CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019625
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ran-binding protein 9 
Protein Synonyms/Alias
 RanBP9; BPM-L; BPM90; Ran-binding protein M; RanBPM; RanBP7 
Gene Name
 RANBP9 
Gene Synonyms/Alias
 RANBPM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
174RSWSPKDKFSYIGLSubiquitination[1]
197KGHGKTPKDAASVRAubiquitination[2]
348YMREWRTKIQAQIDRubiquitination[1]
405LEELASIKNRQRIQKacetylation[3]
405LEELASIKNRQRIQKubiquitination[1, 4, 5]
412KNRQRIQKLVLAGRMubiquitination[1]
445PNLLFTLKVRQFIEMubiquitination[1, 6, 7]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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]
 [7] 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
 May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity). 
Sequence Annotation
 DOMAIN 147 334 B30.2/SPRY.
 DOMAIN 365 397 LisH.
 DOMAIN 403 460 CTLH.
 REGION 401 407 Interaction with CALB1 (Probable).
 REGION 615 729 Interaction with FMR1.
 MOD_RES 405 405 N6-acetyllysine.
 MOD_RES 487 487 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 729 AA 
Protein Sequence
MSGQPPPPPP QQQQQQQQLS PPPPAALAPV SGVVLPAPPA VSAGSSPAGS PGGGAGGEGL 60
GAAAAALLLH PPPPPPPATA APPPPPPPPP PPASAAAPAS GPPAPPGLAA GPGPAGGAPT 120
PALVAGSSAA APFPHGDSAL NEQEKELQRR LKRLYPAVDE QETPLPRSWS PKDKFSYIGL 180
SQNNLRVHYK GHGKTPKDAA SVRATHPIPA ACGIYYFEVK IVSKGRDGYM GIGLSAQGVN 240
MNRLPGWDKH SYGYHGDDGH SFCSSGTGQP YGPTFTTGDV IGCCVNLINN TCFYTKNGHS 300
LGIAFTDLPP NLYPTVGLQT PGEVVDANFG QHPFVFDIED YMREWRTKIQ AQIDRFPIGD 360
REGEWQTMIQ KMVSSYLVHH GYCATAEAFA RSTDQTVLEE LASIKNRQRI QKLVLAGRMG 420
EAIETTQQLY PSLLERNPNL LFTLKVRQFI EMVNGTDSEV RCLGGRSPKS QDSYPVSPRP 480
FSSPSMSPSH GMNIHNLASG KGSTAHFSGF ESCSNGVISN KAHQSYCHSN KHQSSNLNVP 540
ELNSINMSRS QQVNNFTSND VDMETDHYSN GVGETSSNGF LNGSSKHDHE MEDCDTEMEV 600
DSSQLRRQLC GGSQAAIERM IHFGRELQAM SEQLRRDCGK NTANKKMLKD AFSLLAYSDP 660
WNSPVGNQLD PIQREPVCSA LNSAILETHN LPKQPPLALA MGQATQCLGL MARSGIGSCA 720
FATVEDYLH 729 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005875; C:microtubule associated complex; TAS:ProtInc.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007020; P:microtubule nucleation; NAS:UniProtKB.
 GO:0006461; P:protein complex assembly; TAS:ProtInc. 
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