CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019801
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calcium and integrin-binding protein 1 
Protein Synonyms/Alias
 CIB; Calcium- and integrin-binding protein; CIBP; Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; SNK-interacting protein 2-28; SIP2-28 
Gene Name
 CIB1 
Gene Synonyms/Alias
 CIB; KIP; PRKDCIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10GSGSRLSKELLAEYQubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
24QDLTFLTKQEILLAHubiquitination[2, 3]
65ILSLPELKANPFKERubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
70ELKANPFKERICRVFubiquitination[3, 4, 5, 8]
188PDFASSFKIVL****ubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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]
 [8] 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
Functional Description
 May convert the inactive conformation of integrin alpha- IIb/beta3 to an active form through binding to the integrin cytoplasmic domain. Induces cell migration and spreading mediated through integrin (possibly via focal adhesion complexes). Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. May play a role in regulation of apoptosis. Interacts with and up-regulates PTK2/FAK1 activity. Down regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Participates in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation. 
Sequence Annotation
 DOMAIN 103 138 EF-hand 1.
 DOMAIN 148 183 EF-hand 2.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 3D-structure; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 191 AA 
Protein Sequence
MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPQ EQRSVESSLR AQVPFEQILS 60
LPELKANPFK ERICRVFSTS PAKDSLSFED FLDLLSVFSD TATPDIKSHY AFRIFDFDDD 120
GTLNREDLSR LVNCLTGEGE DTRLSASEMK QLIDNILEES DIDRDGTINL SEFQHVISRS 180
PDFASSFKIV L 191 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IMP:HGNC.
 GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IMP:HGNC.
 GO:0042383; C:sarcolemma; IDA:BHF-UCL.
 GO:0005509; F:calcium ion binding; IMP:HGNC.
 GO:0043495; F:protein anchor; IGI:BHF-UCL.
 GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO:0006302; P:double-strand break repair; TAS:ProtInc.
 GO:0007113; P:endomitotic cell cycle; IDA:UniProtKB.
 GO:0097191; P:extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
 GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
 GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IGI:BHF-UCL. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom. 
Pfam
 PF13499; EF_hand_5 
SMART
 SM00054; EFh 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS