CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041069
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Annexin 
Protein Synonyms/Alias
  
Gene Name
 Anxa6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MAKIAQGAMYacetylation[1, 2, 3]
3*****MAKIAQGAMYsuccinylation[3]
3*****MAKIAQGAMYubiquitination[4]
34EALYTAMKGFGSDKEubiquitination[4]
40MKGFGSDKESILELIubiquitination[4]
63QEICQNYKSLYGKDLubiquitination[4]
68NYKSLYGKDLIEDLKacetylation[2]
68NYKSLYGKDLIEDLKubiquitination[4]
75KDLIEDLKYELTGKFacetylation[1, 5]
81LKYELTGKFERLIVNacetylation[1, 2, 3]
81LKYELTGKFERLIVNsuccinylation[3]
81LKYELTGKFERLIVNubiquitination[4]
99PLAYCDAKEIKDAISubiquitination[4]
135HQLVAAYKDAYERDLubiquitination[4]
224EYLKTTGKPIEASIRacetylation[1]
247KLMLAVVKCIRSTPEacetylation[1]
299IFRTKYEKSLYSMIKacetylation[2, 6, 7]
306KSLYSMIKNDTSGEYacetylation[1, 7]
306KSLYSMIKNDTSGEYubiquitination[4]
314NDTSGEYKKALLKLCacetylation[1]
370FNPDADAKALRKAMKacetylation[1, 2, 5, 6, 7]
370FNPDADAKALRKAMKubiquitination[4]
377KALRKAMKGIGTDEAubiquitination[4]
406QQIRQTFKSHFGRDLubiquitination[4]
418RDLMADLKSEISGDLacetylation[1, 2, 5]
442PPAHYDAKQLKKAMEacetylation[2, 7]
442PPAHYDAKQLKKAMEphosphoglycerylation[8]
442PPAHYDAKQLKKAMEubiquitination[4]
445HYDAKQLKKAMEGAGphosphoglycerylation[8]
446YDAKQLKKAMEGAGTphosphoglycerylation[8]
456EGAGTDEKTLIEILAubiquitination[4]
478RAINEAYKEDYHKSLacetylation[1, 6]
478RAINEAYKEDYHKSLubiquitination[4]
483AYKEDYHKSLEDALSacetylation[2]
483AYKEDYHKSLEDALSubiquitination[4]
562RVFQEFIKKTNYDIEacetylation[1]
594IVQSVKNKPLFFADKubiquitination[4]
601KPLFFADKLYKSMKGubiquitination[4]
614KGAGTDEKTLTRVMVacetylation[1, 2, 3, 5, 6, 7]
638IRREFIEKYDKSLHQacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [8] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
  
Sequence Annotation
  
Keyword
 Annexin; Calcium; Calcium/phospholipid-binding; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 667 AA 
Protein Sequence
MAKIAQGAMY RGSVHDFPEF DANQDAEALY TAMKGFGSDK ESILELITSR SNKQRQEICQ 60
NYKSLYGKDL IEDLKYELTG KFERLIVNLM RPLAYCDAKE IKDAISGVGT DEKCLIEILA 120
SRTNEQMHQL VAAYKDAYER DLESDIIGDT SGHFQKMLVV LLQGTRENDD VVSEDLVQQD 180
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK 240
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 300
LYSMIKNDTS GEYKKALLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVSR VELKGTVCAA 360
NDFNPDADAK ALRKAMKGIG TDEATIIDIV THRSNAQRQQ IRQTFKSHFG RDLMADLKSE 420
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKTLIE ILATRTNAEI RAINEAYKED 480
YHKSLEDALS SDTSGHFRRI LISLATGNRE EGGENRDQAQ EDAQEIADTP SGDKTSLETR 540
FMTVLCTRSY PHLRRVFQEF IKKTNYDIEH VIKKEMSGDV KDAFVAIVQS VKNKPLFFAD 600
KLYKSMKGAG TDEKTLTRVM VSRSEIDLLN IRREFIEKYD KSLHQAIEGD TSGDFMKALL 660
ALCGGED 667 
Gene Ontology
 GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
 GO:0006816; P:calcium ion transport; IMP:MGI.
 GO:0006937; P:regulation of muscle contraction; IMP:MGI. 
Interpro
 IPR001464; Annexin.
 IPR018502; Annexin_repeat.
 IPR018252; Annexin_repeat_CS.
 IPR002393; AnnexinVI. 
Pfam
 PF00191; Annexin 
SMART
 SM00335; ANX 
PROSITE
 PS00223; ANNEXIN 
PRINTS
 PR00196; ANNEXIN.
 PR00202; ANNEXINVI.