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P07202 (PERT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid peroxidase

Short name=TPO
EC=1.11.1.8
Gene names
Name:TPO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T3 and T4.

Catalytic activity

2 iodide + H2O2 + 2 H+ = 2 iodine + 2 H2O.

[Thyroglobulin]-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O.

[Thyroglobulin]-3-iodo-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O.

2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H2O.

[Thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H2O.

Cofactor

Binds 1 calcium ion per heterodimer By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer By similarity.

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with DUOX1, DUOX2 and CYBA. Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

Isoform 3: Cell surface.

Post-translational modification

Glycosylated.

Heme is covalently bound through a H2O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface.

Cleaved in its N-terminal part.

Involvement in disease

An alternative splicing in the thyroperoxidase mRNA can cause Graves' disease. Ref.9

Thyroid dyshormonogenesis 2A (TDH2A) [MIM:274500]: A disorder due to defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Contains 1 EGF-like domain.

Contains 1 Sushi (CCP/SCR) domain.

Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital hypothyroidism
Disease mutation
   DomainEGF-like domain
Signal
Sushi
Transmembrane
Transmembrane helix
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

embryonic hemopoiesis

Inferred from direct assay PubMed 21149635. Source: DFLAT

hormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

small molecule metabolic process

Traceable author statement. Source: Reactome

thyroid hormone generation

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.3. Source: ProtInc

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iodide peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

peroxidase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P07202-1)

Also known as: TPO1;

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.
Isoform 2 (identifier: P07202-2)

Also known as: TPO2;

The sequence of this isoform differs from the canonical sequence as follows:
     534-590: Missing.
Note: Lacks exon 10. Found in normal thyroid tissues as well as Graves'tissues. Rapidly degraded after synthesis, does not reach the cell surface. Inactive.
Isoform 3 (identifier: P07202-3)

Also known as: TPO3; Graves' disease; TPOzaninelli;

The sequence of this isoform differs from the canonical sequence as follows:
     874-933: TRTGTKSTLP...RDTHRLPRAL → RVLGWKAGIL...SAGRLFSQHG
Note: Lacks exon 16. Found in normal thyroid tissues as well as Graves'tissues. Active.
Isoform 4 (identifier: P07202-4)

Also known as: TPO4;

The sequence of this isoform differs from the canonical sequence as follows:
     796-839: Missing.
Note: Lacks exon 14. Active.
Isoform 5 (identifier: P07202-5)

Also known as: TPO5;

The sequence of this isoform differs from the canonical sequence as follows:
     274-446: Missing.
Note: Lacks exon 8. Does not fold correctly. Does not reach the cell surface.
Isoform 6 (identifier: P07202-6)

Also known as: TPO6;

The sequence of this isoform differs from the canonical sequence as follows:
     534-590: Missing.
     669-933: Missing.
Note: Lacks exons 10, 12, 13, 14 and 16.
Isoform 2-3 (identifier: P07202-7)

The sequence of this isoform differs from the canonical sequence as follows:
     534-590: Missing.
     874-933: TRTGTKSTLP...RDTHRLPRAL → RVLGWKAGIL...SAGRLFSQHG
Note: Lacks exons 10 and 16.
Isoform 2-4 (identifier: P07202-8)

The sequence of this isoform differs from the canonical sequence as follows:
     534-590: Missing.
     796-839: Missing.
Note: Lacks exons 10 and 14.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 933915Thyroid peroxidase
PRO_0000023662

Regions

Topological domain19 – 846828Extracellular Potential
Transmembrane847 – 87125Helical; Potential
Topological domain872 – 93362Cytoplasmic Potential
Domain740 – 79556Sushi
Domain796 – 83944EGF-like; calcium-binding Potential

Sites

Active site2391Proton acceptor By similarity
Metal binding2401Calcium By similarity
Metal binding3211Calcium By similarity
Metal binding3231Calcium; via carbonyl oxygen By similarity
Metal binding3251Calcium By similarity
Metal binding3271Calcium By similarity
Metal binding4941Iron (heme axial ligand) By similarity
Binding site2381Heme (covalent; via 2 links) By similarity
Binding site3991Heme (covalent; via 2 links) By similarity
Site3961Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1291N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Disulfide bond142 ↔ 158 By similarity
Disulfide bond259 ↔ 269 By similarity
Disulfide bond263 ↔ 286 By similarity
Disulfide bond598 ↔ 655 By similarity
Disulfide bond696 ↔ 721 By similarity
Disulfide bond800 ↔ 814 By similarity
Disulfide bond808 ↔ 823 By similarity
Disulfide bond825 ↔ 838 By similarity

Natural variations

Alternative sequence274 – 446173Missing in isoform 5.
VSP_007268
Alternative sequence534 – 59057Missing in isoform 2, isoform 2-3, isoform 2-4 and isoform 6.
VSP_004665
Alternative sequence669 – 933265Missing in isoform 6.
VSP_007270
Alternative sequence796 – 83944Missing in isoform 4 and isoform 2-4.
VSP_007269
Alternative sequence874 – 93360TRTGT…LPRAL → RVLGWKAGILTGCREPSEGK VAGHCRTASCSQNHRTTLFQ TQANRKSAGRLFSQHG in isoform 3 and isoform 2-3.
VSP_004666
Natural variant531A → P in TDH2A. Ref.19
VAR_021622
Natural variant2401D → N in TDH2A; loss of activity. Ref.15
VAR_021623
Natural variant2571A → S. Ref.5 Ref.6 Ref.11
Corresponds to variant rs4927611 [ dbSNP | Ensembl ].
VAR_006057
Natural variant3071N → T in TDH2A. Ref.23
VAR_021624
Natural variant3261A → T in TDH2A. Ref.16
VAR_021625
Natural variant3731A → S. Ref.11
Corresponds to variant rs2280132 [ dbSNP | Ensembl ].
VAR_006058
Natural variant3781E → K in TDH2A. Ref.25
VAR_025784
Natural variant3981S → T. Ref.11
Corresponds to variant rs2175977 [ dbSNP | Ensembl ].
VAR_006059
Natural variant4331V → M in TDH2A. Ref.23
VAR_021626
Natural variant4471I → F in TDH2A. Ref.12 Ref.16
VAR_015375
Natural variant4531Y → D in TDH2A. Ref.11 Ref.16 Ref.26
VAR_006060
Natural variant4581L → P in TDH2A. Ref.17
VAR_021627
Natural variant4911R → H in TDH2A. Ref.17
Corresponds to variant rs201165648 [ dbSNP | Ensembl ].
VAR_021628
Natural variant4931G → S in TDH2A. Ref.20
VAR_021629
Natural variant4991P → L in TDH2A. Ref.23
VAR_021630
Natural variant5271W → C in TDH2A. Ref.16
VAR_021631
Natural variant5331G → C in TDH2A; partial defect; expression slightly lower in efficiency and more degenerative than wild-type enzyme. Ref.22
VAR_027229
Natural variant574 – 5752Missing in TDH2A; partial defect; expressed on the plasma membrane surface at less than half the rate of wild-type enzyme.
VAR_027230
Natural variant5901G → S in TDH2A. Ref.11
VAR_027231
Natural variant6181V → M.
Corresponds to variant rs10189135 [ dbSNP | Ensembl ].
VAR_027232
Natural variant6481R → Q in TDH2A. Ref.14
VAR_013138
Natural variant6601Q → E in TDH2A. Ref.13
Corresponds to variant rs121908088 [ dbSNP | Ensembl ].
VAR_021632
Natural variant6651R → W in TDH2A; fails to localize to the plasma membrane. Ref.18
VAR_021633
Natural variant6931R → W in TDH2A. Ref.16 Ref.24
VAR_021634
Natural variant7061M → V.
Corresponds to variant rs13431173 [ dbSNP | Ensembl ].
VAR_027233
Natural variant7251T → P. Ref.1 Ref.2 Ref.6 Ref.7 Ref.11
Corresponds to variant rs732609 [ dbSNP | Ensembl ].
VAR_006061
Natural variant7711G → R in TDH2A; fails to localize to the plasma membrane. Ref.18
VAR_021635
Natural variant7931L → P.
Corresponds to variant rs28991293 [ dbSNP | Ensembl ].
VAR_027234
Natural variant7961D → Y in TDH2A. Ref.20
VAR_021636
Natural variant7991E → K in TDH2A. Ref.11 Ref.14 Ref.16
Corresponds to variant rs121908085 [ dbSNP | Ensembl ].
VAR_006062
Natural variant8081C → R in TDH2A. Ref.23
VAR_021637
Natural variant8391V → I in TDH2A. Ref.21
VAR_027235
Natural variant8461R → W.
Corresponds to variant rs28913014 [ dbSNP | Ensembl ].
VAR_027236
Natural variant8471V → A. Ref.1 Ref.2 Ref.6 Ref.7
Corresponds to variant rs1126799 [ dbSNP | Ensembl ].
VAR_027237

Experimental info

Sequence conflict701P → G in AAA61217. Ref.5
Sequence conflict3541A → G Ref.5
Sequence conflict3541A → G Ref.8
Sequence conflict3711A → R in AAA61215. Ref.1
Sequence conflict3711A → R in AAA61216. Ref.1
Sequence conflict3811I → N Ref.5
Sequence conflict3811I → N Ref.8
Sequence conflict5741D → N in CAA68467. Ref.2
Sequence conflict7321W → C in AAN11302. Ref.7
Sequence conflict7481V → M Ref.2
Sequence conflict7481V → M Ref.7
Sequence conflict8161N → S in AAL74416. Ref.6
Sequence conflict8721R → K Ref.2
Sequence conflict8721R → K Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TPO1) [UniParc].

Last modified November 13, 2007. Version 4.
Checksum: F67C5F1A4AEE0B29

FASTA933102,963
        10         20         30         40         50         60 
MRALAVLSVT LVMACTEAFF PFISRGKELL WGKPEESRVS SVLEESKRLV DTAMYATMQR 

        70         80         90        100        110        120 
NLKKRGILSP AQLLSFSKLP EPTSGVIARA AEIMETSIQA MKRKVNLKTQ QSQHPTDALS 

       130        140        150        160        170        180 
EDLLSIIANM SGCLPYMLPP KCPNTCLANK YRPITGACNN RDHPRWGASN TALARWLPPV 

       190        200        210        220        230        240 
YEDGFSQPRG WNPGFLYNGF PLPPVREVTR HVIQVSNEVV TDDDRYSDLL MAWGQYIDHD 

       250        260        270        280        290        300 
IAFTPQSTSK AAFGGGADCQ MTCENQNPCF PIQLPEEARP AAGTACLPFY RSSAACGTGD 

       310        320        330        340        350        360 
QGALFGNLST ANPRQQMNGL TSFLDASTVY GSSPALERQL RNWTSAEGLL RVHARLRDSG 

       370        380        390        400        410        420 
RAYLPFVPPR APAACAPEPG IPGETRGPCF LAGDGRASEV PSLTALHTLW LREHNRLAAA 

       430        440        450        460        470        480 
LKALNAHWSA DAVYQEARKV VGALHQIITL RDYIPRILGP EAFQQYVGPY EGYDSTANPT 

       490        500        510        520        530        540 
VSNVFSTAAF RFGHATIHPL VRRLDASFQE HPDLPGLWLH QAFFSPWTLL RGGGLDPLIR 

       550        560        570        580        590        600 
GLLARPAKLQ VQDQLMNEEL TERLFVLSNS STLDLASINL QRGRDHGLPG YNEWREFCGL 

       610        620        630        640        650        660 
PRLETPADLS TAIASRSVAD KILDLYKHPD NIDVWLGGLA ENFLPRARTG PLFACLIGKQ 

       670        680        690        700        710        720 
MKALRDGDWF WWENSHVFTD AQRRELEKHS LSRVICDNTG LTRVPMDAFQ VGKFPEDFES 

       730        740        750        760        770        780 
CDSITGMNLE AWRETFPQDD KCGFPESVEN GDFVHCEESG RRVLVYSCRH GYELQGREQL 

       790        800        810        820        830        840 
TCTQEGWDFQ PPLCKDVNEC ADGAHPPCHA SARCRNTKGG FQCLCADPYE LGDDGRTCVD 

       850        860        870        880        890        900 
SGRLPRVTWI SMSLAALLIG GFAGLTSTVI CRWTRTGTKS TLPISETGGG TPELRCGKHQ 

       910        920        930 
AVGTSPQRAA AQDSEQESAG MEGRDTHRLP RAL 

« Hide

Isoform 2 (TPO2) [UniParc].

Checksum: F4CF0D050608F808
Show »

FASTA87696,699
Isoform 3 (TPO3) (Graves' disease) (TPOzaninelli) [UniParc].

Checksum: 423AC29EEB27277B
Show »

FASTA929102,771
Isoform 4 (TPO4) [UniParc].

Checksum: F9C575FC93A450C8
Show »

FASTA88998,327
Isoform 5 (TPO5) [UniParc].

Checksum: 3C6150EA7E602B78
Show »

FASTA76084,581
Isoform 6 (TPO6) [UniParc].

Checksum: 7AD0B6FA3206066A
Show »

FASTA61167,293
Isoform 2-3 [UniParc].

Checksum: 3EDC31BFE86C24E2
Show »

FASTA87296,507
Isoform 2-4 [UniParc].

Checksum: 7C6D17A3B62C1D7D
Show »

FASTA83292,063

References

[1]"Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs."
Kimura S., Kotani T., McBride O.W., Umeki K., Hirai K., Nakayama T., Ohtaki S.
Proc. Natl. Acad. Sci. U.S.A. 84:5555-5559(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-725 AND ALA-847.
[2]"Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA."
Libert F., Ruel J., Ludgate M., Swillens S., Alexander N., Vassart G., Dinsart C.
Nucleic Acids Res. 15:6735-6735(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-725 AND ALA-847.
Tissue: Thyroid.
[3]"Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene."
Kimura S., Hong Y.S., Kotani T., Ohtaki S., Kikkawa F.
Biochemistry 28:4481-4489(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2."
Barnett P.S., Banga J.P., Watkins J., Huang G.C., Gluckman D.R.B., Page M.J., McGregor A.M.
Nucleic Acids Res. 18:670-670(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Thyroid.
[5]Rapoport B.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-257.
Tissue: Thyroid.
[6]"Homo sapiens thyroid peroxidase (TPO) variant mRNA, alternatively spliced sequence."
Hennen G.P., Igout A., Melen L.B.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANTS SER-257; PRO-725 AND ALA-847.
Tissue: Thyroid.
[7]"Increasing diversity of human thyroperoxidase generated by alternative splicing. Characterization by molecular cloning of new transcripts with single- and multispliced mRNAs."
Ferrand M., Le Fourn V., Franc J.-L.
J. Biol. Chem. 278:3793-3800(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 2-3 AND 2-4), VARIANTS PRO-725 AND ALA-847.
Tissue: Thyroid.
[8]"Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase."
Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., Degroot L.J., Rapoport B.
J. Clin. Invest. 80:1205-1208(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 217-496.
[9]"Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease."
Zanelli E., Henry M., Charvet B., Malthiery Y.
Biochem. Biophys. Res. Commun. 170:735-741(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 670-933 (ISOFORM 3), ALTERNATIVE SPLICING IN GRAVES' DISEASE.
Tissue: Thyroid.
[10]"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DUOX1; DUOX2 AND CYBA.
[11]"Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis."
Bikker H., Vulsma T., Baas F., de Vijlder J.J.M.
Hum. Mutat. 6:9-16(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A ASP-453; SER-590 AND LYS-799, VARIANTS SER-257; SER-373; THR-398 AND PRO-725.
[12]"Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects."
Bikker H., Baas F., De Vijlder J.J.M.
J. Clin. Endocrinol. Metab. 82:649-653(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A PHE-447.
[13]"A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect."
Santos C.L.S., Bikker H., Rego K.G.M., Nascimento A.C., Tambascia M., De Vijlder J.J.M., Medeiros-Neto G.
Clin. Endocrinol. (Oxf.) 51:165-172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A GLU-660.
[14]"Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping."
Pannain S., Weiss R.E., Jackson C.E., Dian D., Beck J.C., Sheffield V.C., Cox N., Refetoff S.
J. Clin. Endocrinol. Metab. 84:1061-1071(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A GLN-648 AND LYS-799.
[15]"A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect."
Kotani T., Umeki K., Yamamoto I., Maesaka H., Tachibana K., Ohtaki S.
J. Endocrinol. 160:267-273(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A ASN-240, CHARACTERIZATION OF VARIANT TDH2A ASN-240.
[16]"Two decades of screening for congenital hypothyroidism in The Netherlands: TPO gene mutations in total iodide organification defects (an update)."
Bakker B., Bikker H., Vulsma T., de Randamie J.S.E., Wiedijk B.M., De Vijlder J.J.M.
J. Clin. Endocrinol. Metab. 85:3708-3712(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A THR-326; PHE-447; ASP-453; CYS-527; TRP-693 AND LYS-799.
[17]"Novel mutations of the thyroid peroxidase gene in patients with permanent congenital hypothyroidism."
Ambrugger P., Stoeva I., Biebermann H., Torresani T., Leitner C., Grueters A.
Eur. J. Endocrinol. 145:19-24(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A PRO-458 AND HIS-491.
[18]"Two novel missense mutations in the thyroid peroxidase gene, R665W and G771R, result in a localization defect and cause congenital hypothyroidism."
Umeki K., Kotani T., Kawano J., Suganuma T., Yamamoto I., Aratake Y., Furujo M., Ichiba Y.
Eur. J. Endocrinol. 146:491-498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A TRP-665 AND ARG-771, CHARACTERIZATION OF VARIANTS TDH2A TRP-665 AND ARG-771.
[19]"High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase gene in Taiwanese patients with total iodide organification defect, and evidence for a founder effect."
Niu D.-M., Hwang B., Chu Y.-K., Liao C.-J., Wang P.-L., Lin C.-Y.
J. Clin. Endocrinol. Metab. 87:4208-4212(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A PRO-53.
[20]"Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations."
Wu J.-Y., Shu S.-G., Yang C.-F., Lee C.-C., Tsai F.-J.
J. Endocrinol. 172:627-635(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A SER-493 AND TYR-796.
[21]"Genetics of specific phenotypes of congenital hypothyroidism: a population-based approach."
Calaciura F., Miscio G., Coco A., Leonardi D., Cisternino C., Regalbuto C., Bozzali M., Maiorana R., Ranieri A., Carta A., Buscema M., Trischitta V., Sava L., Tassi V.
Thyroid 12:945-951(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A ILE-839.
[22]"Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings."
Kotani T., Umeki K., Kawano J., Suganuma T., Hishinuma A., Ieiri T., Harada S.
Clin. Endocrinol. (Oxf.) 59:198-206(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL, CHARACTERIZATION OF VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL.
[23]"Five novel inactivating mutations in the thyroid peroxidase gene responsible for congenital goiter and iodide organification defect."
Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Moya C.M., Domene S., Varela V., Targovnik H.M.
Hum. Mutat. 22:259-259(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH2A THR-307; MET-433; LEU-499 AND ARG-808.
[24]"Monoallelic expression of mutant thyroid peroxidase allele causing total iodide organification defect."
Fugazzola L., Cerutti N., Mannavola D., Vannucchi G., Fallini C., Persani L., Beck-Peccoz P.
J. Clin. Endocrinol. Metab. 88:3264-3271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A TRP-693.
[25]"Two novel mutations in the thyroid peroxidase gene with goitrous hypothyroidism."
Tajima T., Tsubaki J., Fujieda K.
Endocr. J. 52:643-645(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A LYS-378.
[26]"Goitrous congenital hypothyroidism and hearing impairment associated with mutations in the TPO and SLC26A4/PDS genes."
Pfarr N., Borck G., Turk A., Napiontek U., Keilmann A., Mueller-Forell W., Kopp P., Pohlenz J.
J. Clin. Endocrinol. Metab. 91:2678-2681(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH2A ASP-453.
+Additional computationally mapped references.

Web resources

Wikipedia

Thyroid peroxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02969 mRNA. Translation: AAA61215.1.
J02970 mRNA. Translation: AAA61216.1.
Y00406 mRNA. Translation: CAA68467.1.
M25715 expand/collapse EMBL AC list , M25702, M25703, M25704, M25705, M25706, M25707, M25708, M25709, M25710, M25711, M25712, M25713, M25714 Genomic DNA. Translation: AAA97517.1.
X17358 mRNA. Translation: CAA35235.1.
M17755 mRNA. Translation: AAA61217.2.
AF439430 mRNA. Translation: AAL74416.1.
AF533528 mRNA. Translation: AAN04471.1.
AY136822 mRNA. Translation: AAN11302.1.
AF533529 mRNA. Translation: AAN04472.1.
AF533530 mRNA. Translation: AAN04473.1.
AF533531 mRNA. Translation: AAN04474.1.
M55702 mRNA. Translation: AAA61219.1.
M55702 mRNA. Translation: AAA61218.1.
PIROPHUIT. A32413.
RefSeqNP_000538.3. NM_000547.5.
NP_001193673.1. NM_001206744.1.
NP_001193674.1. NM_001206745.1.
NP_783650.1. NM_175719.3.
NP_783652.1. NM_175721.3.
NP_783653.1. NM_175722.3.
UniGeneHs.467554.

3D structure databases

ProteinModelPortalP07202.
SMRP07202. Positions 149-843.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP07202.
ChEMBLCHEMBL1839.
DrugBankDB00389. Carbimazole.
DB00763. Methimazole.
DB00550. Propylthiouracil.
GuidetoPHARMACOLOGY2526.

Protein family/group databases

Allergome9554. Hom s TPO.
PeroxiBase3318. HsTPO01.

PTM databases

PhosphoSiteP07202.

Polymorphism databases

DMDM160281455.

Proteomic databases

PaxDbP07202.
PRIDEP07202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329066; ENSP00000329869; ENSG00000115705. [P07202-1]
ENST00000345913; ENSP00000318820; ENSG00000115705. [P07202-1]
ENST00000346956; ENSP00000263886; ENSG00000115705. [P07202-4]
ENST00000349624; ENSP00000332044; ENSG00000115705. [P07202-5]
ENST00000382198; ENSP00000371633; ENSG00000115705. [P07202-5]
ENST00000382201; ENSP00000371636; ENSG00000115705. [P07202-2]
GeneID7173.
KEGGhsa:7173.
UCSCuc002qwr.3. human. [P07202-1]
uc002qwu.3. human. [P07202-2]
uc010yio.2. human. [P07202-5]
uc010yip.2. human. [P07202-4]

Organism-specific databases

CTD7173.
GeneCardsGC02P001396.
H-InvDBHIX0029848.
HGNCHGNC:12015. TPO.
HPACAB009587.
HPA007987.
MIM274500. phenotype.
606765. gene.
neXtProtNX_P07202.
Orphanet95716. Familial thyroid dyshormonogenesis.
PharmGKBPA36694.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262194.
HOVERGENHBG000071.
InParanoidP07202.
KOK00431.
OMAIMETSIQ.
OrthoDBEOG7D2FD6.
PhylomeDBP07202.
TreeFamTF314316.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00194.

Gene expression databases

ArrayExpressP07202.
BgeeP07202.
GenevestigatorP07202.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00032. CCP. 1 hit.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPO. human.
GenomeRNAi7173.
NextBio28112.
PROP07202.
SOURCESearch...

Entry information

Entry namePERT_HUMAN
AccessionPrimary (citable) accession number: P07202
Secondary accession number(s): P09934 expand/collapse secondary AC list , P09935, Q8IUL0, Q8NF94, Q8NF95, Q8NF96, Q8NF97, Q8TCI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 185 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM