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O08710

- THYG_MOUSE

UniProt

O08710 - THYG_MOUSE

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Protein

Thyroglobulin

Gene

Tg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. hormone biosynthetic process Source: UniProtKB-KW
  2. iodide transport Source: MGI
  3. regulation of myelination Source: MGI
  4. thyroid gland development Source: Ensembl
  5. thyroid hormone generation Source: RefGenome
  6. thyroid hormone metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Thyroid hormones biosynthesis

Protein family/group databases

MEROPSiI31.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroglobulin
Short name:
Tg
Gene namesi
Name:Tg
Synonyms:Tgn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:98733. Tg.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Tg are the cause of some forms of goiter. Goiter is an enlargement of the thyroid gland. The variant Pro-2283 exhibits a defect in exit from the endoplasmic reticulum.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 27662746ThyroglobulinPRO_0000008637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Sulfotyrosine; alternateBy similarity
Modified residuei25 – 251Thyroxine; alternateBy similarity
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi64 ↔ 71PROSITE-ProRule annotation
Disulfide bondi73 ↔ 93PROSITE-ProRule annotation
Disulfide bondi97 ↔ 121PROSITE-ProRule annotation
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi132 ↔ 139PROSITE-ProRule annotation
Disulfide bondi141 ↔ 161PROSITE-ProRule annotation
Disulfide bondi165 ↔ 184PROSITE-ProRule annotation
Disulfide bondi195 ↔ 236PROSITE-ProRule annotation
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi302 ↔ 320PROSITE-ProRule annotation
Disulfide bondi331 ↔ 337PROSITE-ProRule annotation
Disulfide bondi339 ↔ 359PROSITE-ProRule annotation
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi608 ↔ 620PROSITE-ProRule annotation
Disulfide bondi631 ↔ 636PROSITE-ProRule annotation
Disulfide bondi638 ↔ 658PROSITE-ProRule annotation
Disulfide bondi662 ↔ 687PROSITE-ProRule annotation
Disulfide bondi698 ↔ 703PROSITE-ProRule annotation
Disulfide bondi705 ↔ 726PROSITE-ProRule annotation
Disulfide bondi730 ↔ 763PROSITE-ProRule annotation
Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi774 ↔ 899PROSITE-ProRule annotation
Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi901 ↔ 922PROSITE-ProRule annotation
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1043 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1074PROSITE-ProRule annotation
Disulfide bondi1078 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1146PROSITE-ProRule annotation
Glycosylationi1141 – 11411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1150 ↔ 1170PROSITE-ProRule annotation
Disulfide bondi1182 ↔ 1189PROSITE-ProRule annotation
Disulfide bondi1191 ↔ 1211PROSITE-ProRule annotation
Glycosylationi1349 – 13491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1365 – 13651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1513 ↔ 1522PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1564PROSITE-ProRule annotation
Glycosylationi1715 – 17151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1729 – 17291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1773 – 17731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1864 – 18641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1935 – 19351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2010 – 20101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2120 – 21201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2249 – 22491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2263 ↔ 2280PROSITE-ProRule annotation
Glycosylationi2294 – 22941N-linked (GlcNAc...)Sequence Analysis
Modified residuei2572 – 25721ThyroxineBy similarity
Glycosylationi2581 – 25811N-linked (GlcNAc...)Sequence Analysis
Modified residuei2586 – 25861ThyroxineBy similarity
Modified residuei2764 – 27641TriiodothyronineBy similarity

Post-translational modificationi

Sulfated tyrosines are desulfated during iodination.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Iodination, Sulfation

Proteomic databases

PRIDEiO08710.

PTM databases

PhosphoSiteiO08710.

Expressioni

Tissue specificityi

Thyroid gland specific.

Gene expression databases

BgeeiO08710.
CleanExiMM_TG.
ExpressionAtlasiO08710. baseline and differential.
GenevestigatoriO08710.

