CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021458
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ran-binding protein 3 
Protein Synonyms/Alias
 RanBP3 
Gene Name
 RANBP3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21PPVFVFQKDKGQKSPacetylation[1]
21PPVFVFQKDKGQKSPubiquitination[2]
23VFVFQKDKGQKSPAEubiquitination[2]
413CKLFVFDKTSQSWVEubiquitination[3, 4]
Reference
 [1] 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]
 [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] 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]
 [4] 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] 
Functional Description
 Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF- beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. 
Sequence Annotation
 DOMAIN 378 518 RanBD1.
 MOD_RES 21 21 N6-acetyllysine.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 108 108 Phosphoserine.
 MOD_RES 115 115 Phosphotyrosine (By similarity).
 MOD_RES 124 124 Phosphothreonine.
 MOD_RES 219 219 Phosphoserine (By similarity).
 MOD_RES 221 221 Phosphoserine (By similarity).
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 353 353 Phosphoserine.
 MOD_RES 355 355 Phosphoserine.
 MOD_RES 539 539 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 567 AA 
Protein Sequence
MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE 60
HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK 120
RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP 180
QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES 240
SNASEEEACE KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL 300
QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA AESGSESSSQ 360
EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN VLQMQCKLFV FDKTSQSWVE 420
RGRGLLRLND MASTDDGTLQ SRLVMRTQGS LRLILNTKLW AQMQIDKASE KSIRITAMDT 480
EDQGVKVFLI SASSKDTGQL YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD 540
DDDVLAPSGA TAAGAGDEGD GQTTGST 567 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:LIFEdb.
 GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
 GO:0046907; P:intracellular transport; IEA:InterPro.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR011993; PH_like_dom.
 IPR000156; Ran_bind_dom. 
Pfam
 PF00638; Ran_BP1 
SMART
 SM00160; RanBD 
PROSITE
 PS50196; RANBD1 
PRINTS