CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015442
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ran-binding protein 10 
Protein Synonyms/Alias
 RanBP10 
Gene Name
 Ranbp10 
Gene Synonyms/Alias
 Kiaa1464 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
62RSWSPKDKYNYIGLSubiquitination[1]
293QEEQASIKNRQKIQKacetylation[2]
293QEEQASIKNRQKIQKubiquitination[1]
357SLSSRSPKSQDSYPGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function. 
Sequence Annotation
 DOMAIN 35 222 B30.2/SPRY.
 DOMAIN 253 285 LisH.
 DOMAIN 291 348 CTLH.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 369 369 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 620 AA 
Protein Sequence
MAAATADPGA GNPQAGDSSG GDSGGGLPSP GEQELSRRLQ RLYPAVNQHE TPLPRSWSPK 60
DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI 120
GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC 180
FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT 240
VHGFPISARL GEWQAVLQNM VSSYLVHHGY CSTATAFARM TETPIQEEQA SIKNRQKIQK 300
LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD 360
SYPGSPSLSP RHGPSSSHIH NTGADSPSCS NGVASTKNKQ NHSKYPAPSS SSSSSSSSSS 420
SSPSSVNYSE SNSTDSTKSQ PHSSTSNQET SDSEMEMEAE HYPNGVLESV STRIVNGAYK 480
HDDLQTDESS MDDGHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ 540
DAFSLLAYSD PWSCPVGHQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR 600
LMARAGLGSC SFARVDDYLH 620 
Gene Ontology
 GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048487; F:beta-tubulin binding; IDA:MGI.
 GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI.
 GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013144; CRA_dom.
 IPR024964; CTLH/CRA.
 IPR006595; CTLH_C.
 IPR006594; LisH_dimerisation.
 IPR013720; LisH_dimerisation_subgr.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt. 
Pfam
 PF10607; CLTH
 PF08513; LisH
 PF00622; SPRY 
SMART
 SM00757; CRA
 SM00668; CTLH
 SM00667; LisH
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS50897; CTLH
 PS50896; LISH 
PRINTS