Search Results

Overview

Uniprot IDP46100
Protein NameChromatin remodeler ATRX
Gene NameATRX
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1030 EEICHFPKGIKQIKN
1182 KKKAVIVKEKKRNSL
1408 RPRTRSAKKAELEEN
1409 PRTRSAKKAELEENQ
153 FRSRSKMKTENLKKR
304 KIKVDSEKSNKVYEH
307 VDSEKSNKVYEHTSR
427 MDAVNKEKNTKEHKV
433 EKNTKEHKVIDAKFE
438 EHKVIDAKFETKARK
463 DISKSEAKLSRKQVD
467 SEAKLSRKQVDSEHM
568 VKLNISSKDNRGGIK
584 KTTAKVTKELYVKLT
623 KSCGLNPKLEKCGLG
690 ETVKEKQKLSVPVRK
715 IDNPKPNKLPKSKQS
720 PNKLPKSKQSETVDQ
768 HKTLYDLKTQAGKDD
799 TKKGKSAKSSIISKK
805 AKSSIISKKKRQTQS
830 KEIKSMSKIGAARTT
911 LRDRLPKKQQASAST
956 LKTKTCKKVQDGLSD
967 GLSDIAEKFLKKDQS

Function

Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as a negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCF within the H19 imprinting control region (ICR) and involved in establishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610)

Protein Sequence

10 MTAEPMSESK 20 LNTLVQKLHD 30 FLAHSSEESE 40 ETSSPPRLAM 50 NQNTDKISGS 60 GSNSDMMENS 70 KEEGTSSSEK 80 SKSSGSSRSK 90 RKPSIVTKYV 100 ESDDEKPLDD 110 ETVNEDASNE 120 NSENDITMQS 130 LPKGTVIVQP 140 EPVLNEDKDD 150 FKGPEFRSRS 160 KMKTENLKKR 170 GEDGLHGIVS 180 CTACGQQVNH 190 FQKDSIYRHP 200 SLQVLICKNC 210 FKYYMSDDIS 220 RDSDGMDEQC 230 RWCAEGGNLI 240 CCDFCHNAFC 250 KKCILRNLGR 260 KELSTIMDEN 270 NQWYCYICHP 280 EPLLDLVTAC 290 NSVFENLEQL 300 LQQNKKKIKV 310 DSEKSNKVYE 320 HTSRFSPKKT 330 SSNCNGEEKK 340 LDDSCSGSVT 350 YSYSALIVPK 360 EMIKKAKKLI 370 ETTANMNSSY 380 VKFLKQATDN 390 SEISSATKLR 400 QLKAFKSVLA 410 DIKKAHLALE 420 EDLNSEFRAM 430 DAVNKEKNTK 440 EHKVIDAKFE 450 TKARKGEKPC 460 ALEKKDISKS 470 EAKLSRKQVD 480 SEHMHQNVPT 490 EEQRTNKSTG 500 GEHKKSDRKE 510 EPQYEPANTS 520 EDLDMDIVSV 530 PSSVPEDIFE 540 NLETAMEVQS 550 SVDHQGDGSS 560 GTEQEVESSS 570 VKLNISSKDN 580 RGGIKSKTTA 590 KVTKELYVKL 600 TPVSLSNSPI 610 KGADCQEVPQ 620 DKDGYKSCGL 630 NPKLEKCGLG 640 QENSDNEHLV 650 ENEVSLLLEE 660 SDLRRSPRVK 670 TTPLRRPTET 680 NPVTSNSDEE 690 CNETVKEKQK 700 LSVPVRKKDK 710 RNSSDSAIDN 720 PKPNKLPKSK 730 QSETVDQNSD 740 SDEMLAILKE 750 VSRMSHSSSS 760 DTDINEIHTN 770 HKTLYDLKTQ 780 AGKDDKGKRK 790 RKSSTSGSDF 800 DTKKGKSAKS 810 SIISKKKRQT 820 QSESSNYDSE 830 LEKEIKSMSK 840 IGAARTTKKR 850 IPNTKDFDSS 860 EDEKHSKKGM 870 DNQGHKNLKT 880 SQEGSSDDAE 890 RKQERETFSS 900 AEGTVDKDTT 910 IMELRDRLPK 920 KQQASASTDG 930 VDKLSGKEES 940 FTSLEVRKVA 950 ETKEKSKHLK 960 TKTCKKVQDG 970 LSDIAEKFLK 980 KDQSDETSED 990 DKKQSKKGTE 1000 EKKKPSDFKK 1010 KVIKMEQQYE 1020 SSSDGTEKLP 1030 EREEICHFPK 1040 GIKQIKNGTT 1050 DGEKKSKKIR 1060 DKTSKKKDEL 1070 SDYAEKSTGK 1080 GDSCDSSEDK 1090 KSKNGAYGRE 1100 KKRCKLLGKS 1110 SRKRQDCSSS 1120 DTEKYSMKED 1130 GCNSSDKRLK 1140 RIELRERRNL 1150 SSKRNTKEIQ 1160 SGSSSSDAEE 1170 SSEDNKKKKQ 1180 RTSSKKKAVI 1190 VKEKKRNSLR 1200 TSTKRKQADI 1210 TSSSSSDIED 1220 DDQNSIGEGS 1230 SDEQKIKPVT 1240 ENLVLSSHTG 1250 FCQSSGDEAL 1260 SKSVPVTVDD 1270 DDDDNDPENR 1280 IAKKMLLEEI 1290 KANLSSDEDG 1300 SSDDEPEEGK 1310 KRTGKQNEEN 1320 PGDEEAKNQV 1330 NSESDSDSEE 1340 SKKPRYRHRL 1350 LRHKLTVSDG 1360 ESGEEKKTKP 1370 KEHKEVKGRN 1380 RRKVSSEDSE 1390 DSDFQESGVS 1400 EEVSESEDEQ 1410 RPRTRSAKKA 1420 ELEENQRSYK 1430 QKKKRRRIKV 1440 QEDSSSENKS 1450 NSEEEEEEKE 1460 EEEEEEEEEE 1470 EEEEDENDDS 1480 KSPGKGRKKI 1490 RKILKDDKLR 1500 TETQNALKEE 1510 EERRKRIAER 1520 EREREKLREV 1530 IEIEDASPTK 1540 CPITTKLVLD 1550 EDEETKEPLV 1560 QVHRNMVIKL 1570 KPHQVDGVQF 1580 MWDCCCESVK 1590 KTKKSPGSGC 1600 ILAHCMGLGK 1610 TLQVVSFLHT 1620 VLLCDKLDFS 1630 TALVVCPLNT 1640 ALNWMNEFEK 1650 WQEGLKDDEK 1660 LEVSELATVK 1670 RPQERSYMLQ 1680 RWQEDGGVMI 1690 IGYEMYRNLA 1700 QGRNVKSRKL 1710 KEIFNKALVD 1720 PGPDFVVCDE 1730 GHILKNEASA 1740 VSKAMNSIRS 1750 RRRIILTGTP 1760 LQNNLIEYHC 1770 MVNFIKENLL 1780 GSIKEFRNRF 1790 INPIQNGQCA 1800 DSTMVDVRVM 1810 KKRAHILYEM 1820 LAGCVQRKDY 1830 TALTKFLPPK 1840 HEYVLAVRMT 1850 SIQCKLYQYY 1860 LDHLTGVGNN 1870 SEGGRGKAGA 1880 KLFQDFQMLS 1890 RIWTHPWCLQ 1900 LDYISKENKG 1910 YFDEDSMDEF 1920 IASDSDETSM 1930 SLSSDDYTKK 1940 KKKGKKGKKD 1950 SSSSGSGSDN 1960 DVEVIKVWNS 1970 RSRGGGEGNV 1980 DETGNNPSVS 1990 LKLEESKATS 2000 SSNPSSPAPD 2010 WYKDFVTDAD 2020 AEVLEHSGKM 2030 VLLFEILRMA 2040 EEIGDKVLVF 2050 SQSLISLDLI 2060 EDFLELASRE 2070 KTEDKDKPLI 2080 YKGEGKWLRN 2090 IDYYRLDGST 2100 TAQSRKKWAE 2110 EFNDETNVRG 2120 RLFIISTKAG 2130 SLGINLVAAN 2140 RVIIFDASWN 2150 PSYDIQSIFR 2160 VYRFGQTKPV 2170 YVYRFLAQGT 2180 MEDKIYDRQV 2190 TKQSLSFRVV 2200 DQQQVERHFT 2210 MNELTELYTF 2220 EPDLLDDPNS 2230 EKKKKRDTPM 2240 LPKDTILAEL 2250 LQIHKEHIVG 2260 YHEHDSLLDH 2270 KEEEELTEEE 2280 RKAAWAEYEA 2290 EKKGLTMRFN 2300 IPTGTNLPPV 2310 SFNSQTPYIP 2320 FNLGALSAMS 2330 NQQLEDLINQ 2340 GREKVVEATN 2350 SVTAVRIQPL 2360 EDIISAVWKE 2370 NMNLSEAQVQ 2380 ALALSRQASQ 2390 ELDVKRREAI 2400 YNDVLTKQQM 2410 LISCVQRILM 2420 NRRLQQQYNQ 2430 QQQQQMTYQQ 2440 ATLGHLMMPK 2450 PPNLIMNPSN 2460 YQQIDMRGMY 2470 QPVAGGMQPP 2480 PLQRAPPPMR 2490 SKNPGPSQGK SM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0099115 chromosome, subtelomeric region
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0000779 condensed chromosome, centromeric region
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0000228 nuclear chromosome
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005721 pericentric heterochromatin
Cellular Component GO:0016605 PML body
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0031490 chromatin DNA binding
Molecular Function GO:0070087 chromo shadow domain binding
Molecular Function GO:0003678 DNA helicase activity
Molecular Function GO:0015616 DNA translocase activity
Molecular Function GO:0042393 histone binding
Molecular Function GO:0062072 histone H3K9me2/3 reader activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0072711 cellular response to hydroxyurea
Biological Process GO:0006325 chromatin organization
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0030330 DNA damage response, signal transduction by p53 class mediator
Biological Process GO:0006281 DNA repair
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:1904908 negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0010571 positive regulation of nuclear cell cycle DNA replication
Biological Process GO:0032206 positive regulation of telomere maintenance
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0070198 protein localization to chromosome, telomeric region
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0031297 replication fork processing
Biological Process GO:0031509 subtelomeric heterochromatin formation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.