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P32241 (VIPR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vasoactive intestinal polypeptide receptor 1

Short name=VIP-R-1
Alternative name(s):
Pituitary adenylate cyclase-activating polypeptide type II receptor
Short name=PACAP type II receptor
Short name=PACAP-R-2
Short name=PACAP-R2
VPAC1
Gene names
Name:VIPR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The affinity is VIP = PACAP-27 > PACAP-38. Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

In lung, HT-29 colonic epithelial cells, Raji B-lymphoblasts. Lesser extent in brain, heart, kidney, liver and placenta. Not expressed in CD4+ or CD8+ T-cells. Expressed in the T-cell lines HARRIS, HuT 78, Jurkat and SUP-T1, but not in the T-cell lines Peer, MOLT-4, HSB and YT. Ref.11

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VIPP012822EBI-3917984,EBI-6656819

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform Short (identifier: P32241-1)

Also known as: hIVR8;

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.
Isoform Long (identifier: P32241-2)

Also known as: hIVR5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MRPPSPLPARWLCVLAGALAWALGPAGGQAAR → MPPPPLLSLR...RAARSLLGSS
Isoform 3 (identifier: P32241-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: MRPPSPLPAR...YFWGYILIGW → MTRQRVWMRW...PSSLSGSTSG
Isoform 4 (identifier: P32241-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLEEAQLENETI → MRAGRRPRLGPWAG
     134-134: Missing.
Isoform 5 (identifier: P32241-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 457427Vasoactive intestinal polypeptide receptor 1
PRO_0000012855

Regions

Topological domain31 – 142112Extracellular Potential
Transmembrane143 – 16725Helical; Name=1; Potential
Topological domain168 – 1747Cytoplasmic Potential
Transmembrane175 – 19420Helical; Name=2; Potential
Topological domain195 – 21622Extracellular Potential
Transmembrane217 – 24024Helical; Name=3; Potential
Topological domain241 – 25414Cytoplasmic Potential
Transmembrane255 – 27622Helical; Name=4; Potential
Topological domain277 – 29216Extracellular Potential
Transmembrane293 – 31624Helical; Name=5; Potential
Topological domain317 – 34125Cytoplasmic Potential
Transmembrane342 – 36120Helical; Name=6; Potential
Topological domain362 – 37312Extracellular Potential
Transmembrane374 – 39320Helical; Name=7; Potential
Topological domain394 – 45764Cytoplasmic Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 72 By similarity
Disulfide bond63 ↔ 105 By similarity
Disulfide bond86 ↔ 122 By similarity
Disulfide bond215 ↔ 285 Ref.12

Natural variations

Alternative sequence1 – 263263MRPPS…ILIGW → MTRQRVWMRWAVRQPWSFSN IVSWLTSSGCWWRASTCTPC LPSPSSLSGSTSG in isoform 3.
VSP_045143
Alternative sequence1 – 6161MRPPS…ENETI → MRAGRRPRLGPWAG in isoform 4.
VSP_047271
Alternative sequence1 – 4141Missing in isoform 5.
VSP_047272
Alternative sequence1 – 3232MRPPS…GQAAR → MPPPPLLSLRRLGGGWSAVT RLVVAAAGARSRGGRGGSRG AGGGGRGGVARRRRLELRAA RSLLGSS in isoform Long.
VSP_002010
Alternative sequence1341Missing in isoform 4.
VSP_047273
Natural variant3411R → M. Ref.8
Corresponds to variant rs17855906 [ dbSNP | Ensembl ].
VAR_055041
Natural variant4451R → L.
Corresponds to variant rs3733055 [ dbSNP | Ensembl ].
VAR_020021

Experimental info

Sequence conflict801Q → R in BAG57795. Ref.5
Sequence conflict2841G → GLLR in CAA54814. Ref.2
Sequence conflict2841G → GLLR in CAA53046. Ref.2
Sequence conflict3201L → F in BAG51813. Ref.5
Sequence conflict3691K → R in BAG57795. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Short (hIVR8) [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: DAA40CF5BEC47D7D

FASTA45751,547
        10         20         30         40         50         60 
MRPPSPLPAR WLCVLAGALA WALGPAGGQA ARLQEECDYV QMIEVQHKQC LEEAQLENET 

        70         80         90        100        110        120 
IGCSKMWDNL TCWPATPRGQ VVVLACPLIF KLFSSIQGRN VSRSCTDEGW THLEPGPYPI 

       130        140        150        160        170        180 
ACGLDDKAAS LDEQQTMFYG SVKTGYTIGY GLSLATLLVA TAILSLFRKL HCTRNYIHMH 

       190        200        210        220        230        240 
LFISFILRAA AVFIKDLALF DSGESDQCSE GSVGCKAAMV FFQYCVMANF FWLLVEGLYL 

       250        260        270        280        290        300 
YTLLAVSFFS ERKYFWGYIL IGWGVPSTFT MVWTIARIHF EDYGCWDTIN SSLWWIIKGP 

       310        320        330        340        350        360 
ILTSILVNFI LFICIIRILL QKLRPPDIRK SDSSPYSRLA RSTLLLIPLF GVHYIMFAFF 

       370        380        390        400        410        420 
PDNFKPEVKM VFELVVGSFQ GFVVAILYCF LNGEVQAELR RKWRRWHLQG VLGWNPKYRH 

       430        440        450 
PSGGSNGATC STQVSMLTRV SPGARRSSSF QAEVSLV 

« Hide

Isoform Long (hIVR5) [UniParc].

Checksum: D6E529795785C3AA
Show »

FASTA49255,009
Isoform 3 [UniParc].

Checksum: 271C125CB317C516
Show »

FASTA24728,164
Isoform 4 [UniParc].

Checksum: C66EA5C02820AB12
Show »

FASTA40946,268
Isoform 5 [UniParc].

Checksum: 4236FD602880CB8C
Show »

FASTA41647,201

References

« Hide 'large scale' references
[1]"Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor."
Sreedharan S.P., Patel D.R., Huang J.-X., Goetzl E.J.
Biochem. Biophys. Res. Commun. 193:546-553(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT).
Tissue: Intestine.
[2]"Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains."
Couvineau A., Rouyer-Fessard C., Darmoul D., Maoret J.J., Carrero I., Ogier-Denis E., Laburthe M.
Biochem. Biophys. Res. Commun. 200:769-776(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), ALTERNATIVE SPLICING.
Tissue: Intestine.
[3]"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Martin A.L., Kaighin V.A., Aronstam R.S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Lung.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT; 3; 4 AND 5).
Tissue: Brain, Cerebellum, Lung and Prostate.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(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 (JUL-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] (ISOFORM SHORT), VARIANT MET-341.
[9]"Molecular cloning and functional characterization of a human liver vasoactive intestinal peptide receptor."
Gagnon A.W., Aiyar N., Elshourbagy N.A.
Cell. Signal. 6:321-333(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-457.
Tissue: Liver.
[10]"Highly conserved aspartate 68, tryptophan 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP."
Couvineau A., Gaudin P., Maoret J.J., Rouyer-Fessard C., Nicole P., Laburthe M.
Biochem. Biophys. Res. Commun. 206:246-252(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VIP.
[11]"Predominant expression of type II vasoactive intestinal peptide receptors by human T lymphoblastoma cells: transduction of both Ca2+ and cyclic AMP signals."
Xia M., Sreedharan S.P., Goetzl E.J.
J. Clin. Immunol. 16:21-30(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Importance of conserved cysteines in the extracellular loops of human PACAP/VIP1 receptor for ligand binding and stimulation of cAMP production."
Knudsen S.M., Tams J.W., Wulff B.S., Fahrenkrug J.
Ann. N. Y. Acad. Sci. 865:259-265(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[13]"Dual, HLA-B27 subtype-dependent conformation of a self-peptide."
Hulsmeyer M., Fiorillo M.T., Bettosini F., Sorrentino R., Saenger W., Ziegler A., Uchanska-Ziegler B.
J. Exp. Med. 199:271-281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
[14]"Citrullination-dependent differential presentation of a self-peptide by HLA-B27 subtypes."
Beltrami A., Rossmann M., Fiorillo M.T., Paladini F., Sorrentino R., Saenger W., Kumar P., Ziegler A., Uchanska-Ziegler B.
J. Biol. Chem. 283:27189-27199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13288 mRNA. Translation: AAA36805.1.
U11087 expand/collapse EMBL AC list , U11079, U11080, U11081, U11083, U11084, U11085, U11086 Genomic DNA. Translation: AAB60362.1.
X75299 mRNA. Translation: CAA53046.1.
X77777 mRNA. Translation: CAA54814.1.
AB065669 Genomic DNA. Translation: BAC05895.1.
EF577396 mRNA. Translation: ABQ52416.1.
AK314334 mRNA. Translation: BAG36980.1.
AK293548 mRNA. Translation: BAG57026.1.
AK294609 mRNA. Translation: BAG57795.1.
AK056819 mRNA. Translation: BAG51813.1.
AC092047 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64649.1.
CH471055 Genomic DNA. Translation: EAW64650.1.
BC064424 mRNA. Translation: AAH64424.1.
L20295 mRNA. Translation: AAA36802.1.
PIRJC2194.
JC2195.
RefSeqNP_001238811.1. NM_001251882.1.
NP_001238812.1. NM_001251883.1.
NP_001238813.1. NM_001251884.1.
NP_001238814.1. NM_001251885.1.
NP_004615.2. NM_004624.3.
XP_005265495.1. XM_005265438.2.
UniGeneHs.348500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OF2X-ray2.20C400-408[»]
1OGTX-ray1.47C400-408[»]
3B3IX-ray1.86C400-408[»]
ProteinModelPortalP32241.
SMRP32241. Positions 46-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113274. 7 interactions.
IntActP32241. 3 interactions.
MINTMINT-1217405.
STRING9606.ENSP00000327246.

Chemistry

BindingDBP32241.
ChEMBLCHEMBL5144.
GuidetoPHARMACOLOGY371.

Protein family/group databases

TCDB9.A.14.4.9. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP32241.

Polymorphism databases

DMDM418253.

Proteomic databases

PaxDbP32241.
PRIDEP32241.

Protocols and materials databases

DNASU7433.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325123; ENSP00000327246; ENSG00000114812. [P32241-1]
ENST00000433647; ENSP00000394950; ENSG00000114812. [P32241-5]
ENST00000438259; ENSP00000415371; ENSG00000114812. [P32241-3]
ENST00000543411; ENSP00000445701; ENSG00000114812. [P32241-4]
GeneID7433.
KEGGhsa:7433.
UCSCuc003clf.2. human. [P32241-1]
uc011azm.1. human.

Organism-specific databases

CTD7433.
GeneCardsGC03P042520.
HGNCHGNC:12694. VIPR1.
HPAHPA026777.
MIM192321. gene.
neXtProtNX_P32241.
PharmGKBPA37313.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293423.
HOGENOMHOG000008249.
HOVERGENHBG008318.
InParanoidP32241.
KOK04589.
OMAEDYGCWD.
OrthoDBEOG7TF78W.
PhylomeDBP32241.
TreeFamTF315710.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP32241.
BgeeP32241.
CleanExHS_VIPR1.
GenevestigatorP32241.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR001571. GPCR_2_VIP_rcpt.
IPR001771. GPCR_2_VIP_rcpt_1.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSPR00249. GPCRSECRETIN.
PR00491. VASOACTVEIPR.
PR01154. VIP1RECEPTOR.
SMARTSM00008. HormR. 1 hit.
[Graphical view]
PROSITEPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVIPR1. human.
EvolutionaryTraceP32241.
GeneWikiVIPR1.
GenomeRNAi7433.
NextBio29114.
PROP32241.
SOURCESearch...

Entry information

Entry nameVIPR1_HUMAN
AccessionPrimary (citable) accession number: P32241
Secondary accession number(s): A5JUT9 expand/collapse secondary AC list , B3KPV1, B4DEB5, B4DGI4, F5H1F5, G3V0I1, Q15871, Q6P2M6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 138 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 3

Human chromosome 3: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries