CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022250
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pre-mRNA-splicing factor RBM22 
Protein Synonyms/Alias
 RNA-binding motif protein 22; Zinc finger CCCH domain-containing protein 16 
Gene Name
 RBM22 
Gene Synonyms/Alias
 ZC3H16; 199G4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76EVCQTCSKLKNVCQTubiquitination[1]
78CQTCSKLKNVCQTCLubiquitination[1, 2]
104RDAGLSFKDDMPKSDubiquitination[1]
114MPKSDVNKEYYTQNMubiquitination[1, 3, 4, 5]
139RPVGMLGKATSTSDMubiquitination[1]
149STSDMLLKLARTTPYubiquitination[1]
170HICSFWVKGECKRGEubiquitination[1]
212INDPVADKLLKRASTacetylation[6]
212INDPVADKLLKRASTubiquitination[3, 5]
286AAEVAAEKSFNKLIVubiquitination[1]
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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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] 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] 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] 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] 
Functional Description
 Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses. 
Sequence Annotation
 DOMAIN 232 305 RRM.
 ZN_FING 159 186 C3H1-type.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 212 212 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding; Spliceosome; Transport; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 420 AA 
Protein Sequence
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG 60
VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN 120
MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP 180
YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG 240
DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV 300
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV 360
VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP 420 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005487; F:nucleocytoplasmic transporter activity; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
 GO:0017069; F:snRNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0033554; P:cellular response to stress; IDA:UniProtKB.
 GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
 GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
 GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
 GO:0000060; P:protein import into nucleus, translocation; IDA:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR000571; Znf_CCCH. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM
 SM00356; ZnF_C3H1 
PROSITE
 PS50102; RRM
 PS50103; ZF_C3H1 
PRINTS