CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017081
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 C-Maf-inducing protein 
Protein Synonyms/Alias
 c-Mip; Truncated c-Maf-inducing protein; Tc-Mip 
Gene Name
 CMIP 
Gene Synonyms/Alias
 KIAA1694; TCMIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20PRQIEETKPLLGGDVubiquitination[1, 2, 3, 4]
74HPRTFLSKILTSKFLubiquitination[1, 2, 4, 5, 6, 7, 8, 9, 10]
79LSKILTSKFLRRWEPubiquitination[2, 4, 6, 8, 9, 10]
272PVVQRILKHNMDFGKubiquitination[3]
353RDNSPSLKEIRNGCQubiquitination[1, 3, 4]
646TRLTLPSKSTDADLAubiquitination[3]
756ADTYEDLKAKLPNLKubiquitination[1, 3]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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
Functional Description
 Plays a role in T-cell signaling pathway. Isoform 2 may play a role in T-helper 2 (Th2) signaling pathway and seems to represent the first proximal signaling protein that links T-cell receptor-mediated signal to the activation of c-Maf Th2 specific factor. 
Sequence Annotation
 DOMAIN 54 163 PH.
 REPEAT 663 686 LRR 1.
 REPEAT 687 707 LRR 2.
 REPEAT 712 732 LRR 3.
 REPEAT 736 756 LRR 4.
 MOD_RES 349 349 Phosphoserine.
 MOD_RES 377 377 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 773 AA 
Protein Sequence
MDVTSSSGGG GDPRQIEETK PLLGGDVSAP EGTKMGAVPC RRALLLCNGM RYKLLQEGDI 60
QVCVIRHPRT FLSKILTSKF LRRWEPHHLT LADNSLASAT PTGYMENSVS YSAIEDVQLL 120
SWENAPKYCL QLTIPGGTVL LQAANSYLRD QWFHSLQWKK KIYKYKKVLS NPSRWEVVLK 180
EIRTLVDMAL TSPLQDDSIN QAPLEIVSKL LSENTNLTTQ EHENIIVAIA PLLENNHPPP 240
DLCEFFCKHC RERPRSMVVI EVFTPVVQRI LKHNMDFGKC PRLRLFTQEY ILALNELNAG 300
MEVVKKFIQS MHGPTGHCPH PRVLPNLVAV CLAAIYSCYE EFINSRDNSP SLKEIRNGCQ 360
QPCDRKPTLP LRLLHPSPDL VSQEATLSEA RLKSVVVASS EIHVEVERTS TAKPALTASA 420
GNDSEPNLID CLMVSPACST MSIELGPQAD RTLGCYVEIL KLLSDYDDWR PSLASLLQPI 480
PFPKEALAHE KFTKELKYVI QRFAEDPRQE VHSCLLSVRA GKDGWFQLYS PGGVACDDDG 540
ELFASMVHIL MGSCYKTKKF LLSLAENKLG PCMLLALRGN QTMVEILCLM LEYNIIDNND 600
TQLQIISTLE STDVGKRMYE QLCDRQRELK ELQRKGGPTR LTLPSKSTDA DLARLLSSGS 660
FGNLENLSLA FTNVTSACAE HLIKLPSLKQ LNLWSTQFGD AGLRLLSEHL TMLQVLNLCE 720
TPVTDAGLLA LSSMKSLCSL NMNSTKLSAD TYEDLKAKLP NLKEVDVRYT EAW 773 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005543; F:phospholipid binding; IEA:InterPro. 
Interpro
 IPR001849; Pleckstrin_homology. 
Pfam
  
SMART
 SM00233; PH 
PROSITE
 PS50003; PH_DOMAIN 
PRINTS