CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019524
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein 14 
Protein Synonyms/Alias
 Paraspeckle protein 2; PSP2; RNA-binding motif protein 14; RRM-containing coactivator activator/modulator; Synaptotagmin-interacting protein; SYT-interacting protein 
Gene Name
 RBM14 
Gene Synonyms/Alias
 SIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112VIECDVVKDYAFVHMubiquitination[1, 2, 3]
121YAFVHMEKEADAKAAubiquitination[2]
126MEKEADAKAAIAQLNubiquitination[1, 2, 3, 4, 5]
135AIAQLNGKEVKGKRIacetylation[3, 6, 7]
135AIAQLNGKEVKGKRIubiquitination[1, 2, 3, 4]
149INVELSTKGQKKGPGubiquitination[1, 2, 3, 5]
153LSTKGQKKGPGLAVQubiquitination[2]
164LAVQSGDKTKKPGAGacetylation[3]
164LAVQSGDKTKKPGAGubiquitination[3]
594SYDDPYKKAVAMSKRubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] 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
 Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1. 
Sequence Annotation
 DOMAIN 1 73 RRM 1.
 DOMAIN 79 149 RRM 2.
 REGION 307 354 TRBP-interacting domain.
 MOD_RES 161 161 Phosphoserine.
 MOD_RES 206 206 Phosphothreonine.
 MOD_RES 220 220 Phosphoserine.
 MOD_RES 256 256 Phosphoserine.
 MOD_RES 520 520 Phosphoserine (By similarity).
 MOD_RES 562 562 Phosphoserine.
 MOD_RES 572 572 Phosphothreonine.
 MOD_RES 582 582 Phosphoserine (By similarity).
 MOD_RES 618 618 Phosphoserine.
 MOD_RES 629 629 Phosphothreonine (By similarity).
 MOD_RES 632 632 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 669 AA 
Protein Sequence
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR AIEALHGHEL 60
RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME 120
KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG 180
FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ 240
PSVSLGAAYR AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS 300
SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA 360
AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYNAQPSASY NAQSAPYAAQ 420
QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASM 480
GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY 540
RGQPGNAYDG AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK 600
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ 660
MHSGYQRRM 669 
Gene Ontology
 GO:0016592; C:mediator complex; NAS:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; TAS:UniProtKB.
 GO:0005667; C:transcription factor complex; IPI:UniProtKB.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IPI:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0001104; F:RNA polymerase II transcription cofactor activity; NAS:UniProtKB.
 GO:0006310; P:DNA recombination; NAS:UniProtKB.
 GO:0006281; P:DNA repair; NAS:UniProtKB.
 GO:0006260; P:DNA replication; NAS:UniProtKB.
 GO:0042921; P:glucocorticoid receptor signaling pathway; NAS:UniProtKB.
 GO:0016575; P:histone deacetylation; IPI:UniProtKB.
 GO:0030520; P:intracellular estrogen receptor signaling pathway; NAS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0009725; P:response to hormone stimulus; TAS:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS