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Protein

Glycoprotein hormones alpha chain

Gene

CGA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. hormone activity Source: AgBase

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. cellular protein metabolic process Source: Reactome
  3. peptide hormone processing Source: Reactome
  4. positive regulation of cell migration Source: BHF-UCL
  5. positive regulation of cell proliferation Source: BHF-UCL
  6. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  7. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_11047. Mineralocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
REACT_15292. Thyroxine biosynthesis.
REACT_15398. Glycoprotein hormones.
REACT_16942. Hormone ligand-binding receptors.
REACT_19327. G alpha (s) signalling events.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:1885. CGA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26433.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24244 PublicationsAdd
BLAST
Chaini25 – 11692Glycoprotein hormones alpha chainPRO_0000011640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 552 Publications
Disulfide bondi34 ↔ 842 Publications
Disulfide bondi52 ↔ 1062 Publications
Disulfide bondi56 ↔ 1082 Publications
Glycosylationi76 – 761N-linked (GlcNAc...)1 PublicationCAR_000036
Disulfide bondi83 ↔ 1112 Publications
Glycosylationi102 – 1021N-linked (GlcNAc...)1 PublicationCAR_000037

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01215.
PaxDbiP01215.
PRIDEiP01215.

PTM databases

PhosphoSiteiP01215.
UniCarbKBiP01215.

Expressioni

Gene expression databases

BgeeiP01215.
CleanExiHS_CGA.
ExpressionAtlasiP01215. baseline and differential.
GenevestigatoriP01215.

Organism-specific databases

HPAiCAB023350.
HPA029698.

Interactioni

Subunit structurei

Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FSHBP012252EBI-718913,EBI-1030645

Protein-protein interaction databases

BioGridi107507. 5 interactions.
DIPiDIP-6182N.
IntActiP01215. 3 interactions.
MINTiMINT-1197885.
STRINGi9606.ENSP00000358595.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386Combined sources
Turni40 – 423Combined sources
Beta strandi50 – 6213Combined sources
Helixi65 – 684Combined sources
Beta strandi76 – 805Combined sources
Beta strandi83 – 9412Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 10912Combined sources
Beta strandi112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4MQWX-ray2.90A/D/G25-116[»]
ProteinModelPortaliP01215.
SMRiP01215. Positions 29-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01215.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG44826.
HOGENOMiHOG000232008.
HOVERGENiHBG000452.
InParanoidiP01215.
KOiK08522.
OMAiDGEFTMQ.
OrthoDBiEOG73FQPJ.
PhylomeDBiP01215.
TreeFamiTF332733.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000476. Glyco_hormone.
[Graphical view]
PANTHERiPTHR11509. PTHR11509. 1 hit.
PfamiPF00236. Hormone_6. 1 hit.
[Graphical view]
PRINTSiPR00274. GLYCOHORMONE.
SMARTiSM00067. GHA. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00779. GLYCO_HORMONE_ALPHA_1. 1 hit.
PS00780. GLYCO_HORMONE_ALPHA_2. 1 hit.
PS50277. GLYCO_HORMONE_ALPHA_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYYRKYAAI FLVTLSVFLH VLHSAPDVQD CPECTLQENP FFSQPGAPIL
60 70 80 90 100
QCMGCCFSRA YPTPLRSKKT MLVQKNVTSE STCCVAKSYN RVTVMGGFKV
110
ENHTACHCST CYYHKS
Length:116
Mass (Da):13,075
Last modified:July 21, 1986 - v1
Checksum:iF0623CD8CC90CFCD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291Q → E AA sequence (PubMed:1158880).Curated
Sequence conflicti108 – 1092CS → SC AA sequence (PubMed:890569).Curated
Sequence conflicti108 – 1092CS → SC AA sequence (PubMed:5065401).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5007.1.
PIRiA93213. TTHUAP.
RefSeqiNP_000726.1. NM_000735.3.
NP_001239312.1. NM_001252383.1.
UniGeneiHs.119689.

Genome annotation databases

EnsembliENST00000369582; ENSP00000358595; ENSG00000135346.
GeneIDi1081.
KEGGihsa:1081.
UCSCiuc003plj.2. human.

Polymorphism databases

DMDMi121312.

Cross-referencesi

Web resourcesi

Protein Spotlight

Proteic grace - Issue 77 of December 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5007.1.
PIRiA93213. TTHUAP.
RefSeqiNP_000726.1. NM_000735.3.
NP_001239312.1. NM_001252383.1.
UniGeneiHs.119689.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4MQWX-ray2.90A/D/G25-116[»]
ProteinModelPortaliP01215.
SMRiP01215. Positions 29-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107507. 5 interactions.
DIPiDIP-6182N.
IntActiP01215. 3 interactions.
MINTiMINT-1197885.
STRINGi9606.ENSP00000358595.

Chemistry

ChEMBLiCHEMBL2146305.

PTM databases

PhosphoSiteiP01215.
UniCarbKBiP01215.

Polymorphism databases

DMDMi121312.

Proteomic databases

MaxQBiP01215.
PaxDbiP01215.
PRIDEiP01215.

Protocols and materials databases

DNASUi1081.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369582; ENSP00000358595; ENSG00000135346.
GeneIDi1081.
KEGGihsa:1081.
UCSCiuc003plj.2. human.

Organism-specific databases

CTDi1081.
GeneCardsiGC06M087795.
HGNCiHGNC:1885. CGA.
HPAiCAB023350.
HPA029698.
MIMi118850. gene.
neXtProtiNX_P01215.
PharmGKBiPA26433.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44826.
HOGENOMiHOG000232008.
HOVERGENiHBG000452.
InParanoidiP01215.
KOiK08522.
OMAiDGEFTMQ.
OrthoDBiEOG73FQPJ.
PhylomeDBiP01215.
TreeFamiTF332733.

Enzyme and pathway databases

ReactomeiREACT_11047. Mineralocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
REACT_15292. Thyroxine biosynthesis.
REACT_15398. Glycoprotein hormones.
REACT_16942. Hormone ligand-binding receptors.
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiCGA. human.
EvolutionaryTraceiP01215.
GeneWikiiChorionic_gonadotropin_alpha.
GenomeRNAii1081.
NextBioi4504.
PROiP01215.
SOURCEiSearch...

Gene expression databases

BgeeiP01215.
CleanExiHS_CGA.
ExpressionAtlasiP01215. baseline and differential.
GenevestigatoriP01215.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000476. Glyco_hormone.
[Graphical view]
PANTHERiPTHR11509. PTHR11509. 1 hit.
PfamiPF00236. Hormone_6. 1 hit.
[Graphical view]
PRINTSiPR00274. GLYCOHORMONE.
SMARTiSM00067. GHA. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00779. GLYCO_HORMONE_ALPHA_1. 1 hit.
PS00780. GLYCO_HORMONE_ALPHA_2. 1 hit.
PS50277. GLYCO_HORMONE_ALPHA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGLHA_HUMAN
AccessioniPrimary (citable) accession number: P01215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 4, 2015
This is version 161 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.