Reviewed, UniProtKB/Swiss-Prot Q5VVJ2 (MYSM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone H2A deubiquitinase MYSM1
      Short name=2A-DUB
    EC=3.1.2.15
Alternative name(s):
    Myb-like, SWIRM and MPN domain-containing protein 1

Gene names

Name:	MYSM1
Synonyms:	KIAA1915

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

General annotation (Comments)

Function	Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation. Ref.5
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Subunit structure	Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Binds histones.
Subcellular location	Nucleus Ref.5.
Domain	Binds double-stranded DNA via the SANT domain. The SWIRM domain does not bind double-stranded DNA.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the peptidase M67A family. MYSM1 subfamily. Contains 1 MPN (JAB/Mov34) domain. Contains 1 SANT domain. Contains 1 SWIRM domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	histone deubiquitination Ref.7 Inferred from direct assay. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Ref.7 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin remodeling complex Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone binding Ref.7 Inferred from direct assay. Source: UniProtKB metallopeptidase activity Ref.7 Inferred from mutant phenotype. Source: UniProtKB transcription coactivator activity Ref.7 Inferred from direct assay. Source: UniProtKB ubiquitin thiolesterase activity Ref.7 Inferred from direct assay. Source: UniProtKB ubiquitin-specific protease activity Ref.7 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q5VVJ2-1)

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 2 (identifier: Q5VVJ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-253: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q5VVJ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-594: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 828

828

Histone H2A deubiquitinase MYSM1

PRO_0000234073

Regions

Domain

116 – 167

52

SANT

Domain

372 – 470

99

SWIRM

Domain

572 – 682

111

MPN

Motif

656 – 669

14

JAMM motif

Motif

774 – 778

5

LXXLL motif

Sites

Metal binding

656

1

Zinc; catalytic By similarity

Metal binding

658

1

Zinc; catalytic By similarity

Metal binding

669

1

Zinc; catalytic Probable

Amino acid modifications

Modified residue

218

1

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

234

1

Phosphoserine Ref.6

Modified residue

236

1

Phosphothreonine Ref.8

Modified residue

267

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

1 – 594

594

Missing in isoform 3.

VSP_018210

Alternative sequence

1 – 253

253

Missing in isoform 2.

VSP_018211

Natural variant

200

1

C → S: dbSNP rs17118103.

VAR_051814

Natural variant

264

1

T → A: dbSNP rs12139511. Ref.1 Ref.2

VAR_051815

Natural variant

825

1

E → K: dbSNP rs232777.

VAR_051816

Experimental info

Mutagenesis

669

1

D → N: Abolishes H2A deubiquitination. Ref.5

Sequence conflict

231

1

E → G in BAG54377. Ref.2

Sequence conflict

540

1

G → D in BAG54377. Ref.2

Sequence conflict

782

1

R → G in CAH18287. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

828

Helix Strand Turn

Details...

Helix

123 – 135

13

Helix

140 – 147

8

Beta strand

148 – 150

3

Helix

152 – 166

15

Helix

388 – 391

4

Helix

395 – 398

4

Helix

406 – 423

18

Helix

430 – 432

3

Turn

433 – 437

5

Beta strand

438 – 441

4

Helix

443 – 456

14

Beta strand

457 – 460

4

Beta strand

466 – 468

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 9EE635A30AF3B089	FASTA	828	95,032
	10 20 30 40 50 60 MAAEEADVDI EGDVVAAAGA QPGSGENTAS VLQKDHYLDS SWRTENGLIP WTLDNTISEE 70 80 90 100 110 120 NRAVIEKMLL EEEYYLSKKS QPEKVWLDQK EDDKKYMKSL QKTAKIMVHS PTKPASYSVK 130 140 150 160 170 180 WTIEEKELFE QGLAKFGRRW TKISKLIGSR TVLQVKSYAR QYFKNKVKCG LDKETPNQKT 190 200 210 220 230 240 GHNLQVKNED KGTKAWTPSC LRGRADPNLN AVKIEKLSDD EEVDITDEVD ELSSQTPQKN 250 260 270 280 290 300 SSSDLLLDFP NSKMHETNQG EFITSDSQEA LFSKSSRGCL QNEKQDETLS SSEITLWTEK 310 320 330 340 350 360 QSNGDKKSIE LNDQKFNELI KNCNKHDGRG IIVDARQLPS PEPCEIQKNL NDNEMLFHSC 370 380 390 400 410 420 QMVEESHEEE ELKPPEQEIE IDRNIIQEEE KQAIPEFFEG RQAKTPERYL KIRNYILDQW 430 440 450 460 470 480 EICKPKYLNK TSVRPGLKNC GDVNCIGRIH TYLELIGAIN FGCEQAVYNR PQTVDKVRIR 490 500 510 520 530 540 DRKDAVEAYQ LAQRLQSMRT RRRRVRDPWG NWCDAKDLEG QTFEHLSAEE LAKRREEEKG 550 560 570 580 590 600 RPVKSLKVPR PTKSSFDPFQ LIPCNFFSEE KQEPFQVKVA SEALLIMDLH AHVSMAEVIG 610 620 630 640 650 660 LLGGRYSEVD KVVEVCAAEP CNSLSTGLQC EMDPVSQTQA SETLAVRGFS VIGWYHSHPA 670 680 690 700 710 720 FDPNPSLRDI DTQAKYQSYF SRGGAKFIGM IVSPYNRNNP LPYSQITCLV ISEEISPDGS 730 740 750 760 770 780 YRLPYKFEVQ QMLEEPQWGL VFEKTRWIIE KYRLSHSSVP MDKIFRRDSD LTCLQKLLEC 790 800 810 820 MRKTLSKVTN CFMAEEFLTE IENLFLSNYK SNQENGVTEE NCTKELLM
	Isoform 2. Checksum: EC1B07CACB78B111	FASTA	575	66,421
	10 20 30 40 50 60 MHETNQGEFI TSDSQEALFS KSSRGCLQNE KQDETLSSSE ITLWTEKQSN GDKKSIELND 70 80 90 100 110 120 QKFNELIKNC NKHDGRGIIV DARQLPSPEP CEIQKNLNDN EMLFHSCQMV EESHEEEELK 130 140 150 160 170 180 PPEQEIEIDR NIIQEEEKQA IPEFFEGRQA KTPERYLKIR NYILDQWEIC KPKYLNKTSV 190 200 210 220 230 240 RPGLKNCGDV NCIGRIHTYL ELIGAINFGC EQAVYNRPQT VDKVRIRDRK DAVEAYQLAQ 250 260 270 280 290 300 RLQSMRTRRR RVRDPWGNWC DAKDLEGQTF EHLSAEELAK RREEEKGRPV KSLKVPRPTK 310 320 330 340 350 360 SSFDPFQLIP CNFFSEEKQE PFQVKVASEA LLIMDLHAHV SMAEVIGLLG GRYSEVDKVV 370 380 390 400 410 420 EVCAAEPCNS LSTGLQCEMD PVSQTQASET LAVRGFSVIG WYHSHPAFDP NPSLRDIDTQ 430 440 450 460 470 480 AKYQSYFSRG GAKFIGMIVS PYNRNNPLPY SQITCLVISE EISPDGSYRL PYKFEVQQML 490 500 510 520 530 540 EEPQWGLVFE KTRWIIEKYR LSHSSVPMDK IFRRDSDLTC LQKLLECMRK TLSKVTNCFM 550 560 570 AEEFLTEIEN LFLSNYKSNQ ENGVTEENCT KELLM
	Isoform 3. Checksum: B9F47C517543A052	FASTA	234	26,716
	10 20 30 40 50 60 MAEVIGLLGG RYSEVDKVVE VCAAEPCNSL STGLQCEMDP VSQTQASETL AVRGFSVIGW 70 80 90 100 110 120 YHSHPAFDPN PSLRDIDTQA KYQSYFSRGG AKFIGMIVSP YNRNNPLPYS QITCLVISEE 130 140 150 160 170 180 ISPDGSYRLP YKFEVQQMLE EPQWGLVFEK TRWIIEKYRL SHSSVPMDKI FRRDSDLTCL 190 200 210 220 230 QKLLECMRKT LSKVTNCFMA EEFLTEIENL FLSNYKSNQE NGVTEENCTK ELLM

References

[1]	"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:179-187(2001) [PubMed: 11572484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-264. Tissue: Brain.
[2]	"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-828 (ISOFORM 1), VARIANT ALA-264. Tissue: Trachea.
[3]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133 (ISOFORM 1). Tissue: Fetal skin and Liver.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation." Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G. Mol. Cell 27:609-621(2007) [PubMed: 17707232] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN COMPLEX, MUTAGENESIS OF ASP-669.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-234 AND SER-267, MASS SPECTROMETRY.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND THR-236, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Structural and functional differences of SWIRM domain subtypes." Yoneyama M., Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T., Watanabe S., Tomo Y., Nishimura Y., Harada T., Terada T., Shirouzu M., Hayashizaki Y., Ohara O., Tanaka A., Kigawa T., Yokoyama S. J. Mol. Biol. 369:222-238(2007) [PubMed: 17428495] [Abstract] Cited for: STRUCTURE BY NMR OF 117-181 AND OF 367-470, INTERACTION WITH DNA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB067502 mRNA. Translation: BAB67808.1. Different initiation.
AK126835 mRNA. Translation: BAG54377.1. Different initiation.
AK292919 mRNA. Translation: BAF85608.1.
BX537912 mRNA. Translation: CAD97896.1.
CR627323 mRNA. Translation: CAH10370.1.
CR749450 mRNA. Translation: CAH18287.1.
AL450024, AL035411 Genomic DNA. Translation: CAH70737.1.
AL035411, AL450024 Genomic DNA. Translation: CAI21908.1.

IPI

IPI00044725.
IPI00740485.
IPI00747702.

RefSeq

NP_001078956.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CU7	NMR	-	A	117-181	[»]
2DCE	NMR	-	A	367-470	[»]

SMR

Q5VVJ2. Positions 577-698.

ModBase

Search...

Protein-protein interaction databases

STRING

Q5VVJ2.

Protein family/group databases

MEROPS

M67.005.

PTM databases

PhosphoSite

Q5VVJ2.

Proteomic databases

PRIDE

Q5VVJ2.

Genome annotation databases

Ensembl

ENST00000472487; ENSP00000418734; ENSG00000162601; Homo sapiens. [Genome view]

GeneID

114803.

KEGG

hsa:114803.

UCSC

uc009waa.1. human.
uc009wab.1. human.

Organism-specific databases

CTD

114803.

GeneCards

GC01M058892.

H-InvDB

HIX0000634.

HGNC

HGNC:29401. MYSM1.

PharmGKB

PA142671301.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14867.

HOVERGEN

Q5VVJ2.

InParanoid

Q5VVJ2.

OMA

DKIFRRD.

OrthoDB

EOG94J53B.

Gene expression databases

ArrayExpress

Q5VVJ2.

Bgee

Q5VVJ2.

CleanEx

HS_MYSM1.

Genevestigator

Q5VVJ2.

GermOnline

ENSG00000162601. Homo sapiens.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR000555. Mov34_MPN_PAD1.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017884. SANT_eukarya.
IPR007526. SWIRM.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

Pfam

PF01398. Mov34. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]

SMART

SM00232. JAB_MPN. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]

PROSITE

PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

79254.

Entry information

Entry name

MYSM1_HUMAN

Accession

Primary (citable) accession number: Q5VVJ2
Secondary accession number(s): A8KA54 , B3KX65, Q68DD3, Q6AI53, Q7Z3G8, Q96PX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	December 7, 2004
Last modified:	January 19, 2010
This is version 68 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.