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P38159 (RBMX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding motif protein, X chromosome
Alternative name(s):
Glycoprotein p43
Heterogeneous nuclear ribonucleoprotein G
Short name=hnRNP G
Gene names
Name:RBMX
Synonyms:HNRPG, RBMXP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.20 Ref.23

Subunit structure

Homomultimer. Interacts with SAFB/SAFB1 By similarity. Found in the supraspliceosome complex. Identified in the spliceosome C complex. Interacts with KHDRBS3. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-independent. Ref.10 Ref.11 Ref.12 Ref.16 Ref.17 Ref.20

Subcellular location

Nucleus. Note: Component of ribonucleosomes. Localizes in numerous small granules in the nucleus. Ref.20 Ref.23

Tissue specificity

Expressed strongly in oral keratinocytes, but only weakly detected in oral squamous cell carcinomas (at protein level). Ref.15

Domain

The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA By similarity.

Post-translational modification

O-glycosylated. Ref.1

Arg-185 is dimethylated, probably to asymmetric dimethylarginine.

Cleavage of initiator Met is partial. If Met-1 is not removed, it is acetylated. If it is removed, Val-2 is acetylated. Ref.9

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   LigandRNA-binding
   Molecular functionActivator
Repressor
Ribonucleoprotein
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

cellular response to interleukin-1

Inferred from direct assay Ref.17. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA splice site selection

Inferred from electronic annotation. Source: Ensembl

mRNA splicing, via spliceosome

Inferred by curator Ref.11. Source: UniProtKB

membrane protein ectodomain proteolysis

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

positive regulation of mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.18. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from direct assay Ref.12Ref.13. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.23. Source: UniProtKB

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.11. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay Ref.17. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

nuclear euchromatin

Inferred from direct assay Ref.23. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.20. Source: UniProtKB

ribonucleoprotein complex

Non-traceable author statement Ref.1. Source: UniProtKB

supraspliceosomal complex

Inferred from direct assay Ref.20. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.23. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.18. Source: UniProtKB

core promoter binding

Inferred from direct assay Ref.18. Source: UniProtKB

mRNA binding

Inferred from direct assay Ref.12Ref.13. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.17. Source: UniProtKB

single-stranded RNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HNRNPKP619783EBI-743526,EBI-304185
KHDRBS2Q5VWX12EBI-743526,EBI-742808
Srek1Q9JKL73EBI-743526,EBI-6452221From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P38159-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P38159-2)

The sequence of this isoform differs from the canonical sequence as follows:
     45-57: Missing.
Isoform 3 (identifier: P38159-3)

The sequence of this isoform differs from the canonical sequence as follows:
     73-196: SLDGKAIKVE...RDSYGGPPRR → LLYHVEEIVM...YGRGVLIDSQ
     197-391: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391RNA-binding motif protein, X chromosome
PRO_0000081854
Initiator methionine11Removed; alternate Ref.9
Chain2 – 391390RNA-binding motif protein, X chromosome, N-terminally processed
PRO_0000304582

Regions

Domain8 – 8679RRM
Region186 – 23651Necessary for the association to nascent RNAPII transcripts and nuclear localization
Region333 – 39159Necessary for RNA-binding

Amino acid modifications

Modified residue11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate Ref.9
Modified residue21N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed Ref.9
Modified residue301N6-acetyllysine Ref.22
Modified residue881Phosphoserine Ref.14 Ref.19 Ref.21 Ref.24 Ref.26
Modified residue3291Phosphoserine Ref.19
Modified residue3321Phosphoserine Ref.19 Ref.26
Modified residue3521Phosphoserine Ref.24 Ref.26

Natural variations

Alternative sequence45 – 5713Missing in isoform 2.
VSP_042203
Alternative sequence73 – 196124SLDGK…GPPRR → LLYHVEEIVMEVHLEGNRCP LVEMFICPQEMMGILLKTAI QAEITQVLVILEIMHHHHEI ILTVIMVIPVHVMTIHQEDI AIEMDMVVIVTIQIIQVEVP TEIHMRVMVGDFAHYGRGVL IDSQ in isoform 3.
VSP_043650
Alternative sequence197 – 391195Missing in isoform 3.
VSP_043651

Experimental info

Mutagenesis221K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. Ref.15 Ref.18
Sequence conflict2591G → E in CAA80599. Ref.1

Secondary structure

................. 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2002. Version 3.
Checksum: 904FEB9BFC573546

FASTA39142,332
        10         20         30         40         50         60 
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA 

        70         80         90        100        110        120 
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGRGGSGGTR 

       130        140        150        160        170        180 
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR 

       190        200        210        220        230        240 
APVSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD 

       250        260        270        280        290        300 
YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP 

       310        320        330        340        350        360 
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP 

       370        380        390 
RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y 

« Hide

Isoform 2 [UniParc].

Checksum: 032DD488FA08CE19
Show »

FASTA37840,846
Isoform 3 [UniParc].

Checksum: 7FB2ABEE20A3D582
Show »

FASTA19622,172

References

« Hide 'large scale' references
[1]"hnRNP G: sequence and characterization of a glycosylated RNA-binding protein."
Soulard M., Della Valle V., Siomi M., Pinol-Roma S., Codogno P., Bauvy C., Belli M., Lacroix J.-C., Monod G., Dreyfuss G., Larsen C.-J.
Nucleic Acids Res. 21:4210-4217(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION.
Tissue: Mammary gland.
[2]Venables J.P., Larsen C.-J.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Expression and conservation of processed copies of the RBMX gene."
Lingenfelter P.A., Delbridge M.L., Thomas S., Hoekstra H.E., Mitchell M.J., Graves J.A., Disteche C.M.
Mamm. Genome 12:538-545(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]Lin T.-Y., Chiou S.-H.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Kidney and Uterus.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[9]Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-30; 34-41; 50-63; 81-93; 126-144; 188-195; 204-210; 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[10]"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis."
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.
Hum. Mol. Genet. 8:959-969(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KHDRBS3.
Tissue: Testis.
[11]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]"hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1."
Hofmann Y., Wirth B.
Hum. Mol. Genet. 11:2037-2049(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRA2B, RNA-BINDING.
[13]"HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism in RNA binding."
Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.
Hum. Mol. Genet. 12:1337-1348(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells."
Shin K.H., Kang M.K., Kim R.H., Christensen R., Park N.H.
Clin. Cancer Res. 12:3222-3228(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-22, TISSUE SPECIFICITY.
[16]"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; NCOA5 AND PPP1CA.
[17]"An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release."
Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.
Biochem. Biophys. Res. Commun. 371:505-509(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERAP1.
[18]"hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip."
Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.
Biochem. Biophys. Res. Commun. 372:880-885(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHROMATIN ASSOCIATION, MUTAGENESIS OF LYS-22.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-329 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA."
Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S.
J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX, INTERACTION WITH CLK2; KHDRBS2; SAFB; TRA2B AND YTHDC1, SUBCELLULAR LOCATION.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA binding and targeting nascent transcripts."
Kanhoush R., Beenders B., Perrin C., Moreau J., Bellini M., Penrad-Mobayed M.
Nucleus 1:109-122(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-332 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"NMR structure of the first RRM domain of the protein RBM39 from Homo sapiens."
Joint center for structural genomics (JCSG)
Submitted (MAR-2014) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z23064 mRNA. Translation: CAA80599.1.
AF266723 expand/collapse EMBL AC list , AF266720, AF266721, AF266722 Genomic DNA. Translation: AAK58567.1.
AY464692 mRNA. Translation: AAR28036.1.
AK096015 mRNA. Translation: BAC04674.1.
AK304868 mRNA. Translation: BAG65606.1.
AL683813 Genomic DNA. Translation: CAI39448.1.
CH471150 Genomic DNA. Translation: EAW88453.1.
CH471150 Genomic DNA. Translation: EAW88454.1.
CH471150 Genomic DNA. Translation: EAW88455.1.
CH471150 Genomic DNA. Translation: EAW88457.1.
BC006550 mRNA. Translation: AAH06550.1.
BC007435 mRNA. Translation: AAH07435.1.
CCDSCCDS14661.1. [P38159-1]
CCDS55510.1. [P38159-3]
RefSeqNP_001158275.1. NM_001164803.1. [P38159-3]
NP_002130.2. NM_002139.3. [P38159-1]
UniGeneHs.380118.
Hs.710162.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MB0NMR-B1-95[»]
2MKSNMR-A1-90[»]
ProteinModelPortalP38159.
SMRP38159. Positions 1-90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118134. 94 interactions.
DIPDIP-34447N.
IntActP38159. 46 interactions.
MINTMINT-5000999.
STRING9606.ENSP00000359645.

PTM databases

PhosphoSiteP38159.

Polymorphism databases

DMDM23503093.

2D gel databases

SWISS-2DPAGEP38159.

Proteomic databases

MaxQBP38159.
PaxDbP38159.
PRIDEP38159.

Protocols and materials databases

DNASU27316.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
GeneID27316.
KEGGhsa:27316.
UCSCuc004fae.2. human. [P38159-1]
uc011mwf.1. human. [P38159-3]

Organism-specific databases

CTD27316.
GeneCardsGC0XM135951.
HGNCHGNC:9910. RBMX.
HPAHPA057707.
MIM300199. gene.
neXtProtNX_P38159.
PharmGKBPA34277.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000070250.
HOVERGENHBG063314.
InParanoidP38159.
KOK12885.
OMAGMARSRY.
OrthoDBEOG780RPD.
PhylomeDBP38159.
TreeFamTF331833.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP38159.
BgeeP38159.
CleanExHS_RBMX.
GenevestigatorP38159.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBMX. human.
GeneWikiRBMX.
GenomeRNAi27316.
NextBio50322.
PROP38159.
SOURCESearch...

Entry information

Entry nameRBMX_HUMAN
AccessionPrimary (citable) accession number: P38159
Secondary accession number(s): B4E3U4 expand/collapse secondary AC list , D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM