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Q8NER1 (TRPV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient receptor potential cation channel subfamily V member 1

Short name=TrpV1
Alternative name(s):
Capsaicin receptor
Osm-9-like TRP channel 1
Short name=OTRPC1
Vanilloid receptor 1
Gene names
Name:TRPV1
Synonyms:VR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length839 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis By similarity. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca2+-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Ref.1 Ref.2 Ref.3 Ref.9

Enzyme regulation

Channel activity is activated via the interaction with PIRT and phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT and PIP2 are required to activate channel activity By similarity. The channel is sensitized by ATP binding. Repeated stimulation with capsaicin gives rise to progressively smaller responses, due to desensitization. This desensitization is triggered by the influx of calcium ions and is inhibited by elevated ATP levels. Ca2+ and CALM displace ATP from its binding site and trigger a conformation change that leads to a closed, desensitized channel. Intracellular PIP2 inhibits desensitization. The double-knot toxin (DkTx) from the Chinese earth tiger tarantula activates the channel and traps it in an open conformation By similarity.

Subunit structure

Homotetramer. Interacts with CALM, PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric complex. Interacts with PIRT By similarity. Interacts with TRPV3 and may also form a heteromeric channel with TRPV3. Ref.9

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein By similarity. Cell projectiondendritic spine membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein. Note: Mostly, but not exclusively expressed in postsynaptic dendritic spines By similarity. Ref.9

Tissue specificity

Widely expressed at low levels. Expression is elevated in dorsal root ganglia. In skin, expressed in cutaneous sensory nerve fibers, mast cells, epidermal keratinocytes, dermal blood vessels, the inner root sheet and the infundibulum of hair follicles, differentiated sebocytes, sweat gland ducts, and the secretory portion of eccrine sweat glands (at protein level). Ref.1 Ref.2 Ref.10

Domain

The association domain (AD) is necessary for self-association By similarity.

Post-translational modification

Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-117 as a major phosphorylation site. Phoshphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity By similarity.

Miscellaneous

Responses evoked by low pH and heat, and capsaicin can be antagonized by capsazepine.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily. [View classification]

Contains 6 ANK repeats.

Sequence caution

The sequence AAG43467.1 differs from that shown. Reason: Frameshift at position 498.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Calmodulin-binding
Nucleotide-binding
   Molecular functionCalcium channel
Ion channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface receptor signaling pathway

Traceable author statement PubMed 9349813. Source: ProtInc

cellular response to ATP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to alkaloid

Inferred from sequence or structural similarity. Source: UniProtKB

chemosensory behavior

Traceable author statement PubMed 9349813. Source: ProtInc

ion transmembrane transport

Traceable author statement. Source: Reactome

thermoception

Inferred from direct assay PubMed 123456. Source: MGI

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement PubMed 9349813. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendritic spine membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay PubMed 123456. Source: MGI

integral component of plasma membrane

Traceable author statement PubMed 9349813. Source: ProtInc

intrinsic component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium channel activity

Traceable author statement PubMed 9349813. Source: ProtInc

calcium-release channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

excitatory extracellular ligand-gated ion channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoprotein binding

Inferred from physical interaction PubMed 19801576. Source: UniProt

transmembrane signaling receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 839839Transient receptor potential cation channel subfamily V member 1
PRO_0000215338

Regions

Topological domain1 – 433433Cytoplasmic By similarity
Transmembrane434 – 45421Helical; By similarity
Topological domain455 – 47117Extracellular By similarity
Transmembrane472 – 49726Helical; By similarity
Topological domain498 – 51013Cytoplasmic By similarity
Transmembrane511 – 53121Helical; By similarity
Topological domain532 – 5354Extracellular By similarity
Transmembrane536 – 55621Helical; By similarity
Topological domain557 – 57115Cytoplasmic By similarity
Transmembrane572 – 59928Helical; By similarity
Topological domain600 – 62728Extracellular By similarity
Intramembrane628 – 65023Pore-forming; By similarity
Transmembrane659 – 68729Helical; By similarity
Topological domain688 – 839152Cytoplasmic By similarity
Repeat111 – 15343ANK 1
Repeat154 – 20047ANK 2
Repeat201 – 24747ANK 3
Repeat248 – 28336ANK 4
Repeat284 – 33249ANK 5
Repeat333 – 35927ANK 6
Region685 – 71329AD By similarity
Region768 – 80235Interaction with calmodulin By similarity
Region778 – 79316Required for PIP2-mediated channel inhibition By similarity
Motif644 – 6474Selectivity filter By similarity

