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P01215 (GLHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 151. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycoprotein hormones alpha chain
Alternative name(s):
Anterior pituitary glycoprotein hormones common subunit alpha
Choriogonadotropin alpha chain
Chorionic gonadotrophin subunit alpha
Short name=CG-alpha
Follicle-stimulating hormone alpha chain
Short name=FSH-alpha
Follitropin alpha chain
Luteinizing hormone alpha chain
Short name=LSH-alpha
Lutropin alpha chain
Thyroid-stimulating hormone alpha chain
Short name=TSH-alpha
Thyrotropin alpha chain
Gene names
Name:CGA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycoprotein hormones subunit alpha family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

developmental growth

Inferred from electronic annotation. Source: Ensembl

follicle-stimulating hormone secretion

Inferred from electronic annotation. Source: Ensembl

gonad development

Inferred from electronic annotation. Source: Ensembl

luteinizing hormone secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

peptide hormone processing

Traceable author statement. Source: Reactome

positive regulation of cell migration

Non-traceable author statement PubMed 20613903. Source: BHF-UCL

positive regulation of cell proliferation

Non-traceable author statement PubMed 20613903. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Non-traceable author statement PubMed 20613903. Source: BHF-UCL

signal transduction

Traceable author statement Ref.1. Source: ProtInc

thyroid gland development

Inferred from electronic annotation. Source: Ensembl

thyroid hormone generation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

   Molecular_functionhormone activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FSHBP012252EBI-718913,EBI-1030645

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1 Ref.9 Ref.11 Ref.12
Chain25 – 11692Glycoprotein hormones alpha chain
PRO_0000011640

Amino acid modifications

Glycosylation761N-linked (GlcNAc...) Ref.18
CAR_000036
Glycosylation1021N-linked (GlcNAc...) Ref.18
CAR_000037
Disulfide bond31 ↔ 55 Ref.13 Ref.14 Ref.16 Ref.18
Disulfide bond34 ↔ 84 Ref.13 Ref.14 Ref.16 Ref.18
Disulfide bond52 ↔ 106 Ref.13 Ref.14 Ref.16 Ref.18
Disulfide bond56 ↔ 108 Ref.13 Ref.14 Ref.16 Ref.18
Disulfide bond83 ↔ 111 Ref.13 Ref.14 Ref.16 Ref.18

Experimental info

Sequence conflict291Q → E AA sequence Ref.9
Sequence conflict108 – 1092CS → SC AA sequence Ref.6
Sequence conflict108 – 1092CS → SC AA sequence Ref.7

Secondary structure

................. 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01215 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F0623CD8CC90CFCD

FASTA11613,075
        10         20         30         40         50         60 
MDYYRKYAAI FLVTLSVFLH VLHSAPDVQD CPECTLQENP FFSQPGAPIL QCMGCCFSRA 

        70         80         90        100        110 
YPTPLRSKKT MLVQKNVTSE STCCVAKSYN RVTVMGGFKV ENHTACHCST CYYHKS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit of human chorionic gonadotropin."
Fiddes J.C., Goodman H.M.
Nature 281:351-356(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and regulation of human thyroid-stimulating hormone (TSH) gene."
Miyoshi I., Kasai N., Hayashizaki Y.
Nippon Rinsho 52:940-947(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Placenta.
[4]"The gene encoding the common alpha subunit of the four human glycoprotein hormones."
Fiddes J.C., Goodman H.M.
J. Mol. Appl. Genet. 1:3-18(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
[5]"The amino acid sequences of the prepeptides contained in the alpha and beta subunits of human choriogonadotropin."
Birken S., Fetherston J., Canfield R.E., Boime I.
J. Biol. Chem. 256:1816-1823(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-24.
[6]"Human pituitary thyrotropin. The primary structure of the alpha and beta subunits."
Sairam M.R., Li C.H.
Can. J. Biochem. 55:755-760(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-116.
[7]"Human pituitary interstitial cell stimulating hormone: primary structure of the alpha-subunit."
Sairam M.R., Papkoff H., Li C.H.
Biochem. Biophys. Res. Commun. 48:530-537(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-116.
[8]"Structure of human luteninizing hormone."
Keutmann H.T., Williams R.M., Bishop W.H., Ryan R.J.
Fed. Proc. 37:1828-1828(1978)
Cited for: PROTEIN SEQUENCE, SEQUENCE REVISION.
[9]"Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit."
Rathnam P., Saxena B.B.
J. Biol. Chem. 250:6735-6746(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-116.
Tissue: Pituitary.
[10]"Human follicle stimulating hormone (hFSH): first proposal for the amino acid sequence of the alpha-subunit (hFSHa) and first demonstration of its identity with the alpha-subunit of human luteinizing hormone (hLHa)."
Shome B., Parlow A.F.
J. Clin. Endocrinol. Metab. 39:199-202(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-116.
[11]"The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit."
Morgan F.J., Birken S., Canfield R.E.
J. Biol. Chem. 250:5247-5258(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-116.
[12]"Human chorionic gonadotropin. Linear amino acid sequence of the alpha subunit."
Bellisario R., Carlsen R.B., Bahl O.P.
J. Biol. Chem. 248:6796-6809(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-116.
[13]"Studies on the disulfide bonds in human pituitary follicle-stimulating hormone."
Fujiki Y., Rathnam P., Saxena B.B.
Biochim. Biophys. Acta 624:428-435(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
[14]"Assignment of disulfide bonds in the alpha subunit of human chorionic gonadotropin."
Mise T., Bahl O.P.
J. Biol. Chem. 255:8516-8522(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
[15]"NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin."
Weisshaar G., Hiyama J., Renwick A.G.C., Nimtz M.
Eur. J. Biochem. 195:257-268(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[16]"Crystal structure of human chorionic gonadotropin."
Lapthorn A.J., Harris D.C., Littlejohn A., Lustbader J.W., Canfield R.E., Machin K.J., Morgan F.J., Isaacs N.W.
Nature 369:455-461(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[17]"NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit."
de Beer T., van Zuylen C.W.E.M., Leeflang B.R., Haard K., Boelens R., Kaptein R., Kamerling J.P., Vliegenthart J.F.G.
Eur. J. Biochem. 241:229-242(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[18]"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 25-116 IN COMPLEX WITH FSHB AND FSHR, DISULFIDE BONDS, GLYCOSYLATION AT ASN-76 AND ASN-102.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Proteic grace - Issue 77 of December 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00152, J00150, J00151 Genomic DNA. Translation: AAD13690.1.
S70585, S70583, S70584 Genomic DNA. Translation: AAB30827.1.
BC020782 mRNA. Translation: AAH20782.1.
BC055080 mRNA. Translation: AAH55080.1.
V00518 mRNA. Translation: CAA23777.1.
PIRTTHUAP. A93213.
RefSeqNP_000726.1. NM_000735.3.
NP_001239312.1. NM_001252383.1.
UniGeneHs.119689.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZ7NMR-A25-116[»]
1E9JNMR-A25-116[»]
1FL7X-ray3.00A/C25-116[»]
1HCNX-ray2.60A25-116[»]
1HD4NMR-A25-116[»]
1HRPX-ray3.00A25-116[»]
1QFWX-ray3.50A25-116[»]
1XULmodel-A25-116[»]
1XWDX-ray2.92A/D25-116[»]
4AY9X-ray2.50A/D/G25-116[»]
ProteinModelPortalP01215.
SMRP01215. Positions 27-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107507. 5 interactions.
DIPDIP-6182N.
IntActP01215. 3 interactions.
MINTMINT-1197885.
STRING9606.ENSP00000358595.

Chemistry

ChEMBLCHEMBL2146305.

PTM databases

PhosphoSiteP01215.
UniCarbKBP01215.

Polymorphism databases

DMDM121312.

Proteomic databases

PaxDbP01215.
PRIDEP01215.

Protocols and materials databases

DNASU1081.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369582; ENSP00000358595; ENSG00000135346.
GeneID1081.
KEGGhsa:1081.
UCSCuc003plj.2. human.

Organism-specific databases

CTD1081.
GeneCardsGC06M087795.
HGNCHGNC:1885. CGA.
HPACAB023350.
HPA029698.
MIM118850. gene.
neXtProtNX_P01215.
PharmGKBPA26433.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44826.
HOGENOMHOG000232008.
HOVERGENHBG000452.
InParanoidP01215.
KOK08522.
OMATCCVAKS.
OrthoDBEOG73FQPJ.
PhylomeDBP01215.
TreeFamTF332733.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP01215.
BgeeP01215.
CleanExHS_CGA.
GenevestigatorP01215.

Family and domain databases

InterProIPR000476. Glyco_hormone.
[Graphical view]
PANTHERPTHR11509. PTHR11509. 1 hit.
PfamPF00236. Hormone_6. 1 hit.
[Graphical view]
PRINTSPR00274. GLYCOHORMONE.
SMARTSM00067. GHA. 1 hit.
[Graphical view]
PROSITEPS00779. GLYCO_HORMONE_ALPHA_1. 1 hit.
PS00780. GLYCO_HORMONE_ALPHA_2. 1 hit.
PS50277. GLYCO_HORMONE_ALPHA_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCGA. human.
EvolutionaryTraceP01215.
GeneWikiChorionic_gonadotropin_alpha.
GenomeRNAi1081.
NextBio4504.
PROP01215.
SOURCESearch...

Entry information

Entry nameGLHA_HUMAN
AccessionPrimary (citable) accession number: P01215
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 151 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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 chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM