P01266 (THYG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thyroglobulin
Short name=Tg

Gene names

Name:

TG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2768 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Thyroid hormones biosynthesis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital hypothyroidism Disease mutation
Domain	Repeat Signal
Molecular function	Hormone Thyroid hormone
PTM	Disulfide bond Glycoprotein Iodination Sulfation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW iodide transport Inferred from electronic annotation. Source: Compara regulation of myelination Inferred from electronic annotation. Source: Compara signal transduction Non-traceable author statement PubMed 3016640. Source: ProtInc thyroid gland development Inferred from expression pattern PubMed 15494458. Source: UniProtKB thyroid hormone generation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	extracellular space Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19
	Chain	20 – 2768	2749	Thyroglobulin		PRO_0000008636
Regions
	Domain	31 – 92	62	Thyroglobulin type-1 1
	Domain	93 – 160	68	Thyroglobulin type-1 2
	Domain	161 – 297	137	Thyroglobulin type-1 3
	Domain	298 – 358	61	Thyroglobulin type-1 4
	Domain	605 – 658	54	Thyroglobulin type-1 5
	Domain	659 – 726	68	Thyroglobulin type-1 6
	Domain	727 – 921	195	Thyroglobulin type-1 7
	Domain	922 – 1073	152	Thyroglobulin type-1 8
	Domain	1074 – 1145	72	Thyroglobulin type-1 9
	Domain	1146 – 1210	65	Thyroglobulin type-1 10
	Repeat	1456 – 1469	14	Type II
	Repeat	1470 – 1486	17	Type II
	Repeat	1487 – 1503	17	Type II
	Domain	1511 – 1565	55	Thyroglobulin type-1 11
	Repeat	1603 – 1723	121	Type IIIA
	Repeat	1724 – 1892	169	Type IIIB
	Repeat	1893 – 1995	103	Type IIIA
	Repeat	1996 – 2129	134	Type IIIB
	Repeat	2130 – 2187	58	Type IIIA
Sites
	Site	110	1	Not glycosylated
	Site	496	1	Not glycosylated
	Site	1869	1	Not glycosylated
	Site	2122	1	Not glycosylated
Amino acid modifications
	Modified residue	24	1	Sulfotyrosine; alternate By similarity
	Modified residue	24	1	Thyroxine; alternate
	Modified residue	1310	1	Thyroxine
	Modified residue	2573	1	Thyroxine
	Modified residue	2587	1	Thyroxine
	Modified residue	2766	1	Triiodothyronine
	Glycosylation	76	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	198	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	484	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	529	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	748	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	816	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	947	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	1220	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	1348	1	N-linked (GlcNAc...) Probable
	Glycosylation	1349	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	1365	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	1716	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	1774	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	2013	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	2250	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	2295	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	2582	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	2749	1	O-linked (Xyl...) (chondroitin sulfate) Ref.18
	Disulfide bond	34 ↔ 52		By similarity
	Disulfide bond	63 ↔ 70		By similarity
	Disulfide bond	72 ↔ 92		By similarity
	Disulfide bond	96 ↔ 120		By similarity
	Disulfide bond	131 ↔ 138		By similarity
	Disulfide bond	140 ↔ 160		By similarity
	Disulfide bond	164 ↔ 183		By similarity
	Disulfide bond	194 ↔ 235		By similarity
	Disulfide bond	301 ↔ 319		By similarity
	Disulfide bond	330 ↔ 336		By similarity
	Disulfide bond	338 ↔ 358		By similarity
	Disulfide bond	608 ↔ 620		By similarity
	Disulfide bond	631 ↔ 636		By similarity
	Disulfide bond	638 ↔ 658		By similarity
	Disulfide bond	662 ↔ 687		By similarity
	Disulfide bond	698 ↔ 703		By similarity
	Disulfide bond	705 ↔ 726		By similarity
	Disulfide bond	730 ↔ 763		By similarity
	Disulfide bond	774 ↔ 898		By similarity
	Disulfide bond	900 ↔ 921		By similarity
	Disulfide bond	1042 ↔ 1049		By similarity
	Disulfide bond	1051 ↔ 1073		By similarity
	Disulfide bond	1077 ↔ 1108		By similarity
	Disulfide bond	1126 ↔ 1145		By similarity
	Disulfide bond	1149 ↔ 1169		By similarity
	Disulfide bond	1181 ↔ 1188		By similarity
	Disulfide bond	1190 ↔ 1210		By similarity
	Disulfide bond	1514 ↔ 1523		By similarity
	Disulfide bond	1543 ↔ 1565		By similarity
	Disulfide bond	2264 ↔ 2281		Potential
Natural variations
	Alternative sequence	1510 – 1567	58	CVTDC…SQCLM → L in isoform 2.		VSP_012655
	Natural variant	135	1	Q → H. Ref.20 Corresponds to variant rs2069546 [ dbSNP | Ensembl ].		VAR_010212
	Natural variant	183	1	C → Y in TDH3. Ref.23		VAR_063034
	Natural variant	515	1	Q → E. Ref.3 Corresponds to variant rs180222 [ dbSNP | Ensembl ].		VAR_016190
	Natural variant	604	1	S → D Requires 2 nucleotide substitutions. Ref.1 Ref.4 Ref.20 Corresponds to variant rs2069547 [ dbSNP | Ensembl ].		VAR_016852
	Natural variant	653	1	G → D. Ref.1 Ref.4 Ref.20 Corresponds to variant rs2069548 [ dbSNP | Ensembl ].		VAR_016853
	Natural variant	734	1	S → A Polymorphism associated with AITD3. Ref.5 Ref.20 Ref.21 Corresponds to variant rs180223 [ dbSNP | Ensembl ].		VAR_010213
	Natural variant	777	1	P → L. Corresponds to variant rs3739274 [ dbSNP | Ensembl ].		VAR_049077
	Natural variant	815	1	G → R. Corresponds to variant rs16904774 [ dbSNP | Ensembl ].		VAR_049078
	Natural variant	830	1	Q → E. Ref.20 Corresponds to variant rs2076737 [ dbSNP | Ensembl ].		VAR_010214
	Natural variant	870	1	Q → H. Ref.19 Corresponds to variant rs2229843 [ dbSNP | Ensembl ].		VAR_002365
	Natural variant	985	1	Missing. Ref.1 Ref.20		VAR_016854
	Natural variant	988	1	R → P. Corresponds to variant rs16893332 [ dbSNP | Ensembl ].		VAR_049079
	Natural variant	1028	1	M → V Polymorphism associated with AITD3. Ref.20 Ref.21 Corresponds to variant rs853326 [ dbSNP | Ensembl ].		VAR_010215
	Natural variant	1043	1	H → Y. Ref.1 Ref.20		VAR_016855
	Natural variant	1059	1	I → T. Ref.1 Ref.20		VAR_016856
	Natural variant	1063	1	L → M. Corresponds to variant rs11992497 [ dbSNP | Ensembl ].		VAR_049080
	Natural variant	1222	1	S → L. Corresponds to variant rs12549018 [ dbSNP | Ensembl ].		VAR_049081
	Natural variant	1264	1	C → R in TDH3; autosomal recessive. Ref.20 Corresponds to variant rs2076738 [ dbSNP | Ensembl ].		VAR_010216
	Natural variant	1312	1	D → G. Ref.1 Ref.2 Ref.7 Corresponds to variant rs2069556 [ dbSNP | Ensembl ].		VAR_010217
	Natural variant	1437	1	W → R. Ref.1 Ref.20 Corresponds to variant rs2069558 [ dbSNP | Ensembl ].		VAR_016857
	Natural variant	1463	1	P → H. Ref.1 Ref.20		VAR_016858
	Natural variant	1740	1	T → K. Corresponds to variant rs16904791 [ dbSNP | Ensembl ].		VAR_049082
	Natural variant	1838	1	D → N. Ref.20 Corresponds to variant rs2069561 [ dbSNP | Ensembl ].		VAR_010218
	Natural variant	1897	1	C → Y in TDH3. Ref.22		VAR_063035
	Natural variant	1936	1	A → T. Ref.1 Ref.20 Corresponds to variant rs2069562 [ dbSNP | Ensembl ].		VAR_016859
	Natural variant	1974	1	M → T. Corresponds to variant rs56230101 [ dbSNP | Ensembl ].		VAR_061173
	Natural variant	1979	1	R → W Polymorphism associated with AITD3. Ref.21		VAR_032013
	Natural variant	1996	1	C → S in TDH3; autosomal recessive. Ref.20 Corresponds to variant rs2076739 [ dbSNP | Ensembl ].		VAR_010219
	Natural variant	1999	1	R → W. Ref.20 Corresponds to variant rs2076740 [ dbSNP | Ensembl ].		VAR_010220
	Natural variant	2091	1	D → E. Ref.1 Ref.20		VAR_016860
	Natural variant	2149	1	P → L. Ref.1 Ref.8 Ref.20 Corresponds to variant rs2069564 [ dbSNP | Ensembl ].		VAR_016861
	Natural variant	2170	1	Q → R. Ref.1 Ref.8 Ref.20 Corresponds to variant rs2069565 [ dbSNP | Ensembl ].		VAR_016862
	Natural variant	2234	1	A → D in TDH3; reduces thyroglobulin synthesis and secretion; promotes thyroglobulin retention within the endoplasmic reticulum. Ref.23 Ref.25		VAR_063036
	Natural variant	2242	1	R → H. Ref.1 Ref.20 Corresponds to variant rs2069566 [ dbSNP | Ensembl ].		VAR_016863
	Natural variant	2336	1	R → Q in TDH3. Ref.22		VAR_063037
	Natural variant	2375	1	G → R in TDH3. Ref.24		VAR_063038
	Natural variant	2455	1	R → H. Corresponds to variant rs2272707 [ dbSNP | Ensembl ].		VAR_049083
	Natural variant	2469	1	L → P. Corresponds to variant rs2069568 [ dbSNP | Ensembl ].		VAR_049084
	Natural variant	2501	1	W → R. Ref.20 Corresponds to variant rs2069569 [ dbSNP | Ensembl ].		VAR_010221
	Natural variant	2526	1	F → L. Corresponds to variant rs12114109 [ dbSNP | Ensembl ].		VAR_049085
	Natural variant	2530	1	R → Q. Ref.20 Corresponds to variant rs1133076 [ dbSNP | Ensembl ].		VAR_010222
	Natural variant	2616	1	N → S. Corresponds to variant rs10091530 [ dbSNP | Ensembl ].		VAR_049086
Experimental info
	Sequence conflict	23 – 25	3	EYQ → GKF in CAA26527. Ref.6
	Sequence conflict	848	1	Missing AA sequence Ref.13
	Sequence conflict	984 – 985	2	EQ → DR in CAA29456. Ref.5
	Sequence conflict	1359 – 1360	2	Missing AA sequence Ref.13
	Sequence conflict	1717	1	L → A AA sequence Ref.13
	Sequence conflict	1776	1	T → S AA sequence Ref.13
	Sequence conflict	2019	1	G → H AA sequence Ref.13
	Sequence conflict	2287	1	F → P AA sequence Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Major) [UniParc]. Last modified February 20, 2007. Version 5. Checksum: 69A87D935F1BAA72	FASTA	2,768	304,790
	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
	Isoform 2 (Minor) [UniParc]. Checksum: EEC6895F22D55EE0	FASTA	2,711	298,383
	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 SAGAFSQTHL MQKFEKVPES KVIFDANAPV AVRSKVPDSE FPVMQCLTDC TEDEACSFFT 1570 1580 1590 1600 1610 1620 VSTTEPEISC DFYAWTSDNV ACMTSDQKRD ALGNSKATSF GSLRCQVKVR SHGQDSPAVY 1630 1640 1650 1660 1670 1680 LKKGQGSTTT LQKRFEPTGF QNMLSGLYNP IVFSASGANL TDAHLFCLLA CDRDLCCDGF 1690 1700 1710 1720 1730 1740 VLTQVQGGAI ICGLLSSPSV LLCNVKDWMD PSEAWANATC PGVTYDQESH QVILRLGDQE 1750 1760 1770 1780 1790 1800 FIKSLTPLEG TQDTFTNFQQ VYLWKDSDMG SRPESMGCRK DTVPRPASPT EAGLTTELFS 1810 1820 1830 1840 1850 1860 PVDLNQVIVN GNQSLSSQKH WLFKHLFSAQ QANLWCLSRC VQEHSFCQLA EITESASLYF 1870 1880 1890 1900 1910 1920 TCTLYPEAQV CDDIMESNAQ GCRLILPQMP KALFRKKVIL EDKVKNFYTR LPFQKLMGIS 1930 1940 1950 1960 1970 1980 IRNKVPMSEK SISNGFFECE RRCDADPCCT GFGFLNVSQL KGGEVTCLTL NSLGIQMCSE 1990 2000 2010 2020 2030 2040 ENGGAWRILD CGSPDIEVHT YPFGWYQKPI AQNNAPSFCP LVVLPSLTEK VSLDSWQSLA 2050 2060 2070 2080 2090 2100 LSSVVVDPSI RHFDVAHVST AATSNFSAVR DLCLSECSQH EACLITTLQT QPGAVRCMFY 2110 2120 2130 2140 2150 2160 ADTQSCTHSL QGQNCRLLLR EEATHIYRKP GISLLSYEAS VPSVPISTHG RLLGRSQAIQ 2170 2180 2190 2200 2210 2220 VGTSWKQVDQ FLGVPYAAPP LAERRFQAPE PLNWTGSWDA SKPRASCWQP GTRTSTSPGV 2230 2240 2250 2260 2270 2280 SEDCLYLNVF IPQNVAPNAS VLVFFHNTMD REESEGWPAI DGSFLAAVGN LIVVTASYRV 2290 2300 2310 2320 2330 2340 GVFGFLSSGS GEVSGNWGLL DQVAALTWVQ THIRGFGGDP RRVSLAADRG GADVASIHLL 2350 2360 2370 2380 2390 2400 TARATNSQLF RRAVLMGGSA LSPAAVISHE RAQQQAIALA KEVSCPMSSS QEVVSCLRQK 2410 2420 2430 2440 2450 2460 PANVLNDAQT KLLAVSGPFH YWGPVIDGHF LREPPARALK RSLWVEVDLL IGSSQDDGLI 2470 2480 2490 2500 2510 2520 NRAKAVKQFE ESRGRTSSKT AFYQALQNSL GGEDSDARVE AAATWYYSLE HSTDDYASFS 2530 2540 2550 2560 2570 2580 RALENATRDY FIICPIIDMA SAWAKRARGN VFMYHAPENY GHGSLELLAD VQFALGLPFY 2590 2600 2610 2620 2630 2640 PAYEGQFSLE EKSLSLKIMQ YFSHFIRSGN PNYPYEFSRK VPTFATPWPD FVPRAGGENY 2650 2660 2670 2680 2690 2700 KEFSELLPNR QGLKKADCSF WSKYISSLKT SADGAKGGQS AESEEEELTA GSGLREDLLS 2710 LQEPGSKTYS K

References

	« Hide 'large scale' referencesShow '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. , 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 , 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 , 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.
IPI	IPI00306129. IPI00549199.
PIR	UIHU. A59110.
RefSeq	NP_003226.4. NM_003235.4.
UniGene	Hs.654591.
3D structure databases
ProteinModelPortal	P01266.
ModBase	Search...
Protein-protein interaction databases
IntAct	P01266. 2 interactions.
Protein family/group databases
MEROPS	I31.950.
PTM databases
PhosphoSite	P01266.
Polymorphism databases
DMDM	126302607.
Proteomic databases
PaxDb	P01266.
PRIDE	P01266.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000220616; ENSP00000220616; ENSG00000042832. ENST00000377869; ENSP00000367100; ENSG00000042832.
GeneID	7038.
KEGG	hsa:7038.
UCSC	uc003ytw.3. human.
Organism-specific databases
CTD	7038.
GeneCards	GC08P133879.
H-InvDB	HIX0034371.
HGNC	HGNC:11764. TG.
HPA	CAB000077. CAB056155. HPA002740.
MIM	188450. gene. 274700. phenotype. 608175. phenotype.
neXtProt	NX_P01266.
PharmGKB	PA36479.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2272.
HOVERGEN	HBG017929.
InParanoid	P01266.
KO	K10809.
OMA	LRSCWCV.
PhylomeDB	P01266.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000042832-MONOMER.
Gene expression databases
ArrayExpress	P01266.
Bgee	P01266.
Genevestigator	P01266.
Family and domain databases
Gene3D	4.10.800.10. 13 hits.
InterPro	IPR002018. CarbesteraseB. IPR019819. Carboxylesterase_B_CS. IPR016324. Thyroglobulin. IPR000716. Thyroglobulin_1. IPR011641. Tyr-kin_ephrin_A/B_rcpt-like. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. PF07699. GCC2_GCC3. 1 hit. PF00086. Thyroglobulin_1. 8 hits. [Graphical view]
PIRSF	PIRSF001831. Thyroglobulin. 1 hit.
SMART	SM00211. TY. 10 hits. [Graphical view]
SUPFAM	SSF57610. Thyroglobulin_1. 11 hits.
PROSITE	PS00941. CARBOXYLESTERASE_B_2. 1 hit. PS00484. THYROGLOBULIN_1_1. 9 hits. PS51162. THYROGLOBULIN_1_2. 11 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TG. human.
GenomeRNAi	7038.
NextBio	27497.
SOURCE	Search...

Entry information

Entry name

THYG_HUMAN

Accession

Primary (citable) accession number: P01266
Secondary accession number(s): O15274 , 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:	May 1, 2013
This is version 155 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.