CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021953
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mid1-interacting protein 1 
Protein Synonyms/Alias
 Gastrulation-specific G12-like protein; Mid1-interacting G12-like protein; Protein STRAIT11499; Spot 14-related protein; S14R; Spot 14-R 
Gene Name
 MID1IP1 
Gene Synonyms/Alias
 MIG12 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11ICDTYNQKHSLFNAMubiquitination[1, 2, 3]
95YSHYVLLKSIRNDIEubiquitination[2, 4]
122SEEGSAWKSKDILVDubiquitination[2, 4, 5, 6]
124EGSAWKSKDILVDLGubiquitination[2, 4, 5]
160GLHTVLSKLTRKANIubiquitination[2]
164VLSKLTRKANILTNRubiquitination[2, 3]
173NILTNRYKQEIGFGNubiquitination[1, 2, 3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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
 Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 75 75 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Lipid biosynthesis; Lipid metabolism; Microtubule; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 183 AA 
Protein Sequence
MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLADPGLDN DVGVEVGGSG 60
GCLEERTPPV PDSGSANGSF FAPSRDMYSH YVLLKSIRND IEWGVLHQPP PPAGSEEGSA 120
WKSKDILVDL GHLEGADAGE EDLEQQFHYH LRGLHTVLSK LTRKANILTN RYKQEIGFGN 180
WGH 183 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
 GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
 GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:UniProtKB.
 GO:0051351; P:positive regulation of ligase activity; ISS:UniProtKB.
 GO:0051258; P:protein polymerization; ISS:UniProtKB. 
Interpro
 IPR009786; Spot_14. 
Pfam
 PF07084; Spot_14 
SMART
  
PROSITE
  
PRINTS