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ATRX_MOUSE
ID   ATRX_MOUSE              Reviewed;        2476 AA.
AC   Q61687; A2ADH4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Transcriptional regulator ATRX;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase ATRX;
DE   AltName: Full=HP1 alpha-interacting protein;
DE   AltName: Full=HP1-BP38 protein;
DE   AltName: Full=Heterochromatin protein 2;
DE   AltName: Full=X-linked nuclear protein;
GN   Name=Atrx; Synonyms=Hp1bp2, Xnp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9545503; DOI=10.1007/s003359900781;
RA   Picketts D.J., Tastan A.O., Higgs D.R., Gibbons R.J.;
RT   "Comparison of the human and murine ATRX gene identifies highly conserved,
RT   functionally important domains.";
RL   Mamm. Genome 9:400-403(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 325-1176.
RX   PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA   Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [4]
RP   SUBCELLULAR LOCATION, AND ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
RX   PubMed=10570185; DOI=10.1073/pnas.96.24.13983;
RA   McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M., Bickmore W.A.,
RA   Pombo A., Turley H., Gatter K., Picketts D.J., Buckle V.J., Chapman L.,
RA   Rhodes D., Higgs D.R.;
RT   "Localization of a putative transcriptional regulator (ATRX) at
RT   pericentromeric heterochromatin and the short arms of acrocentric
RT   chromosomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89; SER-717; SER-801 AND
RP   SER-1339, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   INTERACTION WITH MECP2.
RX   PubMed=17296936; DOI=10.1073/pnas.0608056104;
RA   Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X.,
RA   Kriaucionis S., Bird A.;
RT   "Interaction between chromatin proteins MECP2 and ATRX is disrupted by
RT   mutations that cause inherited mental retardation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89; SER-92; SER-212; SER-315;
RP   SER-626; SER-663; SER-665; SER-717; SER-766; SER-801; SER-854; SER-855;
RP   SER-1223; SER-1224; SER-1232; SER-1339; SER-1891; SER-1898; SER-1975 AND
RP   SER-1979, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21029860; DOI=10.1016/j.cell.2010.09.023;
RA   Law M.J., Lower K.M., Voon H.P., Hughes J.R., Garrick D., Viprakasit V.,
RA   Mitson M., De Gobbi M., Marra M., Morris A., Abbott A., Wilder S.P.,
RA   Taylor S., Santos G.M., Cross J., Ayyub H., Jones S., Ragoussis J.,
RA   Rhodes D., Dunham I., Higgs D.R., Gibbons R.J.;
RT   "ATR-X syndrome protein targets tandem repeats and influences allele-
RT   specific expression in a size-dependent manner.";
RL   Cell 143:367-378(2010).
RN   [11]
RP   FUNCTION, AND ASSOCIATION WITH HISTONE H3.3.
RX   PubMed=20211137; DOI=10.1016/j.cell.2010.01.003;
RA   Goldberg A.D., Banaszynski L.A., Noh K.M., Lewis P.W., Elsaesser S.J.,
RA   Stadler S., Dewell S., Law M., Guo X., Li X., Wen D., Chapgier A.,
RA   DeKelver R.C., Miller J.C., Lee Y.L., Boydston E.A., Holmes M.C.,
RA   Gregory P.D., Greally J.M., Rafii S., Yang C., Scambler P.J., Garrick D.,
RA   Gibbons R.J., Higgs D.R., Cristea I.M., Urnov F.D., Zheng D., Allis C.D.;
RT   "Distinct factors control histone variant H3.3 localization at specific
RT   genomic regions.";
RL   Cell 140:678-691(2010).
RN   [12]
RP   ASSOCIATION WITH HISTONE H3.3.
RX   PubMed=20504901; DOI=10.1101/gad.566910;
RA   Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
RT   "The death-associated protein DAXX is a novel histone chaperone involved in
RT   the replication-independent deposition of H3.3.";
RL   Genes Dev. 24:1253-1265(2010).
RN   [13]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-239 AND VAL-580.
RX   PubMed=21666677; DOI=10.1038/nsmb.2070;
RA   Eustermann S., Yang J.C., Law M.J., Amos R., Chapman L.M., Jelinska C.,
RA   Garrick D., Clynes D., Gibbons R.J., Rhodes D., Higgs D.R., Neuhaus D.;
RT   "Combinatorial readout of histone H3 modifications specifies localization
RT   of ATRX to heterochromatin.";
RL   Nat. Struct. Mol. Biol. 18:777-782(2011).
RN   [14]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2457 AND ARG-2464, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [15]
RP   CITRULLINATION AT ARG-1063.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
RN   [16]
RP   INTERACTION WITH MECP2; SMC1 AND SMC3.
RX   PubMed=20159591; DOI=10.1016/j.devcel.2009.12.017;
RA   Kernohan K.D., Jiang Y., Tremblay D.C., Bonvissuto A.C., Eubanks J.H.,
RA   Mann M.R., Berube N.G.;
RT   "ATRX partners with cohesin and MeCP2 and contributes to developmental
RT   silencing of imprinted genes in the brain.";
RL   Dev. Cell 18:191-202(2010).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H3.3.
RX   PubMed=20110566; DOI=10.1101/gr.101477.109;
RA   Wong L.H., McGhie J.D., Sim M., Anderson M.A., Ahn S., Hannan R.D.,
RA   George A.J., Morgan K.A., Mann J.R., Choo K.H.;
RT   "ATRX interacts with H3.3 in maintaining telomere structural integrity in
RT   pluripotent embryonic stem cells.";
RL   Genome Res. 20:351-360(2010).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH RAD50; MRE11 AND NBN.
RX   PubMed=24651726; DOI=10.1371/journal.pone.0092915;
RA   Clynes D., Jelinska C., Xella B., Ayyub H., Taylor S., Mitson M.,
RA   Bachrati C.Z., Higgs D.R., Gibbons R.J.;
RT   "ATRX dysfunction induces replication defects in primary mouse cells.";
RL   PLoS ONE 9:E92915-E92915(2014).
CC   -!- FUNCTION: Involved in transcriptional regulation and chromatin
CC       remodeling. Facilitates DNA replication in multiple cellular
CC       environments and is required for efficient replication of a subset of
CC       genomic loci. Binds to DNA tandem repeat sequences in both telomeres
CC       and euchromatin and in vitro binds DNA quadruplex structures. May help
CC       stabilizing G-rich regions into regular chromatin structures by
CC       remodeling G4 DNA and incorporating H3.3-containing nucleosomes.
CC       Catalytic component of the chromatin remodeling complex ATRX:DAXX which
CC       has ATP-dependent DNA translocase activity and catalyzes the
CC       replication-independent deposition of histone H3.3 in pericentric DNA
CC       repeats outside S-phase and telomeres, and the in vitro remodeling of
CC       H3.3-containing nucleosomes. Its heterochromatin targeting is proposed
CC       to involve a combinatorial readout of histone H3 modifications
CC       (specifically methylation states of H3K9 and H3K4) and association with
CC       CBX5. Involved in maintaining telomere structural integrity in
CC       embryonic stem cells probably implying recruitment of CBX5 to
CC       telomeres. Reports on the involvement in transcriptional regulation of
CC       telomeric repeat-containing RNA (TERRA) are conflicting; according
CC       (PubMed:20211137) is required for its transcriptional repression in
CC       embryonic stem cells. Acts as negative regulator of chromatin
CC       incorporation of transcriptionally repressive histone MACROH2A1,
CC       particularily at telomeres. Participates in the allele-specific gene
CC       expression at the imprinted IGF2/H19 gene locus. On the maternal
CC       allele, required for the chromatin occupancy of SMC1 and CTCTF within
CC       the H19 imprinting control region (ICR) and involved in esatblishment
CC       of histone tails modifications in the ICR. Binds to zinc-finger coding
CC       genes with atypical chromatin signatures and regulates its H3K9me3
CC       levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate
CC       the deposition and maintenance of H3K9me3 at the 3' exons of zinc-
CC       finger genes (By similarity). {ECO:0000250|UniProtKB:P46100,
CC       ECO:0000269|PubMed:20110566, ECO:0000269|PubMed:20211137,
CC       ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:24651726}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with DAXX to form the chromatin remodeling complex
CC       ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and
CC       phosphatidylcholine/phosphatidylserine-dependent manner. Interacts
CC       directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and
CC       NBN; indicative for an association with the MRN complex. Interacts with
CC       histone MACROH2A1. Interacts with histone H3 peptides methylated at
CC       'Lys-10' with preferences H3K9me3 > H3K9me2 > H3K9me1. Interacts with
CC       histone H3 peptides unmethylated at 'Lys-5' (H3K4me0). Interacts with
CC       MECP2, SMC1 and SMC3. Interacts with SETDB1, TRIM28 and ZNF274 (By
CC       similarity). {ECO:0000250|UniProtKB:P46100,
CC       ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:20110566,
CC       ECO:0000269|PubMed:20159591, ECO:0000269|PubMed:24651726}.
CC   -!- INTERACTION:
CC       Q61687; Q9Z2D6: Mecp2; NbExp=5; IntAct=EBI-2657527, EBI-1188816;
CC       Q61687; Q9CU62: Smc1a; NbExp=4; IntAct=EBI-2657527, EBI-2550016;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body
CC       {ECO:0000250}. Note=Associated with pericentromeric heterochromatin
CC       during interphase and mitosis, probably by interacting with CBX5/HP1
CC       alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-
CC       nuclear bodies (By similarity). In embryonic stem cells localized to
CC       telomeres; localization is reduced after 12 d of induction of cell
CC       differentiation. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at
CC       the maternal H19 ICR and the Gtl2/Dlk1 imprinted cluster in the brain.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The ADD domain predominantly interacts with histone H3
CC       trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono- or
CC       dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated
CC       at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the
CC       presence of H3K4me3 suggesting a readout of the combined histone H3
CC       methylation state (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC       required for interaction with chromoshadow domains. This motif requires
CC       additional residues -7, -6, +4 and +5 of the central Val which contact
CC       the chromoshadow domain.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; AF026032; AAC08741.1; -; mRNA.
DR   EMBL; AL670660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X99643; CAA67962.1; -; mRNA.
DR   CCDS; CCDS41095.1; -.
DR   RefSeq; NP_033556.2; NM_009530.2.
DR   AlphaFoldDB; Q61687; -.
DR   BMRB; Q61687; -.
DR   SMR; Q61687; -.
DR   BioGRID; 204603; 37.
DR   DIP; DIP-55974N; -.
DR   IntAct; Q61687; 32.
DR   MINT; Q61687; -.
DR   STRING; 10090.ENSMUSP00000109203; -.
DR   iPTMnet; Q61687; -.
DR   PhosphoSitePlus; Q61687; -.
DR   SwissPalm; Q61687; -.
DR   EPD; Q61687; -.
DR   jPOST; Q61687; -.
DR   MaxQB; Q61687; -.
DR   PaxDb; Q61687; -.
DR   PeptideAtlas; Q61687; -.
DR   PRIDE; Q61687; -.
DR   ProteomicsDB; 265183; -.
DR   Antibodypedia; 460; 417 antibodies from 36 providers.
DR   DNASU; 22589; -.
DR   Ensembl; ENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
DR   GeneID; 22589; -.
DR   KEGG; mmu:22589; -.
DR   UCSC; uc009ubb.2; mouse.
DR   CTD; 546; -.
DR   MGI; MGI:103067; Atrx.
DR   VEuPathDB; HostDB:ENSMUSG00000031229; -.
DR   eggNOG; KOG1015; Eukaryota.
DR   GeneTree; ENSGT00940000155902; -.
DR   HOGENOM; CLU_000863_1_0_1; -.
DR   InParanoid; Q61687; -.
DR   OMA; QEMGGVM; -.
DR   OrthoDB; 815681at2759; -.
DR   PhylomeDB; Q61687; -.
DR   TreeFam; TF313172; -.
DR   Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR   BioGRID-ORCS; 22589; 9 hits in 117 CRISPR screens.
DR   ChiTaRS; Atrx; mouse.
DR   PRO; PR:Q61687; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q61687; protein.
DR   Bgee; ENSMUSG00000031229; Expressed in metanephric cortical collecting duct and 249 other tissues.
DR   ExpressionAtlas; Q61687; baseline and differential.
DR   Genevisible; Q61687; MM.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; ISO:MGI.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR   GO; GO:0016605; C:PML body; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015616; F:DNA translocase activity; ISO:MGI.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR   GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISS:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; ISO:MGI.
DR   GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; IMP:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IMP:UniProtKB.
DR   GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:UniProtKB.
DR   GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0035128; P:post-embryonic forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
DR   GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR   GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR   GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR025766; ADD.
DR   InterPro; IPR041430; ADD_ATRX.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17981; ADD_ATRX; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51533; ADD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromatin regulator; Chromosome; Citrullination; DNA damage;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW   Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Telomere; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..2476
FT                   /note="Transcriptional regulator ATRX"
FT                   /id="PRO_0000074303"
FT   DOMAIN          158..295
FT                   /note="ADD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   DOMAIN          1566..1753
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          2008..2188
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         169..205
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   ZN_FING         216..271
FT                   /note="PHD-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   REGION          24..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1169..1313
FT                   /note="Interaction with DAXX"
FT                   /evidence="ECO:0000250"
FT   REGION          1898..1982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1993..2263
FT                   /note="Interaction with MECP2"
FT                   /evidence="ECO:0000250"
FT   REGION          2445..2476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           573..586
FT                   /note="PxVxL motif"
FT   MOTIF           1704..1707
FT                   /note="DEGH box"
FT   COMPBIAS        32..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..852
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..921
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..1009
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1079
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1098..1124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1171
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1381..1406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1415..1433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1453
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1898..1925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1952..1981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2453..2467
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1579..1586
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         89
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         583
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         586
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         663
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         717
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         719
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         766
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         801
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         828
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         829
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         941
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         953
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         991
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         992
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         993
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         1041
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1063
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         1223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1313
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1514
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1891
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1898
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1975
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1979
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         2457
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         2464
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   CROSSLNK        10
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        137
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        439
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        984
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1473
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1965
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1965
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1970
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MUTAGEN         239
FT                   /note="C->G: Reduces pericentromeric localization.
FT                   Abolishes pericentromeric localization; when associated
FT                   with E-580."
FT                   /evidence="ECO:0000269|PubMed:21666677"
FT   MUTAGEN         580
FT                   /note="V->E: Reduces pericentromeric localization.
FT                   Abolishes pericentromeric localization; when associated
FT                   with G-239."
FT                   /evidence="ECO:0000269|PubMed:21666677"
FT   CONFLICT        157
FT                   /note="K -> I (in Ref. 1; AAC08741)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1953
FT                   /note="V -> M (in Ref. 1; AAC08741)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2476 AA;  278587 MW;  B2E2218B6CC791EC CRC64;
     MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS GLNSDMMENN
     KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE NVNEKAATEN SENDITMQSL
     PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKADNLKKRG EDGLHGIVSC TACGQQVNHF
     QKDSIYRHPS LKVLICKNCF KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK
     KCILRNLGRK ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD
     SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP KEMIKKTTKL
     IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL DDIKKAHLAL EEDLNSEIQA
     LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS YSTEKREFLK LDARSSVKAI DGEEQRAHKS
     TSGEHKGSGR KDGSQYEPTN TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG
     NSGTEPELES SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV
     SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT PLRRQTESNP
     AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK PHKVPKAKQP VIGDQNSDSD
     EMLAVLKEAS QMGHSSSSDT DINEPQMNHK GKTGKDDNGK RKRKNSTSGS DFDTKKGKST
     ETSIISKKKR QNYSESSNYD SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD
     NGGHERAKTT QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA
     EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK EQSDESSEGE
     KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP EEEEIGPFSK GIKQSKTDTA
     GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS
     PGKRPECSSS DTEKSLKGQC CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS
     SEDNKKQKKQ RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS
     DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI AKKMLLEEIK
     ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE QLAVNQVNSE SDSDSEESKK
     PRYRHRLLRH KLTLSDGESG EEKPTKPKEH KEAKGRNRRK VSSEDSEDTD FQESGVSEEV
     SESEDEQRPR TRSAKKAELE ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED
     EEDEDEDEED ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE
     KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV DGVQFMWDCC
     CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD KLDFSTALVV CPLNTALNWM
     NEFEKWQEGL NDNEKLEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV
     KSRKLKDIFN KALVDPGPDF VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL
     IEYHCMVNFI KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV
     QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR GKAGAKLFQD
     FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS DETSKSLSSD EKKKPKGKKG
     KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD GNVDDTGNNP SVSLKLDESK TTSTSNPSSP
     APDWYKDFVT DTDAEVLEHS GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA
     SREKTEDKEK PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST
     KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA QGTMEDKIYD
     RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD PNSEKKKKRD TPMLPKDTIL
     AELLQIHKEH IVGYHEHDSL LDHKEEEELT EEERKAAWAE YEAEKKGLTM RFNIPTGTNL
     PPVTFTSQTP YIPFNLGALS AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV
     WKENMNLSEA QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ
     YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM QPPPLQRAPP
     PTVRSKNPGP SPGKSM
 
 
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