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Q04721

- NOTC2_HUMAN

UniProt

Q04721 - NOTC2_HUMAN

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Protein
Neurogenic locus notch homolog protein 2
Gene
NOTCH2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs By similarity. Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei614 – 6141Essential for O-xylosylation By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. ligand-activated RNA polymerase II transcription factor binding transcription factor activity Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. receptor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Notch receptor processing Source: Reactome
  2. Notch signaling involved in heart development Source: BHF-UCL
  3. Notch signaling pathway Source: Reactome
  4. apoptotic process Source: UniProtKB
  5. atrial septum morphogenesis Source: BHF-UCL
  6. bone remodeling Source: UniProtKB
  7. cell cycle arrest Source: UniProtKB
  8. cell fate determination Source: UniProtKB
  9. cell growth Source: UniProtKB
  10. determination of left/right symmetry Source: Ensembl
  11. embryonic limb morphogenesis Source: Ensembl
  12. gene expression Source: Reactome
  13. hemopoiesis Source: UniProtKB
  14. humoral immune response Source: Ensembl
  15. in utero embryonic development Source: Ensembl
  16. inflammatory response to antigenic stimulus Source: Ensembl
  17. interleukin-4 secretion Source: Ensembl
  18. intracellular receptor signaling pathway Source: GOC
  19. morphogenesis of an epithelial sheet Source: Ensembl
  20. multicellular organismal development Source: UniProtKB
  21. negative regulation of apoptotic process Source: UniProtKB
  22. negative regulation of cell proliferation Source: UniProtKB
  23. nervous system development Source: UniProtKB
  24. organ morphogenesis Source: UniProtKB
  25. placenta blood vessel development Source: Ensembl
  26. positive regulation of Ras protein signal transduction Source: UniProtKB
  27. positive regulation of apoptotic process Source: Ensembl
  28. pulmonary valve morphogenesis Source: BHF-UCL
  29. regulation of transcription, DNA-templated Source: UniProtKB
  30. stem cell maintenance Source: UniProtKB
  31. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_14835. Notch-HLH transcription pathway.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinkiQ04721.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 2
Short name:
Notch 2
Short name:
hN2
Cleaved into the following 2 chains:
Gene namesi
Name:NOTCH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7882. NOTCH2.

Subcellular locationi

Chain Notch 2 intracellular domain : Nucleus
Note: Following proteolytical processing NICD is translocated to the nucleus.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 16771652Extracellular Reviewed prediction
Add
BLAST
Transmembranei1678 – 169821Helical; Reviewed prediction
Add
BLAST
Topological domaini1699 – 2471773Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. cell surface Source: UniProtKB
  3. endoplasmic reticulum membrane Source: Reactome
  4. extracellular region Source: Reactome
  5. integral component of plasma membrane Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: Reactome
  9. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Alagille syndrome 2 (ALGS2) [MIM:610205]: 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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti444 – 4441C → Y in ALGS2. 1 Publication
VAR_029361
Hajdu-Cheney syndrome (HJCYS) [MIM:102500]: A rare skeletal disorder characterized by the association of facial anomalies, acro-osteolysis, general osteoporosis, insufficient ossification of the skull, and periodontal disease (premature loss of permanent teeth). Other features include cleft palate, congenital heart defects, polycystic kidneys, orthopedic problems and anomalies of the genitalia, intestines and eyes.
Note: The disease is caused by mutations affecting the gene represented in this entry. NOTCH2 mutations associated with Hajdu-Cheney syndrome cluster to the last coding exon of the gene. This suggests that the mutant mRNA products may escape nonsense-mediated decay and the resulting truncated NOTCH2 proteins act in a gain-of-function manner.2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi102500. phenotype.
610205. phenotype.
Orphaneti955. Acroosteolysis dominant type.
261629. Alagille syndrome due to a NOTCH2 point mutation.
PharmGKBiPA31684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 24712446Neurogenic locus notch homolog protein 2
PRO_0000007683Add
BLAST
Chaini1666 – 2471806Notch 2 extracellular truncation By similarity
PRO_0000007684Add
BLAST
Chaini1697 – 2471775Notch 2 intracellular domain By similarity
PRO_0000007685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 41 By similarity
Disulfide bondi35 ↔ 51 By similarity
Glycosylationi46 – 461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi53 ↔ 62 By similarity
Disulfide bondi68 ↔ 79 By similarity
Disulfide bondi73 ↔ 90 By similarity
Disulfide bondi92 ↔ 101 By similarity
Disulfide bondi109 ↔ 121 By similarity
Disulfide bondi115 ↔ 131 By similarity
Disulfide bondi133 ↔ 142 By similarity
Disulfide bondi148 ↔ 159 By similarity
Disulfide bondi153 ↔ 168 By similarity
Glycosylationi155 – 1551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi170 ↔ 179 By similarity
Disulfide bondi186 ↔ 198 By similarity
Disulfide bondi192 ↔ 207 By similarity
Disulfide bondi209 ↔ 218 By similarity
Disulfide bondi225 ↔ 236 By similarity
Disulfide bondi230 ↔ 246 By similarity
Disulfide bondi248 ↔ 257 By similarity
Disulfide bondi264 ↔ 275 By similarity
Disulfide bondi269 ↔ 284 By similarity
Disulfide bondi286 ↔ 295 By similarity
Disulfide bondi302 ↔ 315 By similarity
Disulfide bondi309 ↔ 324 By similarity
Disulfide bondi326 ↔ 335 By similarity
Disulfide bondi342 ↔ 353 By similarity
Disulfide bondi347 ↔ 362 By similarity
Disulfide bondi364 ↔ 373 By similarity
Disulfide bondi379 ↔ 390 By similarity
Disulfide bondi384 ↔ 401 By similarity
Disulfide bondi403 ↔ 412 By similarity
Disulfide bondi419 ↔ 433 By similarity
Disulfide bondi427 ↔ 442 By similarity
Disulfide bondi444 ↔ 453 By similarity
Disulfide bondi460 ↔ 471 By similarity
Disulfide bondi465 ↔ 480 By similarity
Disulfide bondi482 ↔ 491 By similarity
Disulfide bondi498 ↔ 509 By similarity
Disulfide bondi503 ↔ 518 By similarity
Disulfide bondi520 ↔ 529 By similarity
Disulfide bondi536 ↔ 547 By similarity
Disulfide bondi541 ↔ 556 By similarity
Disulfide bondi558 ↔ 567 By similarity
Disulfide bondi574 ↔ 584 By similarity
Disulfide bondi579 ↔ 593 By similarity
Disulfide bondi595 ↔ 604 By similarity
Disulfide bondi611 ↔ 622 By similarity
Glycosylationi613 – 6131O-linked (Glc...); alternate By similarity
Glycosylationi613 – 6131O-linked (Xyl...); alternate By similarity
Disulfide bondi616 ↔ 631 By similarity
Disulfide bondi633 ↔ 642 By similarity
Disulfide bondi649 ↔ 659 By similarity
Disulfide bondi654 ↔ 668 By similarity
Disulfide bondi670 ↔ 679 By similarity
Disulfide bondi686 ↔ 697 By similarity
Disulfide bondi691 ↔ 706 By similarity
Disulfide bondi708 ↔ 717 By similarity
Disulfide bondi724 ↔ 734 By similarity
Disulfide bondi729 ↔ 743 By similarity
Glycosylationi733 – 7331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi745 ↔ 754 By similarity
Disulfide bondi761 ↔ 772 By similarity
Disulfide bondi766 ↔ 781 By similarity
Disulfide bondi783 ↔ 792 By similarity
Disulfide bondi799 ↔ 810 By similarity
Disulfide bondi804 ↔ 819 By similarity
Disulfide bondi821 ↔ 830 By similarity
Disulfide bondi837 ↔ 848 By similarity
Disulfide bondi842 ↔ 859 By similarity
Disulfide bondi861 ↔ 870 By similarity
Disulfide bondi877 ↔ 888 By similarity
Disulfide bondi882 ↔ 897 By similarity
Disulfide bondi899 ↔ 908 By similarity
Disulfide bondi915 ↔ 926 By similarity
Disulfide bondi920 ↔ 935 By similarity
Disulfide bondi937 ↔ 946 By similarity
Disulfide bondi953 ↔ 964 By similarity
Disulfide bondi958 ↔ 973 By similarity
Disulfide bondi975 ↔ 984 By similarity
Disulfide bondi991 ↔ 1002 By similarity
Disulfide bondi996 ↔ 1011 By similarity
Disulfide bondi1013 ↔ 1022 By similarity
Disulfide bondi1029 ↔ 1040 By similarity
Disulfide bondi1034 ↔ 1049 By similarity
Disulfide bondi1051 ↔ 1060 By similarity
Disulfide bondi1067 ↔ 1078 By similarity
Disulfide bondi1072 ↔ 1087 By similarity
Disulfide bondi1089 ↔ 1098 By similarity
Glycosylationi1102 – 11021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1105 ↔ 1126 By similarity
Disulfide bondi1120 ↔ 1135 By similarity
Disulfide bondi1137 ↔ 1146 By similarity
Disulfide bondi1153 ↔ 1164 By similarity
Disulfide bondi1158 ↔ 1173 By similarity
Disulfide bondi1175 ↔ 1184 By similarity
Disulfide bondi1191 ↔ 1202 By similarity
Disulfide bondi1196 ↔ 1211 By similarity
Disulfide bondi1213 ↔ 1222 By similarity
Disulfide bondi1229 ↔ 1241 By similarity
Disulfide bondi1235 ↔ 1250 By similarity
Disulfide bondi1252 ↔ 1261 By similarity
Disulfide bondi1268 ↔ 1281 By similarity
Disulfide bondi1273 ↔ 1290 By similarity
Disulfide bondi1292 ↔ 1301 By similarity
Disulfide bondi1308 ↔ 1319 By similarity
Disulfide bondi1313 ↔ 1331 By similarity
Disulfide bondi1333 ↔ 1342 By similarity
Disulfide bondi1378 ↔ 1389 By similarity
Disulfide bondi1383 ↔ 1400 By similarity
Disulfide bondi1402 ↔ 1411 By similarity
Disulfide bondi1425 ↔ 14481 Publication
Disulfide bondi1430 ↔ 14431 Publication
Disulfide bondi1439 ↔ 14551 Publication
Glycosylationi1465 – 14651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1466 ↔ 14891 Publication
Disulfide bondi1472 ↔ 14841 Publication
Disulfide bondi1480 ↔ 14961 Publication
Disulfide bondi1503 ↔ 15271 Publication
Disulfide bondi1509 ↔ 15221 Publication
Disulfide bondi1518 ↔ 15341 Publication
Disulfide bondi1632 ↔ 16391 Publication
Modified residuei1716 – 17161Phosphothreonine1 Publication
Modified residuei1778 – 17781Phosphoserine2 Publications
Modified residuei1802 – 18021Phosphothreonine1 Publication
Modified residuei1804 – 18041Phosphoserine1 Publication
Modified residuei1808 – 18081Phosphothreonine1 Publication
Modified residuei1842 – 18421Phosphoserine By similarity
Modified residuei1845 – 18451Phosphoserine2 Publications
Modified residuei2070 – 20701Phosphoserine1 Publication
Modified residuei2078 – 20781Phosphoserine By similarity
Modified residuei2081 – 20811Phosphoserine1 Publication
Modified residuei2097 – 20971Phosphothreonine1 Publication

Post-translational modificationi

Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane By similarity.1 Publication
Hydroxylated by HIF1AN.
Can be either O-glucosylated or O-xylosylated at Ser-613 by POGLUT1 By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ04721.
PaxDbiQ04721.
PRIDEiQ04721.

PTM databases

PhosphoSiteiQ04721.

Expressioni

Tissue specificityi

Expressed in the brain, heart, kidney, lung, skeletal muscle and liver. Ubiquitously expressed in the embryo.1 Publication

Gene expression databases

ArrayExpressiQ04721.
BgeeiQ04721.
CleanExiHS_NOTCH2.
GenevestigatoriQ04721.

Organism-specific databases

HPAiHPA046392.

Interactioni

Subunit structurei

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds By similarity. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65 By similarity. Interacts with HIF1AN.3 Publications

Protein-protein interaction databases

BioGridi110915. 25 interactions.
IntActiQ04721. 5 interactions.
MINTiMINT-1187009.
STRINGi9606.ENSP00000256646.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1428 – 14336
Beta strandi1436 – 14383
Helixi1441 – 14433
Turni1446 – 14483
Helixi1449 – 14524
Turni1453 – 14586
Turni1462 – 14654
Helixi1472 – 14743
Beta strandi1477 – 14793
Helixi1482 – 14843
Turni1487 – 14904
Helixi1491 – 14944
Helixi1506 – 15127
Beta strandi1515 – 15173
Helixi1520 – 15223
Helixi1525 – 15328
Beta strandi1544 – 155310
Helixi1555 – 15606
Helixi1562 – 157312
Beta strandi1575 – 15795
Beta strandi1589 – 15946
Beta strandi1617 – 162812
Helixi1632 – 16354
Helixi1643 – 165614
Beta strandi1663 – 16708

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OO4X-ray2.00A/B1423-1677[»]
ProteinModelPortaliQ04721.
SMRiQ04721. Positions 34-1376, 1425-1672, 1777-2063.

Miscellaneous databases

EvolutionaryTraceiQ04721.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6338EGF-like 1
Add
BLAST
Domaini64 – 10239EGF-like 2
Add
BLAST
Domaini105 – 14339EGF-like 3
Add
BLAST
Domaini144 – 18037EGF-like 4
Add
BLAST
Domaini182 – 21938EGF-like 5; calcium-binding Reviewed prediction
Add
BLAST
Domaini221 – 25838EGF-like 6
Add
BLAST
Domaini260 – 29637EGF-like 7; calcium-binding Reviewed prediction
Add
BLAST
Domaini298 – 33639EGF-like 8; calcium-binding Reviewed prediction
Add
BLAST
Domaini338 – 37437EGF-like 9; calcium-binding Reviewed prediction
Add
BLAST
Domaini375 – 41339EGF-like 10
Add
BLAST
Domaini415 – 45440EGF-like 11; calcium-binding Reviewed prediction
Add
BLAST
Domaini456 – 49237EGF-like 12; calcium-binding Reviewed prediction
Add
BLAST
Domaini494 – 53037EGF-like 13; calcium-binding Reviewed prediction
Add
BLAST
Domaini532 – 56837EGF-like 14; calcium-binding Reviewed prediction
Add
BLAST
Domaini570 – 60536EGF-like 15; calcium-binding Reviewed prediction
Add
BLAST
Domaini607 – 64337EGF-like 16; calcium-binding Reviewed prediction
Add
BLAST
Domaini645 – 68036EGF-like 17; calcium-binding Reviewed prediction
Add
BLAST
Domaini682 – 71837EGF-like 18; calcium-binding Reviewed prediction
Add
BLAST
Domaini720 – 75536EGF-like 19
Add
BLAST
Domaini757 – 79337EGF-like 20; calcium-binding Reviewed prediction
Add
BLAST
Domaini795 – 83137EGF-like 21; calcium-binding Reviewed prediction
Add
BLAST
Domaini833 – 87139EGF-like 22
Add
BLAST
Domaini873 – 90937EGF-like 23; calcium-binding Reviewed prediction
Add
BLAST
Domaini911 – 94737EGF-like 24; calcium-binding Reviewed prediction
Add
BLAST
Domaini949 – 98537EGF-like 25; calcium-binding Reviewed prediction
Add
BLAST
Domaini987 – 102337EGF-like 26; calcium-binding Reviewed prediction
Add
BLAST
Domaini1025 – 106137EGF-like 27; calcium-binding Reviewed prediction
Add
BLAST
Domaini1063 – 109937EGF-like 28
Add
BLAST
Domaini1101 – 114747EGF-like 29
Add
BLAST
Domaini1149 – 118537EGF-like 30; calcium-binding Reviewed prediction
Add
BLAST
Domaini1187 – 122337EGF-like 31; calcium-binding Reviewed prediction
Add
BLAST
Domaini1225 – 126238EGF-like 32; calcium-binding Reviewed prediction
Add
BLAST
Domaini1264 – 130239EGF-like 33
Add
BLAST
Domaini1304 – 134340EGF-like 34
Add
BLAST
Domaini1374 – 141239EGF-like 35
Add
BLAST
Repeati1425 – 146541LNR 1
Add
BLAST
Repeati1466 – 150237LNR 2
Add
BLAST
Repeati1503 – 154442LNR 3
Add
BLAST
Repeati1827 – 187145ANK 1
Add
BLAST
Repeati1876 – 190530ANK 2
Add
BLAST
Repeati1909 – 193931ANK 3
Add
BLAST
Repeati1943 – 197230ANK 4
Add
BLAST
Repeati1976 – 200530ANK 5
Add
BLAST
Repeati2009 – 203830ANK 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1425 – 1677253Negative regulatory region (NRR)
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1645 – 16484Poly-Ala
Compositional biasi1994 – 19974Poly-Leu
Compositional biasi2426 – 24294Poly-Ser

Sequence similaritiesi

Belongs to the NOTCH family.
Contains 6 ANK repeats.
Contains 35 EGF-like domains.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ04721.
KOiK02599.
OMAiMEDPWAN.
OrthoDBiEOG7992RD.
PhylomeDBiQ04721.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
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.
IPR008297. Notch.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 29 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04721-1 [UniParc]FASTAAdd to Basket

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MPALRPALLW ALLALWLCCA APAHALQCRD GYEPCVNEGM CVTYHNGTGY     50
CKCPEGFLGE YCQHRDPCEK NRCQNGGTCV AQAMLGKATC RCASGFTGED 100
CQYSTSHPCF VSRPCLNGGT CHMLSRDTYE CTCQVGFTGK ECQWTDACLS 150
HPCANGSTCT TVANQFSCKC LTGFTGQKCE TDVNECDIPG HCQHGGTCLN 200
LPGSYQCQCP QGFTGQYCDS LYVPCAPSPC VNGGTCRQTG DFTFECNCLP 250
GFEGSTCERN IDDCPNHRCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD 300
ECLLQPNACQ NGGTCANRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG 350
STCIDRVASF SCMCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI 400
CTCPQGYKGA DCTEDVDECA MANSNPCEHA GKCVNTDGAF HCECLKGYAG 450
PRCEMDINEC HSDPCQNDAT CLDKIGGFTC LCMPGFKGVH CELEINECQS 500
NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP CLNGAKCIDH 550
PNGYECQCAT GFTGVLCEEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM 600
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGV NCEINFDDCA 650
SNPCIHGICM DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCING 700
VNGFRCICPE GPHHPSCYSQ VNECLSNPCI HGNCTGGLSG YKCLCDAGWV 750
GINCEVDKNE CLSNPCQNGG TCDNLVNGYR CTCKKGFKGY NCQVNIDECA 800
SNPCLNQGTC FDDISGYTCH CVLPYTGKNC QTVLAPCSPN PCENAAVCKE 850
SPNFESYTCL CAPGWQGQRC TIDIDECISK PCMNHGLCHN TQGSYMCECP 900
PGFSGMDCEE DIDDCLANPC QNGGSCMDGV NTFSCLCLPG FTGDKCQTDM 950
NECLSEPCKN GGTCSDYVNS YTCKCQAGFD GVHCENNINE CTESSCFNGG 1000
TCVDGINSFS CLCPVGFTGS FCLHEINECS SHPCLNEGTC VDGLGTYRCS 1050
CPLGYTGKNC QTLVNLCSRS PCKNKGTCVQ KKAESQCLCP SGWAGAYCDV 1100
PNVSCDIAAS RRGVLVEHLC QHSGVCINAG NTHYCQCPLG YTGSYCEEQL 1150
DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG 1200
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA RGPHCLNGGQ CMDRIGGYSC 1250
RCLPGFAGER CEGDINECLS NPCSSEGSLD CIQLTNDYLC VCRSAFTGRH 1300
CETFVDVCPQ MPCLNGGTCA VASNMPDGFI CRCPPGFSGA RCQSSCGQVK 1350
CRKGEQCVHT ASGPRCFCPS PRDCESGCAS SPCQHGGSCH PQRQPPYYSC 1400
QCAPPFSGSR CELYTAPPST PPATCLSQYC ADKARDGVCD EACNSHACQW 1450
DGGDCSLTME NPWANCSSPL PCWDYINNQC DELCNTVECL FDNFECQGNS 1500
KTCKYDKYCA DHFKDNHCDQ GCNSEECGWD GLDCAADQPE NLAEGTLVIV 1550
VLMPPEQLLQ DARSFLRALG TLLHTNLRIK RDSQGELMVY PYYGEKSAAM 1600
KKQRMTRRSL PGEQEQEVAG SKVFLEIDNR QCVQDSDHCF KNTDAAAALL 1650
ASHAIQGTLS YPLVSVVSES LTPERTQLLY LLAVAVVIIL FIILLGVIMA 1700
KRKRKHGSLW LPEGFTLRRD ASNHKRREPV GQDAVGLKNL SVQVSEANLI 1750
GTGTSEHWVD DEGPQPKKVK AEDEALLSEE DDPIDRRPWT QQHLEAADIR 1800
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED 1850
AEDSSANIIT DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG 1900
ADANAQDNMG RCPLHAAVAA DAQGVFQILI RNRVTDLDAR MNDGTTPLIL 1950
AARLAVEGMV AELINCQADV NAVDDHGKSA LHWAAAVNNV EATLLLLKNG 2000
ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD HMDRLPRDVA 2050
RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVICGPNRS FLSLKHTPMG 2100
KKSRRPSAKS TMPTSLPNLA KEAKDAKGSR RKKSLSEKVQ LSESSVTLSP 2150
VDSLESPHTY VSDTTSSPMI TSPGILQASP NPMLATAAPP APVHAQHALS 2200
FSNLHEMQPL AHGASTVLPS VSQLLSHHHI VSPGSGSAGS LSRLHPVPVP 2250
ADWMNRMEVN ETQYNEMFGM VLAPAEGTHP GIAPQSRPPE GKHITTPREP 2300
LPPIVTFQLI PKGSIAQPAG APQPQSTCPP AVAGPLPTMY QIPEMARLPS 2350
VAFPTAMMPQ QDGQVAQTIL PAYHPFPASV GKYPTPPSQH SYASSNAAER 2400
TPSHSGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGAGG 2450
GQRGPGTHMS EPPHNNMQVY A 2471
Length:2,471
Mass (Da):265,405
Last modified:April 3, 2007 - v3
Checksum:i605B1B963C812BE1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti444 – 4441C → Y in ALGS2. 1 Publication
VAR_029361
Natural varianti1667 – 16671V → F.
Corresponds to variant rs17024517 [ dbSNP | Ensembl ].
VAR_031463

