CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014474
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydropyrimidinase-related protein 1 
Protein Synonyms/Alias
 DRP-1; Collapsin response mediator protein 1; CRMP-1 
Gene Name
 Crmp1 
Gene Synonyms/Alias
 Dpysl1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
7*MSHQGKKSIPHITSubiquitination[1]
56LIVPGGVKTIEANGRacetylation[2]
56LIVPGGVKTIEANGRubiquitination[1]
293DGTHYWSKNWAKAAAacetylation[2]
345TAQKAVGKDNFTLIPacetylation[2]
345TAQKAVGKDNFTLIPubiquitination[1]
423KMKTLTAKSHKSTVEubiquitination[1]
463DGNISVSKGMGRFIPacetylation[2]
463DGNISVSKGMGRFIPubiquitination[1]
472MGRFIPRKPFPEHLYubiquitination[1]
487QRVRIRSKVFGLHSVubiquitination[1]
511YEVPATPKHAAPAPSubiquitination[1]
520AAPAPSAKSSPSKHQubiquitination[1]
525SAKSSPSKHQPPPIRubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration (By similarity). 
Sequence Annotation
 MOD_RES 316 316 Nitrated tyrosine (By similarity).
 MOD_RES 431 431 Phosphotyrosine (By similarity).
 MOD_RES 504 504 Phosphotyrosine (By similarity).
 MOD_RES 509 509 Phosphothreonine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; Nitration; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 572 AA 
Protein Sequence
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA 60
NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTRAALAGG TTMIIDHVVP EPGSSLLTSF 120
EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ 180
LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI 240
AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 300
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE 360
RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTL 420
TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ 480
RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS 540
LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG 572 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0043231; C:intracellular membrane-bounded organelle; IEA:Compara.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
 GO:0048666; P:neuron development; IEP:RGD.
 GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro. 
Interpro
 IPR006680; Amidohydro_1.
 IPR011778; Hydantoinase/dihydroPyrase.
 IPR011059; Metal-dep_hydrolase_composite. 
Pfam
 PF01979; Amidohydro_1 
SMART
  
PROSITE
  
PRINTS