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UniProtKB/Swiss-Prot entry O95251


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MYST2_HUMAN
Primary accession number O95251
Secondary accession numbers None
Integrated into Swiss-Prot on July 5, 2005
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 68)
Name and origin of the protein
Protein name Histone acetyltransferase MYST2
Synonyms MYST protein 2
EC 2.3.1.48
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2
Histone acetyltransferase binding to ORC1
Gene name
Name: MYST2
Synonyms: HBO1, HBOa
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ORC1L, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Epithelium;
DOI=10.1074/jbc.274.33.23027; PubMed=10438470 [NCBI, ExPASy, EBI, Israel, Japan]
Iizuka M., Stillman B.;
"Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein.";
J. Biol. Chem. 274:23027-23034(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR, AND FUNCTION.
TISSUE=Prostate;
DOI=10.1074/jbc.M004838200; PubMed=10930412 [NCBI, ExPASy, EBI, Israel, Japan]
Sharma M., Zarnegar M., Li X., Lim B., Sun Z.;
"Androgen receptor interacts with a novel MYST protein, HBO1.";
J. Biol. Chem. 275:35200-35208(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Jian J., Guangtao L., Guangwei D., Yan Z., Jianhe C., Jiangang Y., Boqin Q.;
"Cloning and identifying histone acetyltransferase HBOa.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Borrow J., Housman D.E.;
"Structure and function of the human MYST family: MOZ2, MYST1 and MYST2.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH MCM2 AND ORC1L, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF CYS-371.
DOI=10.1074/jbc.M011556200; PubMed=11278932 [NCBI, ExPASy, EBI, Israel, Japan]
Burke T.W., Cook J.G., Asano M., Nevins J.R.;
"Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1.";
J. Biol. Chem. 276:15397-15408(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-100; SER-102; SER-124 AND THR-128, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-52; SER-53; SER-56 AND SER-57, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF074606; AAC99368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF140360; AAD42348.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF217502; AAL56649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032640; AAH32640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_008998.1; -.
UniGene Hs.21907
3D structure databases
HSSP Q92794; 1M36. [HSSP ENTRY / PDB]
ModBase O95251.
Protein-protein interaction databases
IntAct O95251; -.
PTM databases
PhosphoSite O95251; -.
Organism-specific databases
H-InvDB HIX0013964; -.
HGNC HGNC:17016; MYST2.
GenAtlas MYST2.
MIM 609880; gene. [NCBI / EBI]
PharmGKB PA134886407; -.
GeneCards O95251.
Gene expression databases
ArrayExpress O95251; -.
CleanEx HS_MYST2; -.
GermOnline ENSG00000136504; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0004406; Molecular function: H3/H4 histone acetyltransferase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003700; Molecular function: transcription factor activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0016568; Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006260; Biological process: DNA replication (traceable author statement from ProtInc).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (traceable author statement from ProtInc).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF01853; MOZ_SAS; 1.
PF01530; zf-C2HC; 1.
Pfam graphical view of domain structure.
SMART SM00355; ZnF_C2H2; 1.
SMART graphical view of domain structure.
ProtoNet O95251.
Genome annotation databases
Ensembl ENSG00000136504; Homo sapiens. [Contig view]
GeneID 11143; -.
KEGG hsa:11143; -.
Phylogenomic databases
HOGENOM O95251; -.
HOVERGEN O95251; -.
Other
LinkHub O95251; -.
NextBio 42360; -.
SOURCE MYST2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Chromatin regulator; DNA replication; Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   611  611     Histone acetyltransferase MYST2. PRO_0000051569
ZN_FING   366   388  23     C2HC-type. 
COMPBIAS   10    57  48     Ser-rich. 
ACT_SITE   474   474        By similarity. 
MOD_RES   50    50        Phosphoserine. 
MOD_RES   52    52        Phosphoserine. 
MOD_RES   53    53        Phosphoserine. 
MOD_RES   56    56        Phosphoserine. 
MOD_RES   57    57        Phosphoserine. 
MOD_RES   88    88        Phosphothreonine. 
MOD_RES   99    99        Phosphoserine. 
MOD_RES   100   100        Phosphoserine. 
MOD_RES   102   102        Phosphoserine. 
MOD_RES   124   124        Phosphoserine. 
MOD_RES   128   128        Phosphothreonine. 
MUTAGEN   371   371        C->A: No interaction with MCM2 and ORC1L. 
Sequence information
Length: 611 AA [This is the length of the unprocessed precursor] Molecular weight: 70642 Da [This is the MW of the unprocessed precursor] CRC64: 8368E7C4F07D8D7C [This is a checksum on the sequence]
        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 

O95251 in FASTA format

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