CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022533
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Disco-interacting protein 2 homolog B 
Protein Synonyms/Alias
 DIP2 homolog B 
Gene Name
 DIP2B 
Gene Synonyms/Alias
 KIAA1463 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
47GYEKKRSKLLSPYSPubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
65ETDSAVQKELRNQTPubiquitination[1, 5, 6, 8, 9]
84AQTSAPSKYHRTRSGubiquitination[6, 9]
113AVQAALAKHKEQKMAubiquitination[6, 9]
115QAALAKHKEQKMALPubiquitination[6]
126MALPMPTKRRSTFVQubiquitination[6, 7]
198TLSHGEVKGTSGSLAubiquitination[6]
276VSSRVSTKIQQLLNTubiquitination[1, 3, 5, 6, 7, 8, 9]
285QQLLNTLKRPKRPPLubiquitination[1, 6, 8]
288LNTLKRPKRPPLKEFubiquitination[6]
293RPKRPPLKEFFVDDSubiquitination[2, 4, 7, 10]
480NGEIVQFKGWPRLKWubiquitination[1, 6, 8]
611KAKVALVKCRDLHWAubiquitination[6]
714IRVNTEDKNSALTVQubiquitination[4, 6, 9]
1125AAAAVDVKTWPTIIDubiquitination[2, 7]
1300ALQQSFSKLFKDIGLubiquitination[1, 5, 6, 8, 9]
1303QSFSKLFKDIGLSPRubiquitination[9]
1367LLLSESGKILPGVKVubiquitination[1, 6, 8, 9]
Reference
 [1] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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
Functional Description
  
Sequence Annotation
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 53 53 Phosphoserine.
 MOD_RES 71 71 Phosphothreonine.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 140 140 Phosphothreonine.
 MOD_RES 146 146 Phosphoserine.
 MOD_RES 148 148 Phosphoserine.
 MOD_RES 153 153 Phosphoserine (By similarity).
 MOD_RES 203 203 Phosphoserine.  
Keyword
 Complete proteome; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1576 AA 
Protein Sequence
MAERGLEPSP AAVAALPPEV RAQLAELELE LSEGDITQKG YEKKRSKLLS PYSPQTQETD 60
SAVQKELRNQ TPAPSAAQTS APSKYHRTRS GGARDERYRS DIHTEAVQAA LAKHKEQKMA 120
LPMPTKRRST FVQSPADACT PPDTSSASED EGSLRRQAAL SAALQQSLQN AESWINRSIQ 180
GSSTSSSASS TLSHGEVKGT SGSLADVFAN TRIENFSAPP DVTTTTSSSS SSSSIRPANI 240
DLPPSGIVKG MHKGSNRSSL MDTADGVPVS SRVSTKIQQL LNTLKRPKRP PLKEFFVDDS 300
EEIVEVPQPD PNQPKPEGRQ MTPVKGEPLG VICNWPPALE SALQRWGTTQ AKCSCLTALD 360
MTGKPVYTLT YGKLWSRSLK LAYTLLNKLG TKNEPVLKPG DRVALVYPNN DPVMFMVAFY 420
GCLLAEVIPV PIEVPLTRKD AGGQQIGFLL GSCGIALALT SEVCLKGLPK TQNGEIVQFK 480
GWPRLKWVVT DSKYLSKPPK DWQPHISPAG TEPAYIEYKT SKEGSVMGVT VSRLAMLSHC 540
QALSQACNYS EGETIVNVLD FKKDAGLWHG MFANVMNKMH TISVPYSVMK TCPLSWVQRV 600
HAHKAKVALV KCRDLHWAMM AHRDQRDVSL SSLRMLIVTD GANPWSVSSC DAFLSLFQSH 660
GLKPEAICPC ATSAEAMTVA IRRPGVPGAP LPGRAILSMN GLSYGVIRVN TEDKNSALTV 720
QDVGHVMPGG MMCIVKPDGP PQLCKTDEIG EICVSSRTGG MMYFGLAGVT KNTFEVIPVN 780
SAGSPVGDVP FIRSGLLGFV GPGSLVFVVG KMDGLLMVSG RRHNADDIVA TGLAVESIKT 840
VYRGRIAVFS VSVFYDERIV VVAEQRPDAS EEDSFQWMSR VLQAIDSIHQ VGVYCLALVP 900
ANTLPKTPLG GIHISQTKQL FLEGSLHPCN ILMCPHTCVT NLPKPRQKQP GVGPASVMVG 960
NLVAGKRIAQ AAGRDLGQIE ENDLVRKHQF LAEILQWRAQ ATPDHVLFML LNAKGTTVCT 1020
ASCLQLHKRA ERIASVLGDK GHLNAGDNVV LLYPPGIELI AAFYGCLYAG CIPVTVRPPH 1080
AQNLTATLPT VRMIVDVSKA ACILTSQTLM RLLRSREAAA AVDVKTWPTI IDTDDLPRKR 1140
LPQLYKPPTP EMLAYLDFSV STTGMLTGVK MSHSAVNALC RAIKLQCELY SSRQIAICLD 1200
PYCGLGFALW CLCSVYSGHQ SVLIPPMELE NNLFLWLSTV NQYKIRDTFC SYSVMELCTK 1260
GLGNQVEVLK TRGINLSCVR TCVVVAEERP RVALQQSFSK LFKDIGLSPR AVSTTFGSRV 1320
NVAICLQGTS GPDPTTVYVD LKSLRHDRVR LVERGAPQSL LLSESGKILP GVKVVIVNPE 1380
TKGPVGDSHL GEIWVNSPHT ASGYYTIYDS ETLQADHFNT RLSFGDAAQT LWARTGYLGF 1440
VRRTELTAAT GERHDALYVV GALDETLELR GLRYHPIDIE TSVSRIHRSI AECAVFTWTN 1500
LLVVVVELCG SEQEALDLVP LVTNVVLEEH YLIVGVVVVV DPGVIPINSR GEKQRMHLRD 1560
SFLADQLDPI YVAYNM 1576 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0003824; F:catalytic activity; IEA:InterPro. 
Interpro
 IPR000873; AMP-dep_Synth/Lig.
 IPR010506; DMAP1-bd. 
Pfam
 PF00501; AMP-binding
 PF06464; DMAP_binding 
SMART
  
PROSITE
  
PRINTS