Reviewed, UniProtKB/Swiss-Prot Q9NPF5 (DMAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA methyltransferase 1-associated protein 1
      Short name=DNMT1-associated protein 1
      Short name=DNMAP1

Gene names

Name:	DMAP1
Synonyms:	KIAA1425

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

General annotation (Comments)

Function	Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Ref.12 Ref.13 Ref.14
Subunit structure	Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. DMAP1 also forms a complex with DNMT1 and HDAC2. Throughout S phase it interacts directly with the N-terminus of DNMT1, which serves to recruit DMAP1 to replication foci. DMAP1 interacts with ING1, a component of the mSin3A transcription repressor complex, although this interaction is not required for recruitment of ING1 to heterochromatin. Interacts directly with the transcriptional corepressor TSG101. Interacts with the pro-apoptotic protein DAXX. Ref.12 Ref.13 Ref.1
Subcellular location	Nucleus. Note: Targeted to replication foci throughout S phase by DNMT1. Ref.1
Sequence similarities	Contains 1 SANT domain.

Ontologies

Keywords
Biological process	Growth regulation Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
Molecular function	Activator Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA methylation Ref.1 Traceable author statement. Source: UniProtKB histone H2A acetylation Ref.14 Inferred from direct assay. Source: UniProtKB histone H4 acetylation Ref.14 Inferred from direct assay. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Ref.14 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TSG101	Q99816	1	EBI-399105,EBI-346882

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 467

467

DNA methyltransferase 1-associated protein 1

PRO_0000079935

Regions

Domain

149 – 199

51

SANT

Coiled coil

225 – 275

51

Potential

Compositional bias

454 – 460

7

Poly-Ser

Amino acid modifications

Modified residue

445

1

Phosphothreonine Ref.15 Ref.16 Ref.18 Ref.19

Modified residue

448

1

Phosphoserine Ref.19

Modified residue

456

1

Phosphoserine Ref.17

Experimental info

Sequence conflict

135

1

V → E in CAB66592. Ref.4

Sequence conflict

135

1

V → E in CAL38490. Ref.4

Sequence conflict

150

1

D → N in CAB66592. Ref.4

Sequence conflict

150

1

D → N in CAL38490. Ref.4

Sequence conflict

171

1

F → L in CAD97886. Ref.10

Sequence conflict

424

1

T → S in CAB66592. Ref.4

Sequence conflict

424

1

T → S in CAL38490. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

467

Helix Strand Turn

Details...

Helix

140 – 146

7

Helix

154 – 166

13

Turn

167 – 169

3

Helix

171 – 177

7

Turn

180 – 182

3

Helix

188 – 205

18

Sequences

	Sequence		Length	Mass (Da)
	Q9NPF5-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 54500B252E076A29	FASTA	467	52,993
	10 20 30 40 50 60 MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL 70 80 90 100 110 120 LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE 130 140 150 160 170 180 GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR FVVIHDRYDH 190 200 210 220 230 240 QQFKKRSVED LKERYYHICA KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ 250 260 270 280 290 300 VAEEEYLLQE LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE 310 320 330 340 350 360 KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV ELSPTPTEEL 370 380 390 400 410 420 VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR AGVLGGPATP ASGPGPASAE 430 440 450 460 PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK RRESASSSSS VKKAKKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci." Rountree M.R., Bachman K.E., Baylin S.B. Nat. Genet. 25:269-277(2000) [PubMed: 10888872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH DNMT1 AND TSG101.
[2]	Rhodes S., Huckle E. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed: 10718198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal brain.
[5]	"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]. Tissue: Embryo.
[6]	"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].
[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 (SEP-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]. Tissue: Placenta and Skin.
[9]	"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex." Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W. J. Biol. Chem. 278:42733-42736(2003) [PubMed: 12963728] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-27; 56-66; 117-128; 237-252; 271-282; 369-378; 401-433 AND 434-449, IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[10]	"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] OF 132-467. Tissue: Colon endothelium.
[11]	"The highly conserved and multifunctional NuA4 HAT complex." Doyon Y., Cote J. Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed: 15196461] [Abstract] Cited for: REVIEW ON NUA4 COMPLEX.
[12]	"Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells." Xin H., Yoon H.-G., Singh P.B., Wong J., Qin J. J. Biol. Chem. 279:9539-9546(2004) [PubMed: 14665632] [Abstract] Cited for: FUNCTION, INTERACTION WITH ING1.
[13]	"Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1." Muromoto R., Sugiyama K., Takachi A., Imoto S., Sato N., Yamamoto T., Oritani K., Shimoda K., Matsuda T. J. Immunol. 172:2985-2993(2004) [PubMed: 14978102] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAXX.
[14]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed: 14966270] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, MASS SPECTROMETRY.
[19]	"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 THR-445 AND SER-448, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"SANT domain of human DNA methyltransferase 1 associated protein 1." Structural genomics consortium (SGC) Submitted (JUN-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-212.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF265228 mRNA. Translation: AAF87079.1.
AL137200 mRNA. Translation: CAB69910.1.
AB037846 mRNA. Translation: BAA92663.1. Different initiation.
AL136657 mRNA. Translation: CAB66592.1.
AM393614 mRNA. Translation: CAL38490.1.
AK021605 mRNA. Translation: BAB13854.1.
AK289366 mRNA. Translation: BAF82055.1.
AL035417 Genomic DNA. Translation: CAI23197.1.
CH471059 Genomic DNA. Translation: EAX07046.1.
BC002855 mRNA. Translation: AAH02855.1.
BC008053 mRNA. Translation: AAH08053.1.
BX537895 mRNA. Translation: CAD97886.1.

IPI

IPI00219919.

RefSeq

NP_001029195.1.
NP_001029196.1.
NP_061973.1.

UniGene

Hs.8008

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HM5	X-ray	1.80	A	121-212	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NPF5. 9 interactions.

STRING

Q9NPF5.

PTM databases

PhosphoSite

Q9NPF5.

Proteomic databases

PRIDE

Q9NPF5.

Genome annotation databases

Ensembl

ENST00000315913; ENSP00000312697; ENSG00000178028; Homo sapiens. [Genome view]
ENST00000361745; ENSP00000354697; ENSG00000178028; Homo sapiens. [Genome view]
ENST00000372289; ENSP00000361363; ENSG00000178028; Homo sapiens. [Genome view]

GeneID

55929.

KEGG

hsa:55929.

UCSC

uc001clq.1. human.

Organism-specific databases

CTD

55929.

GeneCards

GC01P044451.

H-InvDB

HIX0020213.

HGNC

HGNC:18291. DMAP1.

MIM

605077. gene.

PharmGKB

PA134927315.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15059.

HOGENOM

HBG714649.

HOVERGEN

Q9NPF5.

InParanoid

Q9NPF5.

OMA

KTQDLQK.

OrthoDB

EOG9X6FVD.

PhylomeDB

Q9NPF5.

Gene expression databases

ArrayExpress

Q9NPF5.

Bgee

Q9NPF5.

CleanEx

HS_DMAP1.

Genevestigator

Q9NPF5.

GermOnline

ENSG00000178028. Homo sapiens.

Family and domain databases

InterPro

IPR008468. DMAP1.
IPR001005. SANT_DNA-bd.
[Graphical view]

Pfam

PF05499. DMAP1. 1 hit.
[Graphical view]

ProDom

PD492828. DMAP1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00717. SANT. 1 hit.
[Graphical view]

PROSITE

PS51293. SANT. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

61337.

SOURCE

Search...

Entry information

Entry name

DMAP1_HUMAN

Accession

Primary (citable) accession number: Q9NPF5
Secondary accession number(s): A8K001 , Q0JSM4, Q5TG41, Q7Z3H7, Q9H0S8, Q9P2C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 94 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.