Histone acetyltransferase MYST2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot O95251 (MYST2_HUMAN)

Last modified November 25, 2008. Version 68. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Histone acetyltransferase MYST2
      Short name=MYST protein 2
    EC=2.3.1.48
Alternative name(s):
    MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2
    Histone acetyltransferase binding to ORC1

Gene names

Name:	MYST2
Synonyms:	HBO1, HBOa

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Histone acetyltransferase which specifically represses AR-mediated transcription. May play a role in DNA replication.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Interacts with MCM2 and ORC1L. Interacts with the androgen receptor (AR) in the presence of dihydrotestosterone.
Subcellular location	Nucleus.
Tissue specificity	Ubiquitously expressed, with highest levels in testis.
Domain	The C2HC-type zinc finger is required for interaction with MCM2 and ORC1L. The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.

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Ontologies

Keywords
Biological process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Chromatin regulator Repressor Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA replication Ref.1 Traceable author statement. Source: ProtInc chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	H3/H4 histone acetyltransferase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.1 Ref.2 Inferred from physical interaction. Source: IntAct transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
AR	P10275	3	EBI-473199,EBI-608057
BARD1	Q99728	1	EBI-473199,EBI-473181
KIAA1377	Q9P2H0	1	EBI-473199,EBI-473176
VIM	P08670	2	EBI-473199,EBI-353844

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 611

611

Histone acetyltransferase MYST2

PRO_0000051569

Regions

Zinc finger

366 – 388

C2HC-type

Compositional bias

10 – 57

Ser-rich

Sites

Active site

474

By similarity

Amino acid modifications

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphothreonine

Modified residue

Phosphoserine

Modified residue

100

Phosphoserine

Modified residue

102

Phosphoserine

Modified residue

124

Phosphoserine

Modified residue

128

Phosphothreonine

Experimental info

Mutagenesis

371

C → A: No interaction with MCM2 and ORC1L

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Sequences

Sequence

Length

Mass (Da)

Tools

O95251-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 8368E7C4F07D8D7C
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FASTA

611

70,642

        10         20         30         40         50         60 
MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR 

        70         80         90        100        110        120 
NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRETKNTAD 

       130        140        150        160        170        180 
HDESPPRTPT GNAPSSESDI DISSPNVSHD ESIAKDMSLK DSGSDLSHRP KRRRFHESYN 

       190        200        210        220        230        240 
FNMKCPTPGC NSLGHLTGKH ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ 

       250        260        270        280        290        300 
DDNNRHATRH QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN 

       310        320        330        340        350        360 
LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW YHSPYPEEYA 

       370        380        390        400        410        420 
RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD GKKNKIYCQN 

       430        440        450        460        470        480 
LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ 

       490        500        510        520        530        540 
YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS 

       550        560        570        580        590        600 
IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP 

       610 
SCLKWTPPKG T

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein." Iizuka M., Stillman B. J. Biol. Chem. 274:23027-23034(1999) [PubMed: 10438470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ORC1L, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Epithelium.
[2]	"Androgen receptor interacts with a novel MYST protein, HBO1." Sharma M., Zarnegar M., Li X., Lim B., Sun Z. J. Biol. Chem. 275:35200-35208(2000) [PubMed: 10930412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR, FUNCTION. Tissue: Prostate.
[3]	"Cloning and identifying histone acetyltransferase HBOa." Jian J., Guangtao L., Guangwei D., Yan Z., Jianhe C., Jiangang Y., Boqin Q. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and function of the human MYST family: MOZ2, MYST1 and MYST2." Borrow J., Housman D.E. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[6]	"Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1." Burke T.W., Cook J.G., Asano M., Nevins J.R. J. Biol. Chem. 276:15397-15408(2001) [PubMed: 11278932] [Abstract] Cited for: INTERACTION WITH MCM2 AND ORC1L, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-371.
[7]	"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 SER-99; SER-100; SER-102; SER-124 AND THR-128, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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-88, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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-50; SER-52; SER-53; SER-56 AND SER-57, MASS SPECTROMETRY.

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Cross-references

Sequence databases
	AF074606 mRNA. Translation: AAC99368.1. AF140360 mRNA. Translation: AAD42348.1. AF217502 mRNA. Translation: AAL56649.1. BC032640 mRNA. Translation: AAH32640.1.
RefSeq	NP_008998.1.
UniGene	Hs.21907
3D structure databases
HSSP	HSSP built from PDB template 1M36 based on UniProtKB Q92794.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95251.
PTM databases
PhosphoSite	O95251.
Genome annotation databases
Ensembl	ENSG00000136504. Homo sapiens. [Contig view]
GeneID	11143.
KEGG	hsa:11143.
Organism-specific databases
H-InvDB	HIX0013964.
HGNC	HGNC:17016. MYST2.
MIM	609880. gene.
PharmGKB	PA134886407.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	O95251.
HOVERGEN	O95251.
Gene expression databases
ArrayExpress	O95251.
CleanEx	HS_MYST2.
GermOnline	ENSG00000136504. Homo sapiens.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. IPR011991. Wing_hlx_DNA_bd. IPR015880. Znf_C2H2-like. IPR002515. Znf_C2HC. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF01853. MOZ_SAS. 1 hit. PF01530. zf-C2HC. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	O95251.
NextBio	42360.
SOURCE	Search...

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Entry information

Entry name

MYST2_HUMAN

Accession

Primary (citable) accession number: O95251

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	May 1, 1999
Last modified:	November 25, 2008
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)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents