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P09529 (INHBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibin beta B chain
Alternative name(s):
Activin beta-B chain
Gene names
Name:INHBB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 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
   DomainSignal
   Molecular functionGrowth factor
Hormone
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivin receptor signaling pathway

Inferred from direct assay PubMed 16650820. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to leptin stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from sequence or structural similarity. Source: UniProtKB

defense response

Traceable author statement PubMed 3122219. Source: UniProtKB

fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

growth

Inferred from electronic annotation. Source: InterPro

negative regulation of follicle-stimulating hormone secretion

Inferred from physical interaction PubMed 3122219. Source: UniProtKB

negative regulation of hepatocyte growth factor biosynthetic process

Inferred from direct assay PubMed 12419948. Source: UniProtKB

negative regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

oocyte development

Inferred from electronic annotation. Source: Ensembl

ovarian follicle development

Non-traceable author statement PubMed 12790766. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of follicle-stimulating hormone secretion

Inferred from physical interaction PubMed 3122219. Source: UniProtKB

positive regulation of ovulation

Inferred from sequence or structural similarity. Source: UniProtKB

response to mechanical stimulus

Inferred from direct assay PubMed 10320815. Source: UniProtKB

   Cellular_componentextracellular region

Traceable author statement PubMed 3122219. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16650820. Source: UniProtKB

   Molecular_functioncytokine activity

Traceable author statement PubMed 3122219. Source: UniProtKB

hormone activity

Traceable author statement PubMed 3122219. Source: UniProtKB

host cell surface receptor binding

Traceable author statement PubMed 12456957. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 292264 Potential
PRO_0000033722
Chain293 – 407115Inhibin beta B chain
PRO_0000033723

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Disulfide bond296 ↔ 304 By similarity
Disulfide bond303 ↔ 372 By similarity
Disulfide bond332 ↔ 404 By similarity
Disulfide bond336 ↔ 406 By similarity
Disulfide bond371Interchain By similarity

Experimental info

Sequence conflict391P → Q in AAH30029. Ref.4
Sequence conflict471S → A in AAA59170. Ref.5
Sequence conflict2951E → G AA sequence Ref.7
Sequence conflict3261G → S in AAH30029. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P09529 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 90316C83597BA6B4

FASTA40745,122
        10         20         30         40         50         60 
MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPTPAAPP PPPPPGSPGG SQDTCTSCGG 

        70         80         90        100        110        120 
FRRPEELGRV DGDFLEAVKR HILSRLQMRG RPNITHAVPK AAMVTALRKL HAGKVREDGR 

       130        140        150        160        170        180 
VEIPHLDGHA SPGADGQERV SEIISFAETD GLASSRVRLY FFISNEGNQN LFVVQASLWL 

       190        200        210        220        230        240 
YLKLLPYVLE KGSRRKVRVK VYFQEQGHGD RWNMVEKRVD LKRSGWHTFP LTEAIQALFE 

       250        260        270        280        290        300 
RGERRLNLDV QCDSCQELAV VPVFVDPGEE SHRPFVVVQA RLGDSRHRIR KRGLECDGRT 

       310        320        330        340        350        360 
NLCCRQQFFI DFRLIGWNDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF HTAVVNQYRM 

       370        380        390        400 
RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI VEECGCA 

« Hide

References

« Hide 'large scale' references
[1]"Activin B: precursor sequences, genomic structure and in vitro activities."
Mason A.J., Berkemeier L.M., Schmelzer C.H., Schwall R.H.
Mol. Endocrinol. 3:1352-1358(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain.
[5]"Characterization and regulation of testicular inhibin beta-subunit mRNA."
Feng Z.M., Bardin C.W., Chen C.L.
Mol. Endocrinol. 3:939-948(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-407.
[6]"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] OF 55-407.
[7]"Purification and characterization of recombinant human activin B."
Schmelzer C.H., Burton L.E., Tamony C.M., Schwall R.H., Mason A.J., Liegeois N.
Biochim. Biophys. Acta 1039:135-141(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 293-307.
[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.
+Additional computationally mapped references.

Web resources

Wikipedia

Inhibin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31669, M31668 Genomic DNA. Translation: AAA59451.1.
AC012363 Genomic DNA. Translation: AAY14801.1.
CH471103 Genomic DNA. Translation: EAW95243.1.
BC030029 mRNA. Translation: AAH30029.1.
M31682 mRNA. Translation: AAA59170.1.
M13437 mRNA. Translation: AAA59169.1.
PIRA40150.
RefSeqNP_002184.2. NM_002193.2.
UniGeneHs.1735.

3D structure databases

ProteinModelPortalP09529.
SMRP09529. Positions 196-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109837. 5 interactions.
IntActP09529. 1 interaction.
STRING9606.ENSP00000295228.

PTM databases

PhosphoSiteP09529.

Polymorphism databases

DMDM1708437.

Proteomic databases

PaxDbP09529.
PRIDEP09529.

Protocols and materials databases

DNASU3625.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295228; ENSP00000295228; ENSG00000163083.
GeneID3625.
KEGGhsa:3625.
UCSCuc002tmn.2. human.

Organism-specific databases

CTD3625.
GeneCardsGC02P121198.
H-InvDBHIX0002419.
HGNCHGNC:6067. INHBB.
HPAHPA035386.
HPA049218.
MIM147390. gene.
neXtProtNX_P09529.
PharmGKBPA29878.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278663.
HOGENOMHOG000220890.
HOVERGENHBG105613.
InParanoidP09529.
KOK04667.
OMAQGHGDRW.
OrthoDBEOG74R1Q4.
PhylomeDBP09529.
TreeFamTF351791.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP09529.
CleanExHS_INHBB.
GenevestigatorP09529.

Family and domain databases

InterProIPR000381. Inhibin_betaB.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF29. PTHR11848:SF29. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSPR00671. INHIBINBB.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiINHBB.
GenomeRNAi3625.
NextBio14185.
PROP09529.
SOURCESearch...

Entry information

Entry nameINHBB_HUMAN
AccessionPrimary (citable) accession number: P09529
Secondary accession number(s): Q53T31, Q8N1D3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 137 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM