||||||
Natural variant | VAR_026302 | 40 | in ALGS1 | |||
Sequence: L → P | ||||||
Natural variant | VAR_026303 | 45 | in biliary atresia; extrahepatic; dbSNP:rs183974372 | |||
Sequence: V → L | ||||||
Natural variant | VAR_026304 | 53 | in biliary atresia; extrahepatic | |||
Sequence: N → D | ||||||
Natural variant | VAR_026305 | 65 | in biliary atresia; extrahepatic | |||
Sequence: K → M | ||||||
Natural variant | VAR_026306 | 75 | in ALGS1; dbSNP:rs2122644646 | |||
Sequence: F → S | ||||||
Natural variant | VAR_026307 | 78 | in ALGS1; dbSNP:rs1555830957 | |||
Sequence: C → S | ||||||
Natural variant | VAR_013187 | 79 | in ALGS1 | |||
Sequence: L → H | ||||||
Natural variant | VAR_026308 | 92 | in ALGS1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_026309 | 92 | in ALGS1 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026310 | 120 | in ALGS1 | |||
Sequence: I → N | ||||||
Natural variant | VAR_026311 | 123 | in ALGS1; dbSNP:rs1282498658 | |||
Sequence: P → S | ||||||
Natural variant | VAR_013188 | 127 | in ALGS1; dbSNP:rs930247415 | |||
Sequence: A → T | ||||||
Natural variant | VAR_013189 | 129 | in ALGS1; dbSNP:rs1032920906 | |||
Sequence: P → R | ||||||
Natural variant | VAR_048985 | 146 | in dbSNP:rs6040067 | |||
Sequence: V → I | ||||||
Natural variant | VAR_013190 | 152 | in ALGS1 | |||
Sequence: I → T | ||||||
Natural variant | VAR_026312 | 155 | in ALGS1 | |||
Sequence: A → P | ||||||
Natural variant | VAR_013191 | 163 | in ALGS1 | |||
Sequence: P → L | ||||||
Natural variant | VAR_026313 | 163 | in ALGS1; dbSNP:rs1555829676 | |||
Sequence: P → R | ||||||
Natural variant | VAR_026314 | 181 | in ALGS1 | |||
Sequence: Y → N | ||||||
Natural variant | VAR_013192 | 184 | in ALGS1; dbSNP:rs121918350 | |||
Sequence: R → C | ||||||
Natural variant | VAR_013193 | 184 | in ALGS1 | |||
Sequence: R → G | ||||||
Natural variant | VAR_013194 | 184 | in ALGS1; loss of expression at the cell membrane; dbSNP:rs121918351 | |||
Sequence: R → H | ||||||
Natural variant | VAR_013195 | 184 | in ALGS1 | |||
Sequence: R → L | ||||||
Natural variant | VAR_013196 | 187 | in ALGS1 | |||
Sequence: C → S | ||||||
Natural variant | VAR_026315 | 187 | in ALGS1 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026316 | 203 | in biliary atresia; extrahepatic | |||
Sequence: R → K | ||||||
Mutagenesis | 207 | Strongly reduced NOTCH1 binding. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_013197 | 220 | in ALGS1 | |||
Sequence: C → F | ||||||
Natural variant | VAR_026317 | 224 | in ALGS1 | |||
Sequence: W → C | ||||||
Natural variant | VAR_013198 | 229 | in ALGS1 | |||
Sequence: C → G | ||||||
Natural variant | VAR_013199 | 229 | in ALGS1 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026318 | 234 | in DCHE; the mutant is unable to activate Notch signaling; dbSNP:rs121918353 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026319 | 252 | in ALGS1 | |||
Sequence: R → G | ||||||
Natural variant | VAR_026320 | 256 | in ALGS1 | |||
Sequence: G → S | ||||||
Natural variant | VAR_026321 | 269 | in ALGS1; dbSNP:rs797044956 | |||
Sequence: P → L | ||||||
Natural variant | VAR_026322 | 271 | in ALGS1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_013200 | 274 | in TOF; temperature sensitive mutation; the protein is abnormally glycosylated and retained intracellularly; unable to activate Notch signaling; dbSNP:rs28939668 | |||
Sequence: G → D | ||||||
