CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029158
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Annexin 
Protein Synonyms/Alias
  
Gene Name
 ANXA6 
Gene Synonyms/Alias
 hCG_39152 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKPAQGAKYacetylation[1]
9AKPAQGAKYRGSIHDacetylation[1]
9AKPAQGAKYRGSIHDubiquitination[2]
40MKGFGSDKEAILDIIacetylation[3]
40MKGFGSDKEAILDIIubiquitination[2]
63QEVCQSYKSLYGKDLacetylation[1]
63QEVCQSYKSLYGKDLubiquitination[1, 2]
68SYKSLYGKDLIADLKacetylation[1, 3]
68SYKSLYGKDLIADLKubiquitination[2, 4]
81LKYELTGKFERLIVGacetylation[1, 3]
81LKYELTGKFERLIVGubiquitination[1, 2, 4]
99PPAYCDAKEIKDAISacetylation[1]
99PPAYCDAKEIKDAISubiquitination[1, 2]
102YCDAKEIKDAISGIGacetylation[1]
102YCDAKEIKDAISGIGubiquitination[1, 2, 5, 6]
113SGIGTDEKCLIEILAubiquitination[2, 5]
135HQLVAAYKDAYERDLubiquitination[1, 2, 4, 5, 7]
220LVFDEYLKTTGKPIEubiquitination[2]
224EYLKTTGKPIEASIRubiquitination[2]
240ELSGDFEKLMLAVVKubiquitination[1, 2]
247KLMLAVVKCIRSTPEubiquitination[2]
299IFRTKYEKSLYSMIKacetylation[3, 8]
306KSLYSMIKNDTSGEYacetylation[1]
306KSLYSMIKNDTSGEYubiquitination[2]
370FNPDADAKALRKAMKacetylation[1, 3, 8]
370FNPDADAKALRKAMKubiquitination[1]
377KALRKAMKGLGTDEDubiquitination[1, 2, 4, 5, 6, 7, 9, 10]
406QQIRQTFKSHFGRDLubiquitination[1, 2]
418RDLMTDLKSEISGDLacetylation[1, 3, 8]
418RDLMTDLKSEISGDLubiquitination[2, 5, 6, 10]
442PPAHYDAKQLKKAMEacetylation[1, 3]
445HYDAKQLKKAMEGAGacetylation[1]
445HYDAKQLKKAMEGAGubiquitination[1]
446YDAKQLKKAMEGAGTubiquitination[2]
456EGAGTDEKALIEILAubiquitination[1, 2]
478RAINEAYKEDYHKSLacetylation[1, 8]
478RAINEAYKEDYHKSLubiquitination[1, 2]
483AYKEDYHKSLEDALSacetylation[1, 3]
483AYKEDYHKSLEDALSubiquitination[2]
534ADTPSGDKTSLETRFubiquitination[5]
562RVFQEFIKMTNYDVEubiquitination[5]
594IVQSVKNKPLFFADKubiquitination[2]
601KPLFFADKLYKSMKGubiquitination[2]
614KGAGTDEKTLTRIMVacetylation[1, 3]
614KGAGTDEKTLTRIMVubiquitination[1, 2]
641EFIEKYDKSLHQAIEubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] 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
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
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 EDAQEIADTP SGDKTSLETR 540
FMTILCTRSY PHLRRVFQEF IKMTNYDVEH TIKKEMSGDV RDAFVAIVQS VKNKPLFFAD 600
KLYKSMKGAG TDEKTLTRIM VSRSEIDLLN IRREFIEKYD KSLHQAIEGD TSGDFLKALL 660
ALCGGED 667 
Gene Ontology
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW. 
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.