Reviewed, UniProtKB/Swiss-Prot P56524 (HDAC4_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 4
      Short name=HD4
    EC=3.5.1.98

Gene names

Name:	HDAC4
Synonyms:	KIAA0288

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	1084 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Ref.6
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with HDAC7 By similarity. Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C, AHRR, and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B By similarity. Interacts with KDM5B. Ref.6 Ref.5 Ref.10 Ref.11 Ref.12
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4. The nuclear localization probably depends on sumoylation. Ref.5 Ref.8
Tissue specificity	Ubiquitous.
Domain	The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.
Post-translational modification	Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues is required for the interaction with 14-3-3. Ref.8 Ref.7 Ref.13 Ref.14 Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.
Sequence similarities	Belongs to the histone deacetylase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	B cell differentiation Traceable author statement. Source: UniProtKB cardiac muscle hypertrophy in response to stress Traceable author statement. Source: UniProtKB chromatin remodeling Inferred from direct assay. Source: UniProtKB histone deacetylation Inferred from direct assay. Source: UniProtKB inflammatory response Traceable author statement. Source: UniProtKB negative regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB negative regulation of glycolysis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of myotube differentiation Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription factor activity Inferred from mutant phenotype. Source: UniProtKB nervous system development Traceable author statement. Source: UniProtKB peptidyl-lysine deacetylation Inferred from direct assay. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB positive regulation of gene-specific transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB positive regulation of protein sumoylation Inferred from direct assay. Source: UniProtKB positive regulation of transcription factor activity Inferred from mutant phenotype. Source: UniProtKB regulation of protein binding Inferred from mutant phenotype. Source: UniProtKB response to denervation involved in regulation of muscle adaptation Inferred from sequence or structural similarity. Source: UniProtKB response to interleukin-1 Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone deacetylase complex Inferred from direct assay. Source: UniProtKB transcriptional repressor complex Inferred from direct assay. Source: UniProtKB
Molecular function	histone deacetylase activity Ref.1 Inferred from direct assay. Source: UniProtKB histone deacetylase binding Inferred from physical interaction. Source: UniProtKB potassium ion binding Inferred from direct assay. Source: UniProtKB specific transcriptional repressor activity Inferred from mutant phenotype. Source: UniProtKB transcription activator activity Inferred from sequence or structural similarity. Source: UniProtKB transcription activator binding Inferred from physical interaction. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB transcription repressor binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL6	P41182	1	EBI-308629,EBI-765407
BRMS1	Q9HCU9	2	EBI-308629,EBI-714781
HDAC9	Q9UKV0-3	1	EBI-308629,EBI-765476
HDAC9	Q9UKV0-7	1	EBI-308629,EBI-1372717
HIST1H4A	P62805	1	EBI-308629,EBI-302023

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1084

1084

Histone deacetylase 4

PRO_0000114699

Regions

Region

118 – 313

196

Interaction with MEF2A

Region

655 – 1084

430

Histone deacetylase

Coiled coil

67 – 177

111

Potential

Motif

1051 – 1084

34

Nuclear export signal By similarity

Sites

Active site

803

1

By similarity

Amino acid modifications

Modified residue

246

1

Phosphoserine; by CaMK4 Ref.7

Modified residue

350

1

Phosphoserine Ref.14

Modified residue

467

1

Phosphoserine; by CaMK4 Ref.7

Modified residue

565

1

Phosphoserine Ref.13

Modified residue

632

1

Phosphoserine; by CaMK4 Ref.7 Ref.13

Modified residue

633

1

Phosphoserine Ref.13

Cross-link

559

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Natural variant

727

1

P → R in a breast cancer sample; somatic mutation. Ref.15

VAR_036042

Experimental info

Mutagenesis

246

1

S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.7

Mutagenesis

467

1

S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.8 Ref.7

Mutagenesis

559

1

K → R: Abolishes sumoylation and reduces the histone deacetylase activity. Ref.11

Mutagenesis

632

1

S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.8 Ref.7

Mutagenesis

803

1

H → L: Abolishes histone deacetylase activity. Ref.6

Mutagenesis

1056

1

V → A: Reduces CaMK-dependent nuclear export. Ref.9

Mutagenesis

1062

1

L → A: Reduces CaMK-dependent nuclear export. Ref.9

Sequence conflict

373

1

A → T in AAD29046. Ref.1

Sequence conflict

373

1

A → T in BAA22957. Ref.2

Secondary structure

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1084

Helix Strand Turn

Details...

Helix

64 – 112

49

Helix

115 – 121

7

Turn

122 – 125

4

Helix

126 – 128

3

Beta strand

652 – 658

7

Helix

660 – 662

3

Beta strand

673 – 675

3

Helix

681 – 691

11

Helix

694 – 697

4

Beta strand

698 – 702

5

Helix

708 – 711

4

Turn

712 – 714

3

Helix

717 – 724

8

Helix

727 – 730

4

Helix

736 – 745

10

Beta strand

746 – 748

3

Beta strand

754 – 756

3

Helix

762 – 786

25

Beta strand

791 – 795

5

Beta strand

813 – 815

3

Helix

817 – 829

13

Beta strand

834 – 838

5

Beta strand

840 – 842

3

Helix

845 – 851

7

Beta strand

857 – 864

8

Helix

866 – 868

3

Helix

883 – 885

3

Beta strand

889 – 894

6

Helix

904 – 913

10

Helix

915 – 922

8

Beta strand

925 – 931

7

Beta strand

936 – 938

3

Turn

941 – 943

3

Helix

950 – 960

11

Helix

964 – 966

3

Beta strand

968 – 972

5

Helix

978 – 992

15

Helix

1002 – 1006

5

Helix

1011 – 1024

14

Turn

1025 – 1027

3

Helix

1029 – 1031

3

Helix

1042 – 1047

6

Sequences

	Sequence		Length	Mass (Da)
	P56524-1 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: BB7FD37652D12398	FASTA	1,084	119,040
	10 20 30 40 50 60 MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD LRLDHQFSLP 70 80 90 100 110 120 VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQEMLA 130 140 150 160 170 180 MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL 190 200 210 220 230 240 NKKKALAHRN LNHCISSDPR YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP 250 260 270 280 290 300 LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP 310 320 330 340 350 360 SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS LPNITLGLPA 370 380 390 400 410 420 TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS PLERDGGAAH SPLLQHMVLL 430 440 450 460 470 480 EQPPAQAPLV TGLGALPLHA QSLVGADRVS PSIHKLRQHR PLGRTQSAPL PQNAQALQHL 490 500 510 520 530 540 VIQQQHQQFL EKHKQQFQQQ QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY 550 560 570 580 590 600 LDRLPGQKEA HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ 610 620 630 640 650 660 RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP RFTTGLVYDT 670 680 690 700 710 720 LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT 730 740 750 760 770 780 LLYGTNPLNR QKLDSKKLLG SLASVFVRLP CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE 790 800 810 820 830 840 LVFKVATGEL KNGFAVVRPP GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD 850 860 870 880 890 900 VHHGNGTQQA FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP 910 920 930 940 950 960 PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA RCFGYLTKQL 970 980 990 1000 1010 1020 MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVLQQRPN ANAVRSMEKV 1030 1040 1050 1060 1070 1080 MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN EEAETVTAMA SLSVGVKPAE KRPDEEPMEE EPPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three proteins define a class of human histone deacetylases related to yeast Hda1p." Grozinger C.M., Hassig C.A., Schreiber S.L. Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999) [PubMed: 10220385] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukemia.
[2]	"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins." Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N. DNA Res. 4:53-59(1997) [PubMed: 9179496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"HDAC4 deacetylase associates with and represses the MEF2 transcription factor." Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T. EMBO J. 18:5099-5107(1999) [PubMed: 10487761] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEF2A.
[6]	"HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor." Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J. Mol. Cell. Biol. 19:7816-7827(1999) [PubMed: 10523670] [Abstract] Cited for: FUNCTION, INTERACTION WITH MEF2C AND MEF2D, MUTAGENESIS OF HIS-803.
[7]	"Regulation of histone deacetylase 4 by binding of 14-3-3 proteins." Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I., Bazett-Jones D.P., Yang X.-J. Mol. Cell. Biol. 20:6904-6912(2000) [PubMed: 10958686] [Abstract] Cited for: PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, MUTAGENESIS OF SER-246; SER-467 AND SER-632.
[8]	"The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking." Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M., Means A.R., Yao T.-P. J. Biol. Chem. 276:35042-35048(2001) [PubMed: 11470791] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-467 AND SER-632.
[9]	"Identification of a signal-responsive nuclear export sequence in class II histone deacetylases." McKinsey T.A., Zhang C.-L., Olson E.N. Mol. Cell. Biol. 21:6312-6321(2001) [PubMed: 11509672] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF VAL-1056 AND LEU-1062.
[10]	"The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases." Franco P.J., Farooqui M., Seto E., Wei L.-N. Mol. Endocrinol. 15:1318-1328(2001) [PubMed: 11463856] [Abstract] Cited for: INTERACTION WITH NR2C1.
[11]	"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase." Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A. EMBO J. 21:2682-2691(2002) [PubMed: 12032081] [Abstract] Cited for: HOMODIMERIZATION, SUMOYLATION AT LYS-559, MUTAGENESIS OF LYS-559.
[12]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed: 17373667] [Abstract] Cited for: INTERACTION WITH KDM5B.
[13]	"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-565; SER-632 AND SER-633, MASS SPECTROMETRY.
[14]	"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-350, MASS SPECTROMETRY. Tissue: T-cell.
[15]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-727.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132607 mRNA. Translation: AAD29046.1.
AB006626 mRNA. Translation: BAA22957.2. Different initiation.
AC017028 Genomic DNA. No translation available.

IPI

IPI00010088.

RefSeq

NP_006028.2.

UniGene

Hs.20516

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H8N	X-ray	2.60	A/B/C/D	62-153	[»]
2O94	X-ray	3.00	A/B/C/D	62-153	[»]
2VQJ	X-ray	2.10	A	648-1057	[»]
2VQM	X-ray	1.80	A	648-1057	[»]
2VQO	X-ray	2.15	A/B	648-1057	[»]
2VQQ	X-ray	1.90	A/B	648-1057	[»]
2VQV	X-ray	3.30	A/B	648-1057	[»]
2VQW	X-ray	3.00	G	648-1057	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P56524. 11 interactions.

STRING

P56524.

PTM databases

PhosphoSite

P56524.

Proteomic databases

PRIDE

P56524.

Genome annotation databases

Ensembl

ENST00000345617; ENSP00000264606; ENSG00000068024; Homo sapiens. [Genome view]

GeneID

9759.

KEGG

hsa:9759.

Organism-specific databases

CTD

9759.

GeneCards

GC02M239707.

H-InvDB

HIX0021592.

HGNC

HGNC:14063. HDAC4.

HPA

CAB004431.

MIM

605314. gene.

PharmGKB

PA29229.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06150.

HOGENOM

HBG716007.

HOVERGEN

P56524.

InParanoid

P56524.

OMA

RVNHMPS.

PhylomeDB

P56524.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Gene expression databases

ArrayExpress

P56524.

Bgee

P56524.

CleanEx

HS_HDAC4.

Genevestigator

P56524.

GermOnline

ENSG00000068024. Homo sapiens.

Family and domain databases

InterPro

IPR019154. Arb2_domain.
IPR000286. His_deacetylse.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]

Gene3D

G3DSA:3.40.800.20. His_deacetylse. 1 hit.

PANTHER

PTHR10625. His_deacetylse. 1 hit.

Pfam

PF09757. Arb2. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]

PIRSF

PIRSF037911. HDAC_II_euk. 1 hit.

PRINTS

PR01270. HDASUPER.

ProtoNet

Search...

Other Resources

NextBio

36731.

SOURCE

Search...

Entry information

Entry name

HDAC4_HUMAN

Accession

Primary (citable) accession number: P56524
Secondary accession number(s): Q9UND6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 22, 2009
Last modified:	January 19, 2010
This is version 105 of the entry and version 3 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.