Reviewed, UniProtKB/Swiss-Prot P10827 (THA_HUMAN)

Names and origin

Protein names

Recommended name:
Thyroid hormone receptor alpha

Alternative name(s):
Nuclear receptor subfamily 1 group A member 1
c-erbA-alpha
c-erbA-1
V-erbA-related protein 7
Short name=EAR-7

Gene names

Name:	THRA
Synonyms:	EAR7, ERBA1, NR1A1, THRA1, THRA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nuclear hormone receptor. High affinity receptor for triiodothyronine.
Subunit structure	Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Probably interacts with SFPQ. Interacts with C1D By similarity. Interacts with AKAP13. Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus.
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-binding domain.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	hormone-mediated signaling pathway Inferred from direct assay. Source: UniProtKB regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nucleus Inferred by curator. Source: UniProtKB
Molecular function	promoter binding Inferred from direct assay. Source: UniProtKB steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro thyroid hormone binding Inferred from physical interaction. Source: MGI thyroid hormone receptor activity Inferred from direct assay. Source: UniProtKB transcription factor activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MED1	Q15648	1	EBI-286285,EBI-394459
Ncoa6	Q9JLI4	1	EBI-286285,EBI-286271	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha-2 (identifier: P10827-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Alpha-1 (identifier: P10827-2)

The sequence of this isoform differs from the canonical sequence as follows:
     371-490: EREVQSSILY...EDLAGNAASP → VTDLRMIGAC...FLEVFEDQEV

Isoform Alpha-3 (identifier: P10827-3)

The sequence of this isoform differs from the canonical sequence as follows:
     371-409: Missing.

Isoform Alpha-4 (identifier: P10827-4)

Also known as: Alpha3;

The sequence of this isoform differs from the canonical sequence as follows:
     371-412: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Thyroid hormone receptor alpha

PRO_0000053424

Regions

DNA binding

53 – 127

75

Nuclear receptor

Zinc finger

53 – 73

21

NR C4-type

Zinc finger

91 – 115

25

NR C4-type

Region

1 – 52

52

Modulating

Region

190 – 370

181

Ligand-binding

Amino acid modifications

Cross-link

190

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Alternative sequence

371 – 490

120

EREVQ…NAASP → VTDLRMIGACHASRFLHMKV ECPTELFPPLFLEVFEDQEV in isoform Alpha-1.

VSP_003621

Alternative sequence

371 – 412

42

Missing in isoform Alpha-4.

VSP_003623

Alternative sequence

371 – 409

39

Missing in isoform Alpha-3.

VSP_003622

Experimental info

Sequence conflict

37

1

T → S Ref.4

Sequence conflict

37

1

T → S Ref.7

Sequence conflict

119

1

G → A Ref.4

Sequence conflict

119

1

G → A Ref.7

Sequence conflict

285

1

E → A in CAB57886. Ref.1

Sequence conflict

285

1

E → A in CAA38899. Ref.1

Secondary structure

1

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490

Helix Strand Turn

Details...

Helix

148 – 151

4

Turn

152 – 154

3

Helix

162 – 176

15

Turn

180 – 184

5

Helix

185 – 188

4

Beta strand

196 – 198

3

Helix

212 – 219

8

Helix

222 – 234

13

Helix

237 – 240

4

Helix

244 – 264

21

Turn

269 – 272

4

Beta strand

273 – 276

4

Turn

277 – 279

3

Beta strand

280 – 283

4

Helix

284 – 289

6

Turn

290 – 293

4

Helix

294 – 306

13

Helix

307 – 309

3

Helix

313 – 324

12

Beta strand

329 – 331

3

Helix

335 – 356

22

Helix

363 – 388

26

Helix

394 – 396

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-2 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: C87C7D2F67B1AE49	FASTA	490	54,816
	10 20 30 40 50 60 MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD EQCVVCGDKA 70 80 90 100 110 120 TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID KITRNQCQLC RFKKCIAVGM 130 140 150 160 170 180 AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA 190 200 210 220 230 240 QGSHWKQRRK FLPDDIGQSP IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS 250 260 270 280 290 300 ELPCEDQIIL LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 310 320 330 340 350 360 ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE HYVNHRKHNI 370 380 390 400 410 420 PHFWPKLLMK EREVQSSILY KGAAAEGRPG GSLGVHPEGQ QLLGMHVVQG PQVRQLEQQL 430 440 450 460 470 480 GEAGSLQGPV LQHQSPKSPQ QRLLELLHRS GILHARAVCG EDDSSEADSP SSSEEEPEVC 490 EDLAGNAASP
	Isoform Alpha-1. Checksum: B9FD7BFAC16D6882	FASTA	410	46,813
	10 20 30 40 50 60 MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD EQCVVCGDKA 70 80 90 100 110 120 TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID KITRNQCQLC RFKKCIAVGM 130 140 150 160 170 180 AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA 190 200 210 220 230 240 QGSHWKQRRK FLPDDIGQSP IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS 250 260 270 280 290 300 ELPCEDQIIL LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 310 320 330 340 350 360 ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE HYVNHRKHNI 370 380 390 400 410 PHFWPKLLMK VTDLRMIGAC HASRFLHMKV ECPTELFPPL FLEVFEDQEV
	Isoform Alpha-3. Checksum: 1495A3F2EE6601DD	FASTA	451	50,747
	10 20 30 40 50 60 MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD EQCVVCGDKA 70 80 90 100 110 120 TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID KITRNQCQLC RFKKCIAVGM 130 140 150 160 170 180 AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA 190 200 210 220 230 240 QGSHWKQRRK FLPDDIGQSP IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS 250 260 270 280 290 300 ELPCEDQIIL LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 310 320 330 340 350 360 ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE HYVNHRKHNI 370 380 390 400 410 420 PHFWPKLLMK GPQVRQLEQQ LGEAGSLQGP VLQHQSPKSP QQRLLELLHR SGILHARAVC 430 440 450 GEDDSSEADS PSSSEEEPEV CEDLAGNAAS P
	Isoform Alpha-4 (Alpha3). Checksum: 15FD778790B4D26B	FASTA	448	50,465
	10 20 30 40 50 60 MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD EQCVVCGDKA 70 80 90 100 110 120 TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID KITRNQCQLC RFKKCIAVGM 130 140 150 160 170 180 AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA 190 200 210 220 230 240 QGSHWKQRRK FLPDDIGQSP IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS 250 260 270 280 290 300 ELPCEDQIIL LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 310 320 330 340 350 360 ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE HYVNHRKHNI 370 380 390 400 410 420 PHFWPKLLMK VRQLEQQLGE AGSLQGPVLQ HQSPKSPQQR LLELLHRSGI LHARAVCGED 430 440 DSSEADSPSS SEEEPEVCED LAGNAASP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization of the human thyroid hormone receptor alpha (c-erbA-1) gene." Laudet V., Begue A., Henry C., Joubel A., Martin P., Stehelin D., Saule S. Nucleic Acids Res. 19:1105-1112(1991) [PubMed: 1850510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
[2]	"Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus." Miyajima N., Horiuchi R., Shibuya Y., Fukushige S., Matsubara K., Toyoshima K., Yamamoto T. Cell 57:31-39(1989) [PubMed: 2539258] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
[3]	"Characterization of a thyroid hormone receptor expressed in human kidney and other tissues." Nakai A., Seino S., Sakurai A., Szilak I., Bell G.I., Degroot L.J. Proc. Natl. Acad. Sci. U.S.A. 85:2781-2785(1988) [PubMed: 3357890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2). Tissue: Kidney.
[4]	"Nucleotide sequence of cDNA encoding a novel human thyroid hormone receptor." Pfahl M., Benbrook D. Nucleic Acids Res. 15:9613-9613(1987) [PubMed: 3684612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2). Tissue: Testis.
[5]	"Characterization of a third human thyroid hormone receptor coexpressed with other thyroid hormone receptors in several tissues." Nakai A., Sakurai A., Bell G.I., Degroot L.J. Mol. Endocrinol. 2:1087-1092(1988) [PubMed: 2464749] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM ALPHA-1).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2). Tissue: Brain.
[7]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA-2 AND ALPHA-3). Tissue: Brain, Hippocampus and Muscle.
[9]	"A novel thyroid hormone receptor encoded by a cDNA clone from a human testis library." Benbrook D., Pfahl M. Science 238:788-791(1987) [PubMed: 3672126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-370.
[10]	Liu C., Li L., Liu B., Zang X. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 280-451 (ISOFORM ALPHA-4). Tissue: Brain cortex.
[11]	"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300." Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M. Cell 90:569-580(1997) [PubMed: 9267036] [Abstract] Cited for: INTERACTION WITH NCOA3.
[12]	"Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action." Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J. Oncogene 16:2513-2526(1998) [PubMed: 9627117] [Abstract] Cited for: INTERACTION WITH AKAP13.
[13]	"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo." Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W. J. Biol. Chem. 274:34283-34293(1999) [PubMed: 10567404] [Abstract] Cited for: INTERACTION WITH NCOA6.
[14]	"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells." Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X. Proteomics 8:2885-2896(2008) [PubMed: 18655026] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-190, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55074 , X55073, X55070, X55071, X55004, X55069, X55068, X55066 Genomic DNA. Translation: CAB57886.1.
X55005 mRNA. Translation: CAA38749.1.
X55074 , X55073, X55070, X55071, X55004, X55069, X55068 Genomic DNA. Translation: CAA38899.1.
M24899 mRNA. Translation: AAA35783.1.
M24900 mRNA. Translation: AAA52333.1.
J03239 mRNA. Translation: AAA61176.1.
Y00479 mRNA. Translation: CAA68539.1.
M24748 Genomic DNA. Translation: AAA66021.1.
AK290530 mRNA. Translation: BAF83219.1.
CH471152 Genomic DNA. Translation: EAW60632.1.
BC000261 mRNA. Translation: AAH00261.1.
BC002728 mRNA. Translation: AAH02728.1.
BC035137 mRNA. Translation: AAH35137.1.
AF522368 mRNA. Translation: AAM77692.1.

IPI

IPI00022991.
IPI00219099.
IPI00219100.
IPI00219101.

PIR

A30893.
A40917.
S06163.

RefSeq

NP_003241.2.
NP_955366.1.

UniGene

Hs.724

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NAV	X-ray	2.50	A	148-370	[»]
2H79	X-ray	1.87	A	148-388	[»]

SMR

P10827. Positions 50-138.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10827. 6 interactions.

STRING

P10827.

PTM databases

PhosphoSite

P10827.

Proteomic databases

PRIDE

P10827.

Genome annotation databases

Ensembl

ENST00000264637; ENSP00000264637; ENSG00000126351; Homo sapiens. [Genome view]

GeneID

7067.

KEGG

hsa:7067.

UCSC

uc002htw.1. human.
uc002htx.2. human.

Organism-specific databases

CTD

7067.

GeneCards

GC17P035472.

HGNC

HGNC:11796. THRA.

HPA

CAB023349.
HPA009654.

MIM

190120. gene.

PharmGKB

PA36507.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06097.

HOGENOM

HBG713785.

HOVERGEN

HBG005606.

InParanoid

P10827.

OMA

ILHSRAV.

PhylomeDB

P10827.

Enzyme and pathway databases

Pathway_Interaction_DB

rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P10827.

Bgee

P10827.

CleanEx

HS_THRA.

Genevestigator

P10827.

GermOnline

ENSG00000126351. Homo sapiens.

Family and domain databases

InterPro

IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00451. Levothyroxine.
DB00279. Liothyronine.

NextBio

27631.

SOURCE

Search...

Entry information

Entry name

THA_HUMAN

Accession

Primary (citable) accession number: P10827
Secondary accession number(s): A8K3B5 , P21205, Q8N6A1, Q96H73

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	March 2, 2010
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.