CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002496
UniProt Accession
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
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28PSAYGSVKAYTNFDAubiquitination[1]
47LNIETAIKTKGVDEVubiquitination[1]
49IETAIKTKGVDEVTIubiquitination[1, 2, 3]
104TVILGLLKTPAQYDAubiquitination[1, 3]
115QYDASELKASMKGLGubiquitination[1]
148QEINRVYKEMYKTDLubiquitination[1, 4]
152RVYKEMYKTDLEKDIubiquitination[1]
157MYKTDLEKDIISDTSubiquitination[1]
204DLYDAGVKRKGTDVPubiquitination[1]
212RKGTDVPKWISIMTEubiquitination[1]
227RSVPHLQKVFDRYKSubiquitination[4]
266LVQCIQNKPLYFADRubiquitination[1]
279DRLYDSMKGKGTRDKubiquitination[5]
302RSEVDMLKIRSEFKRubiquitination[1]
313EFKRKYGKSLYYYIQubiquitination[1, 4]
324YYIQQDTKGDYQKALubiquitination[1, 3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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
 REPEAT 42 102 Annexin 1.
 REPEAT 114 174 Annexin 2.
 REPEAT 199 259 Annexin 3.
 REPEAT 274 334 Annexin 4.
 REGION 2 24 S100A10-binding site (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 24 24 Phosphotyrosine; by SRC.
 MOD_RES 26 26 Phosphoserine; by PKC.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Annexin; Basement membrane; Calcium; Calcium/phospholipid-binding; Complete proteome; Direct protein sequencing; Extracellular matrix; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 339 AA 
Protein Sequence
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 
Gene Ontology
 GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
 GO:0005769; C:early endosome; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0019897; C:extrinsic to plasma membrane; IEA:Compara.
 GO:0005811; C:lipid particle; IDA:UniProtKB.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0035749; C:myelin sheath adaxonal region; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0042383; C:sarcolemma; IEA:Compara.
 GO:0043220; C:Schmidt-Lanterman incisure; IEA:Compara.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Compara.
 GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
 GO:0001525; P:angiogenesis; IEP:UniProtKB.
 GO:0007589; P:body fluid secretion; IEA:Compara.
 GO:0071229; P:cellular response to acid; IEA:Compara.
 GO:0030199; P:collagen fibril organization; IEA:Compara.
 GO:0042730; P:fibrinolysis; IEA:Compara.
 GO:0051099; P:positive regulation of binding; IEA:Compara.
 GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
 GO:0001501; P:skeletal system development; TAS:ProtInc. 
Interpro
 IPR001464; Annexin.
 IPR018502; Annexin_repeat.
 IPR018252; Annexin_repeat_CS.
 IPR002389; AnnexinII. 
Pfam
 PF00191; Annexin 
SMART
 SM00335; ANX 
PROSITE
 PS00223; ANNEXIN 
PRINTS
 PR00196; ANNEXIN.
 PR00198; ANNEXINII.