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P08476 (INHBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Inhibin beta A chain
Alternative name(s):
Activin beta-A chain
Erythroid differentiation protein
Short name=EDF
Gene names
Name:INHBA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.

Subunit structure

Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3. Ref.8

Subcellular location

Secreted.

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGrowth factor
Hormone
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 9884026. Source: HGNC

activin receptor signaling pathway

Inferred from direct assay PubMed 9884026. Source: BHF-UCL

cell cycle arrest

Inferred from direct assay PubMed 9884026. Source: HGNC

cell differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

cell surface receptor signaling pathway

Traceable author statement PubMed 12456957. Source: UniProtKB

cell-cell signaling

Traceable author statement PubMed 12456957. Source: UniProtKB

cellular response to cholesterol

Inferred from electronic annotation. Source: Ensembl

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Ensembl

defense response

Traceable author statement PubMed 12456957. Source: UniProtKB

erythrocyte differentiation

Non-traceable author statement PubMed 1310063. Source: UniProtKB

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 9884026. Source: BHF-UCL

eyelid development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

growth

Inferred from electronic annotation. Source: InterPro

hair follicle development

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

hematopoietic progenitor cell differentiation

Inferred from direct assay PubMed 15451575. Source: UniProtKB

hemoglobin biosynthetic process

Inferred from direct assay PubMed 1310063. Source: UniProtKB

male gonad development

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

mesodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of B cell differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of cell cycle

Inferred from direct assay PubMed 9884026. Source: HGNC

negative regulation of cell growth

Inferred from direct assay PubMed 20573232. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 11948405. Source: UniProtKB

negative regulation of follicle-stimulating hormone secretion

Non-traceable author statement Ref.2. Source: UniProtKB

negative regulation of interferon-gamma biosynthetic process

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of macrophage differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of phosphorylation

Traceable author statement PubMed 12456957. Source: UniProtKB

nervous system development

Non-traceable author statement PubMed 10320815. Source: UniProtKB

odontogenesis

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

ovarian follicle development

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

palate development

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

positive regulation of erythrocyte differentiation

Inferred from direct assay PubMed 9032295. Source: HGNC

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay PubMed 8267637. Source: UniProtKB

positive regulation of follicle-stimulating hormone secretion

Traceable author statement PubMed 12456957. Source: UniProtKB

positive regulation of ovulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 19736306. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12702211PubMed 21281489. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 21281489. Source: UniProtKB

progesterone secretion

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

regulation of follicle-stimulating hormone secretion

Inferred from genetic interaction PubMed 10932194. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11948405. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 20573232. Source: UniProtKB

   Cellular_componentactivin A complex

Inferred from direct assay PubMed 7890768. Source: HGNC

extracellular region

Inferred from direct assay PubMed 12213882. Source: UniProtKB

inhibin A complex

Inferred from direct assay PubMed 7890768. Source: HGNC

   Molecular_functioncytokine activity

Inferred from direct assay PubMed 9884026. Source: HGNC

growth factor activity

Traceable author statement PubMed 12324653. Source: UniProtKB

hormone activity

Traceable author statement PubMed 12456957. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 2575216. Source: UniProtKB

peptide hormone binding

Inferred from physical interaction PubMed 16198295. Source: UniProtKB

type II activin receptor binding

Inferred from physical interaction PubMed 7890768. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FstP216742EBI-8077140,EBI-5746973From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 310290
PRO_0000033708
Chain311 – 426116Inhibin beta A chain
PRO_0000033709

Amino acid modifications

Glycosylation1651N-linked (GlcNAc...) Potential
Disulfide bond314 ↔ 322 Ref.10
Disulfide bond321 ↔ 391 Ref.10
Disulfide bond350 ↔ 423 Ref.10
Disulfide bond354 ↔ 425 Ref.10
Disulfide bond390Interchain Ref.10

Natural variations

Natural variant2991Q → P.
Corresponds to variant rs41294833 [ dbSNP | Ensembl ].
VAR_052566

Experimental info

Sequence conflict377 – 3793RMR → AC in CAA51163. Ref.7

Secondary structure

............................. 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08476 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 201CDEDF99CB6919

FASTA42647,442
        10         20         30         40         50         60 
MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL AALPKDVPNS QPEMVEAVKK 

        70         80         90        100        110        120 
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT 

       130        140        150        160        170        180 
SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK 

       190        200        210        220        230        240 
HPQGSLDTGE EAEEVGLKGE RSELLLSEKV VDARKSTWHV FPVSSSIQRL LDQGKSSLDV 

       250        260        270        280        290        300 
RIACEQCQES GASLVLLGKK KKKEEEGEGK KKGGGEGGAG ADEEKEQSHR PFLMLQARQS 

       310        320        330        340        350        360 
EDHPHRRRRR GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG 

       370        380        390        400        410        420 
TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV 


EECGCS 

« Hide

References

« Hide 'large scale' references
[1]"Structure of two human ovarian inhibins."
Mason A.J., Niall H.D., Seeburg P.H.
Biochem. Biophys. Res. Commun. 135:957-964(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain."
Murata M., Eto Y., Shibai H., Sakai M., Muramatsu M.
Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure and sequence analysis of the human activin beta A subunit gene."
Tanimoto K., Handa S.I., Ueno N., Murakami K., Fukamizu A.
DNA Seq. 2:103-110(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Eye.
[6]"Human inhibin genes. Genomic characterisation and sequencing."
Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.
FEBS Lett. 206:329-334(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-426.
[7]Berg H., Walter M., Northemann W.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 311-426.
Tissue: Testis.
[8]"Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)."
Schneyer A., Schoen A., Quigg A., Sidis Y.
Endocrinology 144:1671-1674(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FST AND FSTL3.
[9]"Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions."
Thompson T.B., Woodruff T.K., Jardetzky T.S.
EMBO J. 22:1555-1566(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH RAT ACTRIIB EXTRACELLULAR DOMAIN.
[10]"The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity."
Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., Thompson T.B.
J. Biol. Chem. 283:32831-32838(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 311-426 IN COMPLEX WITH FSTL3, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Wikipedia

Activin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13436 mRNA. Translation: AAA59168.1.
X04447 Genomic DNA. Translation: CAA28041.1.
X57578, X57579 Genomic DNA. Translation: CAA40805.1.
X57579 Genomic DNA. Translation: CAA40806.1.
AC005027 Genomic DNA. Translation: AAQ96861.1.
BC007858 mRNA. Translation: AAH07858.1.
J03634 mRNA. Translation: AAA35787.1.
X72498 mRNA. Translation: CAA51163.1.
PIRB24248. S30488.
RefSeqNP_002183.1. NM_002192.2.
UniGeneHs.583348.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05B/D311-426[»]
1NYUX-ray3.10B/D311-426[»]
1S4YX-ray2.30B/D311-426[»]
2ARPX-ray2.00A311-426[»]
2ARVX-ray2.00A/B311-426[»]
2B0UX-ray2.80A/B311-426[»]
2P6AX-ray3.40A/B311-426[»]
3B4VX-ray2.48A/B/E/F311-426[»]
ProteinModelPortalP08476.
SMRP08476. Positions 32-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109836. 8 interactions.
DIPDIP-5824N.
IntActP08476. 1 interaction.
MINTMINT-1786936.
STRING9606.ENSP00000242208.

PTM databases

PhosphoSiteP08476.

Polymorphism databases

DMDM124279.

Proteomic databases

PaxDbP08476.
PRIDEP08476.

Protocols and materials databases

DNASU3624.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242208; ENSP00000242208; ENSG00000122641.
ENST00000442711; ENSP00000397197; ENSG00000122641.
GeneID3624.
KEGGhsa:3624.
UCSCuc003thq.3. human.

Organism-specific databases

CTD3624.
GeneCardsGC07M041724.
HGNCHGNC:6066. INHBA.
HPAHPA020031.
MIM147290. gene.
neXtProtNX_P08476.
PharmGKBPA29877.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312557.
HOGENOMHOG000220890.
HOVERGENHBG105613.
InParanoidP08476.
KOK04667.
OMARKSTWHI.
OrthoDBEOG7NSB2Q.
PhylomeDBP08476.
TreeFamTF351791.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP08476.

Gene expression databases

ArrayExpressP08476.
BgeeP08476.
CleanExHS_INHBA.
GenevestigatorP08476.

Family and domain databases

InterProIPR000491. Inhibin_betaA.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSPR00670. INHIBINBA.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08476.
GenomeRNAi3624.
NextBio14181.
PROP08476.
SOURCESearch...

Entry information

Entry nameINHBA_HUMAN
AccessionPrimary (citable) accession number: P08476
Secondary accession number(s): Q14599
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 164 of the entry and version 2 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

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM