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P01266 (THYG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Thyroglobulin

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

Protein attributes

Sequence length2768 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).

Subunit structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Thyroid gland specific.

Post-translational modification

Sulfated tyrosines are desulfated during iodination.

Involvement in disease

Thyroid dyshormonogenesis 3 (TDH3) [MIM:274700]: A disorder due to thyroid dyshormonogenesis, causing large goiters of elastic and soft consistency in the majority of patients. Although the degree of thyroid dysfunction varies considerably among patients with defective thyroglobulin synthesis, patients usually have a relatively high serum free triiodothyronine (T3) concentration with disproportionately low free tetraiodothyronine (T4) level. The maintenance of relatively high free T3 levels prevents profound tissue hypothyroidism except in brain and pituitary, which are dependent on T4 supply, resulting in neurologic and intellectual defects in some cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.22 Ref.23 Ref.24 Ref.25

Autoimmune thyroid disease 3 (AITD3) [MIM:608175]: A complex autoimmune disorder comprising two related diseases affecting the thyroid: Graves disease and Hashimoto thyroiditis. In both disorders, thyroid-reactive T-cells are formed and infiltrate the thyroid gland. In Graves disease, the majority of the T-cells undergo a Th2 differentiation and activate B-cells to produce antibodies against the TSH receptor, which stimulate the thyroid and cause clinical hyperthyroidism. In contrast, Hashimoto thyroiditis is characterized by Th1 switching of the thyroid-infiltrating T-cells, which induces apoptosis of thyroid follicular cells and clinical hypothyroidism.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.21

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Contains 11 thyroglobulin type-1 domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01266-1)

Also known as: Major;

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: P01266-2)

Also known as: Minor;

The sequence of this isoform differs from the canonical sequence as follows:
     1510-1567: CVTDCQRNEAGLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWWETEAPLEDSQCLM → L

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 27682749Thyroglobulin
PRO_0000008636

Regions

Domain31 – 9262Thyroglobulin type-1 1
Domain93 – 16068Thyroglobulin type-1 2
Domain161 – 297137Thyroglobulin type-1 3
Domain298 – 35861Thyroglobulin type-1 4
Domain605 – 65854Thyroglobulin type-1 5
Domain659 – 72668Thyroglobulin type-1 6
Domain727 – 921195Thyroglobulin type-1 7
Domain922 – 1073152Thyroglobulin type-1 8
Domain1074 – 114572Thyroglobulin type-1 9
Domain1146 – 121065Thyroglobulin type-1 10
Repeat1456 – 146914Type II
Repeat1470 – 148617Type II
Repeat1487 – 150317Type II
Domain1511 – 156555Thyroglobulin type-1 11
Repeat1603 – 1723121Type IIIA
Repeat1724 – 1892169Type IIIB
Repeat1893 – 1995103Type IIIA
Repeat1996 – 2129134Type IIIB
Repeat2130 – 218758Type IIIA

Sites

Site1101Not glycosylated (PubMed:8615697)
Site4961Not glycosylated (PubMed:8615697)
Site18691Not glycosylated (PubMed:8615697)
Site21221Not glycosylated (PubMed:8615697)

