UniProt Accession

 RBMX_HUMAN; P38159; B4E3U4; D3DWH0; E9PG86; Q5JQ67; Q8N8Y7; Q969R3 

Genbank Protein ID

 Z23064; AF266723; AF266720; AF266721; AF266722; AY464692; AK096015; AK304868; AL683813; CH471150; CH471150; CH471150; CH471150; BC006550; BC007435 

Genbank Nucleotide ID

 CAA80599.1; AAK58567.1; AAK58567.1; AAK58567.1; AAK58567.1; AAR28036.1; BAC04674.1; BAG65606.1; CAI39448.1; EAW88453.1; EAW88454.1; EAW88455.1; EAW88457.1; AAH06550.1; AAH07435.1 

Protein Name

 RNA-binding motif protein, X chromosome 

Protein Synonyms/Alias

 Glycoprotein p43; Heterogeneous nuclear ribonucleoprotein G; hnRNP G; RNA-binding motif protein, X chromosome, N-terminally processed 

Gene Name

 RBMX 

Gene Synonyms/Alias

 HNRPG; RBMXP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	VEADRPGKLFIGGLN	ubiquitination	[1, 2, 3]
22	LNTETNEKALEAVFG	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
30	ALEAVFGKYGRIVEV	acetylation	[10]
30	ALEAVFGKYGRIVEV	ubiquitination	[1, 2, 3, 5, 6, 7]
41	IVEVLLMKDRETNKS	ubiquitination	[1]
63	FESPADAKDAARDMN	ubiquitination	[2, 7, 9]
86	IKVEQATKPSFESGR	ubiquitination	[2]
150	SRGPLPVKRGPPPRS	ubiquitination	[2, 9]
217	RDDGYSTKDSYSSRD	ubiquitination	[1, 2, 7, 9]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [4] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] 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]
 [8] 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]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] 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

 RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single- stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1- beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. 

Sequence Annotation

 DOMAIN 8 86 RRM.
 REGION 186 236 Necessary for the association to nascent
 REGION 333 391 Necessary for RNA-binding.
 MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
 MOD_RES 2 2 N-acetylvaline; in Heterogeneous nuclear
 MOD_RES 30 30 N6-acetyllysine.
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 168 168 Phosphoserine (By similarity).
 MOD_RES 208 208 Phosphoserine (By similarity).
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 332 332 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.  

Keyword

 Acetylation; Activator; Alternative splicing; Complete proteome; Direct protein sequencing; Glycoprotein; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome; Transcription; Tumor suppressor. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 391 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0001047; F:core promoter binding; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
 GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR012604; RBM1CTR.
 IPR000504; RRM_dom. 

Pfam

 PF08081; RBM1CTR
 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS