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Protein

Inhibin beta B chain

Gene

INHBB

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

  1. cytokine activity Source: UniProtKB
  2. hormone activity Source: UniProtKB
  3. host cell surface receptor binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. transforming growth factor beta receptor binding Source: GO_Central

GO - Biological processi

  1. activin receptor signaling pathway Source: UniProtKB
  2. cell development Source: GO_Central
  3. cell differentiation Source: UniProtKB
  4. cellular response to insulin stimulus Source: UniProtKB
  5. cellular response to leptin stimulus Source: Ensembl
  6. cellular response to starvation Source: UniProtKB
  7. defense response Source: UniProtKB
  8. fat cell differentiation Source: UniProtKB
  9. growth Source: InterPro
  10. negative regulation of follicle-stimulating hormone secretion Source: UniProtKB
  11. negative regulation of hepatocyte growth factor biosynthetic process Source: UniProtKB
  12. negative regulation of insulin secretion Source: UniProtKB
  13. oocyte development Source: Ensembl
  14. ovarian follicle development Source: UniProtKB
  15. positive regulation of apoptotic signaling pathway Source: Ensembl
  16. positive regulation of follicle-stimulating hormone secretion Source: UniProtKB
  17. positive regulation of ovulation Source: UniProtKB
  18. positive regulation of pathway-restricted SMAD protein phosphorylation Source: GO_Central
  19. regulation of apoptotic process Source: GO_Central
  20. regulation of MAPK cascade Source: GO_Central
  21. response to mechanical stimulus Source: UniProtKB
  22. SMAD protein signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Hormone

Enzyme and pathway databases

ReactomeiREACT_150238. Signaling by Activin.
REACT_150276. Antagonism of Activin by Follistatin.
REACT_15398. Glycoprotein hormones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibin beta B chain
Alternative name(s):
Activin beta-B chain
Gene namesi
Name:INHBB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6067. INHBB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: GO_Central
  3. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29878.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 292264Sequence AnalysisPRO_0000033722Add
BLAST
Chaini293 – 407115Inhibin beta B chainPRO_0000033723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi296 ↔ 304By similarity
Disulfide bondi303 ↔ 372By similarity
Disulfide bondi332 ↔ 404By similarity
Disulfide bondi336 ↔ 406By similarity
Disulfide bondi371 – 371InterchainBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP09529.
PaxDbiP09529.
PRIDEiP09529.

PTM databases

PhosphoSiteiP09529.

Expressioni

Gene expression databases

BgeeiP09529.
CleanExiHS_INHBB.
GenevestigatoriP09529.

Organism-specific databases

HPAiHPA035386.
HPA049218.

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 FSTL3.1 Publication

Protein-protein interaction databases

BioGridi109837. 5 interactions.
IntActiP09529. 2 interactions.
STRINGi9606.ENSP00000295228.

Structurei

3D structure databases

ProteinModelPortaliP09529.
SMRiP09529. Positions 196-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG278663.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000220890.
HOVERGENiHBG105613.
InParanoidiP09529.
KOiK04667.
OMAiQREETEC.
OrthoDBiEOG74R1Q4.
PhylomeDBiP09529.
TreeFamiTF351791.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000381. Inhibin_betaB.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF29. PTHR11848:SF29. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00671. INHIBINBB.
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.

P09529-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPTPAAPP PPPPPGSPGG
60 70 80 90 100
SQDTCTSCGG FRRPEELGRV DGDFLEAVKR HILSRLQMRG RPNITHAVPK
110 120 130 140 150
AAMVTALRKL HAGKVREDGR VEIPHLDGHA SPGADGQERV SEIISFAETD
160 170 180 190 200
GLASSRVRLY FFISNEGNQN LFVVQASLWL YLKLLPYVLE KGSRRKVRVK
210 220 230 240 250
VYFQEQGHGD RWNMVEKRVD LKRSGWHTFP LTEAIQALFE RGERRLNLDV
260 270 280 290 300
QCDSCQELAV VPVFVDPGEE SHRPFVVVQA RLGDSRHRIR KRGLECDGRT
310 320 330 340 350
NLCCRQQFFI DFRLIGWNDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF
360 370 380 390 400
HTAVVNQYRM RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI

VEECGCA
Length:407
Mass (Da):45,122
Last modified:October 1, 1996 - v2
Checksum:i90316C83597BA6B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391P → Q in AAH30029. (PubMed:15489334)Curated
Sequence conflicti47 – 471S → A in AAA59170. (PubMed:2739657)Curated
Sequence conflicti295 – 2951E → G AA sequence (PubMed:2364091)Curated
Sequence conflicti326 – 3261G → S in AAH30029. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2132.1.
PIRiA40150.
RefSeqiNP_002184.2. NM_002193.2.
UniGeneiHs.1735.

Genome annotation databases

EnsembliENST00000295228; ENSP00000295228; ENSG00000163083.
GeneIDi3625.
KEGGihsa:3625.
UCSCiuc002tmn.2. human.

Polymorphism databases

DMDMi1708437.

Cross-referencesi

Web resourcesi

Wikipedia

Inhibin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2132.1.
PIRiA40150.
RefSeqiNP_002184.2. NM_002193.2.
UniGeneiHs.1735.

3D structure databases

ProteinModelPortaliP09529.
SMRiP09529. Positions 196-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109837. 5 interactions.
IntActiP09529. 2 interactions.
STRINGi9606.ENSP00000295228.

PTM databases

PhosphoSiteiP09529.

Polymorphism databases

DMDMi1708437.

Proteomic databases

MaxQBiP09529.
PaxDbiP09529.
PRIDEiP09529.

Protocols and materials databases

DNASUi3625.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295228; ENSP00000295228; ENSG00000163083.
GeneIDi3625.
KEGGihsa:3625.
UCSCiuc002tmn.2. human.

Organism-specific databases

CTDi3625.
GeneCardsiGC02P121198.
H-InvDBHIX0002419.
HGNCiHGNC:6067. INHBB.
HPAiHPA035386.
HPA049218.
MIMi147390. gene.
neXtProtiNX_P09529.
PharmGKBiPA29878.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG278663.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000220890.
HOVERGENiHBG105613.
InParanoidiP09529.
KOiK04667.
OMAiQREETEC.
OrthoDBiEOG74R1Q4.
PhylomeDBiP09529.
TreeFamiTF351791.

Enzyme and pathway databases

ReactomeiREACT_150238. Signaling by Activin.
REACT_150276. Antagonism of Activin by Follistatin.
REACT_15398. Glycoprotein hormones.

Miscellaneous databases

GeneWikiiINHBB.
GenomeRNAii3625.
NextBioi14185.
PROiP09529.
SOURCEiSearch...

Gene expression databases

BgeeiP09529.
CleanExiHS_INHBB.
GenevestigatoriP09529.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR000381. Inhibin_betaB.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF29. PTHR11848:SF29. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00671. INHIBINBB.
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...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-407.
  7. 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.

Entry informationi

Entry nameiINHBB_HUMAN
AccessioniPrimary (citable) accession number: P09529
Secondary accession number(s): Q53T31, Q8N1D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 146 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.