P01215 (GLHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CGA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	116 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-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: Compara developmental growth Inferred from electronic annotation. Source: Compara follicle-stimulating hormone secretion Inferred from electronic annotation. Source: Compara gonad development Inferred from electronic annotation. Source: Compara luteinizing hormone secretion Inferred from electronic annotation. Source: Compara negative regulation of organ growth Inferred from electronic annotation. Source: Compara 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: Compara thyroid hormone generation Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	hormone activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FSHB	P01225	2	EBI-718913,EBI-1030645

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.1 Ref.9 Ref.11 Ref.12

Chain

25 – 116

92

Glycoprotein hormones alpha chain

PRO_0000011640

Amino acid modifications

Glycosylation

76

1

N-linked (GlcNAc...) Ref.18

CAR_000036

Glycosylation

102

1

N-linked (GlcNAc...) Ref.18

CAR_000037

Disulfide bond

31 ↔ 55

Ref.13 Ref.14 Ref.16 Ref.18

Disulfide bond

34 ↔ 84

Ref.13 Ref.14 Ref.16 Ref.18

Disulfide bond

52 ↔ 106

Ref.13 Ref.14 Ref.16 Ref.18

Disulfide bond

56 ↔ 108

Ref.13 Ref.14 Ref.16 Ref.18

Disulfide bond

83 ↔ 111

Ref.13 Ref.14 Ref.16 Ref.18

Experimental info

Sequence conflict

29

1

Q → E AA sequence Ref.9

Sequence conflict

108 – 109

2

CS → SC AA sequence Ref.6

Sequence conflict

108 – 109

2

CS → SC AA sequence Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

116

Helix Strand Turn

Details...

Beta strand

33 – 38

6

Turn

40 – 42

3

Beta strand

50 – 62

13

Helix

65 – 68

4

Beta strand

76 – 80

5

Beta strand

83 – 94

12

Turn

95 – 97

3

Beta strand

98 – 109

12

Beta strand

112 – 114

3

Sequences

	Sequence		Length	Mass (Da)
	P01215 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: F0623CD8CC90CFCD	FASTA	116	13,075
	10 20 30 40 50 60 MDYYRKYAAI FLVTLSVFLH VLHSAPDVQD CPECTLQENP FFSQPGAPIL QCMGCCFSRA 70 80 90 100 110 YPTPLRSKKT MLVQKNVTSE STCCVAKSYN RVTVMGGFKV ENHTACHCST CYYHKS

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00000833.

PIR

TTHUAP. A93213.

RefSeq

NP_000726.1. NM_000735.3.
NP_001239312.1. NM_001252383.1.

UniGene

Hs.119689.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DZ7	NMR	-	A	25-116	[»]
1E9J	NMR	-	A	25-116	[»]
1FL7	X-ray	3.00	A/C	25-116	[»]
1HCN	X-ray	2.60	A	25-116	[»]
1HD4	NMR	-	A	25-116	[»]
1HRP	X-ray	3.00	A	25-116	[»]
1QFW	X-ray	3.50	A	25-116	[»]
1XUL	model	-	A	25-116	[»]
1XWD	X-ray	2.92	A/D	25-116	[»]
4AY9	X-ray	2.50	A/D/G	25-116	[»]

ProteinModelPortal

P01215.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6182N.

IntAct

P01215. 2 interactions.

MINT

MINT-1197885.

STRING

9606.ENSP00000358595.

PTM databases

GlycoSuiteDB

P01215.

PhosphoSite

P01215.

Polymorphism databases

DMDM

121312.

Proteomic databases

PaxDb

P01215.

PRIDE

P01215.

Protocols and materials databases

DNASU

1081.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369582; ENSP00000358595; ENSG00000135346.

GeneID

1081.

KEGG

hsa:1081.

UCSC

uc003plj.2. human.

Organism-specific databases

CTD

1081.

GeneCards

GC06M087795.

HGNC

HGNC:1885. CGA.

HPA

CAB023350.

MIM

118850. gene.

neXtProt

NX_P01215.

PharmGKB

PA26433.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44826.

HOGENOM

HOG000232008.

HOVERGEN

HBG000452.

InParanoid

P01215.

KO

K08522.

OMA

TCCVAKS.

OrthoDB

EOG4G7C11.

PhylomeDB

P01215.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P01215.

Bgee

P01215.

CleanEx

HS_CGA.

Genevestigator

P01215.

GermOnline

ENSG00000135346. Homo sapiens.

Family and domain databases

InterPro

IPR000476. Glyco_hormone.
[Graphical view]

PANTHER

PTHR11509. PTHR11509. 1 hit.

Pfam

PF00236. Hormone_6. 1 hit.
[Graphical view]

PRINTS

PR00274. GLYCOHORMONE.

SMART

SM00067. GHA. 1 hit.
[Graphical view]

PROSITE

PS00779. GLYCO_HORMONE_ALPHA_1. 1 hit.
PS00780. GLYCO_HORMONE_ALPHA_2. 1 hit.
PS50277. GLYCO_HORMONE_ALPHA_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CGA. human.

EvolutionaryTrace

P01215.

GenomeRNAi

1081.

NextBio

4504.

SOURCE

Search...

Entry information

Entry name

GLHA_HUMAN

Accession

Primary (citable) accession number: P01215

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 29, 2013
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.