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Protein

Thyroglobulin

Gene

TG

Organism
Bos taurus (Bovine)
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

Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Thyroid hormones biosynthesis

Protein family/group databases

ESTHERibovin-thyro. Thyroglobulin.
MEROPSiS09.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroglobulin
Short name:
Tg
Gene namesi
Name:TG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei11790. Bos d TG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 27692750ThyroglobulinPRO_0000008635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Sulfotyrosine; alternateBy similarity
Modified residuei24 – 241Thyroxine; alternateBy similarity
Disulfide bondi34 ↔ 52PROSITE-ProRule annotation
Disulfide bondi63 ↔ 70PROSITE-ProRule annotation
Disulfide bondi72 ↔ 92PROSITE-ProRule annotation
Disulfide bondi96 ↔ 120PROSITE-ProRule annotation
Glycosylationi110 – 1101N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi110 – 1101N-linked (GlcNAc...) (hybrid); alternate1 Publication
Disulfide bondi131 ↔ 138PROSITE-ProRule annotation
Disulfide bondi140 ↔ 160PROSITE-ProRule annotation
Disulfide bondi164 ↔ 183PROSITE-ProRule annotation
Disulfide bondi194 ↔ 235PROSITE-ProRule annotation
Disulfide bondi301 ↔ 319PROSITE-ProRule annotation
Disulfide bondi330 ↔ 336PROSITE-ProRule annotation
Disulfide bondi338 ↔ 358PROSITE-ProRule annotation
Glycosylationi483 – 4831N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi483 – 4831N-linked (GlcNAc...) (hybrid); alternate1 Publication
Glycosylationi495 – 4951N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi495 – 4951N-linked (GlcNAc...) (hybrid); alternate1 Publication
Disulfide bondi607 ↔ 619PROSITE-ProRule annotation
Disulfide bondi630 ↔ 635PROSITE-ProRule annotation
Disulfide bondi637 ↔ 657PROSITE-ProRule annotation
Disulfide bondi661 ↔ 686PROSITE-ProRule annotation
Disulfide bondi697 ↔ 702PROSITE-ProRule annotation
Disulfide bondi704 ↔ 725PROSITE-ProRule annotation
Disulfide bondi729 ↔ 762PROSITE-ProRule annotation
Glycosylationi747 – 7471N-linked (GlcNAc...)Sequence analysis
Disulfide bondi773 ↔ 898PROSITE-ProRule annotation
Glycosylationi853 – 8531N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi853 – 8531N-linked (GlcNAc...) (hybrid); alternate1 Publication
Disulfide bondi900 ↔ 921PROSITE-ProRule annotation
Glycosylationi947 – 9471N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi947 – 9471N-linked (GlcNAc...) (hybrid); alternate1 Publication
Disulfide bondi1042 ↔ 1049PROSITE-ProRule annotation
Disulfide bondi1051 ↔ 1073PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1108PROSITE-ProRule annotation
Disulfide bondi1126 ↔ 1145PROSITE-ProRule annotation
Glycosylationi1140 – 11401N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi1140 – 11401N-linked (GlcNAc...) (hybrid); alternate1 Publication
Disulfide bondi1149 ↔ 1169PROSITE-ProRule annotation
Disulfide bondi1181 ↔ 1188PROSITE-ProRule annotation
Disulfide bondi1190 ↔ 1210PROSITE-ProRule annotation
Glycosylationi1365 – 13651N-linked (GlcNAc...) (high mannose)1 Publication
Disulfide bondi1516 ↔ 1525PROSITE-ProRule annotation
Disulfide bondi1545 ↔ 1567PROSITE-ProRule annotation
Glycosylationi1776 – 17761N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi1776 – 17761N-linked (GlcNAc...) (hybrid); alternate1 Publication
Glycosylationi1870 – 18701N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi1870 – 18701N-linked (GlcNAc...) (hybrid); alternate1 Publication
Glycosylationi2014 – 20141N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi2123 – 21231N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi2251 – 22511N-linked (GlcNAc...) (complex); alternate1 Publication
Glycosylationi2251 – 22511N-linked (GlcNAc...) (hybrid); alternate1 Publication
Glycosylationi2296 – 22961N-linked (GlcNAc...) (high mannose)1 Publication
Modified residuei2574 – 25741Thyroxine
Modified residuei2588 – 25881Thyroxine
Modified residuei2767 – 27671Triiodothyronine

Post-translational modificationi

Sulfated tyrosines are desulfated during iodination.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei198 – 1981Not glycosylated1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Iodination, Sulfation

Proteomic databases

PaxDbiP01267.
PRIDEiP01267.

PTM databases

UniCarbKBiP01267.

Expressioni

Tissue specificityi

Thyroid gland specific.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010295.

Structurei

3D structure databases

ProteinModelPortaliP01267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9262Thyroglobulin type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini93 – 16068Thyroglobulin type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini161 – 297137Thyroglobulin type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini298 – 35861Thyroglobulin type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini604 – 65754Thyroglobulin type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini658 – 72568Thyroglobulin type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini726 – 921196Thyroglobulin type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini922 – 1073152Thyroglobulin type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1074 – 114572Thyroglobulin type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini1146 – 121065Thyroglobulin type-1 10PROSITE-ProRule annotationAdd
BLAST
Repeati1458 – 147114Type IIAdd
BLAST
Repeati1472 – 148817Type IIAdd
BLAST
Repeati1489 – 150517Type IIAdd
BLAST
Domaini1513 – 156755Thyroglobulin type-1 11PROSITE-ProRule annotationAdd
BLAST
Repeati1605 – 1725121Type IIIAAdd
BLAST
Repeati1726 – 1893168Type IIIBAdd
BLAST
Repeati1894 – 1996103Type IIIAAdd
BLAST
Repeati1997 – 2130134Type IIIBAdd
BLAST
Repeati2131 – 218858Type IIIAAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP01267.
KOiK10809.

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.
IPR009030. Growth_fac_rcpt_.
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.
SSF57184. SSF57184. 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.

P01267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALALWVFGL LDLICLASAN IFEYQVDAQP LRPCELQRER AFLKREDYVP
60 70 80 90 100
QCAEDGSFQT VQCGKDGASC WCVDADGREV PGSRQPGRPA ACLSFCQLQK
110 120 130 140 150
QQILLSSYIN STATSYLPQC QDSGDYSPVQ CDLRRRQCWC VDAEGMEVYG
160 170 180 190 200
TRQQGRPARC PRSCEIRNRR LLHGVGDRSP PQCSPDGAFR PVQCKLVNTT
210 220 230 240 250
DMMIFDLVHS YSRFPDAFVT FSSFRSRFPE VSGYCYCADS QGRELAETGL
260 270 280 290 300
ELLLDEIYDT IFAGLDLAST FAETTLYRIL QRRFLAVQLV ISGRFRCPTK
310 320 330 340 350
CEVERFAATS FRHPYVPSCH PDGEYQAAQC QQGGPCWCVD SRGQEIPGTR
360 370 380 390 400
QRGEPPSCAE DQSCPSERRR AFSRLRFGPS GYFSRRSLLL APEEGPVSQR
410 420 430 440 450
FARFTASCPP SIKELFLDSG IFQPMLQGRD TRFVAPESLK EAIRGLFPSR
460 470 480 490 500
ELARLALQFT TNAKRLQQNL FGGRFLVKVG QFNLSGALGT RGTFNFSHFF
510 520 530 540 550
QQLGLPGFQD GRALADLAKP LSVGLNSNPA SEAPKASKID VALRKPVVGS
560 570 580 590 600
FGFEVNLQEN QNALQFLSSF LELPEFLLFL QHAISVPEDI ARDLGDVMEM
610 620 630 640 650
VFSSQGCGQA PGSLFVPACT AEGSYEEVQC FAGDCWCVDA QGRELAGSRV
660 670 680 690 700
RGGRPRCPTE CEKQRARMQS LLGSQPAGSS LFVPACTSKG NFLPVQCFNS
710 720 730 740 750
ECYCVDTEGQ PIPGTRSALG EPKKCPSPCQ LQAERAFLGT VRTLVSNPST
760 770 780 790 800
LPALSSIYIP QCSASGQWSP VQCDGPPEQA FEWYERWEAQ NSAGQALTPA
810 820 830 840 850
ELLMKIMSYR EAASRNFRLF IQNLYEAGQQ GIFPGLARYS SFQDVPVSVL
860 870 880 890 900
EGNQTQPGGN VFLEPYLFWQ ILNGQLDRYP GPYSDFSAPL AHFDLRSCWC
910 920 930 940 950
VDEAGQKLEG TRNEPNKVPA CPGSCEEVKL RVLQFIREAE EIVTYSNSSR
960 970 980 990 1000
FPLGESFLAA KGIRLTDEEL AFPPLSPSRE TFLEKFLSGS DYAIRLAAQS
1010 1020 1030 1040 1050
TFDFYQRRLV TLAESPRAPS PVWSSAYLPQ CDAFGGWEPV QCHAATGHCW
1060 1070 1080 1090 1100
CVDGKGEYVP TSLTARSRQI PQCPTSCERL RASGLLSSWK QAGVQAEPSP
1110 1120 1130 1140 1150
KDLFIPTCLE TGEFARLQAS EAGTWCVDPA SGEGVPPGTN SSAQCPSLCE
1160 1170 1180 1190 1200
VLQSGVPSRR TSPGYSPACR AEDGGFSPVQ CDPAQGSCWC VLGSGEEVPG
1210 1220 1230 1240 1250
TRVAGSQPAC ESPQCPLPFS VADVAGGAIL CERASGLGAA AGQRCQLRCS
1260 1270 1280 1290 1300
QGYRSAFPPE PLLCSVQRRR WESRPPQPRA CQRPQFWQTL QTQAQFQLLL
1310 1320 1330 1340 1350
PLGKVCSADY SGLLLAFQVF LLDELTARGF CQIQVKTAGT PVSIPVCDDS
1360 1370 1380 1390 1400
SVKVECLSRE RLGVNITWKL QLVDAPPASL PDLQDVEEAL AGKYLAGRFA
1410 1420 1430 1440 1450
DLIQSGTFQL HLDSKTFSAD TSIRFLQGDR FGTSPRTQFG CLEGFGRVVA
1460 1470 1480 1490 1500
ASDASQDALG CVKCPEGSYF QDEQCIPCPA GFYQEQAGSL ACVPCPEGRT
1510 1520 1530 1540 1550
TVYAGAFSQT HCVTDCQKNE VGLQCDQDSQ YRASQRDRTS GKAFCVDGEG
1560 1570 1580 1590 1600
RRLPWTEAEA PLVDAQCLVM RKFEKLPESK VIFSADVAVM VRSEVPGSES
1610 1620 1630 1640 1650
SLMQCLADCA LDEACGFLTV STAGSEVSCD FYAWASDSIA CTTSGRSEDA
1660 1670 1680 1690 1700
LGTSQATSFG SLQCQVKVRS REGDPLAVYL KKGQEFTITG QKRFEQTGFQ
1710 1720 1730 1740 1750
SALSGMYSPV TFSASGASLA EVHLFCLLAC DHDSCCDGFI LVQVQGGPLL
1760 1770 1780 1790 1800
CGLLSSPDVL LCHVRDWRDP AEAQANASCP GVTYDQDSRQ VTLRLGGQEI
1810 1820 1830 1840 1850
RGLTPLEGTQ DTLTSFQQVY LWKDSDMGSR SESMGCRRDT EPRPASPSET
1860 1870 1880 1890 1900
DLTTGLFSPV DLIQVIVDGN VSLPSQQHWL FKHLFSLQQA NLWCLSRCAG
1910 1920 1930 1940 1950
EPSFCQLAEV TDSEPLYFTC TLYPEAQVCD DILESSPKGC RLILPRRPSA
1960 1970 1980 1990 2000
LYRKKVVLQD RVKNFYNRLP FQKLTGISIR NKVPMSDKSI SSGFFECERL
2010 2020 2030 2040 2050
CDMDPCCTGF GFLNVSQLKG GEVTCLTLNS LGLQTCSEEY GGVWRILDCG
2060 2070 2080 2090 2100
SPDTEVRTYP FGWYQKPVSP SDAPSFCPSV ALPALTENVA LDSWQSLALS
2110 2120 2130 2140 2150
SVIVDPSIRN FDVAHISTAA VGNFSAARDR CLWECSRHQD CLVTTLQTQP
2160 2170 2180 2190 2200
GAVRCMFYAD TQSCTHSLQA QNCRLLLHEE ATYIYRKPNI PLPGFGTSSP
2210 2220 2230 2240 2250
SVPIATHGQL LGRSQAIQVG TSWKPVDQFL GVPYAAPPLG EKRFRAPEHL
2260 2270 2280 2290 2300
NWTGSWEATK PRARCWQPGI RTPTPPGVSE DCLYLNVFVP QNMAPNASVL
2310 2320 2330 2340 2350
VFFHNAAEGK GSGDRPAVDG SFLAAVGNLI VVTASYRTGI FGFLSSGSSE
2360 2370 2380 2390 2400
LSGNWGLLDQ VVALTWVQTH IQAFGGDPRR VTLAADRGGA DIASIHLVTT
2410 2420 2430 2440 2450
RAANSRLFRR AVLMGGSALS PAAVIRPERA RQQAAALAKE VGCPSSSVQE
2460 2470 2480 2490 2500
MVSCLRQEPA RILNDAQTKL LAVSGPFHYW GPVVDGQYLR ETPARVLQRA
2510 2520 2530 2540 2550
PRVKVDLLIG SSQDDGLINR AKAVKQFEES QGRTSSKTAF YQALQNSLGG
2560 2570 2580 2590 2600
EAADAGVQAA ATWYYSLEHD SDDYASFSRA LEQATRDYFI ICPVIDMASH
2610 2620 2630 2640 2650
WARTVRGNVF MYHAPESYSH SSLELLTDVL YAFGLPFYPA YEGQFTLEEK
2660 2670 2680 2690 2700
SLSLKIMQYF SNFIRSGNPN YPHEFSRRAP EFAAPWPDFV PRDGAESYKE
2710 2720 2730 2740 2750
LSVLLPNRQG LKKADCSFWS KYIQSLKASA DETKDGPSAD SEEEDQPAGS
2760
GLTEDLLGLP ELASKTYSK
Length:2,769
Mass (Da):303,222
Last modified:July 21, 1986 - v1
Checksum:i1C7F227E9101DE2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1206 – 12061S → R in CAA29457 (PubMed:3681978).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02815 mRNA. Translation: CAA26584.1.
X02155 mRNA. Translation: CAA26090.1.
X05380 Genomic DNA. Translation: CAA28971.1. Sequence problems.
X06071
, X06072, X06073, X06074, X06075 Genomic DNA. Translation: CAA29457.1.
PIRiA01533. UIBO.
RefSeqiNP_776308.1. NM_173883.2.
UniGeneiBt.88019.

Genome annotation databases

GeneIDi280706.
KEGGibta:280706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02815 mRNA. Translation: CAA26584.1.
X02155 mRNA. Translation: CAA26090.1.
X05380 Genomic DNA. Translation: CAA28971.1. Sequence problems.
X06071
, X06072, X06073, X06074, X06075 Genomic DNA. Translation: CAA29457.1.
PIRiA01533. UIBO.
RefSeqiNP_776308.1. NM_173883.2.
UniGeneiBt.88019.

3D structure databases

ProteinModelPortaliP01267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010295.

Protein family/group databases

Allergomei11790. Bos d TG.
ESTHERibovin-thyro. Thyroglobulin.
MEROPSiS09.978.

PTM databases

UniCarbKBiP01267.

Proteomic databases

PaxDbiP01267.
PRIDEiP01267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280706.
KEGGibta:280706.

Organism-specific databases

CTDi7038.

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP01267.
KOiK10809.

Miscellaneous databases

NextBioi20804887.

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.
IPR009030. Growth_fac_rcpt_.
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.
SSF57184. SSF57184. 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...

Publicationsi

  1. "Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA."
    Mercken L., Simons M.-J., Swillens S., Massaer M., Vassart G.
    Nature 316:647-651(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Presence of hormonogenic and repetitive domains in the first 930 amino acids of bovine thyroglobulin as deduced from the cDNA sequence."
    Mercken L., Simons M.-J., de Martynhoff G., Swillens S., Vassart G.
    Eur. J. Biochem. 147:59-64(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-930.
  3. "Structural organization of the bovine thyroglobulin gene and of its 5'-flanking region."
    de Martynhoff G., Pohl V., Mercken L., van Ommen G.-J., Vassart G.
    Eur. J. Biochem. 164:591-599(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  4. "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 1002-1209.
  5. "Thyroglobulin glycosylation: location and nature of the N-linked oligosaccharide units in bovine thyroglobulin."
    Rawitch A.B., Pollock H.G., Yang S.X.
    Arch. Biochem. Biophys. 300:271-279(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-110; ASN-483; ASN-495; ASN-853; ASN-947; ASN-1140; ASN-1365; ASN-1776; ASN-1870; ASN-2014; ASN-2123; ASN-2251 AND ASN-2296, ABSENCE OF GLYCOSYLATION AT ASN-198, STRUCTURE OF CARBOHYDRATE.

Entry informationi

Entry nameiTHYG_BOVIN
AccessioniPrimary (citable) accession number: P01267
Secondary accession number(s): O18976, Q28196, Q95478
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 132 of the entry and version 1 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. 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.