Amino acid modifications

Modified residue241Sulfotyrosine; alternate By similarity
Modified residue241Thyroxine; alternate
Modified residue13101Thyroxine
Modified residue25731Thyroxine
Modified residue25871Thyroxine
Modified residue27661Triiodothyronine
Glycosylation761N-linked (GlcNAc...) Ref.13
Glycosylation1981N-linked (GlcNAc...) Ref.13
Glycosylation4841N-linked (GlcNAc...) Ref.13
Glycosylation5291N-linked (GlcNAc...) Ref.13
Glycosylation7481N-linked (GlcNAc...) Ref.13
Glycosylation8161N-linked (GlcNAc...) Ref.13
Glycosylation9471N-linked (GlcNAc...) Ref.13
Glycosylation12201N-linked (GlcNAc...) Ref.13
Glycosylation13481N-linked (GlcNAc...) Probable
Glycosylation13491N-linked (GlcNAc...) Ref.13
Glycosylation13651N-linked (GlcNAc...) Ref.13
Glycosylation17161N-linked (GlcNAc...) Ref.13
Glycosylation17741N-linked (GlcNAc...) Ref.13
Glycosylation20131N-linked (GlcNAc...) Ref.13
Glycosylation22501N-linked (GlcNAc...) Ref.13
Glycosylation22951N-linked (GlcNAc...) Ref.13
Glycosylation25821N-linked (GlcNAc...) Ref.13
Glycosylation27491O-linked (Xyl...) (chondroitin sulfate) Ref.18
Disulfide bond34 ↔ 52 By similarity
Disulfide bond63 ↔ 70 By similarity
Disulfide bond72 ↔ 92 By similarity
Disulfide bond96 ↔ 120 By similarity
Disulfide bond131 ↔ 138 By similarity
Disulfide bond140 ↔ 160 By similarity
Disulfide bond164 ↔ 183 By similarity
Disulfide bond194 ↔ 235 By similarity
Disulfide bond301 ↔ 319 By similarity
Disulfide bond330 ↔ 336 By similarity
Disulfide bond338 ↔ 358 By similarity
Disulfide bond608 ↔ 620 By similarity
Disulfide bond631 ↔ 636 By similarity
Disulfide bond638 ↔ 658 By similarity
Disulfide bond662 ↔ 687 By similarity
Disulfide bond698 ↔ 703 By similarity
Disulfide bond705 ↔ 726 By similarity
Disulfide bond730 ↔ 763 By similarity
Disulfide bond774 ↔ 898 By similarity
Disulfide bond900 ↔ 921 By similarity
Disulfide bond1042 ↔ 1049 By similarity
Disulfide bond1051 ↔ 1073 By similarity
Disulfide bond1077 ↔ 1108 By similarity
Disulfide bond1126 ↔ 1145 By similarity
Disulfide bond1149 ↔ 1169 By similarity
Disulfide bond1181 ↔ 1188 By similarity
Disulfide bond1190 ↔ 1210 By similarity
Disulfide bond1514 ↔ 1523 By similarity
Disulfide bond1543 ↔ 1565 By similarity
Disulfide bond2264 ↔ 2281 Potential

Natural variations

Alternative sequence1510 – 156758CVTDC…SQCLM → L in isoform 2.
VSP_012655
Natural variant1351Q → H. Ref.20
Corresponds to variant rs2069546 [ dbSNP | Ensembl ].
VAR_010212
Natural variant1831C → Y in TDH3. Ref.23
VAR_063034
Natural variant5151Q → E. Ref.3
Corresponds to variant rs180222 [ dbSNP | Ensembl ].
VAR_016190
Natural variant6041S → D Requires 2 nucleotide substitutions. Ref.1 Ref.4 Ref.20
Corresponds to variant rs2069547 [ dbSNP | Ensembl ].
VAR_016852
Natural variant6531G → D. Ref.1 Ref.4 Ref.20
Corresponds to variant rs2069548 [ dbSNP | Ensembl ].
VAR_016853
Natural variant7341S → A Polymorphism associated with AITD3. Ref.5 Ref.20 Ref.21
Corresponds to variant rs180223 [ dbSNP | Ensembl ].
VAR_010213
Natural variant7771P → L.
Corresponds to variant rs3739274 [ dbSNP | Ensembl ].
VAR_049077
Natural variant8151G → R.
Corresponds to variant rs16904774 [ dbSNP | Ensembl ].
VAR_049078
Natural variant8301Q → E. Ref.20
Corresponds to variant rs2076737 [ dbSNP | Ensembl ].
VAR_010214
Natural variant8701Q → H. Ref.19
Corresponds to variant rs2229843 [ dbSNP | Ensembl ].
VAR_002365
Natural variant9851Missing. Ref.1 Ref.20
VAR_016854
Natural variant9881R → P.
Corresponds to variant rs16893332 [ dbSNP | Ensembl ].
VAR_049079
Natural variant10281M → V Polymorphism associated with AITD3. Ref.20 Ref.21
Corresponds to variant rs853326 [ dbSNP | Ensembl ].
VAR_010215
Natural variant10431H → Y. Ref.1 Ref.20
VAR_016855
Natural variant10591I → T. Ref.1 Ref.20
VAR_016856
Natural variant10631L → M.
Corresponds to variant rs11992497 [ dbSNP | Ensembl ].
VAR_049080
Natural variant12221S → L.
Corresponds to variant rs12549018 [ dbSNP | Ensembl ].
VAR_049081
Natural variant12641C → R in TDH3; autosomal recessive. Ref.20
Corresponds to variant rs2076738 [ dbSNP | Ensembl ].
VAR_010216
Natural variant13121D → G. Ref.1 Ref.2 Ref.7
Corresponds to variant rs2069556 [ dbSNP | Ensembl ].
VAR_010217
Natural variant14371W → R. Ref.1 Ref.20
Corresponds to variant rs2069558 [ dbSNP | Ensembl ].
VAR_016857
Natural variant14631P → H. Ref.1 Ref.20
VAR_016858
Natural variant17401T → K.
Corresponds to variant rs16904791 [ dbSNP | Ensembl ].
VAR_049082
Natural variant18381D → N. Ref.20
Corresponds to variant rs2069561 [ dbSNP | Ensembl ].
VAR_010218
Natural variant18971C → Y in TDH3. Ref.22
VAR_063035
Natural variant19361A → T. Ref.1 Ref.20
Corresponds to variant rs2069562 [ dbSNP | Ensembl ].
VAR_016859
Natural variant19741M → T.
Corresponds to variant rs56230101 [ dbSNP | Ensembl ].
VAR_061173
Natural variant19791R → W Polymorphism associated with AITD3. Ref.21
VAR_032013
Natural variant19961C → S in TDH3; autosomal recessive. Ref.20
Corresponds to variant rs2076739 [ dbSNP | Ensembl ].
VAR_010219
Natural variant19991R → W. Ref.20
Corresponds to variant rs2076740 [ dbSNP | Ensembl ].
VAR_010220
Natural variant20911D → E. Ref.1 Ref.20
VAR_016860
Natural variant21491P → L. Ref.1 Ref.8 Ref.20
Corresponds to variant rs2069564 [ dbSNP | Ensembl ].
VAR_016861
Natural variant21701Q → R. Ref.1 Ref.8 Ref.20
Corresponds to variant rs2069565 [ dbSNP | Ensembl ].
VAR_016862
Natural variant22341A → D in TDH3; reduces thyroglobulin synthesis and secretion; promotes thyroglobulin retention within the endoplasmic reticulum. Ref.23 Ref.25
VAR_063036
Natural variant22421R → H. Ref.1 Ref.20
Corresponds to variant rs2069566 [ dbSNP | Ensembl ].
VAR_016863
Natural variant23361R → Q in TDH3. Ref.22
VAR_063037
Natural variant23751G → R in TDH3. Ref.24
VAR_063038
Natural variant24551R → H.
Corresponds to variant rs2272707 [ dbSNP | Ensembl ].
VAR_049083
Natural variant24691L → P.
Corresponds to variant rs2069568 [ dbSNP | Ensembl ].
VAR_049084
Natural variant25011W → R. Ref.20
Corresponds to variant rs2069569 [ dbSNP | Ensembl ].
VAR_010221
Natural variant25261F → L.
Corresponds to variant rs12114109 [ dbSNP | Ensembl ].
VAR_049085
Natural variant25301R → Q. Ref.20
Corresponds to variant rs1133076 [ dbSNP | Ensembl ].
VAR_010222
Natural variant26161N → S.
Corresponds to variant rs10091530 [ dbSNP | Ensembl ].
VAR_049086

Experimental info

Sequence conflict23 – 253EYQ → GKF in CAA26527. Ref.6
Sequence conflict8481Missing AA sequence Ref.13
Sequence conflict984 – 9852EQ → DR in CAA29456. Ref.5
Sequence conflict1359 – 13602Missing AA sequence Ref.13
Sequence conflict17171L → A AA sequence Ref.13
Sequence conflict17761T → S AA sequence Ref.13
Sequence conflict20191G → H AA sequence Ref.13
Sequence conflict22871F → P AA sequence Ref.13

Sequences

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

Last modified February 20, 2007. Version 5.
Checksum: 69A87D935F1BAA72

FASTA2,768304,790
        10         20         30         40         50         60 
MALVLEIFTL LASICWVSAN IFEYQVDAQP LRPCELQRET AFLKQADYVP QCAEDGSFQT 

        70         80         90        100        110        120 
VQCQNDGRSC WCVGANGSEV LGSRQPGRPV ACLSFCQLQK QQILLSGYIN STDTSYLPQC 

       130        140        150        160        170        180 
QDSGDYAPVQ CDVQQVQCWC VDAEGMEVYG TRQLGRPKRC PRSCEIRNRR LLHGVGDKSP 

       190        200        210        220        230        240 
PQCSAEGEFM PVQCKFVNTT DMMIFDLVHS YNRFPDAFVT FSSFQRRFPE VSGYCHCADS 

       250        260        270        280        290        300 
QGRELAETGL ELLLDEIYDT IFAGLDLPST FTETTLYRIL QRRFLAVQSV ISGRFRCPTK 

       310        320        330        340        350        360 
CEVERFTATS FGHPYVPSCR RNGDYQAVQC QTEGPCWCVD AQGKEMHGTR QQGEPPSCAE 

       370        380        390        400        410        420 
GQSCASERQQ ALSRLYFGTS GYFSQHDLFS SPEKRWASPR VARFATSCPP TIKELFVDSG 

       430        440        450        460        470        480 
LLRPMVEGQS QQFSVSENLL KEAIRAIFPS RGLARLALQF TTNPKRLQQN LFGGKFLVNV 

       490        500        510        520        530        540 
GQFNLSGALG TRGTFNFSQF FQQLGLASFL NGGRQEDLAK PLSVGLDSNS STGTPEAAKK 

       550        560        570        580        590        600 
DGTMNKPTVG SFGFEINLQE NQNALKFLAS LLELPEFLLF LQHAISVPED VARDLGDVME 

       610        620        630        640        650        660 
TVLSSQTCEQ TPERLFVPSC TTEGSYEDVQ CFSGECWCVN SWGKELPGSR VRGGQPRCPT 

       670        680        690        700        710        720 
DCEKQRARMQ SLMGSQPAGS TLFVPACTSE GHFLPVQCFN SECYCVDAEG QAIPGTRSAI 

       730        740        750        760        770        780 
GKPKKCPTPC QLQSEQAFLR TVQALLSNSS MLPTLSDTYI PQCSTDGQWR QVQCNGPPEQ 

       790        800        810        820        830        840 
VFELYQRWEA QNKGQDLTPA KLLVKIMSYR EAASGNFSLF IQSLYEAGQQ DVFPVLSQYP 

       850        860        870        880        890        900 
SLQDVPLAAL EGKRPQPREN ILLEPYLFWQ ILNGQLSQYP GSYSDFSTPL AHFDLRNCWC 

       910        920        930        940        950        960 
VDEAGQELEG MRSEPSKLPT CPGSCEEAKL RVLQFIRETE EIVSASNSSR FPLGESFLVA 

       970        980        990       1000       1010       1020 
KGIRLRNEDL GLPPLFPPRE AFAEQFLRGS DYAIRLAAQS TLSFYQRRRF SPDDSAGASA 

      1030       1040       1050       1060       1070       1080 
LLRSGPYMPQ CDAFGSWEPV QCHAGTGHCW CVDEKGGFIP GSLTARSLQI PQCPTTCEKS 

      1090       1100       1110       1120       1130       1140 
RTSGLLSSWK QARSQENPSP KDLFVPACLE TGEYARLQAS GAGTWCVDPA SGEELRPGSS 

      1150       1160       1170       1180       1190       1200 
SSAQCPSLCN VLKSGVLSRR VSPGYVPACR AEDGGFSPVQ CDQAQGSCWC VMDSGEEVPG 

      1210       1220       1230       1240       1250       1260 
TRVTGGQPAC ESPRCPLPFN ASEVVGGTIL CETISGPTGS AMQQCQLLCR QGSWSVFPPG 

      1270       1280       1290       1300       1310       1320 
PLICSLESGR WESQLPQPRA CQRPQLWQTI QTQGHFQLQL PPGKMCSADY ADLLQTFQVF 

