P38159 (RBMX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA-binding motif protein, X chromosome

Alternative name(s):
Glycoprotein p43
Heterogeneous nuclear ribonucleoprotein G
Short name=hnRNP G

Cleaved into the following chain:

1. RNA-binding motif protein, X chromosome, N-terminally processed

Gene names

Name:	RBMX
Synonyms:	HNRPG, RBMXP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	Transcription mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Ligand	RNA-binding
Molecular function	Activator Repressor Ribonucleoprotein
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interleukin-1 Inferred from direct assay Ref.17. Source: UniProtKB 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 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_component	catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay Ref.17. Source: UniProtKB nuclear euchromatin Inferred from direct assay Ref.23. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome supraspliceosomal complex Inferred from direct assay Ref.20. Source: UniProtKB
Molecular_function	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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KHDRBS2	Q5VWX1	2	EBI-743526,EBI-742808
Srek1	Q9JKL7	3	EBI-743526,EBI-6452221	From 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	RNA-binding motif protein, X chromosome		PRO_0000081854
	Initiator methionine	1	1	Removed; alternate Ref.9
	Chain	2 – 391	390	RNA-binding motif protein, X chromosome, N-terminally processed		PRO_0000304582
Regions
	Domain	8 – 86	79	RRM
	Region	186 – 236	51	Necessary for the association to nascent RNAPII transcripts and nuclear localization
	Region	333 – 391	59	Necessary for RNA-binding
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate Ref.9
	Modified residue	2	1	N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed Ref.9
	Modified residue	30	1	N6-acetyllysine Ref.22
	Modified residue	88	1	Phosphoserine Ref.14 Ref.19 Ref.21 Ref.24 Ref.26
	Modified residue	165	1	Phosphoserine By similarity
	Modified residue	168	1	Phosphoserine By similarity
	Modified residue	208	1	Phosphoserine By similarity
	Modified residue	329	1	Phosphoserine Ref.19
	Modified residue	332	1	Phosphoserine Ref.19 Ref.26
	Modified residue	352	1	Phosphoserine Ref.24 Ref.26
Natural variations
	Alternative sequence	45 – 57	13	Missing in isoform 2.		VSP_042203
	Alternative sequence	73 – 196	124	SLDGK…GPPRR → LLYHVEEIVMEVHLEGNRCP LVEMFICPQEMMGILLKTAI QAEITQVLVILEIMHHHHEI ILTVIMVIPVHVMTIHQEDI AIEMDMVVIVTIQIIQVEVP TEIHMRVMVGDFAHYGRGVL IDSQ in isoform 3.		VSP_043650
	Alternative sequence	197 – 391	195	Missing in isoform 3.		VSP_043651
Experimental info
	Mutagenesis	22	1	K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. Ref.15 Ref.18
	Sequence conflict	259	1	G → E in CAA80599. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 3. Checksum: 904FEB9BFC573546	FASTA	391	42,332
	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
	Isoform 2 [UniParc]. Checksum: 032DD488FA08CE19	FASTA	378	40,846
	10 20 30 40 50 60 MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRESPADAK DAARDMNGKS 70 80 90 100 110 120 LDGKAIKVEQ ATKPSFESGR RGPPPPPRSR GPPRGLRGGR GGSGGTRGPP SRGGHMDDGG 130 140 150 160 170 180 YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSAPSGPVRS SSGMGGRAPV SRGRDSYGGP 190 200 210 220 230 240 PRREPLPSRR DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY RDYGHSSSRD 250 260 270 280 290 300 DYPSRGYSDR DGYGRDRDYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS YGGSSRYDDY 310 320 330 340 350 360 SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS YSSSSRGAPR 370 GGGRGGSRSD RGGGRSRY
	Isoform 3 [UniParc]. Checksum: 7FB2ABEE20A3D582	FASTA	196	22,172
	10 20 30 40 50 60 MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA 70 80 90 100 110 120 DAKDAARDMN GKLLYHVEEI VMEVHLEGNR CPLVEMFICP QEMMGILLKT AIQAEITQVL 130 140 150 160 170 180 VILEIMHHHH EIILTVIMVI PVHVMTIHQE DIAIEMDMVV IVTIQIIQVE VPTEIHMRVM 190 VGDFAHYGRG VLIDSQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z23064 mRNA. Translation: CAA80599.1. AF266723 , 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.
IPI	IPI00304692. IPI00552938.
RefSeq	NP_001158275.1. NM_001164803.1. NP_002130.2. NM_002139.3.
UniGene	Hs.380118. Hs.710162.
3D structure databases
ProteinModelPortal	P38159.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34447N.
IntAct	P38159. 39 interactions.
MINT	MINT-5000999.
STRING	9606.ENSP00000359645.
PTM databases
PhosphoSite	P38159.
Polymorphism databases
DMDM	23503093.
2D gel databases
SWISS-2DPAGE	P38159.
Proteomic databases
PaxDb	P38159.
PRIDE	P38159.
Protocols and materials databases
DNASU	27316.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000320676; ENSP00000359645; ENSG00000147274. ENST00000431446; ENSP00000411989; ENSG00000147274.
GeneID	27316.
KEGG	hsa:27316.
UCSC	uc004fad.1. human.
Organism-specific databases
CTD	27316.
GeneCards	GC0XM135951.
HGNC	HGNC:9910. RBMX.
MIM	300199. gene.
neXtProt	NX_P38159.
PharmGKB	PA34277.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0724.
HOGENOM	HOG000070250.
HOVERGEN	HBG063314.
InParanoid	P38159.
KO	K12885.
OMA	PFFKGMS.
OrthoDB	EOG4CNQSK.
PhylomeDB	P38159.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P38159.
Bgee	P38159.
CleanEx	HS_RBMX.
Genevestigator	P38159.
GermOnline	ENSG00000147274. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR012604. RBM1CTR. IPR000504. RRM_dom. [Graphical view]
Pfam	PF08081. RBM1CTR. 1 hit. PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RBMX. human.
GenomeRNAi	27316.
NextBio	50322.
SOURCE	Search...

Entry information

Entry name

RBMX_HUMAN

Accession

Primary (citable) accession number: P38159
Secondary accession number(s): B4E3U4 , D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 148 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.