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P38159

- RBMX_HUMAN

UniProt

P38159 - RBMX_HUMAN

Protein

RNA-binding motif protein, X chromosome

Gene

RBMX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. core promoter binding Source: UniProtKB
    3. mRNA binding Source: UniProtKB
    4. nucleotide binding Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. RNA binding Source: UniProtKB
    8. single-stranded RNA binding Source: Ensembl

    GO - Biological processi

    1. cellular response to interleukin-1 Source: UniProtKB
    2. gene expression Source: Reactome
    3. membrane protein ectodomain proteolysis Source: UniProtKB
    4. mRNA splice site selection Source: Ensembl
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    7. osteoblast differentiation Source: UniProt
    8. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. protein homooligomerization Source: UniProtKB
    11. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    12. RNA splicing Source: Reactome
    13. transcription from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Repressor, Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    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:
    Gene namesi
    Name:RBMX
    Synonyms:HNRPG, RBMXP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9910. RBMX.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Component of ribonucleosomes. Localizes in numerous small granules in the nucleus.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProtKB
    4. membrane Source: UniProt
    5. nuclear euchromatin Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB
    8. ribonucleoprotein complex Source: UniProtKB
    9. supraspliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. 2 Publications

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34277.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391RNA-binding motif protein, X chromosomePRO_0000081854Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 391390RNA-binding motif protein, X chromosome, N-terminally processedPRO_0000304582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate1 Publication
    Modified residuei2 – 21N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed1 Publication
    Modified residuei30 – 301N6-acetyllysine1 Publication
    Modified residuei88 – 881Phosphoserine5 Publications
    Modified residuei329 – 3291Phosphoserine1 Publication
    Modified residuei332 – 3321Phosphoserine2 Publications
    Modified residuei352 – 3521Phosphoserine2 Publications

    Post-translational modificationi

    O-glycosylated.1 Publication
    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.2 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP38159.
    PaxDbiP38159.
    PRIDEiP38159.

    2D gel databases

    SWISS-2DPAGEP38159.

    PTM databases

    PhosphoSiteiP38159.

    Expressioni

    Tissue specificityi

    Expressed strongly in oral keratinocytes, but only weakly detected in oral squamous cell carcinomas (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP38159.
    BgeeiP38159.
    CleanExiHS_RBMX.
    GenevestigatoriP38159.

    Organism-specific databases

    HPAiHPA057707.

    Interactioni

    Subunit structurei

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HNRNPKP619783EBI-743526,EBI-304185
    KHDRBS2Q5VWX12EBI-743526,EBI-742808
    Srek1Q9JKL73EBI-743526,EBI-6452221From a different organism.

    Protein-protein interaction databases

    BioGridi118134. 93 interactions.
    DIPiDIP-34447N.
    IntActiP38159. 46 interactions.
    MINTiMINT-5000999.
    STRINGi9606.ENSP00000359645.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Helixi21 – 288
    Turni29 – 313
    Beta strandi34 – 396
    Turni43 – 453
    Beta strandi50 – 589
    Helixi61 – 666
    Beta strandi67 – 748
    Beta strandi80 – 834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MB0NMR-B1-95[»]
    2MKSNMR-A1-90[»]
    ProteinModelPortaliP38159.
    SMRiP38159. Positions 1-90.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 8679RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 23651Necessary for the association to nascent RNAPII transcripts and nuclear localizationAdd
    BLAST
    Regioni333 – 39159Necessary for RNA-bindingAdd
    BLAST

    Domaini

    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

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000070250.
    HOVERGENiHBG063314.
    InParanoidiP38159.
    KOiK12885.
    OMAiGMARSRY.
    OrthoDBiEOG780RPD.
    PhylomeDBiP38159.
    TreeFamiTF331833.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR012604. RBM1CTR.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF08081. RBM1CTR. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P38159-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG    50
    FAFVTFESPA DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP 100
    RSRGPPRGLR GGRGGSGGTR GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK 150
    RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR APVSRGRDSY GGPPRREPLP 200
    SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD YTYRDYGHSS 250
    SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP 300
    PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP 350
    PSMERGYPPP RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y 391
    Length:391
    Mass (Da):42,332
    Last modified:September 19, 2002 - v3
    Checksum:i904FEB9BFC573546
    GO
    Isoform 2 (identifier: P38159-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         45-57: Missing.

    Show »
    Length:378
    Mass (Da):40,846
    Checksum:i032DD488FA08CE19
    GO
    Isoform 3 (identifier: P38159-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:196
    Mass (Da):22,172
    Checksum:i7FB2ABEE20A3D582
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591G → E in CAA80599. (PubMed:7692398)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei45 – 5713Missing in isoform 2. 1 PublicationVSP_042203Add
    BLAST
    Alternative sequencei73 – 196124SLDGK…GPPRR → LLYHVEEIVMEVHLEGNRCP LVEMFICPQEMMGILLKTAI QAEITQVLVILEIMHHHHEI ILTVIMVIPVHVMTIHQEDI AIEMDMVVIVTIQIIQVEVP TEIHMRVMVGDFAHYGRGVL IDSQ in isoform 3. 1 PublicationVSP_043650Add
    BLAST
    Alternative sequencei197 – 391195Missing in isoform 3. 1 PublicationVSP_043651Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14661.1. [P38159-1]
    CCDS55510.1. [P38159-3]
    RefSeqiNP_001158275.1. NM_001164803.1. [P38159-3]
    NP_002130.2. NM_002139.3. [P38159-1]
    UniGeneiHs.380118.
    Hs.710162.

    Genome annotation databases

    EnsembliENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
    ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
    GeneIDi27316.
    KEGGihsa:27316.
    UCSCiuc004fae.2. human. [P38159-1]
    uc011mwf.1. human. [P38159-3]

    Polymorphism databases

    DMDMi23503093.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14661.1. [P38159-1 ]
    CCDS55510.1. [P38159-3 ]
    RefSeqi NP_001158275.1. NM_001164803.1. [P38159-3 ]
    NP_002130.2. NM_002139.3. [P38159-1 ]
    UniGenei Hs.380118.
    Hs.710162.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MB0 NMR - B 1-95 [» ]
    2MKS NMR - A 1-90 [» ]
    ProteinModelPortali P38159.
    SMRi P38159. Positions 1-90.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118134. 93 interactions.
    DIPi DIP-34447N.
    IntActi P38159. 46 interactions.
    MINTi MINT-5000999.
    STRINGi 9606.ENSP00000359645.

    PTM databases

    PhosphoSitei P38159.

    Polymorphism databases

    DMDMi 23503093.

    2D gel databases

    SWISS-2DPAGE P38159.

    Proteomic databases

    MaxQBi P38159.
    PaxDbi P38159.
    PRIDEi P38159.

    Protocols and materials databases

    DNASUi 27316.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320676 ; ENSP00000359645 ; ENSG00000147274 . [P38159-1 ]
    ENST00000431446 ; ENSP00000411989 ; ENSG00000147274 . [P38159-3 ]
    GeneIDi 27316.
    KEGGi hsa:27316.
    UCSCi uc004fae.2. human. [P38159-1 ]
    uc011mwf.1. human. [P38159-3 ]

    Organism-specific databases

    CTDi 27316.
    GeneCardsi GC0XM135951.
    HGNCi HGNC:9910. RBMX.
    HPAi HPA057707.
    MIMi 300199. gene.
    neXtProti NX_P38159.
    PharmGKBi PA34277.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000070250.
    HOVERGENi HBG063314.
    InParanoidi P38159.
    KOi K12885.
    OMAi GMARSRY.
    OrthoDBi EOG780RPD.
    PhylomeDBi P38159.
    TreeFami TF331833.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi RBMX. human.
    GeneWikii RBMX.
    GenomeRNAii 27316.
    NextBioi 50322.
    PROi P38159.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38159.
    Bgeei P38159.
    CleanExi HS_RBMX.
    Genevestigatori P38159.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR012604. RBM1CTR.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF08081. RBM1CTR. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiRBMX_HUMAN
    AccessioniPrimary (citable) accession number: P38159
    Secondary accession number(s): B4E3U4
    , D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3