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Overview

Uniprot IDQ12797
Protein NameAspartyl/asparaginyl beta-hydroxylase
Gene NameASPH
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
110 AKVLLGLKERSTSEP
356 EKLRKRGKIEEAVNA
370 AFKELVRKYPQSPRA
475 GDNDNAKKVYEEVLS
545 VGNKEAYKWYELGHK
579 AQPWWTPKETGYTEL
609 LAVMDKAKGLFLPED
646 NACKGAPKTCTLLEK
8 MAQRKNAKSSGNSSS

Function

Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins

Protein Sequence

10 MAQRKNAKSS 20 GNSSSSGSGS 30 GSTSAGSSSP 40 GARRETKHGG 50 HKNGRKGGLS 60 GTSFFTWFMV 70 IALLGVWTSV 80 AVVWFDLVDY 90 EEVLGKLGIY 100 DADGDGDFDV 110 DDAKVLLGLK 120 ERSTSEPAVP 130 PEEAEPHTEP 140 EEQVPVEAEP 150 QNIEDEAKEQ 160 IQSLLHEMVH 170 AEHVEGEDLQ 180 QEDGPTGEPQ 190 QEDDEFLMAT 200 DVDDRFETLE 210 PEVSHEETEH 220 SYHVEETVSQ 230 DCNQDMEEMM 240 SEQENPDSSE 250 PVVEDERLHH 260 DTDDVTYQVY 270 EEQAVYEPLE 280 NEGIEITEVT 290 APPEDNPVED 300 SQVIVEEVSI 310 FPVEEQQEVP 320 PETNRKTDDP 330 EQKAKVKKKK 340 PKLLNKFDKT 350 IKAELDAAEK 360 LRKRGKIEEA 370 VNAFKELVRK 380 YPQSPRARYG 390 KAQCEDDLAE 400 KRRSNEVLRG 410 AIETYQEVAS 420 LPDVPADLLK 430 LSLKRRSDRQ 440 QFLGHMRGSL 450 LTLQRLVQLF 460 PNDTSLKNDL 470 GVGYLLIGDN 480 DNAKKVYEEV 490 LSVTPNDGFA 500 KVHYGFILKA 510 QNKIAESIPY 520 LKEGIESGDP 530 GTDDGRFYFH 540 LGDAMQRVGN 550 KEAYKWYELG 560 HKRGHFASVW 570 QRSLYNVNGL 580 KAQPWWTPKE 590 TGYTELVKSL 600 ERNWKLIRDE 610 GLAVMDKAKG 620 LFLPEDENLR 630 EKGDWSQFTL 640 WQQGRRNENA 650 CKGAPKTCTL 660 LEKFPETTGC 670 RRGQIKYSIM 680 HPGTHVWPHT 690 GPTNCRLRMH 700 LGLVIPKEGC 710 KIRCANETKT 720 WEEGKVLIFD 730 DSFEHEVWQD 740 ASSFRLIFIV 750 DVWHPELTPQ QRRSLPAI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0034704 calcium channel complex
Cellular Component GO:0033018 sarcoplasmic reticulum lumen
Cellular Component GO:0033017 sarcoplasmic reticulum membrane
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0009055 electron transfer activity
Molecular Function GO:0062101 peptidyl-aspartic acid 3-dioxygenase activity
Molecular Function GO:0008307 structural constituent of muscle
Molecular Function GO:0005198 structural molecule activity
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0032237 activation of store-operated calcium channel activity
Biological Process GO:0055074 calcium ion homeostasis
Biological Process GO:0070588 calcium ion transmembrane transport
Biological Process GO:0071277 cellular response to calcium ion
Biological Process GO:0005513 detection of calcium ion
Biological Process GO:0006936 muscle contraction
Biological Process GO:0048015 phosphatidylinositol-mediated signaling
Biological Process GO:0010524 positive regulation of calcium ion transport into cytosol
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0090316 positive regulation of intracellular protein transport
Biological Process GO:0045862 positive regulation of proteolysis
Biological Process GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Biological Process GO:0010649 regulation of cell communication by electrical coupling
Biological Process GO:0051480 regulation of cytosolic calcium ion concentration
Biological Process GO:1901879 regulation of protein depolymerization
Biological Process GO:0031647 regulation of protein stability
Biological Process GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
Biological Process GO:0033198 response to ATP
Cellular Component GO:0032541 cortical endoplasmic reticulum
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0014701 junctional sarcoplasmic reticulum membrane
Cellular Component GO:0005886 plasma membrane

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] 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] 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.

[4] 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.