Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00551
Entry Name
UniProt Accession
Theoretical PI
7.57
Molecular Weight
38604.04
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Annexin A2
Protein Synonyms/Alias
Annexin II; Annexin-2; Calpactin I heavy chain; Calpactin-1 heavy chain; Chromobindin-8; Lipocortin II; Placental anticoagulant protein IV; PAP-IV; Protein I; p36;
Gene Name
ANXA2
Gene Synonyms/Alias
ANX2; ANX2L4; CAL1H; LPC2D;
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
335
Canonical
QKALLYLCGGDD***
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kho Y, Kim SC, Jiang C, Barma D, Kwon SW, Cheng J, Jaunbergs J, Weinbaum C,Tamanoi F, Falck J, Zhao Y. A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. Proc Natl Acad Sci U S A. 2004 Aug24;101(34):12479-84. Epub 2004 Aug 12.[PMID:15308774]
Functional Description
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.
Sequence Annotation
Region: 2 24 S100A10-binding site.
Modified residue: 2 2 N-acetylserine.
Modified residue: 24 24 Phosphotyrosine; by SRC.
Modified residue: 26 26 Phosphoserine; by PKC.
Modified residue: 49 49 N6-acetyllysine.
Modified residue: 152 152 N6-acetyllysine.
Modified residue: 199 199 Phosphotyrosine.
Modified residue: 227 227 N6-acetyllysine.
Protein Length
339 AA.
Protein Sequence
(Canonical)
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL  60
TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG  120
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA  180
EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM  240
LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM  300
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD                         339
FASTA
(Canonical)
>LipidDB-9606-00551|P07355
MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNIL
TNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKG
LGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRA
EDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDM
LESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDM
LKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
Gene Ontology
GO:0005604; C:basement membrane; IEA:UniProtKB-KW
GO:0005938; C:cell cortex; IEA:Ensembl
GO:0009986; C:cell surface; IDA:UniProt
GO:0005769; C:early endosome; IEA:Ensembl
GO:0005768; C:endosome; IDA:UniProtKB
GO:0005615; C:extracellular space; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl
GO:0031902; C:late endosome membrane; IDA:UniProt
GO:0005811; C:lipid particle; IDA:UniProtKB
GO:0005765; C:lysosomal membrane; IDA:UniProt
GO:0044354; C:macropinosome; IEA:Ensembl
GO:0016020; C:membrane; IDA:UniProtKB
GO:0030496; C:midbody; IDA:UniProtKB
GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl
GO:0005634; C:nucleus; IDA:UniProt
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:BHF-UCL
GO:0043234; C:protein complex; IEA:Ensembl
GO:0001726; C:ruffle; IEA:Ensembl
GO:0042383; C:sarcolemma; IEA:Ensembl
GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB
GO:0048306; F:calcium-dependent protein binding; IPI:AgBase
GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:UniProt
GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProt
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0044548; F:S100 protein binding; IPI:UniProt
GO:0001525; P:angiogenesis; IEP:UniProtKB
GO:0007589; P:body fluid secretion; IEA:Ensembl
GO:0071229; P:cellular response to acid chemical; IEA:Ensembl
GO:0030199; P:collagen fibril organization; IEA:Ensembl
GO:0042730; P:fibrinolysis; IEA:Ensembl
GO:0006900; P:membrane budding; IMP:UniProt
GO:0001765; P:membrane raft assembly; IMP:UniProt
GO:0043086; P:negative regulation of catalytic activity; IDA:GOC
GO:0036035; P:osteoclast development; IDA:UniProt
GO:0051099; P:positive regulation of binding; IEA:Ensembl
GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl
GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl
GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB
GO:0051290; P:protein heterotetramerization; IDA:UniProt
GO:0072661; P:protein targeting to plasma membrane; IEA:Ensembl
Interpro
InterPro; IPR001464; Annexin
InterPro; IPR018502; Annexin_repeat
InterPro; IPR018252; Annexin_repeat_CS
InterPro; IPR002389; AnnexinII
Pfam
Pfam; PF00191; Annexin;
SMART
SMART; SM00335; ANX;
PROSITE
PROSITE; PS00223; ANNEXIN;
PRINTS
PRINTS; PR00196; ANNEXIN;
PRINTS; PR00198; ANNEXINII;