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O08710

- THYG_MOUSE

UniProt

O08710 - THYG_MOUSE

Protein

Thyroglobulin

Gene

Tg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Hormone, Thyroid hormone

    Keywords - Biological processi

    Thyroid hormones biosynthesis

    Protein family/group databases

    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
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:98733. Tg.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. extracellular space Source: MGI

    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

    ArrayExpressiO08710.
    BgeeiO08710.
    CleanExiMM_TG.
    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.
    InParanoidiQ2NKY1.
    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

    MTALVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQAEYV     50
    PQCSEDGSFQ TVQCQNDGQS CWCVDSDGRE VPGSRQLGRP TVCLSFCQLH 100
    KQRILLGSYI NSTDALYLPQ CQDSGNYAPV QCDLQRVQCW CVDTEGMEVY 150
    GTRQQGRPTR CPRSCEIRNR RLLHGVGDRS PPQCTADGEF MPVQCKFVNT 200
    TDMMIFDLIH NYNRFPDAFV TFSSFRGRFP EVSGYCYCAD SQGRELAETG 250
    LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT 300
    KCEVEQFAAT RFGHSYIPRC HRDGHYQTVQ CQTEGMCWCV DAQGREVPGT 350
    RQQGQPPSCA ADQSCALERQ QALSRFYFET PDYFSPQDLL SSEDRLAPVS 400
    GVRSDTSCPP RIKELFVDSG LLRSIAVEHY QRLSESRSLL REAIRAVFPS 450
    RELAGLALQF TTNPKRLQQN LFGGTFLANA AQFNLSGALG TRSTFNFSQF 500
    FQQFGLPGFL NRDRVTTLAK LLPVRLDSSS TPETLRVSEK TVAMNKRVVG 550
    NFGFKVNLQE NQDALKFLVS LLELPEFLVF LQRAVSVPED IARDLGDVME 600
    MVFSAQACKQ MPGKFFVPSC TAGGSYEDIQ CYAGECWCVD SRGKELDGSR 650
    VRGGRPRCPT KCEKQRAQMQ SLASAQPAGS SFFVPTCTRE GYFLPVQCFN 700
    SECYCVDTEG QVIPGTQSTV GEAKQCPSVC QLQAEQAFLG VVGVLLSNSS 750
    MVPSISNVYI PQCSASGQWR HVQCDGPHEQ VFEWYERWKT QNGDGQELTP 800
    AALLMKIVSY REVASRNFSL FLQSLYDAGQ QRIFPVLAQY PSLQDVPQVV 850
    LEGATTPPGE NIFLDPYIFW QILNGQLSQY PGPYSDFNMP LEHFNLRSCW 900
    CVDEAGQKLD GTQTKPGEIP ACPGPCEEVK LRVLKFIKET EEIVSASNAS 950
    SFPLGESFLV AKGIQLTSEE LDLPPQFPSR DAFSEKFLRG GEYAIRLAAQ 1000
    STLTFYQSLR ASLGKSDGAA SLLWSGPYMP QCNMIGGWEP VQCHAGTGQC 1050
    WCVDGRGEFI PGSLMSRSSQ MPQCPTNCEL SRASGLISAW KQAGPQRNPG 1100
    PGDLFIPVCL QTGEYVRKQT SGTGTWCVDP ASGEGMPVNT NGSAQCPGLC 1150
    DVLKSRALSR KVGLGYSPVC EALDGAFSPV QCDLAQGSCW CVLGSGEEVP 1200
    GTRVVGTQPA CESPQCPLPF SGSDVADGVI FCETASSSGV TTVQQCQLLC 1250
    RQGLRSAFSP GPLICSLESQ HWVTLPPPRA CQRPQLWQTM QTQAHFQLLL 1300
    PPGKMCSVDY SGLLQAFQVF ILDELIARGF CQIQVKTFGT LVSSTVCDNS 1350
    SIQVGCLTAE RLGVNVTWKL QLEDISVGSL PDLYSIERAV TGQDLLGRFA 1400
    DLIQSGRFQL HLDSKTFSAD TTLYFLNGDS FVTSPRTQLG CMEGFYRVPT 1450
    TRQDALGCVK CPEGSFSQDG RCTPCPAGTY QEQAGSSACI PCPRGRTTIT 1500
    TGAFSKTHCV TDCQKNEAGL QCDQNGQYQA SQKNRDSGEV FCVDSEGRKL 1550
    QWLQTEAGLS ESQCLMIRKF DKAPESKVIF DANSPVIVKS SVPSADSPLV 1600
    QCLTDCANDE ACSFLTVSTM ESEVSCDFYS WTRDNFACVT SDQEQDAMGS 1650
    LKATSFGSLR CQVKVRNSGK DSLAVYVKKG YESTAAGQKS FEPTGFQNVL 1700
    SGLYSPVVFS ASGANLTDTH TYCLLACDND SCCDGFIITQ VKGGPTICGL 1750
    LSSPDILLCH INDWRDTSAT QANATCAGVT YDQGSRQMTL SLGGQEFLQG 1800
    LALLEGTQDS FTSFQQVYLW KDSDMGSRPE SMGCERGMVP RSDFPGDMAT 1850
    ELFSPVDITQ VIVNTSHSLP SQQYWLFTHL FSAEQANLWC LSRCAQEPIF 1900
    CQLADITKSS SLYFTCFLYP EAQVCDNVME SNAKNCSQIL PHQPTALFRR 1950
    KVVLNDRVKN FYTRLPFQKL TGISIRDKVP MSGKLISNGF FECERLCDRD 2000
    PCCTGFGFLN VSQLQGGEVT CLTLNSMGIQ TCNEESGATW RILDCGSEDT 2050
    EVHTYPFGWY QKPAVWSDTP SFCPSAALQS LTEEKVTSDS WQTLALSSVI 2100
    VDPSIKHFDV AHISTAATSN FSMAQDFCLQ QCSRHQDCLV TTLQIQPGVV 2150
    RCVFYPDIQN CIHSLRSHTC WLLLHEEATY IYRKSGIPLV QSDVTSTPSV 2200
    RIDSFGQLQG GSQVIKVGTA WKQVYRFLGV PYAAPPLADN RFRAPEVLNW 2250
    TGSWDATKPR ASCWQPGTRT PTPPQINEDC LYLNVFVPEN LVSNASVLVF 2300
    FHNTMEMEGS GGQLTIDGSI LAAVGNFIVV TANYRLGVFG FLSSGSDEVA 2350
    GNWGLLDQVA ALTWVQSHIG AFGGDPQRVT LAADRSGADV ASIHLLISRP 2400
    TRLQLFRKAL LMGGSALSPA AIISPERAQQ QAAALAKEVG CPTSSIQEVV 2450
    SCLRQKPANI LNDAQTKLLA VSGPFHYWGP VVDGQYLREL PSRRLKRPLP 2500
    VKVDLLIGGS QDDGLINRAK AVKQFEESQG RTNSKTAFYQ ALQNSLGGED 2550
    SDARILAAAV WYYSLEHSTD DYASFSRALE NATRDYFIIC PMVNMASLWA 2600
    RRTRGNVFMY HVPESYGHGS LELLADVQYA FGLPFYSAYQ GQFSTEEQSL 2650
    SLKVMQYFSN FIRSGNPNYP HEFSRKAAEF ATPWPDFIPG AGGESYKELS 2700
    AQLPNRQGLK QADCSFWSKY IQTLKDADGA KDAQLTKSEE EDLEVGPGLE 2750
    EDLSGSLEPV PKSYSK 2766
    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 S09.978.

    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 Q2NKY1.
    KOi K10809.
    OMAi LRSCWCV.
    OrthoDBi EOG77M8MP.
    TreeFami TF351833.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi O08710.
    Bgeei O08710.
    CleanExi MM_TG.
    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

    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 1, 2014
    This is version 127 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