CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006035
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein S100-A11 
Protein Synonyms/Alias
 Calgizzarin; Metastatic lymph node gene 70 protein; MLN 70; Protein S100-C; S100 calcium-binding protein A11 
Gene Name
 S100A11 
Gene Synonyms/Alias
 MLN70; S100C 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKISSPTETacetylation[1, 2, 3]
23SLIAVFQKYAGKDGYubiquitination[4, 5]
27VFQKYAGKDGYNYTLacetylation[3]
27VFQKYAGKDGYNYTLubiquitination[4, 5, 6, 7, 8, 9, 10]
52TELAAFTKNQKDPGVubiquitination[5]
55AAFTKNQKDPGVLDRubiquitination[4, 11]
Reference
 [1] 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]
 [2] 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]
 [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] 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] 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]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] 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]
 [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] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266
Functional Description
 Facilitates the differentiation and the cornification of keratinocytes. 
Sequence Annotation
 DOMAIN 13 49 EF-hand 1.
 DOMAIN 55 90 EF-hand 2.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 N6-acetyllysine.
 MOD_RES 6 6 Phosphoserine.
 MOD_RES 10 10 Phosphothreonine.
 DISULFID 13 13 Interchain.  
Keyword
 3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 105 AA 
Protein Sequence
MAKISSPTET ERCIESLIAV FQKYAGKDGY NYTLSKTEFL SFMNTELAAF TKNQKDPGVL 60
DRMMKKLDTN SDGQLDFSEF LNLIGGLAMA CHDSFLKAVP SQKRT 105 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0008156; P:negative regulation of DNA replication; TAS:ProtInc.
 GO:0007165; P:signal transduction; TAS:UniProtKB. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR001751; S100/CaBP-9k_CS.
 IPR013787; S100_Ca-bd_sub. 
Pfam
 PF00036; efhand
 PF01023; S_100 
SMART
  
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00303; S100_CABP 
PRINTS