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P23945 (FSHR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Follicle-stimulating hormone receptor

Short name=FSH-R
Alternative name(s):
Follitropin receptor
Gene names
Name:FSHR
Synonyms:LGR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.

Subunit structure

Interacts with ARRB2 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Sertoli cells and ovarian granulosa cells.

Post-translational modification

N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone By similarity. Ref.15

Involvement in disease

Ovarian dysgenesis 1 (ODG1) [MIM:233300]: An autosomal recessive disease characterized by primary amenorrhea, variable development of secondary sex characteristics, poorly developed streak ovaries, and high serum levels of follicle-stimulating hormone (FSH) and luteinizing hormone (LH).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.19 Ref.20 Ref.21 Ref.25 Ref.26 Ref.27

Ovarian hyperstimulation syndrome (OHSS) [MIM:608115]: Disorder which occurs either spontaneously or most often as an iatrogenic complication of ovarian stimulation treatments for in vitro fertilization. The clinical manifestations vary from abdominal distention and discomfort to potentially life-threatening, massive ovarian enlargement and capillary leak with fluid sequestration. Pathologic features of this syndrome include the presence of multiple serous and hemorrhagic follicular cysts lined by luteinized cells, a condition called hyperreactio luteinalis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.

Contains 9 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 9020851. Source: ProtInc

Sertoli cell development

Inferred from electronic annotation. Source: Ensembl

Sertoli cell proliferation

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

basement membrane organization

Inferred from electronic annotation. Source: Ensembl

cellular water homeostasis

Inferred from electronic annotation. Source: Ensembl

female gamete generation

Traceable author statement PubMed 9020851. Source: ProtInc

female gonad development

Traceable author statement Ref.16. Source: ProtInc

gonad development

Traceable author statement PubMed 9020851. Source: ProtInc

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from expression pattern PubMed 17848411. Source: UniProtKB

negative regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

primary ovarian follicle growth

Inferred from electronic annotation. Source: Ensembl

regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

regulation of acetylcholine metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of chromosome organization

Inferred from electronic annotation. Source: Ensembl

regulation of hormone metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Traceable author statement PubMed 9020851. Source: ProtInc

spermatogenesis, exchange of chromosomal proteins

Inferred from electronic annotation. Source: Ensembl

transcytosis

Inferred from electronic annotation. Source: Ensembl

uterus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Traceable author statement PubMed 9020851. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionfollicle-stimulating hormone receptor activity

Traceable author statement PubMed 9020851. Source: ProtInc

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 15196694PubMed 20600589. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAQP273484EBI-848239,EBI-359854

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P23945-1)

Also known as: R1;

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 Short (identifier: P23945-2)

Also known as: E9Del;

The sequence of this isoform differs from the canonical sequence as follows:
     224-285: Missing.
Isoform 3 (identifier: P23945-3)

Also known as: E6Del;

The sequence of this isoform differs from the canonical sequence as follows:
     149-174: Missing.
Isoform 4 (identifier: P23945-4)

Also known as: E8'Inc;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: L → LNRRTRTPTEPNVLLAKYPSGQGVLEEPESLSSSI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 695678Follicle-stimulating hormone receptor
PRO_0000012771

Regions

Topological domain18 – 366349Extracellular Potential
Transmembrane367 – 38721Helical; Name=1; Potential
Topological domain388 – 39811Cytoplasmic Potential
Transmembrane399 – 42123Helical; Name=2; Potential
Topological domain422 – 44322Extracellular Potential
Transmembrane444 – 46522Helical; Name=3; Potential
Topological domain466 – 48520Cytoplasmic Potential
Transmembrane486 – 50823Helical; Name=4; Potential
Topological domain509 – 52820Extracellular Potential
Transmembrane529 – 55022Helical; Name=5; Potential
Topological domain551 – 57323Cytoplasmic Potential
Transmembrane574 – 59724Helical; Name=6; Potential
Topological domain598 – 60811Extracellular Potential
Transmembrane609 – 63022Helical; Name=7; Potential
Topological domain631 – 69565Cytoplasmic Potential
Domain18 – 4629LRRNT
Repeat49 – 7224LRR 1
Repeat73 – 9725LRR 2
Repeat98 – 11821LRR 3
Repeat119 – 14325LRR 4
Repeat144 – 16926LRR 5
Repeat170 – 19223LRR 6
Repeat193 – 21624LRR 7
Repeat217 – 24024LRR 8
Repeat241 – 25919LRR 9

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Ref.15
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) By similarity
Glycosylation3181N-linked (GlcNAc...) Potential
Disulfide bond18 ↔ 25 Ref.15
Disulfide bond23 ↔ 32 Ref.15
Disulfide bond442 ↔ 517 By similarity

Natural variations

Alternative sequence149 – 17426Missing in isoform 3.
VSP_043181
Alternative sequence2231L → LNRRTRTPTEPNVLLAKYPS GQGVLEEPESLSSSI in isoform 4.
VSP_053411
Alternative sequence224 – 28562Missing in isoform Short.
VSP_001953
Natural variant1281S → Y in OHSS; displays increase in affinity and sensitivity toward hCG and does not show any constitutive activity nor promiscuous activation by TSH. Ref.32
VAR_039279
Natural variant1601I → T in ODG1; impairs cell surface expression. Ref.20
VAR_018045
Natural variant1891A → V in ODG1; very frequent in the Finnish population. Ref.16 Ref.19
VAR_018046
Natural variant2241D → V in ODG1; FSH binding is barely detectable; impaired targeting to the cell membrane; adenylate cyclase stimulation by FSH is 4 +-2% residual activity. Ref.21
VAR_039280
Natural variant3071A → T. Ref.2 Ref.3 Ref.5 Ref.6 Ref.9 Ref.10 Ref.12 Ref.22 Ref.24
Corresponds to variant rs6165 [ dbSNP | Ensembl ].
VAR_013903
Natural variant3481P → R in ODG1. Ref.26
VAR_039281
Natural variant4191A → T in ODG1. Ref.25
VAR_018047
Natural variant4491T → A in OHSS; increase of receptor sensitivity to both hCG and TSH together with an increase in basal activity. Ref.30
VAR_039282
Natural variant4491T → I in OHSS. Ref.28
Corresponds to variant rs28928870 [ dbSNP | Ensembl ].
VAR_017244
Natural variant5191P → T in ODG1; totally impairs adenylate cyclase stimulation in vitro; alters the cell surface targeting of the receptor which remains trapped intracellularly. Ref.27
VAR_039283
Natural variant5241S → R. Ref.22
Corresponds to variant rs6167 [ dbSNP | Ensembl ].
VAR_013904
Natural variant5451I → T in OHSS; displays promiscuous activation by both hCG and TSH together with detectable constitutive activity. Ref.31
VAR_039284
Natural variant5671D → G in FSHR activation; 1.5-fold increase in basal cAMP production compared to the wild-type receptor indicating that this mutation leads to ligand-independent constitutive activation. Ref.18
VAR_039285
Natural variant5671D → N in OHSS. Ref.29
Corresponds to variant rs28928871 [ dbSNP | Ensembl ].
VAR_017245
Natural variant5731R → C in ODG1; alters signal transduction of the receptor; adenylate cyclase stimulation by FSH is 24 +-4% residual activity. Ref.20 Ref.21
VAR_018048
Natural variant5911F → S in ovarian sex cord tumor; loss of function. Ref.17
VAR_018049
Natural variant6011L → V in ODG1; binds FSH with a similar affinity than the wild-type receptor; adenylate cyclase stimulation by FSH is 12 +-3% residual activity. Ref.21
VAR_039286
Natural variant6801N → S Associated with longer menstrual cycles. Ref.1 Ref.7 Ref.8 Ref.9 Ref.12 Ref.22 Ref.24
Corresponds to variant rs6166 [ dbSNP | Ensembl ].
VAR_013905

Experimental info

Sequence conflict131S → R in CAA48179. Ref.10
Sequence conflict1121N → T in AAA52477. Ref.1
Sequence conflict197 – 1982EL → AV in AAA52477. Ref.1
Sequence conflict2951S → P in CAA48179. Ref.10

Secondary structure

.................................................. 695
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (R1) [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 766BC421014CD5A4

FASTA69578,265
        10         20         30         40         50         60 
MALLLVSLLA FLSLGSGCHH RICHCSNRVF LCQESKVTEI PSDLPRNAIE LRFVLTKLRV 

        70         80         90        100        110        120 
IQKGAFSGFG DLEKIEISQN DVLEVIEADV FSNLPKLHEI RIEKANNLLY INPEAFQNLP 

       130        140        150        160        170        180 
NLQYLLISNT GIKHLPDVHK IHSLQKVLLD IQDNINIHTI ERNSFVGLSF ESVILWLNKN 

       190        200        210        220        230        240 
GIQEIHNCAF NGTQLDELNL SDNNNLEELP NDVFHGASGP VILDISRTRI HSLPSYGLEN 

       250        260        270        280        290        300 
LKKLRARSTY NLKKLPTLEK LVALMEASLT YPSHCCAFAN WRRQISELHP ICNKSILRQE 

       310        320        330        340        350        360 
VDYMTQARGQ RSSLAEDNES SYSRGFDMTY TEFDYDLCNE VVDVTCSPKP DAFNPCEDIM 

       370        380        390        400        410        420 
GYNILRVLIW FISILAITGN IIVLVILTTS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS 

       430        440        450        460        470        480 
VDIHTKSQYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TAITLERWHT ITHAMQLDCK 

       490        500        510        520        530        540 
VQLRHAASVM VMGWIFAFAA ALFPIFGISS YMKVSICLPM DIDSPLSQLY VMSLLVLNVL 

       550        560        570        580        590        600 
AFVVICGCYI HIYLTVRNPN IVSSSSDTRI AKRMAMLIFT DFLCMAPISF FAISASLKVP 

       610        620        630        640        650        660 
LITVSKAKIL LVLFHPINSC ANPFLYAIFT KNFRRDFFIL LSKCGCYEMQ AQIYRTETSS 

       670        680        690 
TVHNTHPRNG HCSSAPRVTN GSTYILVPLS HLAQN 

« Hide

Isoform Short (E9Del) [UniParc].

Checksum: AEB5E6DE7905AD41
Show »

FASTA63371,079
Isoform 3 (E6Del) [UniParc].

Checksum: 13EBEE0CB4E1EEB9
Show »

FASTA66975,309
Isoform 4 (E8'Inc) [UniParc].

Checksum: 4C3BE97328EE2E34
Show »

