INHBA

INHBA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1NYS, 1NYU, 1S4Y, 2ARP, 2ARV, 2B0U, 2P6A, 3B4V, 4MID, 5HLY, 5HLZ
Identifiers
Aliases	INHBA, EDF, FRP, inhibin beta A, inhibin beta A subunit, inhibin subunit beta A
External IDs	OMIM: 147290 MGI: 96570 HomoloGene: 1653 GeneCards: INHBA
Gene location (Human)
Chr.	Chromosome 7 (human)[1]
End	41,705,834 bp[1]
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)[2]
End	16,031,621 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• transforming growth factor beta receptor binding; • receptor binding; • hormone activity; • identical protein binding; • growth factor activity; • cytokine activity; • protein heterodimerization activity; • type II activin receptor binding; • peptide hormone binding; • GO:0001948 protein binding; • inhibin binding;
Cellular component	• inhibin A complex; • activin A complex; • perinuclear region of cytoplasm; • extracellular region; • extracellular;
Biological process	• negative regulation of cell proliferation; • eyelid development in camera-type eye; • endodermal cell differentiation; • negative regulation of follicle-stimulating hormone secretion; • GABAergic neuron differentiation; • cell-cell signaling; • progesterone secretion; • mesodermal cell differentiation; • negative regulation of macrophage differentiation; • odontogenesis; • hair follicle development; • hematopoietic progenitor cell differentiation; • regulation of transcription from RNA polymerase II promoter; • negative regulation of phosphorylation; • SMAD protein signal transduction; • extrinsic apoptotic signaling pathway; • cell cycle arrest; • positive regulation of follicle-stimulating hormone secretion; • cell surface receptor signaling pathway; • positive regulation of pathway-restricted SMAD protein phosphorylation; • nervous system development; • positive regulation of ovulation; • positive regulation of gene expression; • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; • cellular response to cholesterol; • mesoderm formation; • activin receptor signaling pathway; • negative regulation of B cell differentiation; • ovarian follicle development; • striatal medium spiny neuron differentiation; • positive regulation of cellular protein metabolic process; • positive regulation of transcription, DNA-templated; • hemoglobin biosynthetic process; • palate development; • positive regulation of erythrocyte differentiation; • cellular response to follicle-stimulating hormone stimulus; • regulation of MAPK cascade; • cell development; • positive regulation of transcription from RNA polymerase II promoter; • negative regulation of cell cycle; • negative regulation of cell growth; • response to drug; • cell differentiation; • defense response; • erythrocyte differentiation; • male gonad development; • regulation of follicle-stimulating hormone secretion; • regulation of receptor activity; • G1/S transition of mitotic cell cycle; • response to wounding; • regulation of apoptotic process; • negative regulation of hair follicle development; • signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	3624
	16323
	ENSG00000122641
	ENSMUSG00000041324
	P08476
	Q04998
	NM_002192
	NM_008380
	NP_002183; NP_002183.1
	NP_032406
	Wikidata
View/Edit Human	View/Edit Mouse

Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene.[5] INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

Function

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.[6]

Interactions

INHBA has been shown to interact with ACVR2A.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000122641 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000041324 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Burger HG, Igarashi M (April 1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
"Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)".
Lewis, K A; Gray P C; Blount A L; MacConell L A; Wiater E; Bilezikjian L M; Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. ENGLAND. 404 (6776): 411–4. doi:10.1038/35006129. ISSN 0028-0836. PMID 10746731. S2CID 4393629.
Martens, J W; de Winter J P; Timmerman M A; McLuskey A; van Schaik R H; Themmen A P; de Jong F H (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells" (PDF). Endocrinology. UNITED STATES. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. ISSN 0013-7227. PMID 9202237.

Munz B, Hübner G, Tretter Y, et al. (1999). "A novel role of activin in inflammation and repair". J. Endocrinol. 161 (2): 187–93. doi:10.1677/joe.0.1610187. PMID 10320815.
Welt C, Sidis Y, Keutmann H, Schneyer A (2002). "Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium". Exp. Biol. Med. (Maywood). 227 (9): 724–52. doi:10.1177/153537020222700905. PMID 12324653. S2CID 19795772.
Shav-Tal Y, Zipori D (2003). "The role of activin a in regulation of hemopoiesis". Stem Cells. 20 (6): 493–500. doi:10.1634/stemcells.20-6-493. PMID 12456957. S2CID 36242096.
Reis FM, Luisi S, Carneiro MM, et al. (2005). "Activin, inhibin and the human breast". Mol. Cell. Endocrinol. 225 (1–2): 77–82. doi:10.1016/j.mce.2004.02.016. PMID 15451571. S2CID 24201803.
Shao L, Frigon NL, Young AL, et al. (1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773–81. doi:10.1182/blood.V79.3.773.bloodjournal793773. PMID 1310063.
Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6): 973–82. doi:10.1016/0092-8674(91)90549-E. PMID 1646080. S2CID 36407277.
Tanimoto K, Handa S, Ueno N, et al. (1992). "Structure and sequence analysis of the human activin beta A subunit gene". DNA Seq. 2 (2): 103–10. doi:10.3109/10425179109039678. PMID 1777673.
Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH (1990). "Activin B: precursor sequences, genomic structure and in vitro activities". Mol. Endocrinol. 3 (9): 1352–8. doi:10.1210/mend-3-9-1352. PMID 2575216.
Barton DE, Yang-Feng TL, Mason AJ, et al. (1989). "Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice". Genomics. 5 (1): 91–9. doi:10.1016/0888-7543(89)90091-8. PMID 2767687.
Murata M, Eto Y, Shibai H, et al. (1988). "Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain". Proc. Natl. Acad. Sci. U.S.A. 85 (8): 2434–8. Bibcode:1988PNAS...85.2434M. doi:10.1073/pnas.85.8.2434. PMC 280011. PMID 3267209.
Burger HG, Igarashi M (1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
Mason AJ, Niall HD, Seeburg PH (1986). "Structure of two human ovarian inhibins". Biochem. Biophys. Res. Commun. 135 (3): 957–64. doi:10.1016/0006-291X(86)91021-1. PMID 3754442.
Stewart AG, Milborrow HM, Ring JM, et al. (1986). "Human inhibin genes. Genomic characterisation and sequencing". FEBS Lett. 206 (2): 329–34. doi:10.1016/0014-5793(86)81006-7. PMID 3758355. S2CID 21261385.
Sumitomo S, Inouye S, Liu XJ, et al. (1995). "The heparin binding site of follistatin is involved in its interaction with activin". Biochem. Biophys. Res. Commun. 208 (1): 1–9. doi:10.1006/bbrc.1995.1297. PMID 7887917.
Xu J, McKeehan K, Matsuzaki K, McKeehan WL (1995). "Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism". J. Biol. Chem. 270 (11): 6308–6313. doi:10.1074/jbc.270.11.6308. PMID 7890768.
Mason AJ (1994). "Functional analysis of the cysteine residues of activin A". Mol. Endocrinol. 8 (3): 325–32. doi:10.1210/me.8.3.325. PMID 8015550.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Nishihara T, Okahashi N, Ueda N (1994). "Activin A induces apoptotic cell death". Biochem. Biophys. Res. Commun. 197 (2): 985–91. doi:10.1006/bbrc.1993.2576. PMID 8267637.
ten Dijke P, Ichijo H, Franzén P, et al. (1993). "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". Oncogene. 8 (10): 2879–87. PMID 8397373.
Tanimoto K, Yoshida E, Mita S, et al. (1997). "Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers". J. Biol. Chem. 271 (51): 32760–9. doi:10.1074/jbc.271.51.32760. PMID 8955111.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000122641 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000041324 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid3345731-5] Burger HG, Igarashi M (April 1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.

[6] "Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)".

[pmid10746731-7] Lewis, K A; Gray P C; Blount A L; MacConell L A; Wiater E; Bilezikjian L M; Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. ENGLAND. 404 (6776): 411–4. doi:10.1038/35006129. ISSN 0028-0836. PMID 10746731. S2CID 4393629.

[pmid9202237-8] Martens, J W; de Winter J P; Timmerman M A; McLuskey A; van Schaik R H; Themmen A P; de Jong F H (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells" (PDF). Endocrinology. UNITED STATES. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. ISSN 0013-7227. PMID 9202237.

INHBA

Function

Interactions

References

Further reading