CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002091
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Annexin A1 
Protein Synonyms/Alias
 Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I; Phospholipase A2 inhibitory protein; p35 
Gene Name
 ANXA1 
Gene Synonyms/Alias
 ANX1; LPC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26QEYVQTVKSSKGGPGubiquitination[1, 2, 3]
29VQTVKSSKGGPGSAVubiquitination[1, 3, 4, 5]
53SDVAALHKAIMVKGVacetylation[6, 7, 8]
53SDVAALHKAIMVKGVubiquitination[1, 3]
58LHKAIMVKGVDEATIubiquitination[1, 3, 4, 5, 9, 10]
71TIIDILTKRNNAQRQacetylation[8]
71TIIDILTKRNNAQRQubiquitination[1, 3]
81NAQRQQIKAAYLQETubiquitination[1, 2, 3, 4]
90AYLQETGKPLDETLKacetylation[7, 8, 11, 12]
90AYLQETGKPLDETLKubiquitination[1, 3, 4, 12]
97KPLDETLKKALTGHLacetylation[12]
97KPLDETLKKALTGHLubiquitination[1, 3]
98PLDETLKKALTGHLEubiquitination[1, 3]
113EVVLALLKTPAQFDAubiquitination[3]
128DELRAAMKGLGTDEDubiquitination[1, 3, 4, 5]
161RVYREELKRDLAKDIacetylation[6]
161RVYREELKRDLAKDIubiquitination[5]
166ELKRDLAKDITSDTSacetylation[7, 8, 12]
166ELKRDLAKDITSDTSubiquitination[1, 3, 4, 5, 9, 10, 12, 13]
185NALLSLAKGDRSEDFacetylation[7]
185NALLSLAKGDRSEDFubiquitination[1, 3, 5]
214YEAGERRKGTDVNVFubiquitination[1, 3, 4, 5, 12]
239QLRRVFQKYTKYSKHacetylation[6, 12]
239QLRRVFQKYTKYSKHubiquitination[5]
250YSKHDMNKVLDLELKacetylation[6, 8]
250YSKHDMNKVLDLELKubiquitination[1, 4]
257KVLDLELKGDIEKCLubiquitination[1, 3, 5]
274IVKCATSKPAFFAEKubiquitination[2, 3, 4, 5, 12, 14]
281KPAFFAEKLHQAMKGacetylation[6]
281KPAFFAEKLHQAMKGubiquitination[3, 4, 5]
287EKLHQAMKGVGTRHKubiquitination[1, 2, 3, 5, 12]
312EIDMNDIKAFYQKMYacetylation[6, 7, 8, 12, 15]
312EIDMNDIKAFYQKMYubiquitination[1, 3, 4]
332QAILDETKGDYEKILubiquitination[2, 5]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] 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]
 [10] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [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]
 [12] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [13] 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]
 [14] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [15] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224
Functional Description
 Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity. 
Sequence Annotation
 REPEAT 51 111 Annexin 1.
 REPEAT 123 183 Annexin 2.
 REPEAT 207 267 Annexin 3.
 REPEAT 282 342 Annexin 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 5 5 Phosphoserine; by TRPM7.
 MOD_RES 21 21 Phosphotyrosine; by EGFR.
 MOD_RES 24 24 Phosphothreonine.
 MOD_RES 27 27 Phosphoserine; by PKC.
 MOD_RES 37 37 Phosphoserine.
 MOD_RES 239 239 N6-acetyllysine.
 MOD_RES 312 312 N6-acetyllysine.
 CROSSLNK 19 19 Isoglutamyl lysine isopeptide (Gln-Lys)  
Keyword
 3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium; Complete proteome; Cytoplasm; Direct protein sequencing; Isopeptide bond; Membrane; Nucleus; Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 346 AA 
Protein Sequence
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV 60
DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA 120
DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL 180
LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY 240
TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM 300
VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN 346 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
 GO:0001533; C:cornified envelope; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0031966; C:mitochondrial membrane; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0042383; C:sarcolemma; IEA:Compara.
 GO:0005509; F:calcium ion binding; TAS:ProtInc.
 GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
 GO:0019834; F:phospholipase A2 inhibitor activity; IDA:BHF-UCL.
 GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
 GO:0005102; F:receptor binding; TAS:ProtInc.
 GO:0005198; F:structural molecule activity; IDA:UniProtKB.
 GO:0046632; P:alpha-beta T cell differentiation; ISS:BHF-UCL.
 GO:0050482; P:arachidonic acid secretion; IEA:Compara.
 GO:0007049; P:cell cycle; IEA:Compara.
 GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
 GO:0006928; P:cellular component movement; TAS:ProtInc.
 GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:BHF-UCL.
 GO:0070301; P:cellular response to hydrogen peroxide; IEA:Compara.
 GO:0031018; P:endocrine pancreas development; IEA:Compara.
 GO:0060206; P:estrous cycle phase; IEA:Compara.
 GO:0042063; P:gliogenesis; IEA:Compara.
 GO:0070365; P:hepatocyte differentiation; IEA:Compara.
 GO:0006954; P:inflammatory response; TAS:ProtInc.
 GO:0030073; P:insulin secretion; IEA:Compara.
 GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
 GO:0002674; P:negative regulation of acute inflammatory response; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0050709; P:negative regulation of protein secretion; IEA:Compara.
 GO:0097350; P:neutrophil clearance; IMP:BHF-UCL.
 GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
 GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Compara.
 GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Compara.
 GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0070555; P:response to interleukin-1; IEA:Compara.
 GO:0043434; P:response to peptide hormone stimulus; IEA:Compara.
 GO:0010165; P:response to X-ray; IEA:Compara. 
Interpro
 IPR001464; Annexin.
 IPR018502; Annexin_repeat.
 IPR018252; Annexin_repeat_CS.
 IPR002388; AnnexinI. 
Pfam
 PF00191; Annexin 
SMART
 SM00335; ANX 
PROSITE
 PS00223; ANNEXIN 
PRINTS
 PR00196; ANNEXIN.
 PR00197; ANNEXINI.