CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026279
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Midasin 
Protein Synonyms/Alias
  
Gene Name
 MDN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22LIAAKNEKSRSELGRubiquitination[1]
33ELGRFLAKQVWTPQDubiquitination[1, 2, 3, 4, 5]
81ERNAEAIKAGGQINHubiquitination[1, 2, 4]
100RLCVSMSKLIGNHPDubiquitination[1, 3]
117PFALRYFKDTSPVFQubiquitination[1, 2, 4, 5, 6]
208HKLSFLKKIFNSDELubiquitination[1]
247PEVSLWRKQKELQYLubiquitination[1, 5]
249VSLWRKQKELQYLQGubiquitination[1, 2, 5]
350AAVTGRTKPPQLLKVubiquitination[1, 2]
356TKPPQLLKVQLGDQTubiquitination[1, 2]
366LGDQTDSKMLLGMYRubiquitination[1, 2, 3, 4]
519SEHTSKLKMAEVIGSubiquitination[1]
527MAEVIGSKLNISRKKubiquitination[1, 2, 3, 4]
563GRVRLLRKQSEAVHLubiquitination[1, 5]
610VGETGTGKTSTIQYLubiquitination[1, 3]
644ADLLGGYKPVDHKLIubiquitination[1, 2]
649GYKPVDHKLIWLPLRubiquitination[1]
669LFAQTFSKKQNFTFLubiquitination[1]
705VHKSAVNKDGKDSETubiquitination[1, 2]
708SAVNKDGKDSETGLLubiquitination[1]
717SETGLLIKEKWEAFGubiquitination[2]
719TGLLIKEKWEAFGLRubiquitination[1]
818NPATDVGKRNLPPGIubiquitination[1, 3, 5]
858LKGLSVNKNTVQGIIubiquitination[1]
935ASHPIVQKLICQHIVubiquitination[1]
947HIVPGNVKSLLKQPIubiquitination[1, 3, 5]
951GNVKSLLKQPIPEPKubiquitination[1, 2, 4]
958KQPIPEPKGGRLIQVubiquitination[1]
1111TETQEVVKAHPRFMLubiquitination[1, 2, 3, 4]
1161ELETILHKRCSLPPSubiquitination[1, 2, 3]
Reference
 [1] 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]
 [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] 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] 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]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1181 AA 
Protein Sequence
MEHFLLEVAA APLRLIAAKN EKSRSELGRF LAKQVWTPQD RQCVLSTLAQ LLLDKDCTVL 60
VGRQLRPLLL DLLERNAEAI KAGGQINHDL HERLCVSMSK LIGNHPDVLP FALRYFKDTS 120
PVFQRLFLES SDANPVRYGR RRMKLRDLME AAFKFLQQEQ SVFRELWDWS VCVPLLRSHD 180
TLVRWYTANC LALVTCMNEE HKLSFLKKIF NSDELIHFRL RLLEEAQLQD LEKALVLANP 240
EVSLWRKQKE LQYLQGHLVS SDLSPRVTAV CGVVLPGQLP APGELGGNRS SSREQELALR 300
SYVLVESVCK SLQTLAMAVA SQNAVLLEGP IGCGKTSLVE YLAAVTGRTK PPQLLKVQLG 360
DQTDSKMLLG MYRCTDVPGE FVWQPGTLTQ AATMGHWILL EDIDYAPLDV VLQSRYPSLL 420
AVVDHLLDIY IQLTGEKHHS WSDSSVGCEQ APEEVSEARR ENKRPTLEGR ELSLRDLLNW 480
CNRIAHSFDS SSLSASLNIF QEALDCFTAM LSEHTSKLKM AEVIGSKLNI SRKKAEFFCQ 540
LYKPEIVINE LDLQVGRVRL LRKQSEAVHL QREKFTFAAT RPSSVLIEQL AVCVSKGEPV 600
LLVGETGTGK TSTIQYLAHI TGHRLRVVNM NQQSDTADLL GGYKPVDHKL IWLPLREAFE 660
ELFAQTFSKK QNFTFLGHIQ TCYRQKRWHD LLRLMQHVHK SAVNKDGKDS ETGLLIKEKW 720
EAFGLRLNHA QQQMKMTENT LLFAFVEGTL AQAVKKGEWI LLDEINLAAP EILECLSGLL 780
EGSSGSLVLL DRGDTEPLVR HPDFRLFACM NPATDVGKRN LPPGIRNRFT ELYVEELESK 840
EDLQVLIVDY LKGLSVNKNT VQGIINFYTA LRKESGTKLV DGTGHRPHYS LRTLCRALRF 900
AASNPCGNIQ RSLYEGFCLG FLTQLDRASH PIVQKLICQH IVPGNVKSLL KQPIPEPKGG 960
RLIQVEGYWI AVGDKEPTID ETYILTSSVK LNLRDIVRVV SAGTYPVLIQ GETSVGKTSL 1020
IQWLAAATGN HCVRINNHEH TDIQEYIGCY TSDSSGKLVF KEGVLIDAMR KGYWIILDEL 1080
NLAPTDVLEA LNRLLDDNRE LLVTETQEVV KAHPRFMLFA TQNPPGLYGG RKVLSRAFRN 1140
RFVELHFDEL PSSELETILH KRCSLPPSYC SKLVKVMLDL Q 1181 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0016887; F:ATPase activity; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR011704; ATPase_dyneun-rel_AAA.
 IPR027417; P-loop_NTPase. 
Pfam
 PF07728; AAA_5 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS