Search Results

Overview

Uniprot IDP08758
Protein NameAnnexin A5
Gene NameANXA5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
101 YELKHALKGAGTNEK
108 KGAGTNEKVLTEIIA
29 ETLRKAMKGLGTDEE
290 NIRKEFRKNFATSLY
70 RDLLDDLKSELTGKF
76 LKSELTGKFEKLIVA
79 ELTGKFEKLIVALMK
97 LYDAYELKHALKGAG

Function

This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade

Protein Sequence

10 MAQVLRGTVT 20 DFPGFDERAD 30 AETLRKAMKG 40 LGTDEESILT 50 LLTSRSNAQR 60 QEISAAFKTL 70 FGRDLLDDLK 80 SELTGKFEKL 90 IVALMKPSRL 100 YDAYELKHAL 110 KGAGTNEKVL 120 TEIIASRTPE 130 ELRAIKQVYE 140 EEYGSSLEDD 150 VVGDTSGYYQ 160 RMLVVLLQAN 170 RDPDAGIDEA 180 QVEQDAQALF 190 QAGELKWGTD 200 EEKFITIFGT 210 RSVSHLRKVF 220 DKYMTISGFQ 230 IEETIDRETS 240 GNLEQLLLAV 250 VKSIRSIPAY 260 LAETLYYAMK 270 GAGTDDHTLI 280 RVMVSRSEID 290 LFNIRKEFRK 300 NFATSLYSMI 310 KGDTSGDYKK 320 ALLLLCGEDD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0072563 endothelial microparticle
Cellular Component GO:0009897 external side of plasma membrane
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0016020 membrane
Cellular Component GO:0042383 sarcolemma
Cellular Component GO:0012506 vesicle membrane
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0005544 calcium-dependent phospholipid binding
Molecular Function GO:0001786 phosphatidylserine binding
Molecular Function GO:0004859 phospholipase inhibitor activity
Molecular Function GO:0005543 phospholipid binding
Biological Process GO:0007596 blood coagulation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0050819 negative regulation of coagulation
Biological Process GO:0007165 signal transduction

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[6] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.

[7] 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.