Search Results

Overview

Uniprot IDQ9H2P0
Protein NameActivity-dependent neuroprotector homeobox protein
Gene NameADNP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1016 SKPAAKKKATMQGDR
1027 QGDREQLKWKNSSYG
1029 DREQLKWKNSSYGKV
1035 WKNSSYGKVEGFWSK
1042 KVEGFWSKDQSQWKN
1048 SKDQSQWKNASENDE
144 SSSLSTFKDKNKNDG
146 SLSTFKDKNKNDGLK
203 YIAKAGEKSLNGAVP
21 KARKTVKKILSDIGL
266 NVVVPRSKPLMLIAP
408 SLSSGQLKSPSLSQS
596 VPPKPQPKVQEKADI
600 PQPKVQEKADIPVKS
606 EKADIPVKSSPQAAV
616 PQAAVPYKKDVGKTL
617 QAAVPYKKDVGKTLC
621 PYKKDVGKTLCPLCF
658 QTVHPVEKKLTYKCI
659 TVHPVEKKLTYKCIH
692 VHCRGVGKTQNGQDK
699 KTQNGQDKTNAPSRL
716 SPSLAPVKRTYEQME
728 QMEFPLLKKRKLDDD
729 MEFPLLKKRKLDDDS
731 FPLLKKRKLDDDSDS
807 IASHFSNKRKKCVRD

Function

May be involved in transcriptional regulation. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation. Positively modulates WNT-beta-catenin/CTNN1B signaling, acting by regulating phosphorylation of, and thereby stabilizing, CTNNB1. May be required for neural induction and neuronal differentiation. May be involved in erythroid differentiation (By similarity)

Protein Sequence

10 MFQLPVNNLG 20 SLRKARKTVK 30 KILSDIGLEY 40 CKEHIEDFKQ 50 FEPNDFYLKN 60 TTWEDVGLWD 70 PSLTKNQDYR 80 TKPFCCSACP 90 FSSKFFSAYK 100 SHFRNVHSED 110 FENRILLNCP 120 YCTFNADKKT 130 LETHIKIFHA 140 PNASAPSSSL 150 STFKDKNKND 160 GLKPKQADSV 170 EQAVYYCKKC 180 TYRDPLYEIV 190 RKHIYREHFQ 200 HVAAPYIAKA 210 GEKSLNGAVP 220 LGSNAREESS 230 IHCKRCLFMP 240 KSYEALVQHV 250 IEDHERIGYQ 260 VTAMIGHTNV 270 VVPRSKPLML 280 IAPKPQDKKS 290 MGLPPRIGSL 300 ASGNVRSLPS 310 QQMVNRLSIP 320 KPNLNSTGVN 330 MMSSVHLQQN 340 NYGVKSVGQG 350 YSVGQSMRLG 360 LGGNAPVSIP 370 QQSQSVKQLL 380 PSGNGRSYGL 390 GSEQRSQAPA 400 RYSLQSANAS 410 SLSSGQLKSP 420 SLSQSQASRV 430 LGQSSSKPAA 440 AATGPPPGNT 450 SSTQKWKICT 460 ICNELFPENV 470 YSVHFEKEHK 480 AEKVPAVANY 490 IMKIHNFTSK 500 CLYCNRYLPT 510 DTLLNHMLIH 520 GLSCPYCRST 530 FNDVEKMAAH 540 MRMVHIDEEM 550 GPKTDSTLSF 560 DLTLQQGSHT 570 NIHLLVTTYN 580 LRDAPAESVA 590 YHAQNNPPVP 600 PKPQPKVQEK 610 ADIPVKSSPQ 620 AAVPYKKDVG 630 KTLCPLCFSI 640 LKGPISDALA 650 HHLRERHQVI 660 QTVHPVEKKL 670 TYKCIHCLGV 680 YTSNMTASTI 690 TLHLVHCRGV 700 GKTQNGQDKT 710 NAPSRLNQSP 720 SLAPVKRTYE 730 QMEFPLLKKR 740 KLDDDSDSPS 750 FFEEKPEEPV 760 VLALDPKGHE 770 DDSYEARKSF 780 LTKYFNKQPY 790 PTRREIEKLA 800 ASLWLWKSDI 810 ASHFSNKRKK 820 CVRDCEKYKP 830 GVLLGFNMKE 840 LNKVKHEMDF 850 DAEWLFENHD 860 EKDSRVNASK 870 TADKKLNLGK 880 EDDSSSDSFE 890 NLEEESNESG 900 SPFDPVFEVE 910 PKISNDNPEE 920 HVLKVIPEDA 930 SESEEKLDQK 940 EDGSKYETIH 950 LTEEPTKLMH 960 NASDSEVDQD 970 DVVEWKDGAS 980 PSESGPGSQQ 990 VSDFEDNTCE 1000 MKPGTWSDES 1010 SQSEDARSSK 1020 PAAKKKATMQ 1030 GDREQLKWKN 1040 SSYGKVEGFW 1050 SKDQSQWKNA 1060 SENDERLSNP 1070 QIEWQNSTID 1080 SEDGEQFDNM 1090 TDGVAEPMHG 1100 SLAGVKLSSQ QA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030424 axon
Cellular Component GO:0000785 chromatin
Cellular Component GO:0030425 dendrite
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005634 nucleus
Cellular Component GO:0090575 RNA polymerase II transcription regulator complex
Molecular Function GO:0008013 beta-catenin binding
Molecular Function GO:0048487 beta-tubulin binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0005507 copper ion binding
Molecular Function GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function GO:0042277 peptide binding
Molecular Function GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0046068 cGMP metabolic process
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0044849 estrous cycle
Biological Process GO:0033484 intracellular nitric oxide homeostasis
Biological Process GO:0010629 negative regulation of gene expression
Biological Process GO:0043524 negative regulation of neuron apoptotic process
Biological Process GO:0050805 negative regulation of synaptic transmission
Biological Process GO:0030182 neuron differentiation
Biological Process GO:0045773 positive regulation of axon extension
Biological Process GO:0090263 positive regulation of canonical Wnt signaling pathway
Biological Process GO:0010976 positive regulation of neuron projection development
Biological Process GO:0051965 positive regulation of synapse assembly
Biological Process GO:0010468 regulation of gene expression
Biological Process GO:0080164 regulation of nitric oxide metabolic process
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0009743 response to carbohydrate
Biological Process GO:0007614 short-term memory

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] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] 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.

[9] 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.