CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019106
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 EF-hand domain-containing protein D2 
Protein Synonyms/Alias
 Swiprosin-1 
Gene Name
 EFHD2 
Gene Synonyms/Alias
 SWS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9ATDELATKLSRRLQMacetylation[1, 2]
9ATDELATKLSRRLQMubiquitination[3]
87FNPYTEFKEFSRKQIubiquitination[3, 4, 5]
102KDMEKMFKQYDAGRDubiquitination[3]
138LGLKNMIKEVDEDFDubiquitination[3]
188DVSSEGVKGAKSFFEubiquitination[3]
191SEGVKGAKSFFEAKVubiquitination[3, 6]
233KQRKAAFKELQSTFKacetylation[2, 7, 8]
233KQRKAAFKELQSTFKubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [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
Functional Description
 May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis (By similarity). Plays a role as negative regulator of the canonical NF-kappa-B-activating branch (By similarity). Controls spontaneous apoptosis through the regulation of BCL2L1 abundance (By similarity). 
Sequence Annotation
 DOMAIN 92 127 EF-hand 1.
 DOMAIN 128 163 EF-hand 2.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 74 74 Phosphoserine.
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 83 83 Phosphotyrosine (By similarity).
 MOD_RES 233 233 N6-acetyllysine.  
Keyword
 Acetylation; Calcium; Complete proteome; Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 240 AA 
Protein Sequence
MATDELATKL SRRLQMEGEG GGETPEQPGL NGAAAAAAGA PDEAAEALGS ADCELSAKLL 60
RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM 120
MEKLGAPQTH LGLKNMIKEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LCVLARLSEI 180
DVSSEGVKGA KSFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEMKQRKA AFKELQSTFK 240 
Gene Ontology
 GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:Compara. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR002048; EF_hand_dom. 
Pfam
 PF13499; EF_hand_5 
SMART
 SM00054; EFh 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS