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P01222

- TSHB_HUMAN

UniProt

P01222 - TSHB_HUMAN

Protein

Thyrotropin subunit beta

Gene

TSHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Indispensable for the control of thyroid structure and metabolism.

    GO - Molecular functioni

    1. hormone activity Source: ProtInc

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. cell-cell signaling Source: ProtInc
    3. cellular protein metabolic process Source: Reactome
    4. G-protein coupled receptor signaling pathway Source: ProtInc
    5. peptide hormone processing Source: Reactome
    6. response to calcium ion Source: Ensembl
    7. response to estrogen Source: Ensembl
    8. response to vitamin A Source: Ensembl

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_15292. Thyroxine biosynthesis.
    REACT_15398. Glycoprotein hormones.
    REACT_16942. Hormone ligand-binding receptors.
    REACT_19327. G alpha (s) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyrotropin subunit beta
    Alternative name(s):
    Thyroid-stimulating hormone subunit beta
    Short name:
    TSH-B
    Short name:
    TSH-beta
    Thyrotropin beta chain
    INN: Thyrotropin alfa
    Gene namesi
    Name:TSHB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12372. TSHB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the name Thyrogen (Genzyme). Used in combination with other tests to detect recurring or leftover thyroid cancer cells in patients with a history of certain types of thyroid cancer.

    Organism-specific databases

    MIMi275100. phenotype.
    Orphaneti90674. Isolated thyroid-stimulating hormone deficiency.
    PharmGKBiPA37041.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 132112Thyrotropin subunit betaPRO_0000011746Add
    BLAST
    Propeptidei133 – 1386PRO_0000011747

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi22 ↔ 72By similarity
    Disulfide bondi36 ↔ 87By similarity
    Disulfide bondi39 ↔ 125By similarity
    Glycosylationi43 – 431N-linked (GlcNAc...)
    Disulfide bondi47 ↔ 103By similarity
    Disulfide bondi51 ↔ 105By similarity
    Disulfide bondi108 ↔ 115By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP01222.
    PRIDEiP01222.

    PTM databases

    PhosphoSiteiP01222.

    Expressioni

    Gene expression databases

    BgeeiP01222.
    CleanExiHS_TSHB.
    GenevestigatoriP01222.

    Interactioni

    Subunit structurei

    Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin.

    Protein-protein interaction databases

    STRINGi9606.ENSP00000256592.

    Structurei

    3D structure databases

    ProteinModelPortaliP01222.
    SMRiP01222. Positions 22-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40888.
    HOGENOMiHOG000116098.
    HOVERGENiHBG006698.
    InParanoidiP01222.
    KOiK05251.
    OMAiTNYCTKP.
    OrthoDBiEOG7JQBQF.
    PhylomeDBiP01222.
    TreeFamiTF332940.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR006208. Glyco_hormone_CN.
    IPR001545. Gonadotropin_bsu.
    IPR018245. Gonadotropin_bsu_CS.
    [Graphical view]
    PANTHERiPTHR11515. PTHR11515. 1 hit.
    PfamiPF00007. Cys_knot. 1 hit.
    [Graphical view]
    SMARTiSM00068. GHB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00261. GLYCO_HORMONE_BETA_1. 1 hit.
    PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01222-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTALFLMSML FGLTCGQAMS FCIPTEYTMH IERRECAYCL TINTTICAGY    50
    CMTRDINGKL FLPKYALSQD VCTYRDFIYR TVEIPGCPLH VAPYFSYPVA 100
    LSCKCGKCNT DYSDCIHEAI KTNYCTKPQK SYLVGFSV 138
    Length:138
    Mass (Da):15,639
    Last modified:November 2, 2010 - v2
    Checksum:i6A367538D8393DB7
    GO
    Isoform 2 (identifier: P01222-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MTALFLMSMLFGLTCGQAMSFCIPTEYTMHIERRECAYCLTINTTICAGYCMTR → MLSFLFFPQ

    Note: Major isoform in peripheral blood leukocytes and thyroid, may form heterodimers with isoform 1.

    Show »
    Length:93
    Mass (Da):10,624
    Checksum:iE1989F2A0A00126E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461I → M in AAB30828. (PubMed:8196184)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141T → A.6 Publications
    Corresponds to variant rs10776792 [ dbSNP | Ensembl ].
    VAR_054769

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5454MTALF…YCMTR → MLSFLFFPQ in isoform 2. 1 PublicationVSP_053387Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02866 Genomic DNA. Translation: CAA26618.1.
    X02867 Genomic DNA. Translation: CAA26619.1.
    M23671, M23670 Genomic DNA. Translation: AAB05845.1.
    M25164 Genomic DNA. Translation: AAA61235.1.
    M21024 Genomic DNA. Translation: AAA36782.1.
    S70587 Genomic DNA. Translation: AAB30828.2.
    AL109660 Genomic DNA. Translation: CAI22270.1.
    BC069298 mRNA. Translation: AAH69298.1.
    CCDSiCCDS880.1. [P01222-1]
    PIRiA23997. TTHUB.
    RefSeqiNP_000540.2. NM_000549.4. [P01222-1]
    NP_001264920.1. NM_001277991.1. [P01222-2]
    UniGeneiHs.406687.

    Genome annotation databases

    EnsembliENST00000256592; ENSP00000256592; ENSG00000134200. [P01222-1]
    ENST00000369517; ENSP00000358530; ENSG00000134200. [P01222-1]
    GeneIDi7252.
    KEGGihsa:7252.
    UCSCiuc001efs.2. human. [P01222-1]

    Polymorphism databases

    DMDMi311033515.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Thyrogen

    Clinical information on Thyrogen

    Wikipedia

    Thyroid-stimulating hormone entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02866 Genomic DNA. Translation: CAA26618.1 .
    X02867 Genomic DNA. Translation: CAA26619.1 .
    M23671 , M23670 Genomic DNA. Translation: AAB05845.1 .
    M25164 Genomic DNA. Translation: AAA61235.1 .
    M21024 Genomic DNA. Translation: AAA36782.1 .
    S70587 Genomic DNA. Translation: AAB30828.2 .
    AL109660 Genomic DNA. Translation: CAI22270.1 .
    BC069298 mRNA. Translation: AAH69298.1 .
    CCDSi CCDS880.1. [P01222-1 ]
    PIRi A23997. TTHUB.
    RefSeqi NP_000540.2. NM_000549.4. [P01222-1 ]
    NP_001264920.1. NM_001277991.1. [P01222-2 ]
    UniGenei Hs.406687.

    3D structure databases

    ProteinModelPortali P01222.
    SMRi P01222. Positions 22-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000256592.

    PTM databases

    PhosphoSitei P01222.

    Polymorphism databases

    DMDMi 311033515.

    Proteomic databases

    PaxDbi P01222.
    PRIDEi P01222.

    Protocols and materials databases

    DNASUi 7252.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256592 ; ENSP00000256592 ; ENSG00000134200 . [P01222-1 ]
    ENST00000369517 ; ENSP00000358530 ; ENSG00000134200 . [P01222-1 ]
    GeneIDi 7252.
    KEGGi hsa:7252.
    UCSCi uc001efs.2. human. [P01222-1 ]

    Organism-specific databases

    CTDi 7252.
    GeneCardsi GC01P115572.
    H-InvDB HIX0028781.
    HGNCi HGNC:12372. TSHB.
    MIMi 188540. gene.
    275100. phenotype.
    neXtProti NX_P01222.
    Orphaneti 90674. Isolated thyroid-stimulating hormone deficiency.
    PharmGKBi PA37041.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40888.
    HOGENOMi HOG000116098.
    HOVERGENi HBG006698.
    InParanoidi P01222.
    KOi K05251.
    OMAi TNYCTKP.
    OrthoDBi EOG7JQBQF.
    PhylomeDBi P01222.
    TreeFami TF332940.

    Enzyme and pathway databases

    Reactomei REACT_15292. Thyroxine biosynthesis.
    REACT_15398. Glycoprotein hormones.
    REACT_16942. Hormone ligand-binding receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    GeneWikii TSHB.
    GenomeRNAii 7252.
    NextBioi 28357.
    PROi P01222.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01222.
    CleanExi HS_TSHB.
    Genevestigatori P01222.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR006208. Glyco_hormone_CN.
    IPR001545. Gonadotropin_bsu.
    IPR018245. Gonadotropin_bsu_CS.
    [Graphical view ]
    PANTHERi PTHR11515. PTHR11515. 1 hit.
    Pfami PF00007. Cys_knot. 1 hit.
    [Graphical view ]
    SMARTi SM00068. GHB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00261. GLYCO_HORMONE_BETA_1. 1 hit.
    PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the human thyrotropin-beta subunit gene."
      Hayashizaki Y., Miyai K., Kato K., Matsubara K.
      FEBS Lett. 188:394-400(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-14.
    2. "The human thyrotropin beta-subunit gene differs in 5' structure from murine TSH-beta genes."
      Guidon P.T. Jr., Whitfield G.K., Porti D., Kourides I.A.
      DNA 7:691-699(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-14.
    3. "The structure of the human thyrotropin beta-subunit gene."
      Tatsumi K., Hayashizaki Y., Hiraoka Y., Miyai K., Matsubara K.
      Gene 73:489-497(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-14.
    4. "Isolation and characterization of the human thyrotropin beta-subunit gene. Differences in gene structure and promoter function from murine species."
      Wondisford F.E., Radovick S., Moates J.M., Usala S.J., Weintraub B.D.
      J. Biol. Chem. 263:12538-12542(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-14.
    5. "Structure and regulation of human thyroid-stimulating hormone (TSH) gene."
      Miyoshi I., Kasai N., Hayashizaki Y.
      Nippon Rinsho 52:940-947(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-14.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1), VARIANT ALA-14.
    8. "A novel thyroid stimulating hormone beta-subunit isoform in human pituitary, peripheral blood leukocytes, and thyroid."
      Schaefer J.S., Klein J.R.
      Gen. Comp. Endocrinol. 162:241-244(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    9. "Human pituitary thyrotropin. The primary structure of the alpha and beta subunits."
      Sairam M.R., Li C.H.
      Can. J. Biochem. 55:755-760(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-132.

    Entry informationi

    Entry nameiTSHB_HUMAN
    AccessioniPrimary (citable) accession number: P01222
    Secondary accession number(s): B1AKP0, Q16163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 137 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, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3