CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012704
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Drebrin 
Protein Synonyms/Alias
 Developmentally-regulated brain protein 
Gene Name
 DBN1 
Gene Synonyms/Alias
 D0S117E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
62SGHFENQKVMYGFCSubiquitination[1]
71MYGFCSVKDSQAALPubiquitination[1, 2]
295DNPREFFKQQERVASubiquitination[1]
Reference
 [1] 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]
 [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] 
Functional Description
 Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites, respectively. 
Sequence Annotation
 DOMAIN 3 134 ADF-H.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 134 134 Phosphoserine (By similarity).
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 142 142 Phosphoserine.
 MOD_RES 331 331 Phosphothreonine.
 MOD_RES 335 335 Phosphothreonine.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 342 342 Phosphoserine (By similarity).
 MOD_RES 346 346 Phosphothreonine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 649 AA 
Protein Sequence
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN 60
QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS 120
VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF 180
WEQAKKEEEL RKEEERKKAL DERLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ 240
TLEAEEAKRR LKEQSIFGDH RDEEEETHMK KSESEVEEAA AIIAQRPDNP REFFKQQERV 300
ASASAGSCDV PSPFNHRPGS HLDSHRRMAP TPIPTRSPSD SSTASTPVAE QIERALDEVT 360
SSQPPPLPPP PPPAQETQEP SPILDSEETR AAAPQAWAGP MEEPPQAQAP PRGPGSPAED 420
LMFMESAEQA VLAAPVEPAT ADATEIHDAA DTIETDTATA DTTVANNVPP AATSLIDLWP 480
GNGEGASTLQ GEPRAPTPPS GTEVTLAEVP LLDEVAPEPL LPAGEGCATL LNFDELPEPP 540
ATFCDPEEVE GESLAAPQTP TLPSALEELE QEQEPEPHLL TNGETTQKEG TQASEGYFSQ 600
SQEEEFAQSE ELCAKAPPPV FYNKPPEIDI TCWDADPVPE EEEGFEGGD 649 
Gene Ontology
 GO:0042641; C:actomyosin; NAS:UniProtKB.
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0030425; C:dendrite; NAS:UniProtKB.
 GO:0005921; C:gap junction; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0005522; F:profilin binding; ISS:UniProtKB.
 GO:0007015; P:actin filament organization; ISS:UniProtKB.
 GO:0010643; P:cell communication by chemical coupling; IEA:Compara.
 GO:0010644; P:cell communication by electrical coupling; IEA:Compara.
 GO:0032507; P:maintenance of protein location in cell; IEA:Compara.
 GO:0061351; P:neural precursor cell proliferation; IEA:Compara.
 GO:0050773; P:regulation of dendrite development; NAS:UniProtKB.
 GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:UniProtKB. 
Interpro
 IPR002108; Actin-bd_cofilin/tropomyosin. 
Pfam
 PF00241; Cofilin_ADF 
SMART
 SM00102; ADF 
PROSITE
 PS51263; ADF_H 
PRINTS