CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014476
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydropyrimidinase-related protein 3 
Protein Synonyms/Alias
 DRP-3; Collapsin response mediator protein 4; CRMP-4; TOAD-64/Ulip/CRMP; TUC-4b 
Gene Name
 Dpysl3 
Gene Synonyms/Alias
 Crmp4 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
56LIVPGGVKTIEANGKacetylation[1]
157QEVQNLSKEKGVNSFacetylation[1]
157QEVQNLSKEKGVNSFubiquitination[2]
345TAQKAIGKDNFTAIPacetylation[1]
345TAQKAIGKDNFTAIPubiquitination[2]
487KRIKARRKMADLHAVubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration. 
Sequence Annotation
 MOD_RES 259 259 Phosphoserine (By similarity).
 MOD_RES 499 499 Phosphotyrosine (By similarity).
 MOD_RES 509 509 Phosphothreonine; by GSK3 (By
 MOD_RES 514 514 Phosphothreonine; by GSK3 (By
 MOD_RES 518 518 Phosphoserine; by GSK3 (By similarity).
 MOD_RES 522 522 Phosphoserine; by DYRK2 (By similarity).
 MOD_RES 541 541 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Cell projection; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 570 AA 
Protein Sequence
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA 60
NGKMVMPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY 120
EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQNLSKEKG VNSFMVYMAY KDLYQVSNTE 180
LYEIFTCLGE LGAIAQVHAE NGDIIAQEQA RMLEMGITGP EGHVLSRPEE LEAEAVFRAI 240
TVASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA 300
FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE 360
RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDAVKIV 420
SAKNHQSVAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK 480
RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSTR GSPTRPNPPV RNLHQSGFSL 540
SGTQVDEGVR SASKRIVAPP GGRSNITSLS 570 
Gene Ontology
 GO:0044297; C:cell body; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0031941; C:filamentous actin; IDA:UniProtKB.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0035374; F:chondroitin sulfate binding; IDA:RGD.
 GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
 GO:0017124; F:SH3 domain binding; IDA:RGD.
 GO:0051764; P:actin crosslink formation; IDA:UniProtKB.
 GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
 GO:0071345; P:cellular response to cytokine stimulus; IEP:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
 GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
 GO:0048666; P:neuron development; IEP:RGD.
 GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
 GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro.
 GO:0048678; P:response to axon injury; IEP:UniProtKB. 
Interpro
 IPR006680; Amidohydro_1.
 IPR011778; Hydantoinase/dihydroPyrase.
 IPR011059; Metal-dep_hydrolase_composite. 
Pfam
 PF01979; Amidohydro_1 
SMART
  
PROSITE
  
PRINTS