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Overview

Uniprot IDQ9Y4E5
Protein NameE3 SUMO-protein ligase ZNF451
Gene NameZNF451
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
446 LECIAIPKKKMNLKD
832 SEKSNLYKFTASASH
845 SHTERKLKQAINYSK

Function

E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483)

Protein Sequence

10 MGDPGSEIIE 20 SVPPAGPEAS 30 ESTTDENEDD 40 IQFVSEGPLR 50 PVLEYIDLVS 60 SDDEEPSTSY 70 TDENIKRKDH 80 IDYQKDKVAL 90 TLARLARHVE 100 VEKQQKEEKN 110 RAFREKIDFQ 120 HAHGLQELEF 130 IRGHSDTEAA 140 RLCVDQWLKM 150 PGLKTGTINC 160 GTKSSFRRGG 170 HTWVSGKPIL 180 CPIMHCNKEF 190 DNGHLLLGHL 200 KRFDHSPCDP 210 TITLHGPFFS 220 SFACVVCYKK 230 FVTQQQYRDH 240 LFDKEATDDG 250 HNNNLLPQII 260 QCFACPNCFL 270 LFSRKEECSK 280 HMSGKNHFHQ 290 SFKLGDNKGI 300 AHPISFPSFA 310 KKLLISLCKD 320 VPFQVKCVAC 330 HKTLRSHMEL 340 TAHFRVHCRN 350 AGPVAVAEKS 360 ITQVAEKFIL 370 RGYCPDCNQV 380 FVDETSTQNH 390 KQNSGHKVRV 400 INSVEESVLL 410 YCHSSEGNKD 420 PSSDLHLLLD 430 QSKFSSLKRT 440 MSIKESSSLE 450 CIAIPKKKMN 460 LKDKSHEGVA 470 CVQKEKSVVK 480 TWFCECNQRF 490 PSEDAVEKHV 500 FSANTMGYKC 510 VVCGKVCDDS 520 GVIRLHMSRI 530 HGGAHLNNFL 540 FWCRTCKKEL 550 TRKDTIMAHV 560 TEFHNGHRYF 570 YEMDEVEGET 580 LPSSSTTLDN 590 LTANKPSSAI 600 TVIDHSPANS 610 SPRGKWQCRI 620 CEDMFDSQEY 630 VKQHCMSLAS 640 HKFHRYSCAH 650 CRKPFHKIET 660 LYRHCQDEHD 670 NEIKIKYFCG 680 LCDLIFNVEE 690 AFLSHYEEHH 700 SIDYVFVSEK 710 TETSIKTEDD 720 FPVIETSNQL 730 TCGCRESYIC 740 KVNRKEDYSR 750 CLQIMLDKGK 760 LWFRCSLCSA 770 TAQNLTDMNT 780 HIHQVHKEKS 790 DEEEQQYVIK 800 CGTCTKAFHD 810 PESAQQHFHR 820 KHCFLQKPSV 830 AHFGSEKSNL 840 YKFTASASHT 850 ERKLKQAINY 860 SKSLDMEKGV 870 ENDLSYQNIE 880 EEIVELPDLD 890 YLRTMTHIVF 900 VDFDNWSNFF 910 GHLPGHLNQG 920 TFIWGFQGGN 930 TNWKPPLNCK 940 IYNYLNRIGC 950 FFLHPRCSKR 960 KDAADFAICM 970 HAGRLDEQLP 980 KQIPFTILSG 990 DQGFLELENQ 1000 FKKTQRPAHI 1010 LNPHHLEGDM 1020 MCALLNSISD 1030 TTKECDSDDN 1040 MGAKNTSIGE 1050 EFISTEDVEL 1060 EEAIRRSLEE M

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016605 PML body
Molecular Function GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function GO:0043565 sequence-specific DNA binding
Molecular Function GO:0061665 SUMO ligase activity
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0140416 transcription regulator inhibitor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0060633 negative regulation of transcription initiation by RNA polymerase II
Biological Process GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
Biological Process GO:0016925 protein sumoylation

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] 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.