CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022180
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TBC1 domain family member 23 
Protein Synonyms/Alias
 HCV non-structural protein 4A-transactivated protein 1 
Gene Name
 TBC1D23 
Gene Synonyms/Alias
 NS4ATP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
489GMKSLVNKMTVALKTubiquitination[1]
495NKMTVALKTKSVNVRubiquitination[2]
504KSVNVREKVISFIENubiquitination[1, 2]
648VVKITSKKKHPELITubiquitination[3]
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] 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]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048
Functional Description
  
Sequence Annotation
 DOMAIN 44 225 Rab-GAP TBC.
 DOMAIN 334 446 Rhodanese.
 MOD_RES 474 474 Phosphoserine.
 MOD_RES 507 507 Phosphoserine.
 MOD_RES 514 514 Phosphothreonine.  
Keyword
 Alternative splicing; Complete proteome; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 699 AA 
Protein Sequence
MAEGEDVPPL PTSSGDGWEK DLEEALEAGG CDLETLRNII QGRPLPADLR AKVWKIALNV 60
AGKGDSLASW DGILDLPEQN TIHKDCLQFI DQLSVPEEKA AELLLDIESV ITFYCKSRNI 120
KYSTSLSWIH LLKPLVHLQL PRSDLYNCFY AIMNKYIPRD CSQKGRPFHL FRLLIQYHEP 180
ELCSYLDTKK ITPDSYALNW LGSLFACYCS TEVTQAIWDG YLQQADPFFI YFLMLIILVN 240
AKEVILTQES DSKEEVIKFL ENTPSSLNIE DIEDLFSLAQ YYCSKTPASF RKDNHHLFGS 300
TLLGIKDDDA DLSQALCLAI SVSEILQANQ LQGEGVRFFV VDCRPAEQYN AGHLSTAFHL 360
DSDLMLQNPS EFAQSVKSLL EAQKQSIESG SIAGGEHLCF MGSGREEEDM YMNMVLAHFL 420
QKNKEYVSIA SGGFMALQQH LADINVDGPE NGYGHWIAST SGSRSSINSV DGESPNGSSD 480
RGMKSLVNKM TVALKTKSVN VREKVISFIE NTSTPVDRMS FNLPWPDRSC TERHVSSSDR 540
VGKPYRGVKP VFSIGDEEEY DTDEIDSSSM SDDDRKEVVN IQTWINKPDV KHHFPCKEVK 600
ESGHMFPSHL LVTATHMYCL REIVSRKGLA YIQSRQALNS VVKITSKKKH PELITFKYGN 660
SSASGIEILA IERYLIPNAG DATKAIKQQI MKVLDALES 699 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
 GO:0032851; P:positive regulation of Rab GTPase activity; IEA:GOC. 
Interpro
 IPR000195; Rab-GTPase-TBC_dom.
 IPR001763; Rhodanese-like_dom. 
Pfam
 PF00566; RabGAP-TBC
 PF00581; Rhodanese 
SMART
 SM00164; TBC 
PROSITE
 PS50206; RHODANESE_3
 PS50086; TBC_RABGAP 
PRINTS