P05543 (THBG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thyroxine-binding globulin

Alternative name(s):
Serpin A7
T4-binding globulin

Gene names

Name:	SERPINA7
Synonyms:	TBG

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	415 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	Major thyroid hormone transport protein in serum.
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Polymorphism	Two qualitative TBG variants occur in particular populations. TBG-A is found in 40% of Australian aborigines, it has reduced affinity for thyroxine and triiodothyroxine and increased susceptibility to inactivation by heat or acid. TBG-S ('s' for slow shift on isoelectic focusing) is found in blacks, Eskimos, Melanesians, Polynesians and Indonesians, but not in Caucasians; TBG-S is slightly more thermolabile.
Involvement in disease	Thyroxine-binding globulin deficiency (TBG deficiency) [MIM:314200]: Mutations in the SERPINA7 gene can result as a whole spectrum of deficiencies, characterized by either reduced or increased TBG levels in the serum. Patients show, respectively, reduced or elevated protein-bound iodine but are euthyroid. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome response to corticosterone stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara response to prostaglandin E stimulus Inferred from electronic annotation. Source: Compara response to vitamin A Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement PubMed 7499319. Source: ProtInc
Molecular_function	hormone binding Inferred from electronic annotation. Source: Compara serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.7

Chain

21 – 415

395

Thyroxine-binding globulin

PRO_0000032436

Sites

Binding site

293

1

Thyroxine

Binding site

398

1

Thyroxine

Amino acid modifications

Glycosylation

36

1

N-linked (GlcNAc...) (complex) Ref.8 Ref.9

Glycosylation

99

1

N-linked (GlcNAc...)

Glycosylation

116

1

N-linked (GlcNAc...); in variant Gary Probable

Glycosylation

165

1

N-linked (GlcNAc...) Ref.8

Glycosylation

253

1

N-linked (GlcNAc...)

Natural variations

Natural variant

43

1

S → T in TBG deficiency; San Diego; partial TBG deficiency. Ref.18

VAR_007102

Natural variant

116

1

I → N in TBG deficiency; Gary; severe TBG deficiency. Ref.14
Corresponds to variant rs28933689 [ dbSNP | Ensembl ].

VAR_007103

Natural variant

133

1

A → P in TBG deficiency; Montreal/TBG-M; partial TBG deficiency. Ref.16
Corresponds to variant rs28933688 [ dbSNP | Ensembl ].

VAR_007104

Natural variant

191

1

D → N in TBG-S/Slow. Ref.20
Corresponds to variant rs1050086 [ dbSNP | Ensembl ].

VAR_007105

Natural variant

211

1

A → T in TBG-A/Aborigine. Ref.19
Corresponds to variant rs2234036 [ dbSNP | Ensembl ].

VAR_007106

Natural variant

247

1

L → P in TBG deficiency; CD5; complete TBG deficiency. Ref.13
Corresponds to variant rs28937312 [ dbSNP | Ensembl ].

VAR_007107

Natural variant

303

1

L → F Common polymorphism.
Corresponds to variant rs1804495 [ dbSNP | Ensembl ].

VAR_007108

Natural variant

351

1

H → Y in TBG deficiency; Quebec; partial TBG deficiency. Ref.17

VAR_007109

Natural variant

383

1

P → L in TBG deficiency; Kumamoto. Ref.15

VAR_007110

Experimental info

Sequence conflict

30 – 31

2

CH → DS AA sequence Ref.7

Sequence conflict

38

1

T → S AA sequence Ref.7

Sequence conflict

197

1

I → T in AAA60616. Ref.1

Secondary structure

1

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415

Helix Strand Turn

Details...

Helix

41 – 60

20

Beta strand

66 – 68

3

Helix

70 – 82

13

Helix

86 – 95

10

Turn

100 – 102

3

Helix

105 – 119

15

Beta strand

126 – 137

12

Helix

144 – 154

11

Beta strand

156 – 161

6

Helix

166 – 180

15

Turn

181 – 183

3

Beta strand

198 – 212

15

Helix

216 – 218

3

Beta strand

220 – 230

11

Beta strand

232 – 249

18

Turn

250 – 253

4

Beta strand

254 – 272

19

Helix

277 – 283

7

Helix

286 – 295

10

Beta strand

297 – 306

10

Beta strand

308 – 315

8

Helix

317 – 323

7

Turn

327 – 329

3

Turn

336 – 338

3

Beta strand

339 – 342

4

Beta strand

348 – 357

10

Beta strand

359 – 363

5

Beta strand

384 – 386

3

Beta strand

391 – 397

7

Turn

398 – 401

4

Beta strand

402 – 410

9

Sequences

	Sequence		Length	Mass (Da)
	P05543 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 8B24EF8C7CEF8F0A	FASTA	415	46,325
	10 20 30 40 50 60 MSPFLYLVLL VLGLHATIHC ASPEGKVTAC HSSQPNATLY KMSSINADFA FNLYRRFTVE 70 80 90 100 110 120 TPDKNIFFSP VSISAALVML SFGACCSTQT EIVETLGFNL TDTPMVEIQH GFQHLICSLN 130 140 150 160 170 180 FPKKELELQI GNALFIGKHL KPLAKFLNDV KTLYETEVFS TDFSNISAAK QEINSHVEMQ 190 200 210 220 230 240 TKGKVVGLIQ DLKPNTIMVL VNYIHFKAQW ANPFDPSKTE DSSSFLIDKT TTVQVPMMHQ 250 260 270 280 290 300 MEQYYHLVDM ELNCTVLQMD YSKNALALFV LPKEGQMESV EAAMSSKTLK KWNRLLQKGW 310 320 330 340 350 360 VDLFVPKFSI SATYDLGATL LKMGIQHAYS ENADFSGLTE DNGLKLSNAA HKAVLHIGEK 370 380 390 400 410 GTEAAAVPEV ELSDQPENTF LHPIIQIDRS FMLLILERST RSILFLGKVV NPTEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases." Flink I.L., Bayley T.J., Gustafson T.A., Markham B.E., Morkin E. Proc. Natl. Acad. Sci. U.S.A. 83:7708-7712(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The structure of the human thyroxine binding globulin (TBG) gene." Akbari M.T., Kapadi A., Farmer M.J., Fitch N.J.S., McCann K.P., Kordestani S., Flink I.L., Sheppard M.C., Ramsden D.B. Biochim. Biophys. Acta 1216:446-454(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human thyroxine-binding globulin gene: complete sequence and transcriptional regulation." Hayashi Y., Mori Y., Janssen O.E., Sunthornthepvarakul T., Weiss R.E., Takeda K., Weinberg M., Seo H., Bell G.I., Refetoff S. Mol. Endocrinol. 7:1049-1060(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Liver.
[7]	"Partial amino acid sequence of human thyroxine-binding globulin. Further evidence for a single polypeptide chain." Cheng S.-Y. Biochem. Biophys. Res. Commun. 79:1212-1218(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-40.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36 AND ASN-165, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Structural mechanism for the carriage and release of thyroxine in the blood." Zhou A., Wei Z., Read R.J., Carrell R.W. Proc. Natl. Acad. Sci. U.S.A. 103:13321-13326(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 39-415 IN COMPLEX WITH THYROXINE.
[12]	"Molecular basis of inherited thyroxine-binding globulin defects." Janssen O.E., Bertenshaw R., Takeda K., Weiss R., Refetoff S. Trends Endocrinol. Metab. 3:49-53(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[13]	"Replacement of Leu227 by Pro in thyroxine-binding globulin (TBG) is associated with complete TBG deficiency in three of eight families with this inherited defect." Mori Y., Takeda K., Charbonneau M., Refetoff S. J. Clin. Endocrinol. Metab. 70:804-809(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY PRO-247.
[14]	"A mutation causing reduced biological activity and stability of thyroxine-binding globulin probably as a result of abnormal glycosylation of the molecule." Mori Y., Seino S., Takeda K., Flink I.L., Murata Y., Bell G.I., Refetoff S. Mol. Endocrinol. 3:575-579(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY ASN-116.
[15]	"Thyroxine-binding globulin variant (TBG-Kumamoto): identification of a point mutation and genotype analysis of its family." Shirotani T., Kishikawa H., Wake N., Miyamura N., Hashimoto Y., Motoyoshi S., Yamaguchi K., Shichiri M. Endocrinol. Jpn. 39:577-584(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY LEU-383.
[16]	"Sequence of the variant thyroxine-binding globulin (TBG) in a Montreal family with partial TBG deficiency." Janssen O.E., Takeda K., Refetoff S. Hum. Genet. 87:119-122(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY PRO-133.
[17]	"Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals two nucleotide substitutions." Bertenshaw R., Takeda K., Refetoff S. Am. J. Hum. Genet. 48:741-744(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY TYR-351.
[18]	"Sequencing of the variant thyroxine-binding globulin (TBG)-San Diego reveals two nucleotide substitutions." Bertenshaw R., Sarne D., Tornari J., Weinberg M., Refetoff S. Biochim. Biophys. Acta 1139:307-310(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG DEFICIENCY THR-43.
[19]	"Sequence of the variant thyroxine-binding globulin of Australian aborigines. Only one of two amino acid replacements is responsible for its altered properties." Takeda K., Mori Y., Sobieszczyk S., Seo H., Dick M., Watson F., Flink I.L., Seino S., Bell G.I., Refetoff S. J. Clin. Invest. 83:1344-1348(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG-A THR-211.
[20]	"Molecular basis for the properties of the thyroxine-binding globulin-slow variant in American blacks." Waltz M.R., Pullman T.N., Takeda K., Sobieszczyk P., Refetoff S. J. Endocrinol. Invest. 13:343-349(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TBG-S ASN-191.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14091 mRNA. Translation: AAA60616.1.
X64171 Genomic DNA. Translation: CAA45509.1.
L13470 Genomic DNA. Translation: AAA16067.1.
Z83850 Genomic DNA. Translation: CAB06092.1.
CH471120 Genomic DNA. Translation: EAX02747.1.
CH471120 Genomic DNA. Translation: EAX02748.1.
BC020747 mRNA. Translation: AAH20747.1.

IPI

IPI00292946.

PIR

A47224.

RefSeq

NP_000345.2. NM_000354.5.

UniGene

Hs.76838.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CEO	X-ray	2.80	A/B	39-415	[»]
2RIV	X-ray	1.50	A	33-365	[»]
			B	377-415	[»]
2RIW	X-ray	2.04	A	39-365	[»]
			B	377-415	[»]
2XN3	X-ray	2.09	A	33-365	[»]
			B	377-415	[»]
2XN5	X-ray	1.70	A	32-365	[»]
			B	381-415	[»]
2XN6	X-ray	1.29	A	32-365	[»]
			B	381-415	[»]
2XN7	X-ray	1.43	A	32-365	[»]
			B	381-415	[»]

ProteinModelPortal

P05543.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000329374.

Protein family/group databases

MEROPS

I04.955.

PTM databases

PhosphoSite

P05543.

Polymorphism databases

DMDM

1351236.

Proteomic databases

PaxDb

P05543.

PeptideAtlas

P05543.

PRIDE

P05543.

Protocols and materials databases

DNASU

6906.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327674; ENSP00000329374; ENSG00000123561.
ENST00000372563; ENSP00000361644; ENSG00000123561.

GeneID

6906.

KEGG

hsa:6906.

UCSC

uc004eme.2. human.

Organism-specific databases

CTD

6906.

GeneCards

GC0XM105277.

HGNC

HGNC:11583. SERPINA7.

HPA

HPA002803.

MIM

314200. gene+phenotype.

neXtProt

NX_P05543.

Orphanet

209893. Congenital isolated thyroxine-binding globulin deficiency.

PharmGKB

PA36347.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOGENOM

HOG000238521.

HOVERGEN

HBG005957.

InParanoid

P05543.

OMA

ICSLNFP.

OrthoDB

EOG4B2SX7.

PhylomeDB

P05543.

Gene expression databases

Bgee

P05543.

CleanEx

HS_SERPINA7.

Genevestigator

P05543.

GermOnline

ENSG00000123561. Homo sapiens.

Family and domain databases

InterPro

IPR000295. Prot_inh_Lserp2.
IPR023795. Protease_inhib_I4_serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

PRINTS

PR00780. LEUSERPINII.

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3843.

DrugBank

DB00451. Levothyroxine.
DB00279. Liothyronine.

EvolutionaryTrace

P05543.

GenomeRNAi

6906.

NextBio

27007.

SOURCE

Search...

Entry information

Entry name

THBG_HUMAN

Accession

Primary (citable) accession number: P05543
Secondary accession number(s): D3DUX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 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.