CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012184
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras and Rab interactor 1 
Protein Synonyms/Alias
 Ras inhibitor JC99; Ras interaction/interference protein 1 
Gene Name
 RIN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29TGHLAREKPAQDPLYubiquitination[1, 2]
237PGDLGPTKREKFKRSubiquitination[3]
513YSPSAQVKRLLQACKubiquitination[1]
662LNQLCATKFRVTQPNubiquitination[3]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis. 
Sequence Annotation
 DOMAIN 69 163 SH2.
 DOMAIN 456 598 VPS9.
 DOMAIN 624 706 Ras-associating.
 REGION 294 727 Ras and 14-3-3 protein binding region.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 36 36 Phosphotyrosine; by ABL1 and ABL2.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 258 258 Phosphoserine.
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 351 351 Phosphoserine; by PKD/PRKD1.
 MOD_RES 601 601 Phosphoserine (By similarity).
 MOD_RES 609 609 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; GTPase activation; Membrane; Phosphoprotein; Reference proteome; SH2 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 783 AA 
Protein Sequence
MESPGESGAG SPGAPSPSSF TTGHLAREKP AQDPLYDVPN ASGGQAGGPQ RPGRVVSLRE 60
RLLLTRPVWL QLQANAAAAL HMLRTEPPGT FLVRKSNTRQ CQALCMRLPE ASGPSFVSSH 120
YILESPGGVS LEGSELMFPD LVQLICAYCH TRDILLLPLQ LPRAIHHAAT HKELEAISHL 180
GIEFWSSSLN IKAQRGPAGG PVLPQLKARS PQELDQGTGA ALCFFNPLFP GDLGPTKREK 240
FKRSFKVRVS TETSSPLSPP AVPPPPVPVL PGAVPSQTER LPPCQLLRRE SSVGYRVPAG 300
SGPSLPPMPS LQEVDCGSPS SSEEEGVPGS RGSPATSPHL GRRRPLLRSM SAAFCSLLAP 360
ERQVGRAAAA LMQDRHTAAG QLVQDLLTQV RAGPEPQELQ GIRQALSRAR AMLSAELGPE 420
KLLSPKRLEH VLEKSLHCSV LKPLRPILAA RLRRRLAADG SLGRLAEGLR LARAQGPGAF 480
GSHLSLPSPV ELEQVRQKLL QLLRTYSPSA QVKRLLQACK LLYMALRTQE GEGAGADEFL 540
PLLSLVLAHC DLPELLLEAE YMSELLEPSL LTGEGGYYLT SLSASLALLS GLGQAHTLPL 600
SPVQELRRSL SLWEQRRLPA THCFQHLLRV AYQDPSSGCT SKTLAVPPEA SIATLNQLCA 660
TKFRVTQPNT FGLFLYKEQG YHRLPPGALA HRLPTTGYLV YRRAEWPETQ GAVTEEEGSG 720
QSEARSRGEE QGCQGDGDAG VKASPRDIRE QSETTAEGGQ GQAQEGPAQP GEPEAEGSRA 780
AEE 783 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR000159; Ras-assoc.
 IPR000980; SH2.
 IPR003123; VPS9.
 IPR013995; VPS9_subgr. 
Pfam
 PF00788; RA
 PF02204; VPS9 
SMART
 SM00314; RA
 SM00252; SH2
 SM00167; VPS9 
PROSITE
 PS50200; RA
 PS50001; SH2
 PS51205; VPS9 
PRINTS