Transcriptional regulator ATRX - Mus musculus (Mouse)

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Q61687 (ATRX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcriptional regulator ATRX
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase ATRX
HP1 alpha-interacting protein
HP1-BP38 protein
Heterochromatin protein 2
X-linked nuclear protein

Gene names

Name:	Atrx
Synonyms:	Hp1bp2, Xnp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin.
Catalytic activity	ATP + H₂O = ADP + phosphate.
Subunit structure	Probably binds EZH2. Binds annexin V in a calcium and phosphatidylcholine/phosphatidylserine-dependent manner. Interacts directly with CBX5 via the PxVxL motif By similarity.
Subcellular location	Nucleus. Note: Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with HP1. Ref.4
Domain	Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 ADD domain. Contains 1 GATA-type zinc finger. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW forebrain development Inferred from mutant phenotype PubMed 15668733. Source: MGI
Cellular_component	heterochromatin Inferred from direct assay PubMed 14519686 PubMed 15252119 PubMed 17296936. Source: MGI nuclear chromosome Inferred from direct assay PubMed 11555636. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay PubMed 15522233. Source: MGI helicase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2476

2476

Transcriptional regulator ATRX

PRO_0000074303

Regions

Domain

158 – 295

138

ADD

Domain

1566 – 1753

188

Helicase ATP-binding

Domain

2008 – 2188

181

Helicase C-terminal

Zinc finger

169 – 205

GATA-type; atypical

Zinc finger

216 – 271

PHD-type; atypical

Nucleotide binding

1579 – 1586

ATP Potential

Motif

573 – 586

PxVxL motif

Motif

1704 – 1707

DEGH box

Compositional bias

319 – 322

Poly-Ser

Compositional bias

735 – 738

Poly-Ser

Compositional bias

1001 – 1004

Poly-Glu

Compositional bias

1130 – 1135

Poly-Ser

Compositional bias

1182 – 1185

Poly-Ser

Compositional bias

1238 – 1245

Poly-Asp

Compositional bias

1484 – 1487

Poly-Glu

Compositional bias

1924 – 1931

Poly-Ser

Compositional bias

2205 – 2208

Poly-Lys

Compositional bias

2245 – 2248

Poly-Glu

Compositional bias

2403 – 2408

Poly-Gln

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine Ref.5 Ref.6 Ref.8 Ref.9

Modified residue

111

Phosphoserine By similarity

Modified residue

583

Phosphothreonine By similarity

Modified residue

586

Phosphoserine By similarity

Modified residue

588

Phosphoserine Ref.7

Modified residue

590

Phosphoserine By similarity

Modified residue

626

Phosphoserine Ref.7

Modified residue

663

Phosphoserine By similarity

Modified residue

665

Phosphoserine By similarity

Modified residue

717

Phosphoserine Ref.8

Modified residue

719

Phosphoserine Ref.8

Modified residue

854

Phosphoserine By similarity

Modified residue

855

Phosphoserine By similarity

Modified residue

871

Phosphoserine By similarity

Modified residue

1041

Phosphoserine Ref.8

Modified residue

1290

Phosphoserine Ref.8

Modified residue

1309

Phosphoserine By similarity

Modified residue

1311

Phosphoserine By similarity

Modified residue

1313

Phosphoserine By similarity

Modified residue

1335

Phosphoserine Ref.8

Modified residue

1339

Phosphoserine Ref.7 Ref.8

Modified residue

1512

Phosphoserine Ref.7

Modified residue

1975

Phosphoserine By similarity

Modified residue

1979

Phosphoserine By similarity

Modified residue

2203

Phosphoserine By similarity

Experimental info

Sequence conflict

157

K → I in AAC08741. Ref.1

Sequence conflict

1953

V → M in AAC08741. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q61687 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: B2E2218B6CC791EC
Show »

FASTA

2,476

278,587

        10         20         30         40         50         60 
MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS GLNSDMMENN 

        70         80         90        100        110        120 
KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE NVNEKAATEN SENDITMQSL 

       130        140        150        160        170        180 
PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKADNLKKRG EDGLHGIVSC TACGQQVNHF 

       190        200        210        220        230        240 
QKDSIYRHPS LKVLICKNCF KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK 

       250        260        270        280        290        300 
KCILRNLGRK ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD 

       310        320        330        340        350        360 
SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP KEMIKKTTKL 

       370        380        390        400        410        420 
IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL DDIKKAHLAL EEDLNSEIQA 

       430        440        450        460        470        480 
LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS YSTEKREFLK LDARSSVKAI DGEEQRAHKS 

       490        500        510        520        530        540 
TSGEHKGSGR KDGSQYEPTN TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG 

       550        560        570        580        590        600 
NSGTEPELES SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV 

       610        620        630        640        650        660 
SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT PLRRQTESNP 

       670        680        690        700        710        720 
AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK PHKVPKAKQP VIGDQNSDSD 

       730        740        750        760        770        780 
EMLAVLKEAS QMGHSSSSDT DINEPQMNHK GKTGKDDNGK RKRKNSTSGS DFDTKKGKST 

