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Q04999

- INHBB_MOUSE

UniProt

Q04999 - INHBB_MOUSE

Protein

Inhibin beta B chain

Gene

Inhbb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 4 (09 Jan 2007)
      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. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Growth factor, Hormone

    Enzyme and pathway databases

    ReactomeiREACT_196633. Antagonism of Activin by Follistatin.
    REACT_216258. Signaling by Activin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibin beta B chain
    Alternative name(s):
    Activin beta-B chain
    Gene namesi
    Name:Inhbb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:96571. Inhbb.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 296268Sequence AnalysisPRO_0000033724Add
    BLAST
    Chaini297 – 411115Inhibin beta B chainPRO_0000033725Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi300 ↔ 308By similarity
    Disulfide bondi307 ↔ 376By similarity
    Disulfide bondi336 ↔ 408By similarity
    Disulfide bondi340 ↔ 410By similarity
    Disulfide bondi375 – 375InterchainBy similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ04999.

    PTM databases

    PhosphoSiteiQ04999.

    Expressioni

    Tissue specificityi

    Uterus, testis, ovary, lung, kidney, brain, CJ7 embryonic stem cells, and possibly in liver.

    Gene expression databases

    BgeeiQ04999.
    CleanExiMM_INHBB.
    GenevestigatoriQ04999.

    Interactioni

    Subunit structurei

    Homo- or heterodimer; disulfide-linked. 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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200763. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04999.
    SMRiQ04999. Positions 200-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TGF-beta family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG278663.
    GeneTreeiENSGT00620000087864.
    HOGENOMiHOG000220890.
    HOVERGENiHBG105613.
    InParanoidiQ04999.
    KOiK04667.
    OMAiQGHGDRW.
    OrthoDBiEOG74R1Q4.
    PhylomeDBiQ04999.
    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.

    Q04999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGLPGRALG AACLLLLVAG WLGPEAWGSP TPPPSPAAPP PPPPPGAPGG    50
    SQDTCTSCGG GGGGFRRPEE LGRVDGDFLE AVKRHILSRL QLRGRPNITH 100
    AVPKAAMVTA LRKLHAGKVR EDGRVEIPHL DGHASPGADG QERVSEIISF 150
    AETDGLASSR VRLYFFVSNE GNQNLFVVQA SLWLYLKLLP YVLEKGSRRK 200
    VRVKVYFQEQ GHGDRWNVVE KKVDLKRSGW HTFPITEAIQ ALFERGERRL 250
    NLDVQCDSCQ ELAVVPVFVD PGEESHRPFV VVQARLGDSR HRIRKRGLEC 300
    DGRTSLCCRQ QFFIDFRLIG WNDWIIAPTG YYGNYCEGSC PAYLAGVPGS 350
    ASSFHTAVVN QYRMRGLNPG PVNSCCIPTK LSSMSMLYFD DEYNIVKRDV 400
    PNMIVEECGC A 411
    Length:411
    Mass (Da):45,211
    Last modified:January 9, 2007 - v4
    Checksum:i345F6919F583BC49
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911H → D in CAA49326. (PubMed:8330535)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132352 mRNA. Translation: BAE21120.1.
    BC048845 mRNA. Translation: AAH48845.1.
    X83376 mRNA. Translation: CAA58290.1.
    X69620 mRNA. Translation: CAA49326.1.
    CCDSiCCDS15224.1.
    PIRiI48235.
    RefSeqiNP_032407.1. NM_008381.3.
    UniGeneiMm.3092.

    Genome annotation databases

    EnsembliENSMUST00000038765; ENSMUSP00000044918; ENSMUSG00000037035.
    GeneIDi16324.
    KEGGimmu:16324.
    UCSCiuc007cir.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132352 mRNA. Translation: BAE21120.1 .
    BC048845 mRNA. Translation: AAH48845.1 .
    X83376 mRNA. Translation: CAA58290.1 .
    X69620 mRNA. Translation: CAA49326.1 .
    CCDSi CCDS15224.1.
    PIRi I48235.
    RefSeqi NP_032407.1. NM_008381.3.
    UniGenei Mm.3092.

    3D structure databases

    ProteinModelPortali Q04999.
    SMRi Q04999. Positions 200-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200763. 1 interaction.

    PTM databases

    PhosphoSitei Q04999.

    Proteomic databases

    PRIDEi Q04999.

    Protocols and materials databases

    DNASUi 16324.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038765 ; ENSMUSP00000044918 ; ENSMUSG00000037035 .
    GeneIDi 16324.
    KEGGi mmu:16324.
    UCSCi uc007cir.1. mouse.

    Organism-specific databases

    CTDi 3625.
    MGIi MGI:96571. Inhbb.

    Phylogenomic databases

    eggNOGi NOG278663.
    GeneTreei ENSGT00620000087864.
    HOGENOMi HOG000220890.
    HOVERGENi HBG105613.
    InParanoidi Q04999.
    KOi K04667.
    OMAi QGHGDRW.
    OrthoDBi EOG74R1Q4.
    PhylomeDBi Q04999.
    TreeFami TF351791.

    Enzyme and pathway databases

    Reactomei REACT_196633. Antagonism of Activin by Follistatin.
    REACT_216258. Signaling by Activin.

    Miscellaneous databases

    NextBioi 289394.
    PROi Q04999.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04999.
    CleanExi MM_INHBB.
    Genevestigatori Q04999.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.
    2. "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] OF 45-411.
      Strain: Czech II.
      Tissue: Mammary tumor.
    3. "Activin disrupts epithelial branching morphogenesis in developing glandular organs of the mouse."
      Ritvos O., Tuuri T., Eramaa M., Sainio K., Hilden K., Saxen L., Gilbert S.
      Mech. Dev. 50:229-245(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-390.
      Strain: CBA X NMRI.
      Tissue: Testis.
    4. "Activins are expressed in preimplantation mouse embryos and in ES and EC cells and are regulated on their differentiation."
      Albano P.M., Groome N., Smith J.C.
      Development 117:711-723(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 290-411.

    Entry informationi

    Entry nameiINHBB_MOUSE
    AccessioniPrimary (citable) accession number: Q04999
    Secondary accession number(s): Q3V1N0, Q61277, Q80VC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3