Search Results

Overview

Uniprot IDP07355
Protein NameAnnexin A2
Gene NameANXA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 TVHEILCKLSLEGDH
104 TVILGLLKTPAQYDA
115 QYDASELKASMKGLG
119 SELKASMKGLGTDED
148 QEINRVYKEMYKTDL
152 RVYKEMYKTDLEKDI
157 MYKTDLEKDIISDTS
169 DTSGDFRKLMVALAK
176 KLMVALAKGRRAEDG
204 DLYDAGVKRKGTDVP
227 RSVPHLQKVFDRYKS
233 QKVFDRYKSYSPYDM
279 DRLYDSMKGKGTRDK
28 PSAYGSVKAYTNFDA
281 LYDSMKGKGTRDKVL
302 RSEVDMLKIRSEFKR
310 IRSEFKRKYGKSLYY
313 EFKRKYGKSLYYYIQ
324 YYIQQDTKGDYQKAL
47 LNIETAIKTKGVDEV
49 IETAIKTKGVDEVTI
81 AYQRRTKKELASALK

Function

Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic surveillance and neoangiogenesis (By similarity)

Protein Sequence

10 MSTVHEILCK 20 LSLEGDHSTP 30 PSAYGSVKAY 40 TNFDAERDAL 50 NIETAIKTKG 60 VDEVTIVNIL 70 TNRSNAQRQD 80 IAFAYQRRTK 90 KELASALKSA 100 LSGHLETVIL 110 GLLKTPAQYD 120 ASELKASMKG 130 LGTDEDSLIE 140 IICSRTNQEL 150 QEINRVYKEM 160 YKTDLEKDII 170 SDTSGDFRKL 180 MVALAKGRRA 190 EDGSVIDYEL 200 IDQDARDLYD 210 AGVKRKGTDV 220 PKWISIMTER 230 SVPHLQKVFD 240 RYKSYSPYDM 250 LESIRKEVKG 260 DLENAFLNLV 270 QCIQNKPLYF 280 ADRLYDSMKG 290 KGTRDKVLIR 300 IMVSRSEVDM 310 LKIRSEFKRK 320 YGKSLYYYIQ 330 QDTKGDYQKA LLYLCGGDD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005912 adherens junction
Biological Process GO:0050767 regulation of neurogenesis
Biological Process GO:0006900 vesicle budding from membrane
Cellular Component GO:1990665 AnxA2-p11 complex
Cellular Component GO:0035578 azurophil granule lumen
Cellular Component GO:0005604 basement membrane
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0009986 cell surface
Cellular Component GO:0001533 cornified envelope
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005769 early endosome
Cellular Component GO:0005768 endosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0031902 late endosome membrane
Cellular Component GO:0005811 lipid droplet
Cellular Component GO:0005765 lysosomal membrane
Cellular Component GO:0042470 melanosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0030496 midbody
Cellular Component GO:0035749 myelin sheath adaxonal region
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990667 PCSK9-AnxA2 complex
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0042383 sarcolemma
Cellular Component GO:0043220 Schmidt-Lanterman incisure
Cellular Component GO:0031982 vesicle
Cellular Component GO:0012506 vesicle membrane
Molecular Function GO:0098641 cadherin binding involved in cell-cell adhesion
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0005544 calcium-dependent phospholipid binding
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:0008092 cytoskeletal protein binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
Molecular Function GO:0001786 phosphatidylserine binding
Molecular Function GO:0019834 phospholipase A2 inhibitor activity
Molecular Function GO:0002020 protease binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0044548 S100 protein binding
Molecular Function GO:0004867 serine-type endopeptidase inhibitor activity
Biological Process GO:0001525 angiogenesis
Biological Process GO:0007155 cell adhesion
Biological Process GO:0001765 membrane raft assembly
Biological Process GO:0042789 mRNA transcription by RNA polymerase II
Biological Process GO:0032804 negative regulation of low-density lipoprotein particle receptor catabolic process
Biological Process GO:0002091 negative regulation of receptor internalization
Biological Process GO:0036035 osteoclast development
Biological Process GO:0045921 positive regulation of exocytosis
Biological Process GO:1905581 positive regulation of low-density lipoprotein particle clearance
Biological Process GO:1905686 positive regulation of plasma membrane repair
Biological Process GO:0010756 positive regulation of plasminogen activation
Biological Process GO:0001921 positive regulation of receptor recycling
Biological Process GO:1905602 positive regulation of receptor-mediated endocytosis involved in cholesterol transport
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0044090 positive regulation of vacuole organization
Biological Process GO:0031340 positive regulation of vesicle fusion

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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.