      1330       1340       1350       1360       1370       1380 
ILDELTARGF CQIQVKTFGT LVSIPVCNNS SVQVGCLTRE RLGVNVTWKS RLEDIPVASL 

      1390       1400       1410       1420       1430       1440 
PDLHDIERAL VGKDLLGRFT DLIQSGSFQL HLDSKTFPAE TIRFLQGDHF GTSPRTWFGC 

      1450       1460       1470       1480       1490       1500 
SEGFYQVLTS EASQDGLGCV KCPEGSYSQD EECIPCPVGF YQEQAGSLAC VPCPVGRTTI 

      1510       1520       1530       1540       1550       1560 
SAGAFSQTHC VTDCQRNEAG LQCDQNGQYR ASQKDRGSGK AFCVDGEGRR LPWWETEAPL 

      1570       1580       1590       1600       1610       1620 
EDSQCLMMQK FEKVPESKVI FDANAPVAVR SKVPDSEFPV MQCLTDCTED EACSFFTVST 

      1630       1640       1650       1660       1670       1680 
TEPEISCDFY AWTSDNVACM TSDQKRDALG NSKATSFGSL RCQVKVRSHG QDSPAVYLKK 

      1690       1700       1710       1720       1730       1740 
GQGSTTTLQK RFEPTGFQNM LSGLYNPIVF SASGANLTDA HLFCLLACDR DLCCDGFVLT 

      1750       1760       1770       1780       1790       1800 
QVQGGAIICG LLSSPSVLLC NVKDWMDPSE AWANATCPGV TYDQESHQVI LRLGDQEFIK 

      1810       1820       1830       1840       1850       1860 
SLTPLEGTQD TFTNFQQVYL WKDSDMGSRP ESMGCRKDTV PRPASPTEAG LTTELFSPVD 

      1870       1880       1890       1900       1910       1920 
LNQVIVNGNQ SLSSQKHWLF KHLFSAQQAN LWCLSRCVQE HSFCQLAEIT ESASLYFTCT 

      1930       1940       1950       1960       1970       1980 
LYPEAQVCDD IMESNAQGCR LILPQMPKAL FRKKVILEDK VKNFYTRLPF QKLMGISIRN 

      1990       2000       2010       2020       2030       2040 
KVPMSEKSIS NGFFECERRC DADPCCTGFG FLNVSQLKGG EVTCLTLNSL GIQMCSEENG 

      2050       2060       2070       2080       2090       2100 
GAWRILDCGS PDIEVHTYPF GWYQKPIAQN NAPSFCPLVV LPSLTEKVSL DSWQSLALSS 

      2110       2120       2130       2140       2150       2160 
VVVDPSIRHF DVAHVSTAAT SNFSAVRDLC LSECSQHEAC LITTLQTQPG AVRCMFYADT 

      2170       2180       2190       2200       2210       2220 
QSCTHSLQGQ NCRLLLREEA THIYRKPGIS LLSYEASVPS VPISTHGRLL GRSQAIQVGT 

      2230       2240       2250       2260       2270       2280 
SWKQVDQFLG VPYAAPPLAE RRFQAPEPLN WTGSWDASKP RASCWQPGTR TSTSPGVSED 

      2290       2300       2310       2320       2330       2340 
CLYLNVFIPQ NVAPNASVLV FFHNTMDREE SEGWPAIDGS FLAAVGNLIV VTASYRVGVF 

      2350       2360       2370       2380       2390       2400 
GFLSSGSGEV SGNWGLLDQV AALTWVQTHI RGFGGDPRRV SLAADRGGAD VASIHLLTAR 

      2410       2420       2430       2440       2450       2460 
ATNSQLFRRA VLMGGSALSP AAVISHERAQ QQAIALAKEV SCPMSSSQEV VSCLRQKPAN 

      2470       2480       2490       2500       2510       2520 
VLNDAQTKLL AVSGPFHYWG PVIDGHFLRE PPARALKRSL WVEVDLLIGS SQDDGLINRA 

      2530       2540       2550       2560       2570       2580 
KAVKQFEESR GRTSSKTAFY QALQNSLGGE DSDARVEAAA TWYYSLEHST DDYASFSRAL 

      2590       2600       2610       2620       2630       2640 
ENATRDYFII CPIIDMASAW AKRARGNVFM YHAPENYGHG SLELLADVQF ALGLPFYPAY 

      2650       2660       2670       2680       2690       2700 
EGQFSLEEKS LSLKIMQYFS HFIRSGNPNY PYEFSRKVPT FATPWPDFVP RAGGENYKEF 

      2710       2720       2730       2740       2750       2760 
SELLPNRQGL KKADCSFWSK YISSLKTSAD GAKGGQSAES EEEELTAGSG LREDLLSLQE 


PGSKTYSK 

« Hide

Isoform 2 (Minor) [UniParc].

Checksum: EEC6895F22D55EE0
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FASTA2,711298,383

References

« Hide 'large scale' references
[1]"Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA."
Malthiery Y., Lissitzky S.
Eur. J. Biochem. 165:491-498(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-604; ASP-653; GLN-985 DEL; TYR-1043; THR-1059; GLY-1312; ARG-1437; HIS-1463; THR-1936; GLU-2091; LEU-2149; ARG-2170 AND HIS-2242.
[2]"The revised 8307 base pair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells."
van de Graaf S.A.R., Pauws E., de Vijlder J.J.M., Ris-Stalpers C.
Eur. J. Endocrinol. 136:508-515(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-1312.
Tissue: Thyroid.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-515.
[4]"Sequence of the 5'-end quarter of the human-thyroglobulin messenger ribonucleic acid and of its deduced amino-acid sequence."
Malthiery Y., Lissitzky S.
Eur. J. Biochem. 147:53-58(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-730, VARIANTS ASP-604 AND ASP-653.
[5]"Structural organization of the 5' region of the thyroglobulin gene. Evidence for intron loss and 'exonization' during evolution."
Parma J., Christophe D., Pohl V., Vassart G.
J. Mol. Biol. 196:769-779(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-415; 640-737 AND 880-1000, VARIANT ALA-734.
[6]"An unusually long poly(purine)-poly(pyrimidine) sequence is located upstream from the human thyroglobulin gene."
Christophe D., Cabrer B., Bacolla A., Targovnik H.M., Pohl V., Vassart G.
Nucleic Acids Res. 13:5127-5144(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[7]"Genomic organization of the 5' region of the human thyroglobulin gene."
Moya C.M., Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.
Eur. J. Endocrinol. 143:789-798(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1002-1566 (ISOFORM 1), VARIANT GLY-1312.
[8]"Genomic organization of the 3' region of the human thyroglobulin gene."
Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.
Thyroid 9:903-912(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1645-2768, VARIANTS LEU-2149 AND ARG-2170.
[9]"Identification of a minor Tg mRNA transcript in RNA from normal and goitrous thyroids."
Targovnik H.M., Cochaux P., Corach D., Vassart G.
Mol. Cell. Endocrinol. 84:R23-R26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1504-1602 (ISOFORM 2).
[10]"Hormone synthesis in human thyroglobulin: possible cleavage of the polypeptide chain at the tyrosine donor site."
Marriq C., Lejeune P.J., Venot N., Vinet L.
FEBS Lett. 242:414-418(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[11]"Preferential sites of proteolytic cleavage of bovine, human and rat thyroglobulin. The use of limited proteolysis to detect solvent-exposed regions of the primary structure."
Gentile F., Salvatore G.
Eur. J. Biochem. 218:603-621(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[12]"Characterization of hormonogenic sites in an N-terminal, cyanogen bromide fragment of human thyroglobulin."
Xiao S., Pollock H.G., Taurog A., Rawitch A.B.
Arch. Biochem. Biophys. 320:96-105(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[13]"Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin."
Yang S.X., Pollock H.G., Rawitch A.B.
Arch. Biochem. Biophys. 327:61-70(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-76; ASN-198; ASN-484; ASN-529; ASN-748; ASN-816; ASN-947; ASN-1220; ASN-1348; ASN-1349; ASN-1365; ASN-1716; ASN-1774; ASN-2013; ASN-2250; ASN-2295 AND ASN-2582, ABSENCE OF GLYCOSYLATION AT ASN-110; ASN-496; ASN-1869 AND ASN-2122.
[14]"Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families."
Molina F., Bouanani M., Pau B., Granier C.
Eur. J. Biochem. 240:125-133(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PRESENCE OF A 11TH TYROGLOBULIN TYPE-1 REPEAT.
[15]"Consensus sequences for early iodination and hormonogenesis in human thyroglobulin."
Lamas L., Anderson P.C., Fox J.W., Dunn J.T.
J. Biol. Chem. 264:13541-13545(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IODINATION AT TYR-24; TYR-1310; TYR-2573; TYR-2587 AND TYR-2766.
[16]"Sulfated tyrosines of thyroglobulin are involved in thyroid hormone synthesis."
Nlend M.-C., Cauvi D., Venot N., Chabaud O.
Biochem. Biophys. Res. Commun. 262:193-197(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[17]"The hormonogenic tyrosine 5 of porcine thyroglobulin is sulfated."
Venot N., Nlend M.-C., Cauvi D., Chabaud O.
Biochem. Biophys. Res. Commun. 298:193-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-24.
[18]"A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human thyroglobulin enhances hormone formation and limits proteolytic accessibility at the carboxyl terminus. Potential insights into thyroid homeostasis and autoimmunity."
Conte M., Arcaro A., D'Angelo D., Gnata A., Mamone G., Ferranti P., Formisano S., Gentile F.
J. Biol. Chem. 281:22200-22211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-2749.
[19]"Thyroglobulin gene point mutation associated with non-endemic simple goitre."
Corral J., Martin C., Perez R., Sanchez I., Mories M.T., San Millan J.L., Miralles J.M., Gonzalez-Sarmiento R.
Lancet 341:462-464(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-870.
[20]"Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin cause a defect in intracellular transport of thyroglobulin in patients with congenital goiter and the variant type of adenomatous goiter."
Hishinuma A., Takamatsu J., Ohyama Y., Yokozawa T., Kanno Y., Kuma K., Yoshida S., Matsuura N., Ieiri T.
J. Clin. Endocrinol. Metab. 84:1438-1444(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH3 ARG-1264 AND SER-1996, VARIANTS HIS-135; ASP-604; ASP-653; ALA-734; GLU-830; GLN-985 DEL; VAL-1028; TYR-1043; THR-1059; ARG-1437; HIS-1463; ASN-1838; THR-1936; TRP-1999; GLU-2091; LEU-2149; ARG-2170; HIS-2242; ARG-2501 AND GLN-2530.
[21]"Amino acid substitutions in the thyroglobulin gene are associated with susceptibility to human and murine autoimmune thyroid disease."
Ban Y., Greenberg D.A., Concepcion E., Skrabanek L., Villanueva R., Tomer Y.
Proc. Natl. Acad. Sci. U.S.A. 100:15119-15124(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-734; VAL-1028 AND TRP-1979, INVOLVEMENT IN AITD3.
[22]"A novel compound heterozygous mutation in the thyroglobulin gene resulting in congenital goitrous hypothyroidism with high serum triiodothyronine levels."
Kitanaka S., Takeda A., Sato U., Miki Y., Hishinuma A., Ieiri T., Igarashi T.
J. Hum. Genet. 51:379-382(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH3 TYR-1897 AND GLN-2336.
[23]"Congenital hypothyroidism with goitre caused by new mutations in the thyroglobulin gene."
Caputo M., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Pellizas C.G., Gonzalez-Sarmiento R., Targovnik H.M.
Clin. Endocrinol. (Oxf.) 67:351-357(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TDH3 TYR-183 AND ASP-2234.
[24]"Thyroglobulin gene mutations producing defective intracellular transport of thyroglobulin are associated with increased thyroidal type 2 iodothyronine deiodinase activity."
Kanou Y., Hishinuma A., Tsunekawa K., Seki K., Mizuno Y., Fujisawa H., Imai T., Miura Y., Nagasaka T., Yamada C., Ieiri T., Murakami M., Murata Y.
J. Clin. Endocrinol. Metab. 92:1451-1457(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH3 ARG-2375.
[25]"The p.A2215D thyroglobulin gene mutation leads to deficient synthesis and secretion of the mutated protein and congenital hypothyroidism with wide phenotype variation."
Pardo V., Vono-Toniolo J., Rubio I.G., Knobel M., Possato R.F., Targovnik H.M., Kopp P., Medeiros-Neto G.
J. Clin. Endocrinol. Metab. 94:2938-2944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH3 ASP-2234, CHARACTERIZATION OF VARIANT TDH3 ASP-2234.
+Additional computationally mapped references.

Web resources

Wikipedia

Thyroglobulin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05615 mRNA. Translation: CAA29104.1.
U93033 mRNA. Translation: AAC51924.1.
AF230667 Genomic DNA. No translation available.
AF235100 Genomic DNA. No translation available.
AF230666 Genomic DNA. No translation available.
AF305872 Genomic DNA. No translation available.
X02154 mRNA. Translation: CAA26089.1.
X06059 expand/collapse EMBL AC list , X06060, X06061, X06062, X06063, X06064, X06065, X06066 Genomic DNA. Translation: CAA29454.1.
X06067, X06068 Genomic DNA. Translation: CAA29455.1.
X06069, X06070 Genomic DNA. Translation: CAA29456.1.
X02749 Genomic DNA. Translation: CAA26527.1.
AH008122 Genomic DNA. Translation: AAD51647.1.
AH007064 Genomic DNA. Translation: AAC95473.1.
AF080484 expand/collapse EMBL AC list , AF169654, AF169655, AF169656, AF169657, AF169658, AF169659, AF169661, AF169662, AF169663, AF169664, AF080472, AF080473, AF080474, AF080475, AF080476, AF080477, AF080478, AF080479, AF080480, AF080481, AF080482, AF080483 Genomic DNA. Translation: AAD50912.2.
S40807 mRNA. Translation: AAB22685.1.
PIRUIHU. A59110.
RefSeqNP_003226.4. NM_003235.4.
UniGeneHs.654591.

3D structure databases

ProteinModelPortalP01266.
SMRP01266. Positions 48-85, 93-161, 314-358, 611-661, 682-798, 1026-1073, 1147-1212, 2204-2728.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112896. 3 interactions.
IntActP01266. 2 interactions.

Protein family/group databases

MEROPSI31.950.

PTM databases

PhosphoSiteP01266.

Polymorphism databases

DMDM126302607.

Proteomic databases

PaxDbP01266.
PRIDEP01266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220616; ENSP00000220616; ENSG00000042832. [P01266-1]
ENST00000377869; ENSP00000367100; ENSG00000042832. [P01266-2]
GeneID7038.
KEGGhsa:7038.
UCSCuc003ytw.3. human. [P01266-1]

Organism-specific databases

CTD7038.
GeneCardsGC08P133879.
H-InvDBHIX0034371.
HGNCHGNC:11764. TG.
HPACAB000077.
CAB056155.
HPA002740.
MIM188450. gene.
274700. phenotype.
608175. phenotype.
neXtProtNX_P01266.
Orphanet95716. Familial thyroid dyshormonogenesis.
PharmGKBPA36479.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2272.
HOVERGENHBG017929.
InParanoidP01266.
KOK10809.
OMALRSCWCV.
OrthoDBEOG77M8MP.
PhylomeDBP01266.
TreeFamTF351833.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000042832-MONOMER.

Gene expression databases

ArrayExpressP01266.
BgeeP01266.
GenevestigatorP01266.

Family and domain databases

Gene3D4.10.800.10. 13 hits.
InterProIPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
PF07699. GCC2_GCC3. 1 hit.
PF00086. Thyroglobulin_1. 8 hits.
[Graphical view]
PIRSFPIRSF001831. Thyroglobulin. 1 hit.
SMARTSM00211. TY. 10 hits.
[Graphical view]
SUPFAMSSF57610. SSF57610. 13 hits.
PROSITEPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTG. human.
GeneWikiThyroglobulin.
GenomeRNAi7038.
NextBio27497.
PROP01266.
SOURCESearch...

Entry information

Entry nameTHYG_HUMAN
AccessionPrimary (citable) accession number: P01266
Secondary accession number(s): O15274 expand/collapse secondary AC list , O43899, Q15593, Q15948, Q9NYR1, Q9NYR2, Q9UMZ0, Q9UNY3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 162 of the entry and version 5 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

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 8

Human chromosome 8: entries, gene names and cross-references to MIM