FASTA72981,974

References

« Hide 'large scale' references
[1]"Cloning and sequencing of human FSH receptor cDNA."
Minegish T., Nakamura K., Takakura Y., Ibuki Y., Igarashi M.
Biochem. Biophys. Res. Commun. 175:1125-1130(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT SER-680.
Tissue: Ovary.
[2]"Expression of recombinant human follicle-stimulating hormone receptor: species-specific ligand binding, signal transduction, and identification of multiple ovarian messenger ribonucleic acid transcripts."
Tilly J.L., Aihara T., Nishimori K., Jia X.-C., Billig H., Kowalski K.I., Perlas E.A., Hsueh A.J.
Endocrinology 131:799-806(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-307.
[3]"The cloning of the human follicle stimulating hormone receptor and its expression in COS-7, CHO, and Y-1 cells."
Kelton C.A., Cheng S.V., Nugent N.P., Schweickhardt R.L., Rosenthal J.L., Overton S.A., Wands G.D., Kuzeja J.B., Luchette C.A., Chappel S.C.
Mol. Cell. Endocrinol. 89:141-151(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-307.
Tissue: Testis.
[4]"FSHR expression in adipose tissue."
Liu X., Huang H., Sheng J.
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Adipose tissue.
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT THR-307.
Tissue: Testis.
[6]"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] (ISOFORM LONG), VARIANT THR-307.
Tissue: Testis.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-680.
[8]Mural R.J., Istrail S., Sutton 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], VARIANT SER-680.
[9]"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] (ISOFORMS LONG AND 3), VARIANTS THR-307 AND SER-680.
[10]"Molecular cloning of a truncated isoform of the human follicle stimulating hormone receptor."
Gromoll J., Gudermann T., Nieschlag E.
Biochem. Biophys. Res. Commun. 188:1077-1083(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-342 (ISOFORM SHORT), VARIANT THR-307.
Tissue: Testis.
[11]"Characterization of the 5' flanking region of the human follicle-stimulating hormone receptor gene."
Gromoll J., Dankbar B., Gudermann T.
Mol. Cell. Endocrinol. 102:93-102(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
[12]"Localization of the human FSH receptor to chromosome 2p21 using a genomic probe comprising exon 10."
Gromoll J., Ried T., Holtgreve-Grez H., Nieschlag E., Gudermann T.
J. Mol. Endocrinol. 12:265-271(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-695, VARIANTS THR-307 AND SER-680.
[13]"Alternatively spliced variants of the follicle-stimulating hormone receptor gene in the testis of infertile men."
Song G.J., Park Y.S., Lee Y.S., Lee C.C., Kang I.S.
Fertil. Steril. 77:499-504(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 4).
[14]"Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions."
Jiang X., Dreano M., Buckler D.R., Cheng S., Ythier A., Wu H., Hendrickson W.A., el Tayar N.
Structure 3:1341-1353(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 49-228.
[15]"Structure of human follicle-stimulating hormone in complex with its receptor."
Fan Q.R., Hendrickson W.A.
Nature 433:269-277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 17-268 IN COMPLEX WITH FSHA AND FSHB, DISULFIDE BONDS, GLYCOSYLATION AT ASN-191.
[16]"Mutation in the follicle-stimulating hormone receptor gene causes hereditary hypergonadotropic ovarian failure."
Aittomaeki K., Lucena J.L.D., Pakarinen P., Sistonen P., Tapanainen J., Gromoll J., Kaskikari R., Sankila E.-M., Lehvaslaiho H., Engel A.R., Nieschlag E., Huhtaniemi I., de la Chapelle A.
Cell 82:959-968(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODG1 VAL-189.
[17]"A mutation in the follicle-stimulating hormone receptor occurs frequently in human ovarian sex cord tumors."
Kotlar T.J., Young R.H., Albanese C., Crowley W.F. Jr., Scully R.E., Jameson J.L.
J. Clin. Endocrinol. Metab. 82:1020-1026(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OVARIAN SEX CORD TUMOR SER-591.
[18]"An activating mutation of the follicle-stimulating hormone receptor autonomously sustains spermatogenesis in a hypophysectomized man."
Gromoll J., Simoni M., Nieschlag E.
J. Clin. Endocrinol. Metab. 81:1367-1370(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FSHR ACTIVATION GLY-567, CHARACTERIZATION OF VARIANT FSHR ACTIVATION GLY-567.
[19]"The frequency of an inactivating point mutation (566C-->T) of the human follicle-stimulating hormone receptor gene in four populations using allele-specific hybridization and time-resolved fluorometry."
Jiang M., Aittomaeki K., Nilsson C., Pakarinen P., Iitia A., Torresani T., Simonsen H., Goh V., Pettersson K., de la Chapelle A., Huhtaniemi I.
J. Clin. Endocrinol. Metab. 83:4338-4343(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODG1 VAL-189.
[20]"A novel phenotype related to partial loss of function mutations of the follicle stimulating hormone receptor."
Beau I., Touraine P., Meduri G., Gougeon A., Desroches A., Matuchansky C., Milgrom E., Kuttenn F., Misrahi M.
J. Clin. Invest. 102:1352-1359(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODG1 THR-160 AND CYS-573.
[21]"New natural inactivating mutations of the follicle-stimulating hormone receptor: correlations between receptor function and phenotype."
Touraine P., Beau I., Gougeon A., Meduri G., Desroches A., Pichard C., Detoeuf M., Paniel B., Prieur M., Zorn J.-R., Milgrom E., Kuttenn F., Misrahi M.
Mol. Endocrinol. 13:1844-1854(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODG1 VAL-224 AND VAL-601, CHARACTERIZATION OF VARIANTS ODG1 VAL-224; CYS-573 AND VAL-601.
[22]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-307; ARG-524 AND SER-680.
[23]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[24]"Distribution and function of FSH receptor genetic variants in normal men."
Asatiani K., Gromoll J., Eckardstein S.V., Zitzmann M., Nieschlag E., Simoni M.
Andrologia 34:172-176(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-307 AND SER-680.
[25]"A novel mutation in the FSH receptor inhibiting signal transduction and causing primary ovarian failure."
Doherty E., Pakarinen P., Tiitinen A., Kiilavuori A., Huhtaniemi I., Forrest S., Aittomaeki K.
J. Clin. Endocrinol. Metab. 87:1151-1155(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODG1 THR-419, CHARACTERIZATION OF VARIANT ODG1 THR-419.
[26]"A novel loss of function mutation in exon 10 of the FSH receptor gene causing hypergonadotrophic hypogonadism: clinical and molecular characteristics."
Allen L.A., Achermann J.C., Pakarinen P., Kotlar T.J., Huhtaniemi I.T., Jameson J.L., Cheetham T.D., Ball S.G.
Hum. Reprod. 18:251-256(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODG1 ARG-348.
[27]"Delayed puberty and primary amenorrhea associated with a novel mutation of the human follicle-stimulating hormone receptor: clinical, histological, and molecular studies."
Meduri G., Touraine P., Beau I., Lahuna O., Desroches A., Vacher-Lavenu M.C., Kuttenn F., Misrahi M.
J. Clin. Endocrinol. Metab. 88:3491-3498(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODG1 THR-519, CHARACTERIZATION OF VARIANT ODG1 THR-519.
[28]"A chorionic gonadotropin-sensitive mutation in the follicle-stimulating hormone receptor as a cause of familial gestational spontaneous ovarian hyperstimulation syndrome."
Vasseur C., Rodien P., Beau I., Desroches A., Gerard C., de Poncheville L., Chaplot S., Savagner F., Croue A., Mathieu E., Lahlou N., Descamps P., Misrahi M.
N. Engl. J. Med. 349:753-759(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHSS ILE-449.
[29]"Ovarian hyperstimulation syndrome due to a mutation in the follicle-stimulating hormone receptor."
Smits G., Olatunbosun O., Delbaere A., Pierson R., Vassart G., Costagliola S.
N. Engl. J. Med. 349:760-766(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHSS ASN-567.
[30]"A mutation in the follicle-stimulating hormone receptor as a cause of familial spontaneous ovarian hyperstimulation syndrome."
Montanelli L., Delbaere A., Di Carlo C., Nappi C., Smits G., Vassart G., Costagliola S.
J. Clin. Endocrinol. Metab. 89:1255-1258(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHSS ALA-449, CHARACTERIZATION OF VARIANT OHSS ALA-449.
[31]"Presence and absence of follicle-stimulating hormone receptor mutations provide some insights into spontaneous ovarian hyperstimulation syndrome physiopathology."
De Leener A., Montanelli L., Van Durme J., Chae H., Smits G., Vassart G., Costagliola S.
J. Clin. Endocrinol. Metab. 91:555-562(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHSS THR-545, CHARACTERIZATION OF VARIANT OHSS THR-545.
[32]"Identification of the first germline mutation in the extracellular domain of the follitropin receptor responsible for spontaneous ovarian hyperstimulation syndrome."
De Leener A., Caltabiano G., Erkan S., Idil M., Vassart G., Pardo L., Costagliola S.
Hum. Mutat. 29:91-98(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHSS TYR-128, CHARACTERIZATION OF VARIANT OHSS TYR-128.
+Additional computationally mapped references.

Web resources

GRIS

Glycoprotein-hormone Receptors Information System

SHMPD

The Singapore human mutation and polymorphism database

Sequence-structure-function-analysis of glycoprotein hormone receptors

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65085 mRNA. Translation: AAA52477.1.
M95489 mRNA. Translation: AAA52478.1.
S59900 mRNA. Translation: AAB26480.1.
JN003607 mRNA. Translation: AEI86722.1.
AY429104 mRNA. Translation: AAR07899.1.
AK292562 mRNA. Translation: BAF85251.1.
AC007189 Genomic DNA. No translation available.
AC079394 Genomic DNA. Translation: AAX93229.1.
AC092533 Genomic DNA. Translation: AAX88895.1.
CH471053 Genomic DNA. Translation: EAX00188.1.
CH471053 Genomic DNA. Translation: EAX00189.1.
BC096831 mRNA. Translation: AAH96831.1.
BC118548 mRNA. Translation: AAI18549.1.
BC125270 mRNA. Translation: AAI25271.1.
X68044 mRNA. Translation: CAA48179.1.
S73199 Genomic DNA. Translation: AAB32071.1.
S73526 Genomic DNA. Translation: AAB32225.1.
CCDSCCDS1843.1. [P23945-1]
CCDS1844.2. [P23945-3]
PIRQRHUFT. I57661.
RefSeqNP_000136.2. NM_000145.3.
NP_852111.2. NM_181446.2.
UniGeneHs.1428.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XUNmodel-A49-228[»]
1XWDX-ray2.92C/F17-268[»]
4AY9X-ray2.50X/Y/Z17-366[»]
4MQWX-ray2.90X/Y/Z16-366[»]
ProteinModelPortalP23945.
SMRP23945. Positions 18-359, 368-637.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108770. 15 interactions.
DIPDIP-35605N.
IntActP23945. 2 interactions.
MINTMINT-1177926.
STRING9606.ENSP00000384708.

Chemistry

BindingDBP23945.
ChEMBLCHEMBL2024.
DrugBankDB00097. Choriogonadotropin alfa.
DB00066. Follitropin beta.
DB00032. Menotropins.
DB00094. Urofollitropin.
GuidetoPHARMACOLOGY253.

Protein family/group databases

TCDB9.A.14.1.5. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP23945.

Polymorphism databases

DMDM311033420.

Proteomic databases

PaxDbP23945.
PRIDEP23945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304421; ENSP00000306780; ENSG00000170820.
GeneID2492.
KEGGhsa:2492.
UCSCuc002rwx.3. human.
uc010fbn.3. human. [P23945-3]

Organism-specific databases

CTD2492.
GeneCardsGC02M049189.
H-InvDBHIX0029905.
HGNCHGNC:3969. FSHR.
MIM136435. gene.
233300. phenotype.
608115. phenotype.
neXtProtNX_P23945.
Orphanet243. 46,XX gonadal dysgenesis.
64739. Ovarian hyperstimulation syndrome.
619. Primary ovarian failure.
PharmGKBPA28386.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285844.
HOGENOMHOG000045902.
HOVERGENHBG003521.
InParanoidP23945.
KOK04247.
PhylomeDBP23945.
TreeFamTF316814.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP23945.

Gene expression databases

ArrayExpressP23945.
BgeeP23945.
CleanExHS_FSHR.
GenevestigatorP23945.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR002272. FSH_rcpt.
IPR024635. GnHR_TM.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
[Graphical view]
PANTHERPTHR24372. PTHR24372. 1 hit.
PTHR24372:SF5. PTHR24372:SF5. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
PF12369. GnHR_trans. 1 hit.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PRINTSPR01143. FSHRECEPTOR.
PR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
SMARTSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23945.
GeneWikiFollicle-stimulating_hormone_receptor.
GenomeRNAi2492.
NextBio35518027.
PROP23945.
SOURCESearch...

Entry information

Entry nameFSHR_HUMAN
AccessionPrimary (citable) accession number: P23945
Secondary accession number(s): A8K947 expand/collapse secondary AC list , G5CBS7, G5E967, J3KQ00, Q05AH0, Q16225, Q4QRJ3, Q4ZFZ2, Q53RW2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 168 of the entry and version 3 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 2

Human chromosome 2: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries