CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022981
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prenylated Rab acceptor protein 1 
Protein Synonyms/Alias
 PRA1 family protein 1 
Gene Name
 RABAC1 
Gene Synonyms/Alias
 PRA1; PRAF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAAQKDQQKDAEubiquitination[1]
9AAQKDQQKDAEAEGLubiquitination[2, 3, 4, 5]
24SGTTLLPKLIPSGAGubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
118YLRTLESKLVLFGREubiquitination[2, 3, 4, 5, 7, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] 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]
 [8] 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]
 [9] 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
Functional Description
 General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI (By similarity). 
Sequence Annotation
 REGION 30 54 Required for interaction with prenylated
 REGION 165 185 Required for interaction with GDI1 (By
 REGION 175 185 Homodimerization (By similarity).
 REGION 175 185 Required for interaction with prenylated  
Keyword
 Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane; Reference proteome; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 185 AA 
Protein Sequence
MAAQKDQQKD AEAEGLSGTT LLPKLIPSGA GREWLERRRA TIRPWSTFVD QQRFSRPRNL 60
GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLESKLV 120
LFGREVSPAH QYALAGGISF PFFWLAGAGS AVFWVLGATL VVIGSHAAFH QIEAVDGEEL 180
QMEPV 185 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell. 
Interpro
 IPR004895; Prenylated_rab_accept_PRA1. 
Pfam
 PF03208; PRA1 
SMART
  
PROSITE
  
PRINTS