CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002604
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Annexin A6 
Protein Synonyms/Alias
 67 kDa calelectrin; Annexin VI; Annexin-6; Calphobindin-II; CPB-II; Chromobindin-20; Lipocortin VI; Protein III; p68; p70 
Gene Name
 ANXA6 
Gene Synonyms/Alias
 ANX6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9AKPAQGAKYRGSIHDacetylation[1]
9AKPAQGAKYRGSIHDubiquitination[2]
40MKGFGSDKEAILDIIubiquitination[2]
63QEVCQSYKSLYGKDLacetylation[3]
63QEVCQSYKSLYGKDLubiquitination[2, 4]
68SYKSLYGKDLIADLKacetylation[3]
68SYKSLYGKDLIADLKubiquitination[2, 5, 6]
75KDLIADLKYELTGKFacetylation[3]
81LKYELTGKFERLIVGacetylation[3]
81LKYELTGKFERLIVGubiquitination[2, 4, 5, 6]
99PPAYCDAKEIKDAISubiquitination[2]
102YCDAKEIKDAISGIGubiquitination[2, 7]
113SGIGTDEKCLIEILAubiquitination[2]
135HQLVAAYKDAYERDLubiquitination[2, 4, 5, 6, 8]
220LVFDEYLKTTGKPIEubiquitination[2]
224EYLKTTGKPIEASIRubiquitination[2]
240ELSGDFEKLMLAVVKubiquitination[2]
247KLMLAVVKCIRSTPEubiquitination[2]
299IFRTKYEKSLYSMIKacetylation[3]
306KSLYSMIKNDTSGEYacetylation[3]
306KSLYSMIKNDTSGEYubiquitination[2]
370FNPDADAKALRKAMKacetylation[3]
377KALRKAMKGLGTDEDubiquitination[2, 4, 5, 6, 7, 8, 9]
406QQIRQTFKSHFGRDLubiquitination[2]
418RDLMTDLKSEISGDLacetylation[3, 10]
418RDLMTDLKSEISGDLubiquitination[2, 7]
442PPAHYDAKQLKKAMEacetylation[3]
446YDAKQLKKAMEGAGTubiquitination[2]
456EGAGTDEKALIEILAubiquitination[2]
478RAINEAYKEDYHKSLubiquitination[2]
483AYKEDYHKSLEDALSacetylation[3]
483AYKEDYHKSLEDALSubiquitination[2]
600IVQSVKNKPLFFADKubiquitination[2, 4]
607KPLFFADKLYKSMKGacetylation[3]
607KPLFFADKLYKSMKGubiquitination[2]
620KGAGTDEKTLTRIMVacetylation[3]
620KGAGTDEKTLTRIMVubiquitination[2]
647EFIEKYDKSLHQAIEubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] 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
Functional Description
 May associate with CD21. May regulate the release of Ca(2+) from intracellular stores. 
Sequence Annotation
 REPEAT 29 89 Annexin 1.
 REPEAT 101 161 Annexin 2.
 REPEAT 185 245 Annexin 3.
 REPEAT 260 320 Annexin 4.
 REPEAT 372 432 Annexin 5.
 REPEAT 444 504 Annexin 6.
 REPEAT 533 593 Annexin 7.
 REPEAT 608 668 Annexin 8.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 30 30 Phosphotyrosine.
 MOD_RES 63 63 N6-acetyllysine.
 MOD_RES 68 68 N6-acetyllysine.
 MOD_RES 75 75 N6-acetyllysine.
 MOD_RES 81 81 N6-acetyllysine.
 MOD_RES 201 201 Phosphotyrosine (By similarity).
 MOD_RES 306 306 N6-acetyllysine.
 MOD_RES 370 370 N6-acetyllysine.
 MOD_RES 418 418 N6-acetyllysine.
 MOD_RES 483 483 N6-acetyllysine.
 MOD_RES 620 620 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Annexin; Calcium; Calcium/phospholipid-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 673 AA 
Protein Sequence
MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ 60
SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA 120
SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD 180
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK 240
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 300
LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA 360
NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE 420
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED 480
YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK 540
TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK 600
PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD 660
FLKALLALCG GED 673 
Gene Ontology
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
 GO:0006816; P:calcium ion transport; IEA:Compara.
 GO:0006937; P:regulation of muscle contraction; IEA:Compara. 
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.