       790        800        810        820        830        840 
ETSIISKKKR QNYSESSNYD SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD 

       850        860        870        880        890        900 
NGGHERAKTT QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA 

       910        920        930        940        950        960 
EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK EQSDESSEGE 

       970        980        990       1000       1010       1020 
KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP EEEEIGPFSK GIKQSKTDTA 

      1030       1040       1050       1060       1070       1080 
GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS 

      1090       1100       1110       1120       1130       1140 
PGKRPECSSS DTEKSLKGQC CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS 

      1150       1160       1170       1180       1190       1200 
SEDNKKQKKQ RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS 

      1210       1220       1230       1240       1250       1260 
DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI AKKMLLEEIK 

      1270       1280       1290       1300       1310       1320 
ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE QLAVNQVNSE SDSDSEESKK 

      1330       1340       1350       1360       1370       1380 
PRYRHRLLRH KLTLSDGESG EEKPTKPKEH KEAKGRNRRK VSSEDSEDTD FQESGVSEEV 

      1390       1400       1410       1420       1430       1440 
SESEDEQRPR TRSAKKAELE ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED 

      1450       1460       1470       1480       1490       1500 
EEDEDEDEED ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE 

      1510       1520       1530       1540       1550       1560 
KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV DGVQFMWDCC 

      1570       1580       1590       1600       1610       1620 
CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD KLDFSTALVV CPLNTALNWM 

      1630       1640       1650       1660       1670       1680 
NEFEKWQEGL NDNEKLEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV 

      1690       1700       1710       1720       1730       1740 
KSRKLKDIFN KALVDPGPDF VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL 

      1750       1760       1770       1780       1790       1800 
IEYHCMVNFI KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV 

      1810       1820       1830       1840       1850       1860 
QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR GKAGAKLFQD 

      1870       1880       1890       1900       1910       1920 
FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS DETSKSLSSD EKKKPKGKKG 

      1930       1940       1950       1960       1970       1980 
KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD GNVDDTGNNP SVSLKLDESK TTSTSNPSSP 

      1990       2000       2010       2020       2030       2040 
APDWYKDFVT DTDAEVLEHS GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA 

      2050       2060       2070       2080       2090       2100 
SREKTEDKEK PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST 

      2110       2120       2130       2140       2150       2160 
KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA QGTMEDKIYD 

      2170       2180       2190       2200       2210       2220 
RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD PNSEKKKKRD TPMLPKDTIL 

      2230       2240       2250       2260       2270       2280 
AELLQIHKEH IVGYHEHDSL LDHKEEEELT EEERKAAWAE YEAEKKGLTM RFNIPTGTNL 

      2290       2300       2310       2320       2330       2340 
PPVTFTSQTP YIPFNLGALS AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV 

      2350       2360       2370       2380       2390       2400 
WKENMNLSEA QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ 

      2410       2420       2430       2440       2450       2460 
YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM QPPPLQRAPP 

      2470 
PTVRSKNPGP SPGKSM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the human and murine ATRX gene identifies highly conserved, functionally important domains." Picketts D.J., Tastan A.O., Higgs D.R., Gibbons R.J. Mamm. Genome 9:400-403(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors." le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P. EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-1176.
[4]	"Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes." McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M., Bickmore W.A., Pombo A., Turley H., Gatter K., Picketts D.J., Buckle V.J., Chapman L., Rhodes D., Higgs D.R. Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
[5]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-626; SER-1339 AND SER-1512, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-717; SER-719; SER-1041; SER-1290; SER-1335 AND SER-1339, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF026032 mRNA. Translation: AAC08741.1. AL671893, AL670660 Genomic DNA. Translation: CAM16251.1. AL670660, AL671893 Genomic DNA. Translation: CAM19070.1. X99643 mRNA. Translation: CAA67962.1.
IPI	IPI00322707.
RefSeq	NP_033556.2. NM_009530.2.
UniGene	Mm.10141.
3D structure databases
ProteinModelPortal	Q61687.
SMR	Q61687. Positions 158-295.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61687. 1 interaction.
PTM databases
PhosphoSite	Q61687.
Proteomic databases
PaxDb	Q61687.
PRIDE	Q61687.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
GeneID	22589.
KEGG	mmu:22589.
Organism-specific databases
CTD	546.
MGI	MGI:103067. Atrx.
Phylogenomic databases
eggNOG	COG0553.
GeneTree	ENSGT00550000074619.
HOGENOM	HOG000231302.
HOVERGEN	HBG000104.
InParanoid	A2ADH4.
KO	K10779.
OrthoDB	EOG4PVNXQ.
Gene expression databases
ArrayExpress	Q61687.
Bgee	Q61687.
Genevestigator	Q61687.
GermOnline	ENSMUSG00000031229. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR025766. ADD. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. IPR011011. Znf_FYVE_PHD. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS51533. ADD. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302925.
SOURCE	Search...

Entry information

Entry name

ATRX_MOUSE

Accession

Primary (citable) accession number: Q61687
Secondary accession number(s): A2ADH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents