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Protein

Inhibin beta A chain

Gene

INHBA

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

Functioni

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.

GO - Molecular functioni

  • cytokine activity Source: HGNC
  • growth factor activity Source: UniProtKB
  • hormone activity Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • peptide hormone binding Source: UniProtKB
  • transforming growth factor beta receptor binding Source: GO_Central
  • type II activin receptor binding Source: BHF-UCL

GO - Biological processi

  • activin receptor signaling pathway Source: BHF-UCL
  • cell-cell signaling Source: UniProtKB
  • cell cycle arrest Source: HGNC
  • cell development Source: GO_Central
  • cell differentiation Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • cellular response to cholesterol Source: Ensembl
  • cellular response to follicle-stimulating hormone stimulus Source: Ensembl
  • defense response Source: UniProtKB
  • endodermal cell differentiation Source: BHF-UCL
  • erythrocyte differentiation Source: UniProtKB
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • eyelid development in camera-type eye Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: HGNC
  • GABAergic neuron differentiation Source: ParkinsonsUK-UCL
  • growth Source: InterPro
  • hair follicle development Source: UniProtKB
  • hematopoietic progenitor cell differentiation Source: UniProtKB
  • hemoglobin biosynthetic process Source: UniProtKB
  • male gonad development Source: UniProtKB
  • mesodermal cell differentiation Source: Ensembl
  • negative regulation of B cell differentiation Source: UniProtKB
  • negative regulation of cell cycle Source: HGNC
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of follicle-stimulating hormone secretion Source: UniProtKB
  • negative regulation of interferon-gamma biosynthetic process Source: UniProtKB
  • negative regulation of macrophage differentiation Source: UniProtKB
  • negative regulation of phosphorylation Source: UniProtKB
  • nervous system development Source: UniProtKB
  • odontogenesis Source: UniProtKB
  • ovarian follicle development Source: UniProtKB
  • palate development Source: UniProtKB
  • positive regulation of cellular protein metabolic process Source: BHF-UCL
  • positive regulation of erythrocyte differentiation Source: HGNC
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  • positive regulation of follicle-stimulating hormone secretion Source: UniProtKB
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of ovulation Source: UniProtKB
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • progesterone secretion Source: UniProtKB
  • regulation of follicle-stimulating hormone secretion Source: UniProtKB
  • regulation of MAPK cascade Source: GO_Central
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • response to drug Source: UniProtKB
  • SMAD protein signal transduction Source: GO_Central
  • striatal medium spiny neuron differentiation Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Hormone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122641-MONOMER.
ReactomeiR-HSA-1502540. Signaling by Activin.
R-HSA-209822. Glycoprotein hormones.
R-HSA-2473224. Antagonism of Activin by Follistatin.
SignaLinkiP08476.
SIGNORiP08476.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibin beta A chain
Alternative name(s):
Activin beta-A chain
Erythroid differentiation protein
Short name:
EDF
Gene namesi
Name:INHBA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:6066. INHBA.

Subcellular locationi

GO - Cellular componenti

  • activin A complex Source: HGNC
  • extracellular region Source: UniProtKB
  • inhibin A complex Source: HGNC
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3624.
MalaCardsiINHBA.
OpenTargetsiENSG00000122641.
Orphaneti213504. Adenocarcinoma of ovary.
PharmGKBiPA29877.

Chemistry databases

ChEMBLiCHEMBL3588735.

Polymorphism and mutation databases

BioMutaiINHBA.
DMDMi124279.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
PropeptideiPRO_000003370821 – 310Add BLAST290
ChainiPRO_0000033709311 – 426Inhibin beta A chainAdd BLAST116

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi165N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi314 ↔ 3221 Publication
Disulfide bondi321 ↔ 3911 Publication
Disulfide bondi350 ↔ 4231 Publication
Disulfide bondi354 ↔ 4251 Publication
Disulfide bondi390Interchain1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08476.
PaxDbiP08476.
PeptideAtlasiP08476.
PRIDEiP08476.

PTM databases

iPTMnetiP08476.
PhosphoSitePlusiP08476.

Expressioni

Gene expression databases

BgeeiENSG00000122641.
CleanExiHS_INHBA.
ExpressionAtlasiP08476. baseline and differential.
GenevisibleiP08476. HS.

Organism-specific databases

HPAiHPA020031.

Interactioni

Subunit structurei

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 FSTL3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FstP216742EBI-8077140,EBI-5746973From a different organism.

GO - Molecular functioni

  • cytokine activity Source: HGNC
  • growth factor activity Source: UniProtKB
  • hormone activity Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • transforming growth factor beta receptor binding Source: GO_Central
  • type II activin receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109836. 8 interactors.
DIPiDIP-5824N.
IntActiP08476. 1 interactor.
MINTiMINT-1786936.
STRINGi9606.ENSP00000242208.

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 65Combined sources14
Helixi80 – 89Combined sources10
Beta strandi92 – 95Combined sources4
Helixi97 – 99Combined sources3
Beta strandi101 – 103Combined sources3
Helixi107 – 118Combined sources12
Beta strandi120 – 126Combined sources7
Beta strandi135 – 139Combined sources5
Helixi143 – 146Combined sources4
Beta strandi149 – 160Combined sources12
Beta strandi170 – 180Combined sources11
Beta strandi201 – 212Combined sources12
Beta strandi217 – 222Combined sources6
Helixi224 – 232Combined sources9
Beta strandi237 – 243Combined sources7
Turni245 – 251Combined sources7
Beta strandi253 – 255Combined sources3
Helixi284 – 289Combined sources6
Beta strandi292 – 298Combined sources7
Beta strandi318 – 320Combined sources3
Beta strandi321 – 324Combined sources4
Beta strandi327 – 329Combined sources3
Helixi330 – 333Combined sources4
Turni336 – 338Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi343 – 346Combined sources4
Beta strandi349 – 352Combined sources4
Helixi356 – 358Combined sources3
Beta strandi362 – 364Combined sources3
Helixi368 – 375Combined sources8
Turni378 – 380Combined sources3
Turni382 – 386Combined sources5
Beta strandi391 – 404Combined sources14
Turni406 – 408Combined sources3
Beta strandi410 – 425Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MIDX-ray2.14A334-426[»]
5HLYX-ray2.30A30-426[»]
5HLZX-ray2.85A/C/E/G30-305[»]
B/D/F/H311-426[»]
ProteinModelPortaliP08476.
SMRiP08476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08476.

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000220890.
HOVERGENiHBG105613.
InParanoidiP08476.
KOiK04667.
OMAiNITRPVP.
OrthoDBiEOG091G09LW.
PhylomeDBiP08476.
TreeFamiTF351791.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000491. Inhibin_betaA.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF133. PTHR11848:SF133. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00670. INHIBINBA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL AALPKDVPNS
60 70 80 90 100
QPEMVEAVKK HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY
110 120 130 140 150
VEIEDDIGRR AEMNELMEQT SEIITFAESG TARKTLHFEI SKEGSDLSVV
160 170 180 190 200
ERAEVWLFLK VPKANRTRTK VTIRLFQQQK HPQGSLDTGE EAEEVGLKGE
210 220 230 240 250
RSELLLSEKV VDARKSTWHV FPVSSSIQRL LDQGKSSLDV RIACEQCQES
260 270 280 290 300
GASLVLLGKK KKKEEEGEGK KKGGGEGGAG ADEEKEQSHR PFLMLQARQS
310 320 330 340 350
EDHPHRRRRR GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC
360 370 380 390 400
EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS
410 420
MLYYDDGQNI IKKDIQNMIV EECGCS
Length:426
Mass (Da):47,442
Last modified:July 1, 1989 - v2
Checksum:i201CDEDF99CB6919
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti377 – 379RMR → AC in CAA51163 (Ref. 7) Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072640280G → E Found in a patient with early-onset epithelial ovarian tumor; uncertain pathological significance. 1 Publication1
Natural variantiVAR_052566299Q → P.Corresponds to variant rs41294833dbSNPEnsembl.1
Natural variantiVAR_072641386N → S Found in a patient with early-onset epithelial ovarian tumor; alters the ratio of secreted activins and ihibins; uncertain pathological significance. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5464.1.
PIRiS30488. B24248.
RefSeqiNP_002183.1. NM_002192.3.
XP_016867665.1. XM_017012176.1.
UniGeneiHs.28792.
Hs.583348.

Genome annotation databases

EnsembliENST00000242208; ENSP00000242208; ENSG00000122641.
ENST00000442711; ENSP00000397197; ENSG00000122641.
ENST00000638023; ENSP00000490646; ENSG00000122641.
GeneIDi3624.
KEGGihsa:3624.
UCSCiuc003thq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Activin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5464.1.
PIRiS30488. B24248.
RefSeqiNP_002183.1. NM_002192.3.
XP_016867665.1. XM_017012176.1.
UniGeneiHs.28792.
Hs.583348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MIDX-ray2.14A334-426[»]
5HLYX-ray2.30A30-426[»]
5HLZX-ray2.85A/C/E/G30-305[»]
B/D/F/H311-426[»]
ProteinModelPortaliP08476.
SMRiP08476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109836. 8 interactors.
DIPiDIP-5824N.
IntActiP08476. 1 interactor.
MINTiMINT-1786936.
STRINGi9606.ENSP00000242208.

Chemistry databases

ChEMBLiCHEMBL3588735.

PTM databases

iPTMnetiP08476.
PhosphoSitePlusiP08476.

Polymorphism and mutation databases

BioMutaiINHBA.
DMDMi124279.

Proteomic databases

MaxQBiP08476.
PaxDbiP08476.
PeptideAtlasiP08476.
PRIDEiP08476.

Protocols and materials databases

DNASUi3624.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242208; ENSP00000242208; ENSG00000122641.
ENST00000442711; ENSP00000397197; ENSG00000122641.
ENST00000638023; ENSP00000490646; ENSG00000122641.
GeneIDi3624.
KEGGihsa:3624.
UCSCiuc003thq.4. human.

Organism-specific databases

CTDi3624.
DisGeNETi3624.
GeneCardsiINHBA.
HGNCiHGNC:6066. INHBA.
HPAiHPA020031.
MalaCardsiINHBA.
MIMi147290. gene.
neXtProtiNX_P08476.
OpenTargetsiENSG00000122641.
Orphaneti213504. Adenocarcinoma of ovary.
PharmGKBiPA29877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000220890.
HOVERGENiHBG105613.
InParanoidiP08476.
KOiK04667.
OMAiNITRPVP.
OrthoDBiEOG091G09LW.
PhylomeDBiP08476.
TreeFamiTF351791.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122641-MONOMER.
ReactomeiR-HSA-1502540. Signaling by Activin.
R-HSA-209822. Glycoprotein hormones.
R-HSA-2473224. Antagonism of Activin by Follistatin.
SignaLinkiP08476.
SIGNORiP08476.

Miscellaneous databases

EvolutionaryTraceiP08476.
GenomeRNAii3624.
PROiP08476.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122641.
CleanExiHS_INHBA.
ExpressionAtlasiP08476. baseline and differential.
GenevisibleiP08476. HS.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000491. Inhibin_betaA.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF133. PTHR11848:SF133. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00670. INHIBINBA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINHBA_HUMAN
AccessioniPrimary (citable) accession number: P08476
Secondary accession number(s): Q14599
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 190 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.