Amino acid modifications

Modified residue1171Phosphoserine By similarity
Modified residue1451Phosphothreonine By similarity
Modified residue3711Phosphothreonine By similarity
Modified residue5021Phosphoserine; by PKC/PRKCE By similarity
Modified residue7051Phosphothreonine By similarity
Modified residue7751Phosphoserine By similarity
Modified residue8011Phosphoserine; by PKC/PRKCE By similarity
Modified residue8211Phosphoserine By similarity
Glycosylation6041N-linked (GlcNAc...) By similarity

Natural variations

Natural variant911P → S. Ref.2
Corresponds to variant rs222749 [ dbSNP | Ensembl ].
VAR_057307
Natural variant4691T → I. Ref.2 Ref.5
Corresponds to variant rs224534 [ dbSNP | Ensembl ].
VAR_057308
Natural variant5051T → A.
Corresponds to variant rs17633288 [ dbSNP | Ensembl ].
VAR_057309
Natural variant5851I → V. Ref.1
Corresponds to variant rs8065080 [ dbSNP | Ensembl ].
VAR_022246

Experimental info

Mutagenesis5111Y → A: Loss of sensitivity to capsaicin. Ref.11
Mutagenesis5501T → I: Reduces sensitivity to capsaicin 40-fold. Ref.11
Sequence conflict3151M → I in CAB95729. Ref.1
Sequence conflict3151M → I in AAG43467. Ref.2
Sequence conflict3151M → I in CAB89866. Ref.3
Sequence conflict3151M → I in AAM89472. Ref.4
Sequence conflict3151M → I in CAB66735. Ref.5
Sequence conflict3151M → I in EAW90497. Ref.7
Sequence conflict3151M → I in AAI32821. Ref.8
Sequence conflict3151M → I in AAI36634. Ref.8
Sequence conflict3361T → M in CAB89866. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8NER1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 7142F59D428827FB

FASTA83994,956
        10         20         30         40         50         60 
MKKWSSTDLG AAADPLQKDT CPDPLDGDPN SRPPPAKPQL STAKSRTRLF GKGDSEEAFP 

        70         80         90        100        110        120 
VDCPHEEGEL DSCPTITVSP VITIQRPGDG PTGARLLSQD SVAASTEKTL RLYDRRSIFE 

       130        140        150        160        170        180 
AVAQNNCQDL ESLLLFLQKS KKHLTDNEFK DPETGKTCLL KAMLNLHDGQ NTTIPLLLEI 

       190        200        210        220        230        240 
ARQTDSLKEL VNASYTDSYY KGQTALHIAI ERRNMALVTL LVENGADVQA AAHGDFFKKT 

       250        260        270        280        290        300 
KGRPGFYFGE LPLSLAACTN QLGIVKFLLQ NSWQTADISA RDSVGNTVLH ALVEVADNTA 

       310        320        330        340        350        360 
DNTKFVTSMY NEILMLGAKL HPTLKLEELT NKKGMTPLAL AAGTGKIGVL AYILQREIQE 

       370        380        390        400        410        420 
PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI AYSSSETPNR HDMLLVEPLN 

       430        440        450        460        470        480 
RLLQDKWDRF VKRIFYFNFL VYCLYMIIFT MAAYYRPVDG LPPFKMEKTG DYFRVTGEIL 

       490        500        510        520        530        540 
SVLGGVYFFF RGIQYFLQRR PSMKTLFVDS YSEMLFFLQS LFMLATVVLY FSHLKEYVAS 

       550        560        570        580        590        600 
MVFSLALGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYIVFLFG FSTAVVTLIE 

       610        620        630        640        650        660 
DGKNDSLPSE STSHRWRGPA CRPPDSSYNS LYSTCLELFK FTIGMGDLEF TENYDFKAVF 

       670        680        690        700        710        720 
IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL QRAITILDTE KSFLKCMRKA 

       730        740        750        760        770        780 
FRSGKLLQVG YTPDGKDDYR WCFRVDEVNW TTWNTNVGII NEDPGNCEGV KRTLSFSLRS 

       790        800        810        820        830 
SRVSGRHWKN FALVPLLREA SARDRQSAQP EEVYLRQFSG SLKPEDAEVF KSPAASGEK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional expression of a human orthologue of rat vanilloid receptor-1."
Hayes P., Meadows H.J., Gunthorpe M., Harries M.H., Duckworth M.D., Cairns W., Harrison D.C., Clarke C., Ellington K., Prinjha R.K., Barton A.J., Medhurst A.D., Smith G.D., Topp S., Murdock P., Sanger G.J., Terrett J., Jenkins O. expand/collapse author list , Benham C.D., Randall A.D., Gloger I.S., Davis J.B.
Pain 88:205-215(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-585.
[2]"The tissue distribution and functional characterization of human VR1."
Cortright D.N., Crandall M., Sanchez J.F., Zou T., Krause J.E., White G.
Biochem. Biophys. Res. Commun. 281:1183-1189(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS SER-91 AND ILE-469.
Tissue: Spinal ganglion.
[3]"Pharmacological differences between human and rat vanilloid receptor 1 (VR1)."
McIntyre P., McLatchie L., Chambers A., Phillips E., Clarke M., Savidge J., Peacock M., Shah K., Winter J., Weerasekera N., Webb M., Rang H., Bevan S., James I.
Br. J. Pharmacol. 132:1084-1094(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Spinal ganglion.
[4]Lee D., Ha I.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[5]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-469.
Tissue: Testis.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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.
[9]"TRPV3 is a temperature-sensitive vanilloid receptor-like protein."
Smith G.D., Gunthorpe M.J., Kelsell R.E., Hayes P.D., Reilly P., Facer P., Wright J.E., Jerman J.C., Walhin J.-P., Ooi L., Egerton J., Charles K.J., Smart D., Randall A.D., Anand P., Davis J.B.
Nature 418:186-190(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRPV3.
[10]"Expression of vanilloid receptor subtype 1 in cutaneous sensory nerve fibers, mast cells, and epithelial cells of appendage structures."
Staender S., Moormann C., Schumacher M., Buddenkotte J., Artuc M., Shpacovitch V., Brzoska T., Lippert U., Henz B.M., Luger T.A., Metze D., Steinhoff M.
Exp. Dermatol. 13:129-139(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Molecular determinants of vanilloid sensitivity in TRPV1."
Gavva N.R., Klionsky L., Qu Y., Shi L., Tamir R., Edenson S., Zhang T.J., Viswanadhan V.N., Toth A., Pearce L.V., Vanderah T.W., Porreca F., Blumberg P.M., Lile J., Sun Y., Wild K., Louis J.C., Treanor J.J.
J. Biol. Chem. 279:20283-20295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-511 AND THR-550.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ277028 mRNA. Translation: CAB95729.1.
AF196175 mRNA. Translation: AAG43466.1.
AF196176 mRNA. Translation: AAG43467.1. Frameshift.
AJ272063 mRNA. Translation: CAB89866.2.
AY131289 mRNA. Translation: AAM89472.1.
AL136801 mRNA. Translation: CAB66735.1.
AC027796 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90497.1.
BC132820 mRNA. Translation: AAI32821.1.
BC136633 mRNA. Translation: AAI36634.1.
CCDSCCDS45576.1.
PIRJC7621.
RefSeqNP_061197.4. NM_018727.5.
NP_542435.2. NM_080704.3.
NP_542436.2. NM_080705.3.
NP_542437.2. NM_080706.3.
UniGeneHs.579217.
Hs.655380.

3D structure databases

ProteinModelPortalQ8NER1.
SMRQ8NER1. Positions 112-720.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113281. 7 interactions.
MINTMINT-4721979.
STRING9606.ENSP00000174621.

Chemistry

BindingDBQ8NER1.
ChEMBLCHEMBL4794.
DrugBankDB00132. Alpha-Linolenic Acid.
DB00168. Aspartame.
DB00159. Icosapent.
GuidetoPHARMACOLOGY507.

PTM databases

PhosphoSiteQ8NER1.

Polymorphism databases

DMDM296452849.

Proteomic databases

PaxDbQ8NER1.
PRIDEQ8NER1.

Protocols and materials databases

DNASU7442.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399756; ENSP00000382659; ENSG00000196689.
ENST00000399759; ENSP00000382661; ENSG00000196689.
ENST00000571088; ENSP00000461007; ENSG00000196689.
GeneID7442.
KEGGhsa:7442.
UCSCuc010vrr.2. human.

Organism-specific databases

CTD7442.
GeneCardsGC17M003469.
H-InvDBHIX0013428.
HIX0079948.
HGNCHGNC:12716. TRPV1.
MIM602076. gene.
neXtProtNX_Q8NER1.
PharmGKBPA37329.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278734.
HOVERGENHBG054085.
KOK05222.
OrthoDBEOG7WHH8R.
PhylomeDBQ8NER1.
TreeFamTF314711.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ8NER1.
CleanExHS_TRPV1.
GenevestigatorQ8NER1.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024863. TRPV1_channel.
[Graphical view]
PANTHERPTHR10582:SF17. PTHR10582:SF17. 1 hit.
PfamPF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTRPV1.
GenomeRNAi7442.
NextBio29140.
PROQ8NER1.
SOURCESearch...

Entry information

Entry nameTRPV1_HUMAN
AccessionPrimary (citable) accession number: Q8NER1
Secondary accession number(s): A2RUA9 expand/collapse secondary AC list , Q9H0G9, Q9H303, Q9H304, Q9NQ74, Q9NY22
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM