Q9H5I1 (SUV92_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase SUV39H2
EC=2.1.1.43

Alternative name(s):
Histone H3-K9 methyltransferase 2
Short name=H3-K9-HMTase 2
Lysine N-methyltransferase 1B
Suppressor of variegation 3-9 homolog 2
Short name=Su(var)3-9 homolog 2

Gene names

Name:	SUV39H2
Synonyms:	KMT1B

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	410 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Ref.7
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Interacts with SMAD5. Ref.8
Subcellular location	Nucleus By similarity. Chromosome › centromere By similarity. Note: Associates with centromeric constitutive heterochromatin By similarity.
Domain	Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin By similarity.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 1 chromo domain. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain.

Ontologies

Keywords
Biological process	Cell cycle Differentiation Transcription Transcription regulation
Cellular component	Centromere Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromatin assembly or disassembly Inferred from mutant phenotype PubMed 10949293. Source: UniProtKB chromatin remodeling Inferred from direct assay PubMed 10949293. Source: UniProtKB male meiosis Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin Inferred from direct assay PubMed 10949293. Source: UniProtKB chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear heterochromatin Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara histone methyltransferase activity (H3-K9 specific) Inferred from direct assay PubMed 10949293. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-723127,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: Q9H5I1-1)

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.

Note: No experimental confirmation available.

Isoform 1 (identifier: Q9H5I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Isoform 2 (identifier: Q9H5I1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-283: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 410

410

Histone-lysine N-methyltransferase SUV39H2

PRO_0000186059

Regions

Domain

47 – 105

59

Chromo

Domain

189 – 247

59

Pre-SET

Domain

249 – 377

129

SET

Domain

394 – 410

17

Post-SET

Amino acid modifications

Modified residue

381

1

Phosphoserine Ref.10

Modified residue

384

1

Phosphoserine Ref.9 Ref.10

Modified residue

388

1

Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence

1 – 60

60

Missing in isoform 1.

VSP_002209

Alternative sequence

104 – 283

180

Missing in isoform 2.

VSP_002210

Natural variant

383

1

D → H in a breast cancer sample; somatic mutation. Ref.11

VAR_036344

Secondary structure

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410

Helix Strand Turn

Details...

Helix

125 – 147

23

Beta strand

150 – 152

3

Beta strand

154 – 157

4

Beta strand

159 – 161

3

Turn

196 – 198

3

Helix

202 – 205

4

Helix

244 – 246

3

Beta strand

252 – 256

5

Beta strand

258 – 260

3

Beta strand

263 – 269

7

Beta strand

276 – 280

5

Beta strand

283 – 286

4

Helix

287 – 295

9

Helix

299 – 303

5

Beta strand

305 – 307

3

Beta strand

313 – 318

6

Beta strand

320 – 323

4

Helix

325 – 328

4

Beta strand

336 – 345

10

Beta strand

353 – 360

8

Beta strand

367 – 370

4

Helix

372 – 374

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: ED8BBF80AE838C69	FASTA	410	46,682
	10 20 30 40 50 60 MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD 70 80 90 100 110 120 MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKDNNKTLK 130 140 150 160 170 180 PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG 190 200 210 220 230 240 ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP 250 260 270 280 290 300 NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK 310 320 330 340 350 360 GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR 370 380 390 400 410 TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN
	Isoform 1 [UniParc]. Checksum: F435E9C5EBEA8BAD	FASTA	350	39,946
	10 20 30 40 50 60 MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKDNNKTLK 70 80 90 100 110 120 PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG 130 140 150 160 170 180 ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP 190 200 210 220 230 240 NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK 250 260 270 280 290 300 GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR 310 320 330 340 350 TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN
	Isoform 2 [UniParc]. Checksum: BB9EF88E02C4D74A	FASTA	230	26,350
	10 20 30 40 50 60 MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD 70 80 90 100 110 120 MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVITSEEA ERRGQFYDNK 130 140 150 160 170 180 GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR 190 200 210 220 230 TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[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] (ISOFORMS 1 AND 2). Tissue: Bone marrow and Muscle.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-410. Tissue: Testis.
[7]	"A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells." Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A. EMBO J. 23:605-615(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression." Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M., Lechleider R.J. Oncogene 23:5242-5251(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMAD5.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-388, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, MASS SPECTROMETRY.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-383.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK027067 mRNA. Translation: BAB15645.1.
CR457372 mRNA. Translation: CAG33653.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40028.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40029.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40032.1.
CH471072 Genomic DNA. Translation: EAW86254.1.
CH471072 Genomic DNA. Translation: EAW86253.1.
CH471072 Genomic DNA. Translation: EAW86255.1.
CH471072 Genomic DNA. Translation: EAW86256.1.
BC007754 mRNA. Translation: AAH07754.1.
BC029360 mRNA. Translation: AAH29360.1.
AL834488 mRNA. Translation: CAD39146.1.

IPI

IPI00002929.
IPI00218860.
IPI00218861.

RefSeq

NP_001180353.1. NM_001193424.1.
NP_001180354.1. NM_001193425.1.
NP_001180355.1. NM_001193426.1.
NP_001180356.1. NM_001193427.1.
NP_078946.1. NM_024670.3.

UniGene

Hs.554883.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R3A	X-ray	2.00	A	112-410	[»]

ProteinModelPortal

Q9H5I1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H5I1. 12 interactions.

MINT

MINT-3068157.

STRING

9606.ENSP00000319208.

PTM databases

PhosphoSite

Q9H5I1.

Polymorphism databases

DMDM

25091325.

Proteomic databases

PaxDb

Q9H5I1.

PRIDE

Q9H5I1.

Protocols and materials databases

DNASU

79723.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313519; ENSP00000319208; ENSG00000152455.
ENST00000354919; ENSP00000346997; ENSG00000152455.
ENST00000378325; ENSP00000367576; ENSG00000152455.

GeneID

79723.

KEGG

hsa:79723.

UCSC

uc001ing.3. human.
uc001inh.3. human.

Organism-specific databases

CTD

79723.

GeneCards

GC10P014922.

HGNC

HGNC:17287. SUV39H2.

HPA

HPA045901.

MIM

606503. gene.

neXtProt

NX_Q9H5I1.

PharmGKB

PA134868807.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2940.

HOGENOM

HOG000231244.

HOVERGEN

HBG055621.

InParanoid

Q9H5I1.

KO

K11419.

OMA

PGISLVN.

PhylomeDB

Q9H5I1.

Gene expression databases

ArrayExpress

Q9H5I1.

Bgee

Q9H5I1.

CleanEx

HS_SUV39H2.

Genevestigator

Q9H5I1.

GermOnline

ENSG00000152455. Homo sapiens.

Family and domain databases

InterPro

IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]

Pfam

PF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]

PIRSF

PIRSF009343. SUV39_SET. 1 hit.

SMART

SM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9H5I1.

ChEMBL

CHEMBL1795177.

ChiTaRS

SUV39H2. human.

EvolutionaryTrace

Q9H5I1.

GenomeRNAi

79723.

NextBio

69082.

SOURCE

Search...

Entry information

Entry name

SUV92_HUMAN

Accession

Primary (citable) accession number: Q9H5I1
Secondary accession number(s): D3DRT4 , Q5JSS4, Q5JSS5, Q6I9Y3, Q8ND06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 15, 2002
Last modified:	May 1, 2013
This is version 121 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.