CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002707
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Annexin A5 
Protein Synonyms/Alias
 Anchorin CII; Annexin V; Annexin-5; Calphobindin I; CBP-I; Endonexin II; Lipocortin V; Placental anticoagulant protein 4; PP4; Placental anticoagulant protein I; PAP-I; Thromboplastin inhibitor; Vascular anticoagulant-alpha; VAC-alpha 
Gene Name
 ANXA5 
Gene Synonyms/Alias
 ANX5; ENX2; PP4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29ETLRKAMKGLGTDEEsumoylation[1]
29ETLRKAMKGLGTDEEubiquitination[2, 3, 4, 5, 6]
58QEISAAFKTLFGRDLubiquitination[3, 4, 5]
70RDLLDDLKSELTGKFacetylation[7, 8]
70RDLLDDLKSELTGKFubiquitination[4, 5]
76LKSELTGKFEKLIVAacetylation[7]
76LKSELTGKFEKLIVAubiquitination[2, 3, 4, 5]
79ELTGKFEKLIVALMKacetylation[7]
79ELTGKFEKLIVALMKubiquitination[3]
86KLIVALMKPSRLYDAubiquitination[3, 4, 5, 6]
97LYDAYELKHALKGAGacetylation[7]
97LYDAYELKHALKGAGubiquitination[3, 4, 5, 6]
101YELKHALKGAGTNEKacetylation[9, 10]
101YELKHALKGAGTNEKubiquitination[4]
108KGAGTNEKVLTEIIAubiquitination[2, 3, 4, 5, 6]
126PEELRAIKQVYEEEYubiquitination[4, 6]
186LFQAGELKWGTDEEKubiquitination[4]
193KWGTDEEKFITIFGTubiquitination[3, 4, 5]
290NIRKEFRKNFATSLYubiquitination[3, 5]
301TSLYSMIKGDTSGDYubiquitination[3, 4, 5, 6]
309GDTSGDYKKALLLLCacetylation[11]
Reference
 [1] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [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] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [9] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [10] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [11] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 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. 
Sequence Annotation
 REPEAT 24 84 Annexin 1.
 REPEAT 96 156 Annexin 2.
 REPEAT 180 240 Annexin 3.
 REPEAT 255 315 Annexin 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 70 70 N6-acetyllysine.
 MOD_RES 76 76 N6-acetyllysine.
 MOD_RES 79 79 N6-acetyllysine.
 MOD_RES 97 97 N6-acetyllysine.
 MOD_RES 101 101 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Annexin; Blood coagulation; Calcium; Calcium/phospholipid-binding; Complete proteome; Direct protein sequencing; Hemostasis; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 320 AA 
Protein Sequence
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL 60
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE 120
ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF 180
QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV 240
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI 300
KGDTSGDYKK ALLLLCGEDD 320 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0072563; C:endothelial microparticle; IEA:Compara.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
 GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
 GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
 GO:0010033; P:response to organic substance; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:UniProtKB. 
Interpro
 IPR001464; Annexin.
 IPR018502; Annexin_repeat.
 IPR018252; Annexin_repeat_CS.
 IPR015473; Annexins_V.
 IPR002392; AnnexinV. 
Pfam
 PF00191; Annexin 
SMART
 SM00335; ANX 
PROSITE
 PS00223; ANNEXIN 
PRINTS
 PR00196; ANNEXIN.
 PR00201; ANNEXINV.