Natural variant | VAR_013201 | 284 | in ALGS1; dbSNP:rs1555829067 | |||
Sequence: C → F | ||||||
Natural variant | VAR_013202 | 288 | in ALGS1 | |||
Sequence: W → C | ||||||
Natural variant | VAR_013203 | 386 | in ALGS1; dbSNP:rs863223650 | |||
Sequence: G → R | ||||||
Natural variant | VAR_071513 | 436 | in ALGS1 | |||
Sequence: C → W | ||||||
Natural variant | VAR_013204 | 438 | in ALGS1 | |||
Sequence: C → F | ||||||
Natural variant | VAR_026323 | 504 | in ALGS1; dbSNP:rs527236046 | |||
Sequence: N → S | ||||||
Natural variant | VAR_086413 | 577 | in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum; dbSNP:rs2122606362 | |||
Sequence: S → R | ||||||
Natural variant | VAR_086414 | 650 | in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum; dbSNP:rs2122604480 | |||
Sequence: S → P | ||||||
Natural variant | VAR_080875 | 664 | found in a patient with pulmonary stenosis; uncertain significance; the mutant is able to activate Notch signaling | |||
Sequence: C → S | ||||||
Natural variant | VAR_026324 | 690 | in biliary atresia; extrahepatic | |||
Sequence: Y → D | ||||||
Natural variant | VAR_026325 | 693 | in ALGS1; dbSNP:rs566563238 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026326 | 714 | in ALGS1; dbSNP:rs2067300040 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_013205 | 731 | in ALGS1 | |||
Sequence: C → S | ||||||
Natural variant | VAR_013206 | 740 | in ALGS1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_013207 | 753 | in ALGS1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_080876 | 810 | in TOF; the mutant is unable to activate Notch signaling; dbSNP:rs769531968 | |||
Sequence: P → L | ||||||
Natural variant | VAR_026327 | 818 | ||||
Sequence: R → K | ||||||
Natural variant | VAR_026328 | 871 | in biliary atresia; extrahepatic; dbSNP:rs35761929 | |||
Sequence: P → R | ||||||
Natural variant | VAR_026329 | 889 | in ALGS1; uncertain significance; dbSNP:rs149419694 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026330 | 902 | in ALGS1; dbSNP:rs876661122 | |||
Sequence: C → S | ||||||
Natural variant | VAR_026331 | 908 | in biliary atresia; extrahepatic | |||
Sequence: H → Q | ||||||
Natural variant | VAR_026332 | 911 | in ALGS1; dbSNP:rs1555827782 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_026333 | 913 | in ALGS1; dbSNP:rs766479402 | |||
Sequence: S → R | ||||||
Natural variant | VAR_026334 | 921 | in biliary atresia; extrahepatic; dbSNP:rs1305578649 | |||
Sequence: L → P | ||||||
Natural variant | VAR_026335 | 937 | in ALGS1; likely benign; the mutant is able to activate Notch signaling; dbSNP:rs145895196 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026336 | 1055-1056 | in ALGS1 | |||
Sequence: VR → G | ||||||
Natural variant | VAR_080877 | 1104 | found in patient with tetralogy of Fallot and pulmonary stenosis; uncertain significance; dbSNP:rs1250645531 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_026337 | 1213 | in biliary atresia; extrahepatic; dbSNP:rs138007561 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,492 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-33 | UniProt | |||||
Sequence: MRSPRTRGRSGRPLSLLLALLCALRAKVCGASG | |||||||
Chain | PRO_0000007625 | 34-1218 | UniProt | Protein jagged-1 | |||
Sequence: QFELEILSMQNVNGELQNGNCCGGARNPGDRKCTRDECDTYFKVCLKEYQSRVTAGGPCSFGSGSTPVIGGNTFNLKASRGNDRNRIVLPFSFAWPRSYTLLVEAWDSSNDTVQPDSIIEKASHSGMINPSRQWQTLKQNTGVAHFEYQIRVTCDDYYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPECNRAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCDKCIPHPGCVHGICNEPWQCLCETNWGGQLCDKDLNYCGTHQPCLNGGTCSNTGPDKYQCSCPEGYSGPNCEIAEHACLSDPCHNRGSCKETSLGFECECSPGWTGPTCSTNIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQLDANECEAKPCVNAKSCKNLIASYYCDCLPGWMGQNCDININDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCERDIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQLDIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCSHLKDHCRTTPCEVIDSCTVAMASNDTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCHENINDCESNPCRNGGTCIDGVNSYKCICSDGWEGAYCETNINDCSQNPCHNGGTCRDLVNDFYCDCKNGWKGKTCHSRDSQCDEATCNNGGTCYDEGDAFKCMCPGGWEGTTCNIARNSSCLPNPCHNGGTCVVNGESFTCVCKEGWEGPICAQNTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCRININECQSSPCAFGATCVDEINGYRCVCPPGHSGAKCQEVSGRPCITMGSVIPDGAKWDDDCNTCQCLNGRIACSKVWCGPRPCLLHKGHSECPSGQSCIPILDDQCFVHPCTGVGECRSSSLQPVKTKCTSDSYYQDNCANITFTFNKEMMSPGLTTEHICSELRNLNILKNVSAEYSIYIACEPSPSANNEIHVAISAEDIRDDGNPIKEITDKIIDLVSKRDGNSSLIAAVAEVRVQRRPLKNRTDFLVPLLSSVLTVAWICCLVTAFYWCLRKRRKPGSHTHSASEDNTTNNVREQLNQIKNPIEKHGANTVPIKDYENKNSKMSKIRTHNSEVEEDDMDKHQQKARFAKQPAYTLVDREEKPPNGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV | |||||||
Glycosylation | 143 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 187↔196 | UniProt | |||||
Sequence: CDDYYYGFGC | |||||||
Disulfide bond | 200↔212 | UniProt | |||||
Sequence: CRPRDDFFGHYAC | |||||||
Glycosylation | 217 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 220↔229 | UniProt | |||||
Sequence: CMEGWMGPEC | |||||||
Disulfide bond | 234↔245 | UniProt | |||||
Sequence: CRQGCSPKHGSC | |||||||
Disulfide bond | 238↔251 | UniProt | |||||
Sequence: CSPKHGSCKLPGDC | |||||||
Disulfide bond | 253↔262 | UniProt | |||||
Sequence: CQYGWQGLYC | |||||||
Disulfide bond | 265↔276 | UniProt | |||||
Sequence: CIPHPGCVHGIC | |||||||
Disulfide bond | 271↔282 | UniProt | |||||
Sequence: CVHGICNEPWQC | |||||||
Disulfide bond | 284↔293 | UniProt | |||||
Sequence: CETNWGGQLC | |||||||
Disulfide bond | 300↔312 | UniProt | |||||
Sequence: CGTHQPCLNGGTC | |||||||
Disulfide bond | 306↔322 | UniProt | |||||
Sequence: CLNGGTCSNTGPDKYQC | |||||||
Disulfide bond | 324↔333 | UniProt | |||||
Sequence: CPEGYSGPNC | |||||||
Disulfide bond | 340↔351 | UniProt | |||||
Sequence: CLSDPCHNRGSC | |||||||
Disulfide bond | 345↔360 | UniProt | |||||
Sequence: CHNRGSCKETSLGFEC | |||||||
Disulfide bond | 362↔371 | UniProt | |||||
Sequence: CSPGWTGPTC | |||||||
Disulfide bond | 378↔389 | UniProt | |||||
Sequence: CSPNNCSHGGTC | |||||||
Glycosylation | 382 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 383↔398 | UniProt | |||||
Sequence: CSHGGTCQDLVNGFKC | |||||||
Disulfide bond | 400↔409 | UniProt | |||||
Sequence: CPPQWTGKTC | |||||||
Disulfide bond | 416↔427 | UniProt | |||||
Sequence: CEAKPCVNAKSC | |||||||
Disulfide bond | 421↔436 | UniProt | |||||
Sequence: CVNAKSCKNLIASYYC | |||||||
Disulfide bond | 438↔447 | UniProt | |||||
Sequence: CLPGWMGQNC | |||||||
Disulfide bond | 454↔464 | UniProt | |||||
Sequence: CLGQCQNDASC | |||||||
Disulfide bond | 458↔473 | UniProt | |||||
Sequence: CQNDASCRDLVNGYRC | |||||||
Disulfide bond | 475↔484 | UniProt | |||||
Sequence: CPPGYAGDHC | |||||||
Disulfide bond | 491↔502 | UniProt | |||||
Sequence: CASNPCLNGGHC | |||||||
Disulfide bond | 496↔511 | UniProt | |||||
Sequence: CLNGGHCQNEINRFQC | |||||||
Disulfide bond | 513↔522 | UniProt | |||||
Sequence: CPTGFSGNLC | |||||||
Disulfide bond | 529↔540 | UniProt | |||||
Sequence: CEPNPCQNGAQC | |||||||
Disulfide bond | 534↔549 | UniProt | |||||
Sequence: CQNGAQCYNRASDYFC | |||||||
Disulfide bond | 551↔560 | UniProt | |||||
Sequence: CPEDYEGKNC | |||||||
Glycosylation | 559 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 578↔605 | UniProt | |||||
Sequence: CTVAMASNDTPEGVRYISSNVCGPHGKC | |||||||
Disulfide bond | 599↔615 | UniProt | |||||
Sequence: CGPHGKCKSQSGGKFTC | |||||||
Disulfide bond | 617↔626 | UniProt | |||||
Sequence: CNKGFTGTYC | |||||||
Disulfide bond | 633↔644 | UniProt | |||||
Sequence: CESNPCRNGGTC | |||||||
Disulfide bond | 638↔653 | UniProt | |||||
Sequence: CRNGGTCIDGVNSYKC | |||||||
Disulfide bond | 655↔664 | UniProt | |||||
Sequence: CSDGWEGAYC | |||||||
Disulfide bond | 671↔682 | UniProt | |||||
Sequence: CSQNPCHNGGTC | |||||||
Disulfide bond | 676↔691 | UniProt | |||||
Sequence: CHNGGTCRDLVNDFYC | |||||||
Disulfide bond | 693↔702 | UniProt | |||||
Sequence: CKNGWKGKTC | |||||||
Disulfide bond | 709↔720 | UniProt | |||||
Sequence: CDEATCNNGGTC | |||||||
Disulfide bond | 714↔729 | UniProt | |||||
Sequence: CNNGGTCYDEGDAFKC | |||||||
Disulfide bond | 731↔740 | UniProt | |||||
Sequence: CPGGWEGTTC | |||||||
Glycosylation | 745 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 748↔759 | UniProt | |||||
Sequence: CLPNPCHNGGTC | |||||||
Disulfide bond | 753↔768 | UniProt | |||||
Sequence: CHNGGTCVVNGESFTC | |||||||
Disulfide bond | 770↔779 | UniProt | |||||
Sequence: CKEGWEGPIC | |||||||
Disulfide bond | 786↔797 | UniProt | |||||
Sequence: CSPHPCYNSGTC | |||||||
Disulfide bond | 791↔806 | UniProt | |||||
Sequence: CYNSGTCVDGDNWYRC | |||||||
Disulfide bond | 808↔817 | UniProt | |||||
Sequence: CAPGFAGPDC | |||||||
Disulfide bond | 824↔835 | UniProt | |||||
Sequence: CQSSPCAFGATC | |||||||
Disulfide bond | 829↔844 | UniProt | |||||
Sequence: CAFGATCVDEINGYRC | |||||||
Disulfide bond | 846↔855 | UniProt | |||||
Sequence: CPPGHSGAKC | |||||||
Glycosylation | 960 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 991 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1045 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1064 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 1101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1176 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1189 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1210 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with NOTCH1 (in the presence of calcium ions) (PubMed:18660822).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P78504 | CD46 P15529 | 5 | EBI-2847071, EBI-2623451 | |
BINARY | P78504 | NOTCH1 P46531 | 6 | EBI-2847071, EBI-636374 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 185-229 | DSL | ||||
Sequence: VTCDDYYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPEC | ||||||
Region | 199-207 | Important for interaction with NOTCH1 | ||||
Sequence: FCRPRDDFF | ||||||
Domain | 230-263 | EGF-like 1 | ||||
Sequence: NRAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCD | ||||||
Domain | 264-294 | EGF-like 2; atypical | ||||
Sequence: KCIPHPGCVHGICNEPWQCLCETNWGGQLCD | ||||||
Domain | 296-334 | EGF-like 3 | ||||
Sequence: DLNYCGTHQPCLNGGTCSNTGPDKYQCSCPEGYSGPNCE | ||||||
Domain | 336-372 | EGF-like 4 | ||||
Sequence: AEHACLSDPCHNRGSCKETSLGFECECSPGWTGPTCS | ||||||
Domain | 374-410 | EGF-like 5; calcium-binding | ||||
Sequence: NIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQ | ||||||
Domain | 412-448 | EGF-like 6; calcium-binding | ||||
Sequence: DANECEAKPCVNAKSCKNLIASYYCDCLPGWMGQNCD | ||||||
Domain | 450-485 | EGF-like 7; calcium-binding | ||||
Sequence: NINDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCE | ||||||
Domain | 487-523 | EGF-like 8; calcium-binding | ||||
Sequence: DIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQ | ||||||
Domain | 525-561 | EGF-like 9 | ||||
Sequence: DIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCS | ||||||
Domain | 586-627 | EGF-like 10 | ||||
Sequence: DTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCH | ||||||
Domain | 629-665 | EGF-like 11; calcium-binding | ||||
Sequence: NINDCESNPCRNGGTCIDGVNSYKCICSDGWEGAYCE | ||||||
Domain | 667-703 | EGF-like 12; calcium-binding | ||||
Sequence: NINDCSQNPCHNGGTCRDLVNDFYCDCKNGWKGKTCH | ||||||
Domain | 705-741 | EGF-like 13 | ||||
Sequence: RDSQCDEATCNNGGTCYDEGDAFKCMCPGGWEGTTCN | ||||||
Domain | 744-780 | EGF-like 14 | ||||
Sequence: RNSSCLPNPCHNGGTCVVNGESFTCVCKEGWEGPICA | ||||||
Domain | 782-818 | EGF-like 15; calcium-binding | ||||
Sequence: NTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCR | ||||||
Domain | 820-856 | EGF-like 16; calcium-binding | ||||
Sequence: NINECQSSPCAFGATCVDEINGYRCVCPPGHSGAKCQ | ||||||
Compositional bias | 1152-1169 | Basic and acidic residues | ||||
Sequence: HNSEVEEDDMDKHQQKAR | ||||||
Region | 1152-1218 | Disordered | ||||
Sequence: HNSEVEEDDMDKHQQKARFAKQPAYTLVDREEKPPNGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV | ||||||
Compositional bias | 1190-1209 | Polar residues | ||||
Sequence: PTKHPNWTNKQDNRDLESAQ |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P78504-1
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.
- Name1
- Length1,218
- Mass (Da)133,799
- Last updated2002-05-02 v3
- ChecksumF36EE9FBF64DF162
P78504-2
- Name2
- Differences from canonical
- 1-159: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087X1E8 | A0A087X1E8_HUMAN | JAG1 | 74 | ||
A0A087WXH5 | A0A087WXH5_HUMAN | JAG1 | 172 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056532 | 1-159 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 117 | in Ref. 5; AAB39007 | ||||
Sequence: R → P | ||||||
Sequence conflict | 227 | in Ref. 1; AAC51731 | ||||
Sequence: P → R | ||||||
Sequence conflict | 498 | in Ref. 1; AAC51731 | ||||
Sequence: N → D | ||||||
Compositional bias | 1152-1169 | Basic and acidic residues | ||||
Sequence: HNSEVEEDDMDKHQQKAR | ||||||
Compositional bias | 1190-1209 | Polar residues | ||||
Sequence: PTKHPNWTNKQDNRDLESAQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF003837 EMBL· GenBank· DDBJ | AAC51731.1 EMBL· GenBank· DDBJ | mRNA | ||
U73936 EMBL· GenBank· DDBJ | AAC52020.1 EMBL· GenBank· DDBJ | mRNA | ||
AF028593 EMBL· GenBank· DDBJ | AAB84053.1 EMBL· GenBank· DDBJ | mRNA | ||
U61276 EMBL· GenBank· DDBJ | AAB39007.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302554 EMBL· GenBank· DDBJ | BAG63823.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035456 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC126205 EMBL· GenBank· DDBJ | AAI26206.1 EMBL· GenBank· DDBJ | mRNA | ||
BC126207 EMBL· GenBank· DDBJ | AAI26208.1 EMBL· GenBank· DDBJ | mRNA | ||
U77720 EMBL· GenBank· DDBJ | AAC51323.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |