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P09529

- INHBB_HUMAN

UniProt

P09529 - INHBB_HUMAN

Protein

Inhibin beta B chain

Gene

INHBB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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 binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activin receptor signaling pathway Source: UniProtKB
    2. cell differentiation Source: UniProtKB
    3. cellular response to insulin stimulus Source: UniProtKB
    4. cellular response to leptin stimulus Source: Ensembl
    5. cellular response to starvation Source: UniProtKB
    6. defense response Source: UniProtKB
    7. fat cell differentiation Source: UniProtKB
    8. growth Source: InterPro
    9. negative regulation of follicle-stimulating hormone secretion Source: UniProtKB
    10. negative regulation of hepatocyte growth factor biosynthetic process Source: UniProtKB
    11. negative regulation of insulin secretion Source: UniProtKB
    12. oocyte development Source: Ensembl
    13. ovarian follicle development Source: UniProtKB
    14. positive regulation of apoptotic signaling pathway Source: Ensembl
    15. positive regulation of follicle-stimulating hormone secretion Source: UniProtKB
    16. positive regulation of ovulation Source: UniProtKB
    17. response to mechanical stimulus Source: UniProtKB

    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. perinuclear region of cytoplasm Source: UniProtKB

    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.
    HOGENOMiHOG000220890.
    HOVERGENiHBG105613.
    InParanoidiP09529.
    KOiK04667.
    OMAiQGHGDRW.
    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

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    MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPTPAAPP PPPPPGSPGG    50
    SQDTCTSCGG FRRPEELGRV DGDFLEAVKR HILSRLQMRG RPNITHAVPK 100
    AAMVTALRKL HAGKVREDGR VEIPHLDGHA SPGADGQERV SEIISFAETD 150
    GLASSRVRLY FFISNEGNQN LFVVQASLWL YLKLLPYVLE KGSRRKVRVK 200
    VYFQEQGHGD RWNMVEKRVD LKRSGWHTFP LTEAIQALFE RGERRLNLDV 250
    QCDSCQELAV VPVFVDPGEE SHRPFVVVQA RLGDSRHRIR KRGLECDGRT 300
    NLCCRQQFFI DFRLIGWNDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF 350
    HTAVVNQYRM RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI 400
    VEECGCA 407
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2132.1.
    PIRi A40150.
    RefSeqi NP_002184.2. NM_002193.2.
    UniGenei Hs.1735.

    3D structure databases

    ProteinModelPortali P09529.
    SMRi P09529. Positions 196-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109837. 5 interactions.
    IntActi P09529. 2 interactions.
    STRINGi 9606.ENSP00000295228.

    PTM databases

    PhosphoSitei P09529.

    Polymorphism databases

    DMDMi 1708437.

    Proteomic databases

    MaxQBi P09529.
    PaxDbi P09529.
    PRIDEi P09529.

    Protocols and materials databases

    DNASUi 3625.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295228 ; ENSP00000295228 ; ENSG00000163083 .
    GeneIDi 3625.
    KEGGi hsa:3625.
    UCSCi uc002tmn.2. human.

    Organism-specific databases

    CTDi 3625.
    GeneCardsi GC02P121198.
    H-InvDB HIX0002419.
    HGNCi HGNC:6067. INHBB.
    HPAi HPA035386.
    HPA049218.
    MIMi 147390. gene.
    neXtProti NX_P09529.
    PharmGKBi PA29878.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278663.
    HOGENOMi HOG000220890.
    HOVERGENi HBG105613.
    InParanoidi P09529.
    KOi K04667.
    OMAi QGHGDRW.
    OrthoDBi EOG74R1Q4.
    PhylomeDBi P09529.
    TreeFami TF351791.

    Enzyme and pathway databases

    Reactomei REACT_150238. Signaling by Activin.
    REACT_150276. Antagonism of Activin by Follistatin.
    REACT_15398. Glycoprotein hormones.

    Miscellaneous databases

    GeneWikii INHBB.
    GenomeRNAii 3625.
    NextBioi 14185.
    PROi P09529.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09529.
    CleanExi HS_INHBB.
    Genevestigatori P09529.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR000381. Inhibin_betaB.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    PTHR11848:SF29. PTHR11848:SF29. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view ]
    PRINTSi PR00671. INHIBINBB.
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 143 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