CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007772
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ran GTPase-activating protein 1 
Protein Synonyms/Alias
 RanGAP1 
Gene Name
 RANGAP1 
Gene Synonyms/Alias
 KIAA1835; SD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MASEDIAKLAETLAKsumoylation[1]
8MASEDIAKLAETLAKubiquitination[2]
15KLAETLAKTQVAGGQubiquitination[3]
28GQLSFKGKSLKLNTAubiquitination[2]
43EDAKDVIKEIEDFDSubiquitination[4]
71EAARVIAKALEKKSEubiquitination[2]
148CFTLQELKLNNCGMGubiquitination[2]
183QGKPLALKVFVAGRNubiquitination[2]
251NDNTFTEKGAVAMAEubiquitination[2, 4]
261VAMAETLKTLRQVEVubiquitination[2]
279GDCLVRSKGAVAIADubiquitination[2]
296RGGLPKLKELNLSFCubiquitination[2, 5, 6]
306NLSFCEIKRDAALAVubiquitination[2]
452KLLRLGPKSSVLIAQubiquitination[2, 3, 4, 5, 6, 7, 8]
481LKVSSVFKDEATVRMubiquitination[2]
524LVHMGLLKSEDKVKAacetylation[9]
524LVHMGLLKSEDKVKAsumoylation[1, 10, 11, 12, 13]
524LVHMGLLKSEDKVKAubiquitination[2, 4, 5, 6, 8]
Reference
 [1] In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.
 Blomster HA, Imanishi SY, Siimes J, Kastu J, Morrice NA, Eriksson JE, Sistonen L.
 J Biol Chem. 2010 Jun 18;285(25):19324-9. [PMID: 20388717]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [10] Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1.
 Macauley MS, Errington WJ, Okon M, Schärpf M, Mackereth CD, Schulman BA, McIntosh LP.
 J Biol Chem. 2004 Nov 19;279(47):49131-7. [PMID: 15355965]
 [11] Chip-based analysis of SUMO (small ubiquitin-like modifier) conjugation to a target protein.
 Oh YH, Hong MY, Jin Z, Lee T, Han MK, Park S, Kim HS.
 Biosens Bioelectron. 2007 Feb 15;22(7):1260-7. [PMID: 16820290]
 [12] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [13] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026
Functional Description
 GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. 
Sequence Annotation
 REPEAT 48 71 LRR 1.
 REPEAT 111 134 LRR 2.
 REPEAT 207 230 LRR 3.
 REPEAT 235 258 LRR 4.
 REPEAT 292 319 LRR 5.
 REPEAT 320 343 LRR 6.
 MOTIF 523 526 SUMO conjugation.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 409 409 Phosphothreonine; by CDK2.
 MOD_RES 428 428 Phosphoserine.
 MOD_RES 435 435 Phosphoserine.
 MOD_RES 436 436 Phosphothreonine.
 MOD_RES 442 442 Phosphoserine.
 MOD_RES 524 524 N6-acetyllysine; alternate.
 CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 524 524 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTPase activation; Isopeptide bond; Kinetochore; Leucine-rich repeat; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 587 AA 
Protein Sequence
MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS LEALRLEGNT 60
VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL ISLGEGLITA GAQLVELDLS 120
DNAFGPDGVQ GFEALLKSSA CFTLQELKLN NCGMGIGGGK ILAAALTECH RKSSAQGKPL 180
ALKVFVAGRN RLENDGATAL AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV 240
INLNDNTFTE KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL 300
SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM AKVLASLSDD 360
EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ RGQGEKSATP SRKILDPNTG 420
EPAPVLSSPP PADVSTFLAF PSPEKLLRLG PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF 480
KDEATVRMAV QDAVDALMQK AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM 540
ALNHMVQQDY FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV 587 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; TAS:ProtInc.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0005098; F:Ran GTPase activator activity; TAS:ProtInc.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0046826; P:negative regulation of protein export from nucleus; IDA:BHF-UCL.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR009109; Ran_GTPase_activating_1_C.
 IPR027038; RanGap. 
Pfam
 PF07834; RanGAP1_C 
SMART
  
PROSITE
  
PRINTS