Reviewed, UniProtKB/Swiss-Prot Q9WVG6 (CARM1_MOUSE)

Names and origin

Protein names

Recommended name:
    Histone-arginine methyltransferase CARM1
    EC=2.1.1.125
    EC=2.1.1.-
Alternative name(s):
    Protein arginine N-methyltransferase 4
    Coactivator-associated arginine methyltransferase 1

Gene names

Name:	Carm1
Synonyms:	Prmt4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' and activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs. Ref.1 Ref.6 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19
Catalytic activity	S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.
Subunit structure	Homodimer Probable. Interacts with NR1H4. Interacts with SNRPC By similarity. Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, CREBBP and CTNNB1. Interacts with RELA.
Subcellular location	Nucleus. Cytoplasm. Ref.10
Tissue specificity	Ubiquitously expressed. Within the brain, present in proliferating cells from lateral ventricular zone and dentate gyrus (at protein level). Ref.1 Ref.20
Developmental stage	At E9, expression is prominent in the neural tube and somites. Ref.10
Miscellaneous	Methylation of H3-R17 by CARM1 is stimulated by preacetylation of H3-K18/H3-K23 by EP300 and blocked by citrullination of H3-R17 by PADI4.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	histone methylation Ref.1 Inferred from direct assay. Source: MGI regulation of transcription, DNA-dependent Ref.1 Inferred from direct assay. Source: MGI steroid hormone receptor signaling pathway Inferred from direct assay. Source: HGNC transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC transcription coactivator activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WVG6-1)

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 2 (identifier: Q9WVG6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     540-562: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 608

608

Histone-arginine methyltransferase CARM1

PRO_0000212339

Regions

Region

500 – 608

109

Transactivation domain

Sites

Binding site

160

1

S-adenosyl-L-methionine By similarity

Binding site

169

1

S-adenosyl-L-methionine By similarity

Binding site

193

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

215

1

S-adenosyl-L-methionine By similarity

Binding site

244

1

S-adenosyl-L-methionine By similarity

Natural variations

Alternative sequence

540 – 562

23

Missing in isoform 2.

VSP_012508

Experimental info

Mutagenesis

189 – 191

3

VLD → AAA: Abolishes histone methyltransferase activity and coactivator activity. Ref.1 Ref.6

Mutagenesis

267

1

E → Q: Abolishes histone methyltransferase activity and reduces coactivator activity. Ref.11 Ref.14

Sequence conflict

400

1

I → L in BAE34644. Ref.3

Secondary structure

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608

Helix Strand Turn

Details...

Helix

148 – 153

6

Helix

157 – 164

8

Helix

167 – 179

13

Helix

180 – 183

4

Turn

184 – 186

3

Beta strand

188 – 193

6

Helix

198 – 206

9

Beta strand

209 – 215

7

Helix

219 – 229

11

Turn

233 – 235

3

Beta strand

236 – 241

6

Turn

243 – 245

3

Beta strand

252 – 256

5

Helix

266 – 268

3

Helix

269 – 275

7

Helix

276 – 279

4

Beta strand

280 – 288

9

Beta strand

290 – 298

9

Helix

301 – 311

11

Helix

312 – 315

4

Beta strand

319 – 321

3

Helix

325 – 327

3

Helix

328 – 336

9

Beta strand

340 – 342

3

Helix

346 – 348

3

Beta strand

354 – 359

6

Turn

360 – 362

3

Helix

365 – 369

5

Beta strand

370 – 378

9

Beta strand

383 – 395

13

Beta strand

404 – 406

3

Beta strand

418 – 429

12

Beta strand

434 – 442

9

Beta strand

450 – 457

8

Turn

458 – 461

4

Beta strand

462 – 469

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: C621F2AA9FBA2DA3	FASTA	608	65,854
	10 20 30 40 50 60 MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR HAEQQALRLE 70 80 90 100 110 120 VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI ITLGCNSVLI QFATPHDFCS 130 140 150 160 170 180 FYNILKTCRG HTLERSVFSE RTEESSAVQY FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN 190 200 210 220 230 240 HTDFKDKIVL DVGCGSGILS FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP 250 260 270 280 290 300 GKVEEVSLPE QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD 310 320 330 340 350 360 EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM AKSVKYTVNF 370 380 390 400 410 420 LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI MTVWLSTAPT EPLTHWYQVR 430 440 450 460 470 480 CLFQSPLFAK AGDTLSGTCL LIANKRQSYD ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT 490 500 510 520 530 540 TPSPPPGSHY TSPSENMWNT GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLA 550 560 570 580 590 600 NTGIVNHTHS RMGSIMSTGI VQGSSGAQGG GGSSSAHYAV NNQFTMGGPA ISMASPMSIP TNTMHYGS
	Isoform 2. Checksum: C419059E314B2D51	FASTA	585	63,460
	10 20 30 40 50 60 MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR HAEQQALRLE 70 80 90 100 110 120 VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI ITLGCNSVLI QFATPHDFCS 130 140 150 160 170 180 FYNILKTCRG HTLERSVFSE RTEESSAVQY FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN 190 200 210 220 230 240 HTDFKDKIVL DVGCGSGILS FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP 250 260 270 280 290 300 GKVEEVSLPE QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD 310 320 330 340 350 360 EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM AKSVKYTVNF 370 380 390 400 410 420 LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI MTVWLSTAPT EPLTHWYQVR 430 440 450 460 470 480 CLFQSPLFAK AGDTLSGTCL LIANKRQSYD ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT 490 500 510 520 530 540 TPSPPPGSHY TSPSENMWNT GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLG 550 560 570 580 SSGAQGGGGS SSAHYAVNNQ FTMGGPAISM ASPMSIPTNT MHYGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of transcription by a protein methyltransferase." Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R. Science 284:2174-2177(1999) [PubMed: 10381882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF 189-VAL--ASP-191, FUNCTION, TISSUE SPECIFICITY, METHYLATION OF HISTONE H3, INTERACTION WITH NCOA1; NCOA2 AND NCOA3. Tissue: Embryo.
[2]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-608 (ISOFORM 1). Strain: FVB/N. Tissue: Mammary gland and Mammary tumor.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-608 (ISOFORM 1). Strain: C57BL/6J. Tissue: Visual cortex.
[4]	"Methylation of histone H3 by coactivator-associated arginine methyltransferase 1." Schurter B.T., Koh S.S., Chen D., Bunick G.J., Harp J.M., Hanson B.L., Henschen-Edman A., Mackay D.R., Stallcup M.R., Aswad D.W. Biochemistry 40:5747-5756(2001) [PubMed: 11341840] [Abstract] Cited for: METHYLATION OF HISTONE H3.
[5]	"Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter." Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R. Curr. Biol. 11:1981-1985(2001) [PubMed: 11747826] [Abstract] Cited for: METHYLATION OF HISTONE H3.
[6]	"A transcriptional switch mediated by cofactor methylation." Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M. Science 294:2507-2511(2001) [PubMed: 11701890] [Abstract] Cited for: FUNCTION, METHYLATION OF EP300 AND CREBBP, MUTAGENESIS OF 189-VAL--ASP-191, INTERACTION WITH EP300 AND CREBBP.
[7]	"Crosstalk between CARM1 methylation and CBP acetylation on histone H3." Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T. Curr. Biol. 12:2090-2097(2002) [PubMed: 12498683] [Abstract] Cited for: METHYLATION OF HISTONE H3.
[8]	"Methylation at arginine 17 of histone H3 is linked to gene activation." Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T. EMBO Rep. 3:39-44(2002) [PubMed: 11751582] [Abstract] Cited for: METHYLATION OF HISTONE H3.
[9]	"PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays." Lee J., Bedford M.T. EMBO Rep. 3:268-273(2002) [PubMed: 11850402] [Abstract] Cited for: METHYLATION OF PABPC1.
[10]	"The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2." Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E. J. Biol. Chem. 277:4324-4333(2002) [PubMed: 11713257] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH MEF2C.
[11]	"Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators." Koh S.S., Li H., Lee Y.-H., Widelitz R.B., Chuong C.-M., Stallcup M.R. J. Biol. Chem. 277:26031-26035(2002) [PubMed: 11983685] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-267, INTERACTION WITH CTNNB1.
[12]	"Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase." Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A. J. Biol. Chem. 277:44623-44630(2002) [PubMed: 12237300] [Abstract] Cited for: METHYLATION OF ELAVL1.
[13]	"Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function." Teyssier C., Chen D., Stallcup M.R. J. Biol. Chem. 277:46066-46072(2002) [PubMed: 12351636] [Abstract] Cited for: CHARACTERIZATION, HOMOOLIGOMERIZATION.
[14]	"Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities." Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R. Mol. Cell. Biol. 22:3621-3632(2002) [PubMed: 11997499] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2, MUTAGENESIS OF GLU-267.
[15]	"Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice." Yadav N., Lee J., Kim J., Shen J., Hu M.C.-T., Aldaz C.M., Bedford M.T. Proc. Natl. Acad. Sci. U.S.A. 100:6464-6468(2003) [PubMed: 12756295] [Abstract] Cited for: FUNCTION, METHYLATION OF PABPC1.
[16]	"Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53." An W., Kim J., Roeder R.G. Cell 117:735-748(2004) [PubMed: 15186775] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53.
[17]	"Histone deimination antagonizes arginine methylation." Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., Kouzarides T. Cell 118:545-553(2004) [PubMed: 15339660] [Abstract] Cited for: METHYLATION OF HISTONE H3.
[18]	"Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity." Lee Y.-H., Campbell H.D., Stallcup M.R. Mol. Cell. Biol. 24:2103-2117(2004) [PubMed: 14966289] [Abstract] Cited for: FUNCTION, INTERACTION WITH FLII.
[19]	"Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression." Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O. EMBO J. 24:85-96(2005) [PubMed: 15616592] [Abstract] Cited for: METHYLATION OF HISTONE H3, FUNCTION, INTERACTION WITH RELA.
[20]	"CARM1 regulates proliferation of PC12 cells by methylating HuD." Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H., Yachi K., Kubo T., Yoshikawa H., Tohyama M. Mol. Cell. Biol. 26:2273-2285(2006) [PubMed: 16508003] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF117887 mRNA. Translation: AAD41265.2.
BC003964 mRNA. Translation: AAH03964.1.
BC008263 mRNA. Translation: AAH08263.1.
BC036974 mRNA. Translation: AAH36974.1.
AK158757 mRNA. Translation: BAE34644.1.

IPI

IPI00125950.
IPI00279931.

RefSeq

NP_067506.2.
NP_694781.1.

UniGene

Mm.178115

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V74	X-ray	2.70	B/D/F/H	147-490	[»]
2V7E	X-ray	2.70	A/B	147-490	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9WVG6.

PTM databases

PhosphoSite

Q9WVG6.

Proteomic databases

PRIDE

Q9WVG6.

Genome annotation databases

Ensembl

ENSMUST00000034703; ENSMUSP00000034703; ENSMUSG00000032185; Mus musculus. [Genome view]
ENSMUST00000115394; ENSMUSP00000111052; ENSMUSG00000032185; Mus musculus. [Genome view]
ENSMUST00000115395; ENSMUSP00000111053; ENSMUSG00000032185; Mus musculus. [Genome view]

GeneID

59035.

KEGG

mmu:59035.

UCSC

uc009olu.1. mouse.
uc009olw.1. mouse.

Organism-specific databases

CTD

59035.

MGI

MGI:1913208. Carm1.

Phylogenomic databases

HOGENOM

Q9WVG6.

HOVERGEN

Q9WVG6.

Enzyme and pathway databases

BRENDA

2.1.1.125. 244.

Gene expression databases

ArrayExpress

Q9WVG6.

Bgee

Q9WVG6.

Genevestigator

Q9WVG6.

GermOnline

ENSMUSG00000032185. Mus musculus.

Family and domain databases

InterPro

IPR010456. PrmA_MeTrfase.
[Graphical view]

Pfam

PF06325. PrmA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

314634.

SOURCE

Search...

Entry information

Entry name

CARM1_MOUSE

Accession

Primary (citable) accession number: Q9WVG6
Secondary accession number(s): Q3TYB9 , Q8K1Y5, Q91W24, Q99KX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	September 13, 2004
Last modified:	October 13, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)