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9362Thyroglobulin type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 16168Thyroglobulin type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 298137Thyroglobulin type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35961Thyroglobulin type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini605 – 65854Thyroglobulin type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini659 – 72668Thyroglobulin type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini727 – 922196Thyroglobulin type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini923 – 1074152Thyroglobulin type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1075 – 114672Thyroglobulin type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini1147 – 121165Thyroglobulin type-1 10PROSITE-ProRule annotationAdd
BLAST
Repeati1455 – 146814Type IIAdd
BLAST
Repeati1469 – 148517Type IIAdd
BLAST
Repeati1486 – 150217Type IIAdd
BLAST
Domaini1510 – 156455Thyroglobulin type-1 11PROSITE-ProRule annotationAdd
BLAST
Repeati1602 – 1722121Type IIIAAdd
BLAST
Repeati1723 – 1889167Type IIIBAdd
BLAST
Repeati1890 – 1992103Type IIIAAdd
BLAST
Repeati1993 – 2125133Type IIIBAdd
BLAST
Repeati2126 – 218358Type IIIAAdd
BLAST

Sequence similaritiesi

Contains 11 thyroglobulin type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00680000100015.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiO08710.
KOiK10809.
OMAiLRSCWCV.
OrthoDBiEOG77M8MP.
TreeFamiTF351833.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
4.10.800.10. 13 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
PF07699. GCC2_GCC3. 1 hit.
PF00086. Thyroglobulin_1. 7 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM00211. TY. 10 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08710-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTALVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQAEYV
60 70 80 90 100
PQCSEDGSFQ TVQCQNDGQS CWCVDSDGRE VPGSRQLGRP TVCLSFCQLH
110 120 130 140 150
KQRILLGSYI NSTDALYLPQ CQDSGNYAPV QCDLQRVQCW CVDTEGMEVY
160 170 180 190 200
GTRQQGRPTR CPRSCEIRNR RLLHGVGDRS PPQCTADGEF MPVQCKFVNT
210 220 230 240 250
TDMMIFDLIH NYNRFPDAFV TFSSFRGRFP EVSGYCYCAD SQGRELAETG
260 270 280 290 300
LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
310 320 330 340 350
KCEVEQFAAT RFGHSYIPRC HRDGHYQTVQ CQTEGMCWCV DAQGREVPGT
360 370 380 390 400
RQQGQPPSCA ADQSCALERQ QALSRFYFET PDYFSPQDLL SSEDRLAPVS
410 420 430 440 450
GVRSDTSCPP RIKELFVDSG LLRSIAVEHY QRLSESRSLL REAIRAVFPS
460 470 480 490 500
RELAGLALQF TTNPKRLQQN LFGGTFLANA AQFNLSGALG TRSTFNFSQF
510 520 530 540 550
FQQFGLPGFL NRDRVTTLAK LLPVRLDSSS TPETLRVSEK TVAMNKRVVG
560 570 580 590 600
NFGFKVNLQE NQDALKFLVS LLELPEFLVF LQRAVSVPED IARDLGDVME
610 620 630 640 650
MVFSAQACKQ MPGKFFVPSC TAGGSYEDIQ CYAGECWCVD SRGKELDGSR
660 670 680 690 700
VRGGRPRCPT KCEKQRAQMQ SLASAQPAGS SFFVPTCTRE GYFLPVQCFN
710 720 730 740 750
SECYCVDTEG QVIPGTQSTV GEAKQCPSVC QLQAEQAFLG VVGVLLSNSS
760 770 780 790 800
MVPSISNVYI PQCSASGQWR HVQCDGPHEQ VFEWYERWKT QNGDGQELTP
810 820 830 840 850
AALLMKIVSY REVASRNFSL FLQSLYDAGQ QRIFPVLAQY PSLQDVPQVV
860 870 880 890 900
LEGATTPPGE NIFLDPYIFW QILNGQLSQY PGPYSDFNMP LEHFNLRSCW
910 920 930 940 950
CVDEAGQKLD GTQTKPGEIP ACPGPCEEVK LRVLKFIKET EEIVSASNAS
960 970 980 990 1000
SFPLGESFLV AKGIQLTSEE LDLPPQFPSR DAFSEKFLRG GEYAIRLAAQ
1010 1020 1030 1040 1050
STLTFYQSLR ASLGKSDGAA SLLWSGPYMP QCNMIGGWEP VQCHAGTGQC
1060 1070 1080 1090 1100
WCVDGRGEFI PGSLMSRSSQ MPQCPTNCEL SRASGLISAW KQAGPQRNPG
1110 1120 1130 1140 1150
PGDLFIPVCL QTGEYVRKQT SGTGTWCVDP ASGEGMPVNT NGSAQCPGLC
1160 1170 1180 1190 1200
DVLKSRALSR KVGLGYSPVC EALDGAFSPV QCDLAQGSCW CVLGSGEEVP
1210 1220 1230 1240 1250
GTRVVGTQPA CESPQCPLPF SGSDVADGVI FCETASSSGV TTVQQCQLLC
1260 1270 1280 1290 1300
RQGLRSAFSP GPLICSLESQ HWVTLPPPRA CQRPQLWQTM QTQAHFQLLL
1310 1320 1330 1340 1350
PPGKMCSVDY SGLLQAFQVF ILDELIARGF CQIQVKTFGT LVSSTVCDNS
1360 1370 1380 1390 1400
SIQVGCLTAE RLGVNVTWKL QLEDISVGSL PDLYSIERAV TGQDLLGRFA
1410 1420 1430 1440 1450
DLIQSGRFQL HLDSKTFSAD TTLYFLNGDS FVTSPRTQLG CMEGFYRVPT
1460 1470 1480 1490 1500
TRQDALGCVK CPEGSFSQDG RCTPCPAGTY QEQAGSSACI PCPRGRTTIT
1510 1520 1530 1540 1550
TGAFSKTHCV TDCQKNEAGL QCDQNGQYQA SQKNRDSGEV FCVDSEGRKL
1560 1570 1580 1590 1600
QWLQTEAGLS ESQCLMIRKF DKAPESKVIF DANSPVIVKS SVPSADSPLV
1610 1620 1630 1640 1650
QCLTDCANDE ACSFLTVSTM ESEVSCDFYS WTRDNFACVT SDQEQDAMGS
1660 1670 1680 1690 1700
LKATSFGSLR CQVKVRNSGK DSLAVYVKKG YESTAAGQKS FEPTGFQNVL
1710 1720 1730 1740 1750
SGLYSPVVFS ASGANLTDTH TYCLLACDND SCCDGFIITQ VKGGPTICGL
1760 1770 1780 1790 1800
LSSPDILLCH INDWRDTSAT QANATCAGVT YDQGSRQMTL SLGGQEFLQG
1810 1820 1830 1840 1850
LALLEGTQDS FTSFQQVYLW KDSDMGSRPE SMGCERGMVP RSDFPGDMAT
1860 1870 1880 1890 1900
ELFSPVDITQ VIVNTSHSLP SQQYWLFTHL FSAEQANLWC LSRCAQEPIF
1910 1920 1930 1940 1950
CQLADITKSS SLYFTCFLYP EAQVCDNVME SNAKNCSQIL PHQPTALFRR
1960 1970 1980 1990 2000
KVVLNDRVKN FYTRLPFQKL TGISIRDKVP MSGKLISNGF FECERLCDRD
2010 2020 2030 2040 2050
PCCTGFGFLN VSQLQGGEVT CLTLNSMGIQ TCNEESGATW RILDCGSEDT
2060 2070 2080 2090 2100
EVHTYPFGWY QKPAVWSDTP SFCPSAALQS LTEEKVTSDS WQTLALSSVI
2110 2120 2130 2140 2150
VDPSIKHFDV AHISTAATSN FSMAQDFCLQ QCSRHQDCLV TTLQIQPGVV
2160 2170 2180 2190 2200
RCVFYPDIQN CIHSLRSHTC WLLLHEEATY IYRKSGIPLV QSDVTSTPSV
2210 2220 2230 2240 2250
RIDSFGQLQG GSQVIKVGTA WKQVYRFLGV PYAAPPLADN RFRAPEVLNW
2260 2270 2280 2290 2300
TGSWDATKPR ASCWQPGTRT PTPPQINEDC LYLNVFVPEN LVSNASVLVF
2310 2320 2330 2340 2350
FHNTMEMEGS GGQLTIDGSI LAAVGNFIVV TANYRLGVFG FLSSGSDEVA
2360 2370 2380 2390 2400
GNWGLLDQVA ALTWVQSHIG AFGGDPQRVT LAADRSGADV ASIHLLISRP
2410 2420 2430 2440 2450
TRLQLFRKAL LMGGSALSPA AIISPERAQQ QAAALAKEVG CPTSSIQEVV
2460 2470 2480 2490 2500
SCLRQKPANI LNDAQTKLLA VSGPFHYWGP VVDGQYLREL PSRRLKRPLP
2510 2520 2530 2540 2550
VKVDLLIGGS QDDGLINRAK AVKQFEESQG RTNSKTAFYQ ALQNSLGGED
2560 2570 2580 2590 2600
SDARILAAAV WYYSLEHSTD DYASFSRALE NATRDYFIIC PMVNMASLWA
2610 2620 2630 2640 2650
RRTRGNVFMY HVPESYGHGS LELLADVQYA FGLPFYSAYQ GQFSTEEQSL
2660 2670 2680 2690 2700
SLKVMQYFSN FIRSGNPNYP HEFSRKAAEF ATPWPDFIPG AGGESYKELS
2710 2720 2730 2740 2750
AQLPNRQGLK QADCSFWSKY IQTLKDADGA KDAQLTKSEE EDLEVGPGLE
2760
EDLSGSLEPV PKSYSK
Length:2,766
Mass (Da):304,473
Last modified:July 27, 2011 - v3
Checksum:i06227D4192AC1902
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801E → K in AAC32268. (PubMed:9707574)Curated
Sequence conflicti80 – 801E → K in AAC32269. 1 PublicationCurated
Sequence conflicti92 – 921V → I in AAC32268. (PubMed:9707574)Curated
Sequence conflicti92 – 921V → I in AAC32269. 1 PublicationCurated
Sequence conflicti1327 – 13271A → T in AAB53204. (PubMed:9344706)Curated
Sequence conflicti1427 – 14271N → S in AAB53204. (PubMed:9344706)Curated
Sequence conflicti1436 – 14427RTQLGCM → GLSLDVL in AAB53204. (PubMed:9344706)Curated
Sequence conflicti1721 – 17211T → I in AAB53204. (PubMed:9344706)Curated
Sequence conflicti1813 – 18131S → T in AAB53204. (PubMed:9344706)Curated
Sequence conflicti1957 – 19593RVK → KVN in AAC32268. (PubMed:9707574)Curated
Sequence conflicti1957 – 19593RVK → KVN in AAC32269. 1 PublicationCurated
Sequence conflicti2090 – 20901S → SS in AAB53204. (PubMed:9344706)Curated
Sequence conflicti2407 – 24071R → K in AAC32268. (PubMed:9707574)Curated
Sequence conflicti2407 – 24071R → K in AAC32269. 1 PublicationCurated
Sequence conflicti2414 – 24141G → S in AAC32268. (PubMed:9707574)Curated
Sequence conflicti2414 – 24141G → S in AAC32269. 1 PublicationCurated
Sequence conflicti2427 – 24271R → K in AAC32268. (PubMed:9707574)Curated
Sequence conflicti2427 – 24271R → K in AAC32269. 1 PublicationCurated
Sequence conflicti2434 – 24341A → T in AAC32268. (PubMed:9707574)Curated
Sequence conflicti2434 – 24341A → T in AAC32269. 1 PublicationCurated
Sequence conflicti2443 – 245311TSSIQEVVSCL → NFIHPGSGIMF in AAC32268. (PubMed:9707574)CuratedAdd
BLAST
Sequence conflicti2443 – 245311TSSIQEVVSCL → NFIHPGSGIMF in AAC32269. 1 PublicationCuratedAdd
BLAST
Sequence conflicti2728 – 27281D → GN in AAB53204. (PubMed:9344706)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2283 – 22831L → P in goiter. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76389 mRNA. Translation: AAB53204.1.
AF076186 mRNA. Translation: AAC32268.1.
AF076187 mRNA. Translation: AAC32269.1.
CH466545 Genomic DNA. Translation: EDL29374.1.
BC111467 mRNA. Translation: AAI11468.1.
CCDSiCCDS37091.1.
RefSeqiNP_033401.2. NM_009375.2.
UniGeneiMm.441333.

Genome annotation databases

EnsembliENSMUST00000065916; ENSMUSP00000070239; ENSMUSG00000053469.
GeneIDi21819.
KEGGimmu:21819.
UCSCiuc007wap.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76389 mRNA. Translation: AAB53204.1 .
AF076186 mRNA. Translation: AAC32268.1 .
AF076187 mRNA. Translation: AAC32269.1 .
CH466545 Genomic DNA. Translation: EDL29374.1 .
BC111467 mRNA. Translation: AAI11468.1 .
CCDSi CCDS37091.1.
RefSeqi NP_033401.2. NM_009375.2.
UniGenei Mm.441333.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I31.950.

PTM databases

PhosphoSitei O08710.

Proteomic databases

PRIDEi O08710.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000065916 ; ENSMUSP00000070239 ; ENSMUSG00000053469 .
GeneIDi 21819.
KEGGi mmu:21819.
UCSCi uc007wap.1. mouse.

Organism-specific databases

CTDi 7038.
MGIi MGI:98733. Tg.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00680000100015.
HOGENOMi HOG000128427.
HOVERGENi HBG017929.
InParanoidi O08710.
KOi K10809.
OMAi LRSCWCV.
OrthoDBi EOG77M8MP.
TreeFami TF351833.

Miscellaneous databases

ChiTaRSi TG. mouse.
NextBioi 301232.
PROi O08710.
SOURCEi Search...

Gene expression databases

Bgeei O08710.
CleanExi MM_TG.
ExpressionAtlasi O08710. baseline and differential.
Genevestigatori O08710.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
4.10.800.10. 13 hits.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
PF07699. GCC2_GCC3. 1 hit.
PF00086. Thyroglobulin_1. 7 hits.
[Graphical view ]
PIRSFi PIRSF001831. Thyroglobulin. 1 hit.
SMARTi SM00211. TY. 10 hits.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEi PS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseases."
    Kim P.S., Hossain S.A., Park Y.-N., Lee I., Yoo S.-E., Arvan P.
    Proc. Natl. Acad. Sci. U.S.A. 95:9909-9913(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GOITER PRO-2283.
    Strain: COG.
    Tissue: Thyroid.
  3. "Cloning, characterization, site-directed mutagenesis, and transient expression of 8301-nucleotide AKR/J mouse thyroglobulin cDNA: defective secretion of mutant thyroglobulins."
    Hossain S.A., Yoo S.-E., Kim P.S.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: AKR/J.
    Tissue: Thyroid.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thyroid.

Entry informationi

Entry nameiTHYG_MOUSE
AccessioniPrimary (citable) accession number: O08710
Secondary accession number(s): O88590, Q2NKY1, Q9QWY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3