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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

  • cytokine activity Source: UniProtKB
  • growth factor activity Source: UniProtKB-KW
  • hormone activity Source: UniProtKB
  • host cell surface receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transforming growth factor beta receptor binding Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionGrowth factor, Hormone

Enzyme and pathway databases

ReactomeiR-HSA-1502540. Signaling by Activin.
R-HSA-209822. Glycoprotein hormones.
R-HSA-2473224. Antagonism of Activin by Follistatin.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000163083.5.
HGNCiHGNC:6067. INHBB.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3625.
OpenTargetsiENSG00000163083.
PharmGKBiPA29878.

Polymorphism and mutation databases

BioMutaiINHBB.
DMDMi1708437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000003372229 – 292Sequence analysisAdd BLAST264
ChainiPRO_0000033723293 – 407Inhibin beta B chainAdd BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi296 ↔ 304By similarity
Disulfide bondi303 ↔ 372By similarity
Disulfide bondi332 ↔ 404By similarity
Disulfide bondi336 ↔ 406By similarity
Disulfide bondi371InterchainBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP09529.
PaxDbiP09529.
PeptideAtlasiP09529.
PRIDEiP09529.
TopDownProteomicsiP09529.

PTM databases

iPTMnetiP09529.
PhosphoSitePlusiP09529.

Expressioni

Gene expression databases

BgeeiENSG00000163083.
CleanExiHS_INHBB.
GenevisibleiP09529. HS.

Organism-specific databases

HPAiHPA049218.

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

GO - Molecular functioni

  • cytokine activity Source: UniProtKB
  • growth factor activity Source: UniProtKB-KW
  • hormone activity Source: UniProtKB
  • host cell surface receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transforming growth factor beta receptor binding Source: GO_Central

Protein-protein interaction databases

BioGridi109837. 6 interactors.
IntActiP09529. 2 interactors.
STRINGi9606.ENSP00000295228.

Structurei

3D structure databases

ProteinModelPortaliP09529.
SMRiP09529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000220890.
HOVERGENiHBG105613.
InParanoidiP09529.
KOiK04667.
OMAiQGHGDRW.
OrthoDBiEOG091G09LW.
PhylomeDBiP09529.
TreeFamiTF351791.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiView protein in InterPro
IPR029034. Cystine-knot_cytokine.
IPR000381. Inhibin_betaB.
IPR001839. TGF-b_C.
IPR001111. TGF-b_propeptide.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
PANTHERiPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF181. PTHR11848:SF181. 1 hit.
PfamiView protein in Pfam
PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
PRINTSiPR00671. INHIBINBB.
SMARTiView protein in SMART
SM00204. TGFB. 1 hit.
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiView protein in PROSITE
PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti39P → Q in AAH30029 (PubMed:15489334).Curated1
Sequence conflicti47S → A in AAA59170 (PubMed:2739657).Curated1
Sequence conflicti295E → G AA sequence (PubMed:2364091).Curated1
Sequence conflicti326G → S in AAH30029 (PubMed:15489334).Curated1

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_002193.3.
UniGeneiHs.1735.

Genome annotation databases

EnsembliENST00000295228; ENSP00000295228; ENSG00000163083.
GeneIDi3625.
KEGGihsa:3625.
UCSCiuc002tmn.3. human.

Similar proteinsi

Entry informationi

Entry nameiINHBB_HUMAN
AccessioniPrimary (citable) accession number: P09529
Secondary accession number(s): Q53T31, Q8N1D3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: September 27, 2017
This is version 165 of the entry and version 2 of the sequence. See 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