Search Results

Overview

Uniprot IDQ9BZ95
Protein NameHistone-lysine N-methyltransferase NSD3
Gene NameNSD3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
159 EIKLKITKTIQNGRE
218 RKSHKIPKLEPEEQN
471 PPVKIAWKTAAARKS
574 GSTGSVEKKQQRRSI
575 STGSVEKKQQRRSIR
596 KSTEVVPKKKIKKEQ
601 VPKKKIKKEQVETVP
613 TVPQATVKTGLQKGA

Function

Histone methyltransferase. Preferentially dimethylates 'Lys-4' and 'Lys-27' of histone H3 forming H3K4me2 and H3K27me2. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression

Protein Sequence

10 MDFSFSFMQG 20 IMGNTIQQPP 30 QLIDSANIRQ 40 EDAFDNNSDI 50 AEDGGQTPYE 60 ATLQQGFQYP 70 ATTEDLPPLT 80 NGYPSSISVY 90 ETQTKYQSYN 100 QYPNGSANGF 110 GAVRNFSPTD 120 YYHSEIPNTR 130 PHEILEKPSP 140 PQPPPPPSVP 150 QTVIPKKTGS 160 PEIKLKITKT 170 IQNGRELFES 180 SLCGDLLNEV 190 QASEHTKSKH 200 ESRKEKRKKS 210 NKHDSSRSEE 220 RKSHKIPKLE 230 PEEQNRPNER 240 VDTVSEKPRE 250 EPVLKEEAPV 260 QPILSSVPTT 270 EVSTGVKFQV 280 GDLVWSKVGT 290 YPWWPCMVSS 300 DPQLEVHTKI 310 NTRGAREYHV 320 QFFSNQPERA 330 WVHEKRVREY 340 KGHKQYEELL 350 AEATKQASNH 360 SEKQKIRKPR 370 PQRERAQWDI 380 GIAHAEKALK 390 MTREERIEQY 400 TFIYIDKQPE 410 EALSQAKKSV 420 ASKTEVKKTR 430 RPRSVLNTQP 440 EQTNAGEVAS 450 SLSSTEIRRH 460 SQRRHTSAEE 470 EEPPPVKIAW 480 KTAAARKSLP 490 ASITMHKGSL 500 DLQKCNMSPV 510 VKIEQVFALQ 520 NATGDGKFID 530 QFVYSTKGIG 540 NKTEISVRGQ 550 DRLIISTPNQ 560 RNEKPTQSVS 570 SPEATSGSTG 580 SVEKKQQRRS 590 IRTRSESEKS 600 TEVVPKKKIK 610 KEQVETVPQA 620 TVKTGLQKGA 630 SEISDSCKPL 640 KKRSRASTDV 650 EMTSSAYRDT 660 SDSDSRGLSD 670 LQVGFGKQVD 680 SPSATADADV 690 SDVQSMDSSL 700 SRRGTGMSKK 710 DTVCQICESS 720 GDSLIPCEGE 730 CCKHFHLECL 740 GLASLPDSKF 750 ICMECKTGQH 760 PCFSCKVSGK 770 DVKRCSVGAC 780 GKFYHEACVR 790 KFPTAIFESK 800 GFRCPQHCCS 810 ACSMEKDIHK 820 ASKGRMMRCL 830 RCPVAYHSGD 840 ACIAAGSMLV 850 SSYILICSNH 860 SKRSSNSSAV 870 NVGFCFVCAR 880 GLIVQDHSDP 890 MFSSYAYKSH 900 YLLNESNRAE 910 LMKLPMIPSS 920 SASKKKCEKG 930 GRLLCCESCP 940 ASFHPECLSI 950 EMPEGCWNCN 960 DCKAGKKLHY 970 KQIVWVKLGN 980 YRWWPAEICN 990 PRSVPLNIQG 1000 LKHDLGDFPV 1010 FFFGSHDYYW 1020 VHQGRVFPYV 1030 EGDKSFAEGQ 1040 TSINKTFKKA 1050 LEEAAKRFQE 1060 LKAQRESKEA 1070 LEIEKNSRKP 1080 PPYKHIKANK 1090 VIGKVQIQVA 1100 DLSEIPRCNC 1110 KPADENPCGL 1120 ESECLNRMLQ 1130 YECHPQVCPA 1140 GDRCQNQCFT 1150 KRLYPDAEII 1160 KTERRGWGLR 1170 TKRSIKKGEF 1180 VNEYVGELID 1190 EEECRLRIKR 1200 AHENSVTNFY 1210 MLTVTKDRII 1220 DAGPKGNYSR 1230 FMNHSCNPNC 1240 ETQKWTVNGD 1250 VRVGLFALCD 1260 IPAGMELTFN 1270 YNLDCLGNGR 1280 TECHCGADNC 1290 SGFLGVRPKS 1300 ACASTNEEKA 1310 KNAKLKQKRR 1320 KIKTEPKQMH 1330 EDYCFQCGDG 1340 GELVMCDKKD 1350 CPKAYHLLCL 1360 NLTQPPYGKW 1370 ECPWHQCDEC 1380 SSAAVSFCEF 1390 CPHSFCKDHE 1400 KGALVPSALE 1410 GRLCCSEHDP 1420 MAPVSPEYWS 1430 KIKCKWESQD HGEEVKE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0140938 histone H3 methyltransferase activity
Molecular Function GO:0140952 histone H3K27 dimethyltransferase activity
Molecular Function GO:0140951 histone H3K27 trimethyltransferase activity
Molecular Function GO:0046975 histone H3K36 methyltransferase activity
Molecular Function GO:0140946 histone H3K4 dimethyltransferase activity
Molecular Function GO:0140537 transcription regulator activator activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0032259 methylation
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0006355 regulation of DNA-templated transcription

Reference

[1] 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.

[2] 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.

[3] 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.