CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007678
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ran-specific GTPase-activating protein 
Protein Synonyms/Alias
 Ran-binding protein 1; RanBP1 
Gene Name
 RANBP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50EDEEELFKMRAKLFRubiquitination[1]
68ENDLPEWKERGTGDVubiquitination[1, 2, 3, 4, 5]
76ERGTGDVKLLKHKEKubiquitination[1, 2, 4, 5]
111ITPMMELKPNAGSDRacetylation[6]
111ITPMMELKPNAGSDRubiquitination[1, 3]
134DFADECPKPELLAIRacetylation[6]
134DFADECPKPELLAIRubiquitination[1, 2, 5]
150LNAENAQKFKTKFEEacetylation[7]
150LNAENAQKFKTKFEEubiquitination[1, 2, 3, 4, 5]
152AENAQKFKTKFEECRacetylation[6]
154NAQKFKTKFEECRKEubiquitination[1]
183HAEKVAEKLEALSVKacetylation[7]
183HAEKVAEKLEALSVKubiquitination[1, 2, 3, 4, 5, 8]
190KLEALSVKEETKEDAubiquitination[3]
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] 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]
 [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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] 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]
 [8] 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
 Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane. 
Sequence Annotation
 DOMAIN 26 164 RanBD1.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 13 13 Phosphothreonine.
 MOD_RES 18 18 Phosphothreonine.
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 150 150 N6-acetyllysine.
 MOD_RES 183 183 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; GTPase activation; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 201 AA 
Protein Sequence
MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS 60
ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW 120
VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKAG SGKNDHAEKV 180
AEKLEALSVK EETKEDAEEK Q 201 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005635; C:nuclear envelope; TAS:Reactome.
 GO:0005092; F:GDP-dissociation inhibitor activity; TAS:ProtInc.
 GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
 GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
 GO:0046907; P:intracellular transport; IEA:InterPro.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0046604; P:positive regulation of mitotic centrosome separation; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:UniProtKB.
 GO:0007051; P:spindle organization; IEA:Compara.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR011993; PH_like_dom.
 IPR000156; Ran_bind_dom. 
Pfam
 PF00638; Ran_BP1 
SMART
 SM00160; RanBD 
PROSITE
 PS50196; RANBD1 
PRINTS