CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032808
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Diaphanous homolog 1 (Drosophila), isoform CRA_a 
Protein Synonyms/Alias
 Protein diaphanous homolog 1 
Gene Name
 DIAPH1 
Gene Synonyms/Alias
 hCG_42523 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
193LKRLHDEKEETAGSYubiquitination[1, 2, 3]
294QPLLDGLKSGTTIALubiquitination[1, 3]
368EEDSYDLKGRLDDIRubiquitination[1, 2, 3, 4, 5]
423EARPQYYKLIEECISubiquitination[6]
444NGADPDFKCRHLQIEubiquitination[1, 3]
478KAAELEKKLDSELTAubiquitination[1, 3]
494HELQVEMKKMESDFEubiquitination[1, 2, 3, 4, 7]
495ELQVEMKKMESDFEQubiquitination[1, 3]
511LQDLQGEKDALHSEKacetylation[3]
518KDALHSEKQQIATEKubiquitination[4]
750PFGLTPKKLYKPEVQubiquitination[1, 3]
753LTPKKLYKPEVQLRRubiquitination[1, 3, 4, 8]
765LRRPNWSKLVAEDLSubiquitination[1]
779SQDCFWTKVKEDRFEubiquitination[1, 3]
781DCFWTKVKEDRFENNubiquitination[1, 3]
831ELKVLDSKTAQNLSIubiquitination[1]
1033VSAENLQKNLDQMKKubiquitination[8]
1079DAQEQYNKLRMMHSNacetylation[3]
1200GPRQANRKAGCAVTSubiquitination[1, 3]
1215LLASELTKDDAMAAVubiquitination[1, 3, 7]
1228AVPAKVSKNSETFPTubiquitination[1]
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] 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]
 [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] 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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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]
 [7] 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]
 [8] 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
 1248 AA 
Protein Sequence
MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFL ERFTSMRIKK EKEKPNSAHR 60
NSSASYGDDP TAQSLQDVSD EQVLVLFEQM LLDMNLNEEK QQPLREKDII IKREMVSQYL 120
YTSKAGMSQK ESSKSAMMYI QELRSGLRDM PLLSCLESLR VSLNNNPVSW VQTFGAEGLA 180
SLLDILKRLH DEKEETAGSY DSRNKHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD 240
PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTTIA 300
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQD LREIENEDMR VQLNVFDEQG 360
EEDSYDLKGR LDDIRMEMDD FNEVFQILLN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ 420
YYKLIEECIS QIVLHKNGAD PDFKCRHLQI EIEGLIDQMI DKTKVEKSEA KAAELEKKLD 480
SELTARHELQ VEMKKMESDF EQKLQDLQGE KDALHSEKQQ IATEKQDLEA EVSQLTGEVA 540
KLTKELEDAK KEMASLSAAA ITVPPSVPSR APVPPAPPLP GDSGTIIPPP PAPGDSTTPP 600
PPPPPPPPPP PLPGGTAISP PPPLSGDATI PPPPPLPEGV GIPSPSSLPG GTAIPPPPPL 660
PGSARIPPPP PPLPGSAGIP PPPPPLPGEA GMPPPPPPLP GGPGIPPPPP FPGGPGIPPP 720
PPGMGMPPPP PFGFGVPAAP VLPFGLTPKK LYKPEVQLRR PNWSKLVAED LSQDCFWTKV 780
KEDRFENNEL FAKLTLTFSA QTKTKKDQEG GEEKKSVQKK KVKELKVLDS KTAQNLSIFL 840
GSFRMPYQEI KNVILEVNEA VLTESMIQNL IKQMPEPEQL KMLSELKDEY DDLAESEQFG 900
VVMGTVPRLR PRLNAILFKL QFSEQVENIK PEIVSVTAAC EELRKSESFS NLLEITLLVG 960
NYMNAGSRNA GAFGFNISFL CKLRDTKSTD QKMTLLHFLA ELCENDYPDV LKFPDELAHV 1020
EKASRVSAEN LQKNLDQMKK QISDVERDVQ NFPAATDEKD KFVEKMTIFV KDAQEQYNKL 1080
RMMHSNMETL YKELGEYFLF DPKKLSVEEF FMDLHNFRNM FLQAVKENQK RRETEEKMRR 1140
AKLAKEKAEK ERLEKQQKRE QLIDMNAEGD ETGVMDSLLE ALQSGAAFRR KRGPRQANRK 1200
AGCAVTSLLA SELTKDDAMA AVPAKVSKNS ETFPTILEEA KELVGRAS 1248 
Gene Ontology
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro. 
Interpro
 IPR003104; Actin-bd_FH2/DRF_autoreg.
 IPR016024; ARM-type_fold.
 IPR014767; Diaphanous_autoregulatory.
 IPR010465; Drf_DAD.
 IPR010472; Drf_FH3.
 IPR010473; Drf_GTPase-bd.
 IPR015425; FH2_actin-bd.
 IPR009408; Formin_homology_1.
 IPR014768; GTPase-bd/formin_homology_3. 
Pfam
 PF06345; Drf_DAD
 PF06346; Drf_FH1
 PF06367; Drf_FH3
 PF06371; Drf_GBD
 PF02181; FH2 
SMART
 SM00498; FH2 
PROSITE
 PS51231; DAD
 PS51444; FH2
 PS51232; GBD_FH3 
PRINTS