CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023091
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DCC-interacting protein 13-alpha 
Protein Synonyms/Alias
 Dip13-alpha; Adapter protein containing PH domain, PTB domain and leucine zipper motif 1 
Gene Name
 APPL1 
Gene Synonyms/Alias
 APPL; DIP13A; KIAA1428 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MPGIDKLPIEETLubiquitination[1]
63AATHLTSKLLKEYEKubiquitination[1, 2, 3, 4, 5, 6]
66HLTSKLLKEYEKQRFubiquitination[1, 3, 6]
70KLLKEYEKQRFPLGGubiquitination[1]
124QFKERDLKEILTLKEubiquitination[1, 4]
160KRENDKVKYEVTEDVubiquitination[1]
280VNRNLTRKAGYLNARubiquitination[1]
289GYLNARNKTGLVSSTubiquitination[1, 7]
350QITSFDGKKSSILQAubiquitination[5, 8]
351ITSFDGKKSSILQAEubiquitination[1, 8]
361ILQAESKKDHEEWICubiquitination[1]
375CTINNISKQIYLSENubiquitination[1]
490GESGGSTKSETEDSIubiquitination[4, 8]
513FLGSMEVKSDDHPDVubiquitination[1, 4]
661NKQKQIEKDLEEQSRubiquitination[1, 7]
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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [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
 Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. 
Sequence Annotation
 DOMAIN 277 375 PH.
 DOMAIN 496 656 PID.
 REGION 1 428 Required for RAB5A binding.
 MOTIF 403 414 F&H.
 MOD_RES 399 399 Phosphothreonine.
 MOD_RES 401 401 Phosphoserine.
 MOD_RES 410 410 Phosphoserine; by PKA.  
Keyword
 3D-structure; Cell cycle; Coiled coil; Complete proteome; Endosome; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 709 AA 
Protein Sequence
MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA QNELSAATHL 60
TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH AVLSTQLADA MMFPITQFKE 120
RDLKEILTLK EVFQIASNDH DAAINRYSRL SKKRENDKVK YEVTEDVYTS RKKQHQTMMH 180
YFCALNTLQY KKKIALLEPL LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM 240
DSDIETMQQT IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ 300
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK KSSILQAESK 360
KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP SPSFQQRHES LRPAAGQSRP 420
PTARTSSSGS LGSESTNLAA LSLDSLVAPD TPIQFDIISP VCEDQPGQAK AFGQGGRRTN 480
PFGESGGSTK SETEDSILHQ LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM 540
TESHLLVTCD CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS 600
SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ KELNKQKQIE 660
KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE GGKKRESEA 709 
Gene Ontology
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0010008; C:endosome membrane; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0012506; C:vesicle membrane; IDA:BHF-UCL.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; TAS:Reactome.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; IDA:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; TAS:BHF-UCL.
 GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
 GO:0090003; P:regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
 GO:0046324; P:regulation of glucose import; IMP:BHF-UCL. 
Interpro
 IPR027267; AH/BAR-dom.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR006020; PTyr_interaction_dom. 
Pfam
 PF00640; PID 
SMART
 SM00233; PH 
PROSITE
 PS50003; PH_DOMAIN
 PS01179; PID 
PRINTS