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P25116

- PAR1_HUMAN

UniProt

P25116 - PAR1_HUMAN

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Protein

Proteinase-activated receptor 1

Gene
F2R, CF2R, PAR1, TR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 422Cleavage; by thrombin

GO - Molecular functioni

  1. G-protein alpha-subunit binding Source: UniProtKB
  2. G-protein beta-subunit binding Source: UniProtKB
  3. G-protein coupled receptor activity Source: UniProtKB
  4. protein binding Source: IntAct
  5. receptor binding Source: BHF-UCL
  6. thrombin receptor activity Source: BHF-UCL

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  2. activation of MAPKK activity Source: UniProtKB
  3. anatomical structure morphogenesis Source: ProtInc
  4. blood coagulation Source: Reactome
  5. connective tissue replacement involved in inflammatory response wound healing Source: BHF-UCL
  6. establishment of synaptic specificity at neuromuscular junction Source: UniProtKB
  7. G-protein coupled receptor signaling pathway Source: UniProtKB
  8. homeostasis of number of cells within a tissue Source: UniProtKB
  9. inflammatory response Source: UniProtKB
  10. negative regulation of cell proliferation Source: BHF-UCL
  11. negative regulation of glomerular filtration Source: UniProtKB
  12. negative regulation of neuron apoptotic process Source: UniProtKB
  13. negative regulation of renin secretion into blood stream Source: UniProtKB
  14. phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
  15. platelet activation Source: BHF-UCL
  16. platelet dense granule organization Source: BHF-UCL
  17. positive regulation of blood coagulation Source: BHF-UCL
  18. positive regulation of calcium ion transport Source: UniProtKB
  19. positive regulation of cell migration Source: BHF-UCL
  20. positive regulation of cell proliferation Source: UniProtKB
  21. positive regulation of collagen biosynthetic process Source: BHF-UCL
  22. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  23. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  24. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
  25. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  26. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  27. positive regulation of interleukin-6 secretion Source: UniProtKB
  28. positive regulation of interleukin-8 secretion Source: UniProtKB
  29. positive regulation of JAK-STAT cascade Source: BHF-UCL
  30. positive regulation of MAPK cascade Source: BHF-UCL
  31. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  32. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  33. positive regulation of Rho protein signal transduction Source: UniProtKB
  34. positive regulation of smooth muscle contraction Source: UniProtKB
  35. positive regulation of transcription, DNA-templated Source: BHF-UCL
  36. positive regulation of vasoconstriction Source: UniProtKB
  37. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  38. regulation of blood coagulation Source: BHF-UCL
  39. regulation of interleukin-1 beta production Source: UniProtKB
  40. regulation of sensory perception of pain Source: UniProtKB
  41. release of sequestered calcium ion into cytosol Source: UniProtKB
  42. response to lipopolysaccharide Source: UniProtKB
  43. response to wounding Source: BHF-UCL
  44. STAT protein import into nucleus Source: BHF-UCL
  45. tyrosine phosphorylation of STAT protein Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_18283. G alpha (q) signalling events.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase-activated receptor 1
Short name:
PAR-1
Alternative name(s):
Coagulation factor II receptor
Thrombin receptor
Gene namesi
Name:F2R
Synonyms:CF2R, PAR1, TR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3537. F2R.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 10261Extracellular Reviewed predictionAdd
BLAST
Transmembranei103 – 12826Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini129 – 1379Cytoplasmic Reviewed prediction
Transmembranei138 – 15720Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini158 – 17619Extracellular Reviewed predictionAdd
BLAST
Transmembranei177 – 19822Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini199 – 21820Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei219 – 23921Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini240 – 26829Extracellular Reviewed predictionAdd
BLAST
Transmembranei269 – 28820Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini289 – 31123Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei312 – 33423Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini335 – 35016Extracellular Reviewed predictionAdd
BLAST
Transmembranei351 – 37424Helical; Name=7; Reviewed predictionAdd
BLAST
Topological domaini375 – 42551Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. extracellular region Source: Reactome
  3. Golgi apparatus Source: ProtInc
  4. integral component of plasma membrane Source: ProtInc
  5. neuromuscular junction Source: UniProtKB
  6. plasma membrane Source: BHF-UCL
  7. platelet dense tubular network Source: BHF-UCL
  8. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Propeptidei22 – 4120PRO_0000012740Add
BLAST
Chaini42 – 425384Proteinase-activated receptor 1PRO_0000012741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi62 – 621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi175 ↔ 254 By similarity
Glycosylationi250 – 2501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi259 – 2591N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25116.
PaxDbiP25116.
PRIDEiP25116.

PTM databases

PhosphoSiteiP25116.

Miscellaneous databases

PMAP-CutDBP25116.

Expressioni

Tissue specificityi

Platelets and vascular endothelial cells.

Gene expression databases

ArrayExpressiP25116.
BgeeiP25116.
CleanExiHS_F2R.
GenevestigatoriP25116.

Organism-specific databases

HPAiCAB008973.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAV1Q031353EBI-2803960,EBI-603614
PROCRQ9UNN83EBI-2803960,EBI-719705

Protein-protein interaction databases

BioGridi108448. 14 interactions.
DIPiDIP-29703N.
IntActiP25116. 7 interactions.
STRINGi9606.ENSP00000321326.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413
Turni47 – 504
Helixi92 – 965
Helixi99 – 1024
Helixi104 – 13027
Helixi131 – 1333
Helixi136 – 15217
Helixi155 – 1639
Helixi172 – 20534
Helixi216 – 23823
Beta strandi243 – 2464
Turni247 – 2504
Beta strandi251 – 2577
Helixi265 – 29632
Helixi305 – 32420
Helixi327 – 33812
Helixi347 – 36014
Helixi363 – 37311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NRNX-ray3.10R38-60[»]
1NROX-ray3.10R38-64[»]
1NRPX-ray3.00R38-60[»]
1NRQX-ray3.50R40-60[»]
1NRRX-ray2.40R43-60[»]
3BEFX-ray2.20C/F49-57[»]
3HKIX-ray2.20C/F42-62[»]
3HKJX-ray2.60C/F42-62[»]
3LU9X-ray1.80C/F33-57[»]
3VW7X-ray2.20A86-395[»]
ProteinModelPortaliP25116.
SMRiP25116. Positions 62-389.

Miscellaneous databases

EvolutionaryTraceiP25116.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 604Asp/Glu-rich (acidic)

Domaini

The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150457.
HOGENOMiHOG000232200.
HOVERGENiHBG108233.
InParanoidiP25116.
KOiK03914.
OMAiASKMDTC.
OrthoDBiEOG7V49ZD.
PhylomeDBiP25116.
TreeFamiTF330775.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25116-1 [UniParc]FASTAAdd to Basket

« Hide

MGPRRLLLVA ACFSLCGPLL SARTRARRPE SKATNATLDP RSFLLRNPND    50
KYEPFWEDEE KNESGLTEYR LVSINKSSPL QKQLPAFISE DASGYLTSSW 100
LTLFVPSVYT GVFVVSLPLN IMAIVVFILK MKVKKPAVVY MLHLATADVL 150
FVSVLPFKIS YYFSGSDWQF GSELCRFVTA AFYCNMYASI LLMTVISIDR 200
FLAVVYPMQS LSWRTLGRAS FTCLAIWALA IAGVVPLLLK EQTIQVPGLN 250
ITTCHDVLNE TLLEGYYAYY FSAFSAVFFF VPLIISTVCY VSIIRCLSSS 300
AVANRSKKSR ALFLSAAVFC IFIICFGPTN VLLIAHYSFL SHTSTTEAAY 350
FAYLLCVCVS SISCCIDPLI YYYASSECQR YVYSILCCKE SSDPSSYNSS 400
GQLMASKMDT CSSNLNNSIY KKLLT 425
Length:425
Mass (Da):47,441
Last modified:April 16, 2002 - v2
Checksum:i41B742A99EEC96AB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661S → G.1 Publication
Corresponds to variant rs5893 [ dbSNP | Ensembl ].
VAR_014167
Natural varianti187 – 1871Y → N.
Corresponds to variant rs2230849 [ dbSNP | Ensembl ].
VAR_049432
Natural varianti257 – 2571V → L.
Corresponds to variant rs2227832 [ dbSNP | Ensembl ].
VAR_049433
Natural varianti268 – 2681A → P.
Corresponds to variant rs1055103 [ dbSNP | Ensembl ].
VAR_060680
Natural varianti335 – 3351A → V.2 Publications
Corresponds to variant rs17849599 [ dbSNP | Ensembl ].
VAR_060681
Natural varianti412 – 4121S → Y.
Corresponds to variant rs2227799 [ dbSNP | Ensembl ].
VAR_049434

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381L → V in AAA36743. 1 Publication
Sequence conflicti364 – 3641C → S in AAA36743. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62424 mRNA. Translation: AAA36743.1.
AF391809 Genomic DNA. Translation: AAK69768.1.
BT007279 mRNA. Translation: AAP35943.1.
BC002464 mRNA. Translation: AAH02464.1.
BC051909 mRNA. Translation: AAH51909.1.
CCDSiCCDS4032.1.
PIRiA37912.
RefSeqiNP_001983.2. NM_001992.3.
UniGeneiHs.482562.

Genome annotation databases

EnsembliENST00000319211; ENSP00000321326; ENSG00000181104.
GeneIDi2149.
KEGGihsa:2149.
UCSCiuc003ken.4. human.

Polymorphism databases

DMDMi20178318.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62424 mRNA. Translation: AAA36743.1 .
AF391809 Genomic DNA. Translation: AAK69768.1 .
BT007279 mRNA. Translation: AAP35943.1 .
BC002464 mRNA. Translation: AAH02464.1 .
BC051909 mRNA. Translation: AAH51909.1 .
CCDSi CCDS4032.1.
PIRi A37912.
RefSeqi NP_001983.2. NM_001992.3.
UniGenei Hs.482562.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NRN X-ray 3.10 R 38-60 [» ]
1NRO X-ray 3.10 R 38-64 [» ]
1NRP X-ray 3.00 R 38-60 [» ]
1NRQ X-ray 3.50 R 40-60 [» ]
1NRR X-ray 2.40 R 43-60 [» ]
3BEF X-ray 2.20 C/F 49-57 [» ]
3HKI X-ray 2.20 C/F 42-62 [» ]
3HKJ X-ray 2.60 C/F 42-62 [» ]
3LU9 X-ray 1.80 C/F 33-57 [» ]
3VW7 X-ray 2.20 A 86-395 [» ]
ProteinModelPortali P25116.
SMRi P25116. Positions 62-389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108448. 14 interactions.
DIPi DIP-29703N.
IntActi P25116. 7 interactions.
STRINGi 9606.ENSP00000321326.

Chemistry

BindingDBi P25116.
ChEMBLi CHEMBL3974.
DrugBanki DB00086. Streptokinase.
GuidetoPHARMACOLOGYi 347.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P25116.

Polymorphism databases

DMDMi 20178318.

Proteomic databases

MaxQBi P25116.
PaxDbi P25116.
PRIDEi P25116.

Protocols and materials databases

DNASUi 2149.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319211 ; ENSP00000321326 ; ENSG00000181104 .
GeneIDi 2149.
KEGGi hsa:2149.
UCSCi uc003ken.4. human.

Organism-specific databases

CTDi 2149.
GeneCardsi GC05P076047.
H-InvDB HIX0004960.
HGNCi HGNC:3537. F2R.
HPAi CAB008973.
MIMi 187930. gene.
neXtProti NX_P25116.
PharmGKBi PA27946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG150457.
HOGENOMi HOG000232200.
HOVERGENi HBG108233.
InParanoidi P25116.
KOi K03914.
OMAi ASKMDTC.
OrthoDBi EOG7V49ZD.
PhylomeDBi P25116.
TreeFami TF330775.

Enzyme and pathway databases

Reactomei REACT_14819. Peptide ligand-binding receptors.
REACT_18283. G alpha (q) signalling events.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

ChiTaRSi F2R. human.
EvolutionaryTracei P25116.
GeneWikii Coagulation_factor_II_receptor.
GenomeRNAii 2149.
NextBioi 8685.
PMAP-CutDB P25116.
PROi P25116.
SOURCEi Search...

Gene expression databases

ArrayExpressi P25116.
Bgeei P25116.
CleanExi HS_F2R.
Genevestigatori P25116.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view ]
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation."
    Vu T.-K.H., Hung D.T., Wheaton V.I., Coughlin S.R.
    Cell 64:1057-1068(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. SeattleSNPs variation discovery resource
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-335.
  4. "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], VARIANT VAL-335.
    Tissue: Eye.
  5. "Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization."
    Shapiro M.J., Trejo J., Zeng D., Coughlin S.R.
    J. Biol. Chem. 271:32874-32880(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. "Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin."
    Kahn M.L., Nakanishi-Matsui M., Shapiro M.J., Ishihara H., Coughlin S.R.
    J. Clin. Invest. 103:879-887(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Parstatin, the cleaved peptide on proteinase-activated receptor 1 activation, is a potent inhibitor of angiogenesis."
    Zania P., Gourni D., Aplin A.C., Nicosia R.F., Flordellis C.S., Maragoudakis M.E., Tsopanoglou N.E.
    J. Pharmacol. Exp. Ther. 328:378-389(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANGIOGENESIS INHIBITION PROPERTIES OF PARSTATIN.
  8. "The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression."
    Zampatis D.E., Rutz C., Furkert J., Schmidt A., Wustenhagen D., Kubick S., Tsopanoglou N.E., Schulein R.
    FEBS Lett. 586:2351-2359(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIGNAL SEQUENCE CLEAVAGE SITE.
  9. Cited for: VARIANT GLY-166.
  10. "Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes."
    Mathews I.I., Padmanabhan K.P., Ganesh V., Tulinsky A., Ishii M., Chen J., Turck C.W., Coughlin S.R., Fenton J.W. II
    Biochemistry 33:3266-3279(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 38-64 IN COMPLEX WITH THROMBIN.

Entry informationi

Entry nameiPAR1_HUMAN
AccessioniPrimary (citable) accession number: P25116
Secondary accession number(s): Q53XV0, Q96RF7, Q9BUN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: April 16, 2002
Last modified: September 3, 2014
This is version 165 of the entry and version 2 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. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi