INHBA

Protein-coding gene in the species Homo sapiens
INHBA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1NYS, 1NYU, 1S4Y, 2ARP, 2ARV, 2B0U, 2P6A, 3B4V, 4MID, 5HLY, 5HLZ

Identifiers
AliasesINHBA, EDF, FRP, inhibin beta A, inhibin beta A subunit, inhibin subunit beta A
External IDsOMIM: 147290 MGI: 96570 HomoloGene: 1653 GeneCards: INHBA
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for INHBA
Genomic location for INHBA
Band7p14.1Start41,667,168 bp[1]
End41,705,834 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for INHBA
Genomic location for INHBA
Band13 A1|13 5.85 cMStart16,186,436 bp[2]
End16,206,206 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • saphenous vein

  • vena cava

  • visceral pleura

  • stromal cell of endometrium

  • placenta

  • caput epididymis

  • lower lobe of lung

  • parotid gland

  • right coronary artery

  • Achilles tendon
Top expressed in
  • cumulus cell

  • incisor

  • nasopharynx

  • ascending aorta

  • rib

  • aortic valve

  • barrel cortex

  • right ventricle

  • calvaria

  • internal carotid artery
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transforming growth factor beta receptor binding
  • signaling receptor binding
  • hormone activity
  • identical protein binding
  • growth factor activity
  • cytokine activity
  • protein heterodimerization activity
  • type II activin receptor binding
  • peptide hormone binding
  • protein binding
  • inhibin binding
Cellular component
  • inhibin A complex
  • activin A complex
  • perinuclear region of cytoplasm
  • extracellular region
  • extracellular space
Biological process
  • negative regulation of cell population 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 by RNA polymerase II
  • negative regulation of phosphorylation
  • SMAD protein signal transduction
  • extrinsic apoptotic signaling pathway
  • 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 protein metabolic process
  • positive regulation of transcription, DNA-templated
  • hemoglobin biosynthetic process
  • roof of mouth development
  • positive regulation of erythrocyte differentiation
  • cellular response to follicle-stimulating hormone stimulus
  • regulation of MAPK cascade
  • cell development
  • positive regulation of transcription by RNA polymerase II
  • negative regulation of cell cycle
  • negative regulation of cell growth
  • cell differentiation
  • defense response
  • erythrocyte differentiation
  • male gonad development
  • regulation of follicle-stimulating hormone secretion
  • regulation of signaling 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
SpeciesHumanMouse
Entrez

3624

16323

Ensembl

ENSG00000122641

ENSMUSG00000041324

UniProt

P08476

Q04998

RefSeq (mRNA)

NM_002192

NM_008380

RefSeq (protein)

NP_002183
NP_002183.1

NP_032406

Location (UCSC)Chr 7: 41.67 – 41.71 MbChr 13: 16.19 – 16.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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 several fold 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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000122641 – Ensembl, May 2017
  2. ^ a b c 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.
  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)".
  7. ^ Lewis KA, 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. 404 (6776). ENGLAND: 411–4. Bibcode:2000Natur.404..411L. doi:10.1038/35006129. ISSN 0028-0836. PMID 10746731. S2CID 4393629.
  8. ^ Martens JW, 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. 138 (7). UNITED STATES: 2928–36. doi:10.1210/endo.138.7.5250. ISSN 0013-7227. PMID 9202237.

Further reading

  • 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/mend.8.3.8015550. PMID 8015550. S2CID 7615672.
  • 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.
  • v
  • t
  • e
TGFβ receptor superfamily modulators
Type I
ALK1 (ACVRL1)
  • Kinase inhibitors: K-02288
  • ML-347 (LDN-193719, VU0469381)
  • Other inhibitors: Disitertide
ALK2 (ACVR1A)
  • Kinase inhibitors: DMH-1
  • DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
  • ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK4 (ACVR1B)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
ALK5 (TGFβR1)
ALK6 (BMPR1B)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK7 (ACVR1C)
  • Antagonists: Lefty (1, 2)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
Type II
TGFβR2
  • Kinase inhibitors: DMH-2
  • LY-364947
BMPR2
ACVR2A (ACVR2)
ACVR2B
  • Decoy receptors: Ramatercept
AMHR2 (AMHR)
Type III
TGFβR3 (β-glycan)
Unsorted
  • v
  • t
  • e
  • 1nys: Crystal Structure of Activin A Bound to the ECD of ActRIIB P41
    1nys: Crystal Structure of Activin A Bound to the ECD of ActRIIB P41
  • 1nyu: Crystal Structure of Activin A Bound to the ECD of ActRIIB
    1nyu: Crystal Structure of Activin A Bound to the ECD of ActRIIB
  • 1s4y: Crystal structure of the activin/actrIIb extracellular domain
    1s4y: Crystal structure of the activin/actrIIb extracellular domain
  • 2arp: Activin A in complex with Fs12 fragment of follistatin
    2arp: Activin A in complex with Fs12 fragment of follistatin
  • 2arv: Structure of human Activin A
    2arv: Structure of human Activin A
  • 2b0u: The Structure of the Follistatin:Activin Complex
    2b0u: The Structure of the Follistatin:Activin Complex
  • 2p6a: The structure of the Activin:Follistatin 315 complex
    2p6a: The structure of the Activin:Follistatin 315 complex