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Protein

Thyroglobulin

Gene

Tg

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

Functioni

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

GO - Molecular functioni

GO - Biological processi

  • hormone biosynthetic process Source: UniProtKB-KW
  • iodide transport Source: MGI
  • regulation of myelination Source: MGI
  • thyroid gland development Source: Ensembl
  • 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

ESTHERimouse-thyro. Thyroglobulin.
MEROPSiS09.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroglobulin
Short name:
Tg
Gene namesi
Name:Tg
Synonyms:Tgn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:98733. Tg.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000000863721 – 2766ThyroglobulinAdd BLAST2746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Sulfotyrosine; alternateBy similarity1
Modified residuei25Thyroxine; alternateBy similarity1
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi64 ↔ 71PROSITE-ProRule annotation
Disulfide bondi73 ↔ 93PROSITE-ProRule annotation
Disulfide bondi97 ↔ 121PROSITE-ProRule annotation
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi132 ↔ 139PROSITE-ProRule annotation
Disulfide bondi141 ↔ 161PROSITE-ProRule annotation
Disulfide bondi165 ↔ 184PROSITE-ProRule annotation
Disulfide bondi195 ↔ 236PROSITE-ProRule annotation
Glycosylationi199N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi302 ↔ 320PROSITE-ProRule annotation
Disulfide bondi331 ↔ 337PROSITE-ProRule annotation
Disulfide bondi339 ↔ 359PROSITE-ProRule annotation
Glycosylationi484N-linked (GlcNAc...)Sequence analysis1
Glycosylationi496N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi748N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi774 ↔ 899PROSITE-ProRule annotation
Glycosylationi817N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi901 ↔ 922PROSITE-ProRule annotation
Glycosylationi948N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1043 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1074PROSITE-ProRule annotation
Disulfide bondi1078 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1146PROSITE-ProRule annotation
Glycosylationi1141N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1150 ↔ 1170PROSITE-ProRule annotation
Disulfide bondi1182 ↔ 1189PROSITE-ProRule annotation
Disulfide bondi1191 ↔ 1211PROSITE-ProRule annotation
Glycosylationi1349N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1365N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1513 ↔ 1522PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1564PROSITE-ProRule annotation
Glycosylationi1715N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1729N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1773N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1864N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1935N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2010N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2120N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2249N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2263 ↔ 2280PROSITE-ProRule annotation
Glycosylationi2294N-linked (GlcNAc...)Sequence analysis1
Modified residuei2572ThyroxineBy similarity1
Glycosylationi2581N-linked (GlcNAc...)Sequence analysis1
Modified residuei2586ThyroxineBy similarity1
Modified residuei2764TriiodothyronineBy similarity1

Post-translational modificationi

Sulfated tyrosines are desulfated during iodination.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Iodination, Sulfation

Proteomic databases

MaxQBiO08710.
PaxDbiO08710.
PRIDEiO08710.

PTM databases

iPTMnetiO08710.
PhosphoSitePlusiO08710.

Expressioni

Tissue specificityi

Thyroid gland specific.

Gene expression databases

BgeeiENSMUSG00000053469.
CleanExiMM_TG.
ExpressionAtlasiO08710. baseline and differential.
GenevisibleiO08710. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070239.

Structurei

3D structure databases

ProteinModelPortaliO08710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 93Thyroglobulin type-1 1PROSITE-ProRule annotationAdd BLAST62
Domaini94 – 161Thyroglobulin type-1 2PROSITE-ProRule annotationAdd BLAST68
Domaini162 – 298Thyroglobulin type-1 3PROSITE-ProRule annotationAdd BLAST137
Domaini299 – 359Thyroglobulin type-1 4PROSITE-ProRule annotationAdd BLAST61
Domaini605 – 658Thyroglobulin type-1 5PROSITE-ProRule annotationAdd BLAST54
Domaini659 – 726Thyroglobulin type-1 6PROSITE-ProRule annotationAdd BLAST68
Domaini727 – 922Thyroglobulin type-1 7PROSITE-ProRule annotationAdd BLAST196
Domaini923 – 1074Thyroglobulin type-1 8PROSITE-ProRule annotationAdd BLAST152
Domaini1075 – 1146Thyroglobulin type-1 9PROSITE-ProRule annotationAdd BLAST72
Domaini1147 – 1211Thyroglobulin type-1 10PROSITE-ProRule annotationAdd BLAST65
Repeati1455 – 1468Type IIAdd BLAST14
Repeati1469 – 1485Type IIAdd BLAST17
Repeati1486 – 1502Type IIAdd BLAST17
Domaini1510 – 1564Thyroglobulin type-1 11PROSITE-ProRule annotationAdd BLAST55
Repeati1602 – 1722Type IIIAAdd BLAST121
Repeati1723 – 1889Type IIIBAdd BLAST167
Repeati1890 – 1992Type IIIAAdd BLAST103
Repeati1993 – 2125Type IIIBAdd BLAST133
Repeati2126 – 2183Type IIIAAdd BLAST58

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00680000100015.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiO08710.
KOiK10809.
OMAiLRSCWCV.
OrthoDBiEOG091G004S.
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. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 10 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. 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)DescriptionActionsGraphical viewLength
Sequence conflicti80E → K in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti80E → K in AAC32269 (Ref. 3) Curated1
Sequence conflicti92V → I in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti92V → I in AAC32269 (Ref. 3) Curated1
Sequence conflicti1327A → T in AAB53204 (PubMed:9344706).Curated1
Sequence conflicti1427N → S in AAB53204 (PubMed:9344706).Curated1
Sequence conflicti1436 – 1442RTQLGCM → GLSLDVL in AAB53204 (PubMed:9344706).Curated7
Sequence conflicti1721T → I in AAB53204 (PubMed:9344706).Curated1
Sequence conflicti1813S → T in AAB53204 (PubMed:9344706).Curated1
Sequence conflicti1957 – 1959RVK → KVN in AAC32268 (PubMed:9707574).Curated3
Sequence conflicti1957 – 1959RVK → KVN in AAC32269 (Ref. 3) Curated3
Sequence conflicti2090S → SS in AAB53204 (PubMed:9344706).Curated1
Sequence conflicti2407R → K in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti2407R → K in AAC32269 (Ref. 3) Curated1
Sequence conflicti2414G → S in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti2414G → S in AAC32269 (Ref. 3) Curated1
Sequence conflicti2427R → K in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti2427R → K in AAC32269 (Ref. 3) Curated1
Sequence conflicti2434A → T in AAC32268 (PubMed:9707574).Curated1
Sequence conflicti2434A → T in AAC32269 (Ref. 3) Curated1
Sequence conflicti2443 – 2453TSSIQEVVSCL → NFIHPGSGIMF in AAC32268 (PubMed:9707574).CuratedAdd BLAST11
Sequence conflicti2443 – 2453TSSIQEVVSCL → NFIHPGSGIMF in AAC32269 (Ref. 3) CuratedAdd BLAST11
Sequence conflicti2728D → GN in AAB53204 (PubMed:9344706).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2283L → P in goiter. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliO08710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070239.

Protein family/group databases

ESTHERimouse-thyro. Thyroglobulin.
MEROPSiS09.978.

PTM databases

iPTMnetiO08710.
PhosphoSitePlusiO08710.

Proteomic databases

MaxQBiO08710.
PaxDbiO08710.
PRIDEiO08710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7038.
MGIiMGI:98733. Tg.

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00680000100015.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiO08710.
KOiK10809.
OMAiLRSCWCV.
OrthoDBiEOG091G004S.
TreeFamiTF351833.

Miscellaneous databases

ChiTaRSiTg. mouse.
PROiO08710.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053469.
CleanExiMM_TG.
ExpressionAtlasiO08710. baseline and differential.
GenevisibleiO08710. MM.

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. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 10 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 144 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.