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → T in AAG37073. 1 Publication
Sequence conflicti210 – 2101P → L in AAG37073. 1 Publication
Sequence conflicti1037 – 10371E → D in AAB19224. 1 Publication
Sequence conflicti1084 – 10852ES → SP in AAB19224. 1 Publication
Sequence conflicti1094 – 10941A → V in AAB19224. 1 Publication
Sequence conflicti1139 – 11391L → V in AAB19224. 1 Publication
Sequence conflicti1519 – 15191D → N in AAA36377. 1 Publication
Sequence conflicti2053 – 20531R → H in AAG37073. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF308601 mRNA. Translation: AAA36377.2.
AF315356 mRNA. Translation: AAG37073.1.
AL359752, AL512503, AL596222 Genomic DNA. Translation: CAI18974.1.
AL512503, AL359752, AL596222 Genomic DNA. Translation: CAH72483.1.
AL596222, AL359752, AL512503 Genomic DNA. Translation: CAH70182.1.
U77493 mRNA. Translation: AAB19224.1.
CCDSiCCDS908.1.
RefSeqiNP_001186930.1. NM_001200001.1.
NP_077719.2. NM_024408.3.
UniGeneiHs.487360.

Genome annotation databases

EnsembliENST00000256646; ENSP00000256646; ENSG00000134250.
GeneIDi4853.
KEGGihsa:4853.
UCSCiuc001eik.3. human.

Polymorphism databases

DMDMi143811429.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF308601 mRNA. Translation: AAA36377.2 .
AF315356 mRNA. Translation: AAG37073.1 .
AL359752 , AL512503 , AL596222 Genomic DNA. Translation: CAI18974.1 .
AL512503 , AL359752 , AL596222 Genomic DNA. Translation: CAH72483.1 .
AL596222 , AL359752 , AL512503 Genomic DNA. Translation: CAH70182.1 .
U77493 mRNA. Translation: AAB19224.1 .
CCDSi CCDS908.1.
RefSeqi NP_001186930.1. NM_001200001.1.
NP_077719.2. NM_024408.3.
UniGenei Hs.487360.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OO4 X-ray 2.00 A/B 1423-1677 [» ]
ProteinModelPortali Q04721.
SMRi Q04721. Positions 34-1376, 1425-1672, 1777-2063.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110915. 25 interactions.
IntActi Q04721. 5 interactions.
MINTi MINT-1187009.
STRINGi 9606.ENSP00000256646.

PTM databases

PhosphoSitei Q04721.

Polymorphism databases

DMDMi 143811429.

Proteomic databases

MaxQBi Q04721.
PaxDbi Q04721.
PRIDEi Q04721.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256646 ; ENSP00000256646 ; ENSG00000134250 .
GeneIDi 4853.
KEGGi hsa:4853.
UCSCi uc001eik.3. human.

Organism-specific databases

CTDi 4853.
GeneCardsi GC01M120454.
GeneReviewsi NOTCH2.
HGNCi HGNC:7882. NOTCH2.
HPAi HPA046392.
MIMi 102500. phenotype.
600275. gene.
610205. phenotype.
neXtProti NX_Q04721.
Orphaneti 955. Acroosteolysis dominant type.
261629. Alagille syndrome due to a NOTCH2 point mutation.
PharmGKBi PA31684.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000234369.
HOVERGENi HBG052650.
InParanoidi Q04721.
KOi K02599.
OMAi MEDPWAN.
OrthoDBi EOG7992RD.
PhylomeDBi Q04721.
TreeFami TF351641.

Enzyme and pathway databases

Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_14835. Notch-HLH transcription pathway.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinki Q04721.

Miscellaneous databases

ChiTaRSi NOTCH2. human.
EvolutionaryTracei Q04721.
GeneWikii Notch-2.
GenomeRNAii 4853.
NextBioi 18692.
PROi Q04721.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q04721.
Bgeei Q04721.
CleanExi HS_NOTCH2.
Genevestigatori Q04721.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
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.
IPR008297. Notch.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view ]
Pfami PF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view ]
PIRSFi PIRSF002279. Notch. 1 hit.
PRINTSi PR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTi SM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 hits.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 29 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete human notch 2 (hN2) cDNA sequence."
    Blaumueller C.M., Mann R.S.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Human Notch2, a novel member of cell-fate determining NOTCH family."
    Correa R.G., Camargo A.A., Moreira E.S., Simpson A.J.G.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary tumor.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Partial sequence of EGF-like repeat domain of human Notch2 mRNA."
    Lemasson I., Devaux C., Mesnard J.-M.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1229.
    Tissue: T-cell.
  5. "Human homologs of a Drosophila enhancer of split gene product define a novel family of nuclear proteins."
    Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., Artavanis-Tsakonas S.
    Nat. Genet. 2:119-127(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1810-2447.
    Tissue: Brain.
  6. "Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane."
    Blaumueller C.M., Qi H., Zagouras P., Artavanis-Tsakonas S.
    Cell 90:281-291(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  7. Cited for: IDENTIFICATION OF LIGANDS.
  8. "MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors."
    Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S., Griffin J.D.
    Nat. Genet. 26:484-489(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAML1.
  9. "Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors."
    Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.
    Mol. Cell. Biol. 22:7688-7700(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAML2 AND MAML3.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INTERACTION WITH HIF1AN.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1716; THR-1802; SER-1804; THR-1808; SER-1845; SER-2070; SER-2081 AND THR-2097, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways."
    Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P., Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L., Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J., Peet D.J., Lendahl U., Poellinger L.
    Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION BY HIF1AN.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1778 AND SER-1845, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: FUNCTION, INVOLVEMENT IN HJCYS.
  17. Cited for: FUNCTION, INVOLVEMENT IN HJCYS, TISSUE SPECIFICITY.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1426-1677, DISULFIDE BONDS.
  19. "NOTCH2 mutations cause Alagille syndrome, a heterogeneous disorder of the notch signaling pathway."
    McDaniell R., Warthen D.M., Sanchez-Lara P.A., Pai A., Krantz I.D., Piccoli D.A., Spinner N.B.
    Am. J. Hum. Genet. 79:169-173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALGS2 TYR-444.

Entry informationi

Entry nameiNOTC2_HUMAN
AccessioniPrimary (citable) accession number: Q04721
Secondary accession number(s): Q5T3X7, Q99734, Q9H240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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