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IID50353
 UniprotP07356
ProteinAnnexin A2
GeneAnxa2
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
339
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-339 Hetero hexamer : IID00724Complex,IID00813Complex
 Evidence X-RAY 4hre D Reference
       Region 4hre D 1-1 disorder
       Region 4hre D 2-339 order
 Evidence X-RAY 4hre B Reference
       Region 4hre B 1-1 disorder
       Region 4hre B 2-339 order
Seq 1-339 Hetero hexamer : IID00724Complex,IID00813Complex
 Evidence X-RAY 4hre C Reference
       Region 4hre C 1-1 disorder
       Region 4hre C 2-339 order
 Evidence X-RAY 4hre A Reference
       Region 4hre A 1-1 disorder
       Region 4hre A 2-339 order
SeqProS possible 2-20 Same region of the human homolog (P07355, 98% identity) is disordered in the free state. Hetero hexamer : IID00724Complex,IID00813Complex
       Region 4hre A 2-339 order
       Region 4hre C 2-339 order
SeqProS possible 2-20 Same region of the human homolog (P07355, 98% identity) is disordered in the free state. Hetero hexamer : IID00724Complex,IID00813Complex
       Region 4hre B 2-339 order
       Region 4hre D 2-339 order
Seqphosphorylation
    24-24 Phosphotyrosine; by SRC
    26-26 Phosphoserine; by PKC
    184-184 Phosphoserine
    199-199 Phosphotyrosine
Seqacetylation
    2-2 N-acetylserine
    49-49 N6-acetyllysine; alternate
    152-152 N6-acetyllysine
    227-227 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-20
Order 21-339
ProS 1-16
AlphaFold
Disorder 1-21
Order 22-339
Pfam Hmmer
PF00191 37-102 8e-22
PF00191 109-174 2e-35
PF00191 193-259 4.7e-19
PF00191 269-334 6.5e-29
Function
Function in SwissProt
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 (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:22848640).
Biological Process
See also
Diagram with PDB data
HLTF/S100A10/ANXA2Crystal Structure of p11-Annexin A2(N-terminal) Fusion Protein in Complex with SMARCA3 Peptide