Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thyrotropin subunit beta

Gene

TSHB

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
GeneTreeiENSGT00390000010115.
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. AlignAdd to basket

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

        10         20         30         40         50
MTALFLMSML FGLTCGQAMS FCIPTEYTMH IERRECAYCL TINTTICAGY
60 70 80 90 100
CMTRDINGKL FLPKYALSQD VCTYRDFIYR TVEIPGCPLH VAPYFSYPVA
110 120 130
LSCKCGKCNT DYSDCIHEAI KTNYCTKPQK SYLVGFSV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi9606.ENSP00000256592.

PTM databases

PhosphoSiteiP01222.

Polymorphism databases

DMDMi311033515.

Proteomic databases

PaxDbiP01222.
PRIDEiP01222.

Protocols and materials databases

DNASUi7252.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7252.
GeneCardsiGC01P115572.
H-InvDBHIX0028781.
HGNCiHGNC:12372. TSHB.
MIMi188540. gene.
275100. phenotype.
neXtProtiNX_P01222.
Orphaneti90674. Isolated thyroid-stimulating hormone deficiency.
PharmGKBiPA37041.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40888.
GeneTreeiENSGT00390000010115.
HOGENOMiHOG000116098.
HOVERGENiHBG006698.
InParanoidiP01222.
KOiK05251.
OMAiTNYCTKP.
OrthoDBiEOG7JQBQF.
PhylomeDBiP01222.
TreeFamiTF332940.

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.

Miscellaneous databases

GeneWikiiTSHB.
GenomeRNAii7252.
NextBioi28357.
PROiP01222.
SOURCEiSearch...

Gene expression databases

BgeeiP01222.
CleanExiHS_TSHB.
GenevestigatoriP01222.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 139 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

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.