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Q9BWF3

- RBM4_HUMAN

UniProt

Q9BWF3 - RBM4_HUMAN

Protein

RNA-binding protein 4

Gene

RBM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri160 – 17718CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. miRNA binding Source: UniProtKB
    2. mRNA 3'-UTR binding Source: UniProtKB
    3. mRNA binding Source: UniProtKB
    4. nucleotide binding Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. pre-mRNA intronic binding Source: UniProtKB
    7. pre-mRNA intronic pyrimidine-rich binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. RNA binding Source: UniProtKB
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cap-independent translational initiation Source: UniProtKB
    2. cell differentiation Source: UniProtKB-KW
    3. circadian regulation of translation Source: UniProtKB
    4. entrainment of circadian clock by photoperiod Source: UniProtKB
    5. IRES-dependent translational initiation Source: UniProtKB
    6. mRNA processing Source: UniProtKB-KW
    7. negative regulation of translation Source: UniProtKB
    8. negative regulation of translational initiation Source: UniProtKB
    9. negative regulation of translation in response to stress Source: UniProtKB
    10. negative regulation of translation involved in gene silencing by miRNA Source: UniProtKB
    11. positive regulation of muscle cell differentiation Source: UniProtKB
    12. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    13. regulation of nucleocytoplasmic transport Source: UniProtKB
    14. response to arsenic-containing substance Source: UniProtKB
    15. RNA processing Source: ProtInc
    16. RNA splicing Source: UniProtKB-KW
    17. stress-activated MAPK cascade Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Differentiation, mRNA processing, mRNA splicing, RNA-mediated gene silencing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA-binding protein 4
    Alternative name(s):
    Lark homolog
    Short name:
    hLark
    RNA-binding motif protein 4
    RNA-binding motif protein 4a
    Gene namesi
    Name:RBM4
    Synonyms:RBM4A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9901. RBM4.

    Subcellular locationi

    Nucleus. Nucleusnucleolus. Nucleus speckle. Cytoplasm. Cytoplasmic granule
    Note: Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic stress granule Source: UniProtKB
    3. nuclear speck Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi37 – 371Y → A: Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115. 1 Publication
    Mutagenesisi39 – 391F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115. 1 Publication
    Mutagenesisi113 – 1131Y → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115. 1 Publication
    Mutagenesisi115 – 1151F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113. 1 Publication
    Mutagenesisi309 – 3091S → A: Inhibits IRES-mediated mRNA translation. Does not inhibit interaction with EIF4A1. Inhibits localization in cytoplasm and cytoplasmiic granules upon cell muscle differentiation. Inhibits negative regulation of translation involved in gene silencing by miRNA. 3 Publications

    Organism-specific databases

    PharmGKBiPA34266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364RNA-binding protein 4PRO_0000081754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei309 – 3091Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation on Ser-309 is induced upon cell muscle differentiation By similarity. Phosphorylated. Phosphorylated in vitro on Ser-309 by SRPK1. Phosphorylation on Ser-309 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation.By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BWF3.
    PaxDbiQ9BWF3.
    PRIDEiQ9BWF3.

    PTM databases

    PhosphoSiteiQ9BWF3.

    Expressioni

    Tissue specificityi

    Expressed in the cerebellum. Expressed in neurons and glial cells, including layers II neurons in the frontal cortex and CA1 pyramidal neurons in the hippocampus. Expressed in heart, liver, pancreas, skeletal muscle, placenta, primary fibroblasts and peripheral blood monocytes (at protein level). Ubiquitously expressed. Highly expressed in heart, placenta and skeletal muscle. Weakly expressed in pancreas, kidney, liver, lung and brain.4 Publications

    Developmental stagei

    Found to be expressed in fetal brain. Down-regulated in fetal Down syndrome (DS) brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9BWF3.
    BgeeiQ9BWF3.
    CleanExiHS_RBM4.
    GenevestigatoriQ9BWF3.

    Interactioni

    Subunit structurei

    Interacts with TNPO3; the interaction mediates nuclear import of the protein and is disrupted by nuclear Ran bound to GTP. Interacts with EIF4G1 and WT1. Interacts with EIF4A1; the interaction is modulated under stress-induced conditions. Interacts with AGO1. Interacts with AGO2; the interaction occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation-independent manner. Interacts with DDX5; the interaction occurs in an RNA-independent manner.6 Publications

    Protein-protein interaction databases

    BioGridi111871. 56 interactions.
    DIPiDIP-44199N.
    IntActiQ9BWF3. 32 interactions.
    MINTiMINT-1187795.
    STRINGi9606.ENSP00000309166.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87
    Helixi15 – 239
    Beta strandi28 – 347
    Beta strandi37 – 448
    Helixi45 – 5511
    Beta strandi66 – 683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DNQNMR-A1-77[»]
    ProteinModelPortaliQ9BWF3.
    SMRiQ9BWF3. Positions 1-155.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BWF3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7271RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini78 – 14871RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 364169Interaction with TNPO3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi233 – 2397Poly-Ala
    Compositional biasi282 – 29514Poly-AlaAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri160 – 17718CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG294108.
    HOGENOMiHOG000026790.
    HOVERGENiHBG062217.
    KOiK13187.
    OrthoDBiEOG7SFJ0M.
    PhylomeDBiQ9BWF3.
    TreeFamiTF320661.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BWF3-1) [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

    MVKLFIGNLP REATEQEIRS LFEQYGKVLE CDIIKNYGFV HIEDKTAAED    50
    AIRNLHHYKL HGVNINVEAS KNKSKTSTKL HVGNISPTCT NKELRAKFEE 100
    YGPVIECDIV KDYAFVHMER AEDAVEAIRG LDNTEFQGKR MHVQLSTSRL 150
    RTAPGMGDQS GCYRCGKEGH WSKECPIDRS GRVADLTEQY NEQYGAVRTP 200
    YTMSYGDSLY YNNAYGALDA YYKRCRAARS YEAVAAAAAS VYNYAEQTLS 250
    QLPQVQNTAM ASHLTSTSLD PYDRHLLPTS GAAATAAAAA AAAAAVTAAS 300
    TSYYGRDRSP LRRATAPVPT VGEGYGYGHE SELSQASAAA RNSLYDMARY 350
    EREQYADRAR YSAF 364
    Length:364
    Mass (Da):40,314
    Last modified:June 1, 2001 - v1
    Checksum:i3EA1C80D4C9122A2
    GO
    Isoform 2 (identifier: Q9BWF3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-177: KRMHVQLSTS...EGHWSKECPI → EPPSLGRGLN...TAVGWLVMKK
         178-364: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:177
    Mass (Da):20,044
    Checksum:iD139DCDF1C9FEF5B
    GO
    Isoform 3 (identifier: Q9BWF3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-143: KRMHV → GMCVG
         144-364: Missing.

    Note: May be due to exon skipping.

    Show »
    Length:143
    Mass (Da):16,173
    Checksum:i6067E91D4167261A
    GO
    Isoform 4 (identifier: Q9BWF3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-364: RMHVQLSTSR...YADRARYSAF → ITPVTEGYCCCNKGHTYIFKNCNLILESRKSRRC

    Note: No experimental confirmation available.

    Show »
    Length:173
    Mass (Da):19,788
    Checksum:iA6868F2823CD17B1
    GO

    Sequence cautioni

    The sequence AAC51293.1 differs from that shown. Reason: Frameshift at position 234.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521I → M in BAG64902. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 17739KRMHV…KECPI → EPPSLGRGLNTRLCAENGWI SKRRGLVKITAVGWLVMKK in isoform 2. 2 PublicationsVSP_013414Add
    BLAST
    Alternative sequencei139 – 1435KRMHV → GMCVG in isoform 3. 1 PublicationVSP_013413
    Alternative sequencei140 – 364225RMHVQ…RYSAF → ITPVTEGYCCCNKGHTYIFK NCNLILESRKSRRC in isoform 4. 1 PublicationVSP_044493Add
    BLAST
    Alternative sequencei144 – 364221Missing in isoform 3. 1 PublicationVSP_013415Add
    BLAST
    Alternative sequencei178 – 364187Missing in isoform 2. 2 PublicationsVSP_013416Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89505 mRNA. Translation: AAC51293.1. Frameshift.
    AK097592 mRNA. Translation: BAG53492.1.
    AK303984 mRNA. Translation: BAG64902.1.
    AL832566 mRNA. Translation: CAH10593.1.
    AP001157 Genomic DNA. No translation available.
    BC000307 mRNA. Translation: AAH00307.1.
    BC021120 mRNA. Translation: AAH21120.1.
    BC032735 mRNA. Translation: AAH32735.1.
    BC064960 mRNA. Translation: AAH64960.1.
    CCDSiCCDS41676.1. [Q9BWF3-1]
    CCDS55776.1. [Q9BWF3-3]
    CCDS55777.1. [Q9BWF3-4]
    RefSeqiNP_001185772.1. NM_001198843.1. [Q9BWF3-3]
    NP_001185773.1. NM_001198844.1. [Q9BWF3-4]
    NP_002887.2. NM_002896.3. [Q9BWF3-1]
    UniGeneiHs.523822.
    Hs.728823.

    Genome annotation databases

    EnsembliENST00000310092; ENSP00000309166; ENSG00000173933. [Q9BWF3-1]
    ENST00000396053; ENSP00000413497; ENSG00000173933. [Q9BWF3-4]
    ENST00000398692; ENSP00000381680; ENSG00000173933. [Q9BWF3-3]
    ENST00000408993; ENSP00000386561; ENSG00000173933. [Q9BWF3-1]
    ENST00000409406; ENSP00000386894; ENSG00000173933. [Q9BWF3-1]
    ENST00000483858; ENSP00000435821; ENSG00000173933. [Q9BWF3-2]
    ENST00000530235; ENSP00000432150; ENSG00000173933. [Q9BWF3-3]
    ENST00000532968; ENSP00000432020; ENSG00000173933. [Q9BWF3-2]
    GeneIDi5936.
    KEGGihsa:5936.
    UCSCiuc001oiv.3. human. [Q9BWF3-2]
    uc001oiw.2. human. [Q9BWF3-1]
    uc001oix.2. human. [Q9BWF3-3]
    uc010rpj.2. human. [Q9BWF3-4]

    Polymorphism databases

    DMDMi62511089.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89505 mRNA. Translation: AAC51293.1 . Frameshift.
    AK097592 mRNA. Translation: BAG53492.1 .
    AK303984 mRNA. Translation: BAG64902.1 .
    AL832566 mRNA. Translation: CAH10593.1 .
    AP001157 Genomic DNA. No translation available.
    BC000307 mRNA. Translation: AAH00307.1 .
    BC021120 mRNA. Translation: AAH21120.1 .
    BC032735 mRNA. Translation: AAH32735.1 .
    BC064960 mRNA. Translation: AAH64960.1 .
    CCDSi CCDS41676.1. [Q9BWF3-1 ]
    CCDS55776.1. [Q9BWF3-3 ]
    CCDS55777.1. [Q9BWF3-4 ]
    RefSeqi NP_001185772.1. NM_001198843.1. [Q9BWF3-3 ]
    NP_001185773.1. NM_001198844.1. [Q9BWF3-4 ]
    NP_002887.2. NM_002896.3. [Q9BWF3-1 ]
    UniGenei Hs.523822.
    Hs.728823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DNQ NMR - A 1-77 [» ]
    ProteinModelPortali Q9BWF3.
    SMRi Q9BWF3. Positions 1-155.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111871. 56 interactions.
    DIPi DIP-44199N.
    IntActi Q9BWF3. 32 interactions.
    MINTi MINT-1187795.
    STRINGi 9606.ENSP00000309166.

    PTM databases

    PhosphoSitei Q9BWF3.

    Polymorphism databases

    DMDMi 62511089.

    Proteomic databases

    MaxQBi Q9BWF3.
    PaxDbi Q9BWF3.
    PRIDEi Q9BWF3.

    Protocols and materials databases

    DNASUi 5936.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310092 ; ENSP00000309166 ; ENSG00000173933 . [Q9BWF3-1 ]
    ENST00000396053 ; ENSP00000413497 ; ENSG00000173933 . [Q9BWF3-4 ]
    ENST00000398692 ; ENSP00000381680 ; ENSG00000173933 . [Q9BWF3-3 ]
    ENST00000408993 ; ENSP00000386561 ; ENSG00000173933 . [Q9BWF3-1 ]
    ENST00000409406 ; ENSP00000386894 ; ENSG00000173933 . [Q9BWF3-1 ]
    ENST00000483858 ; ENSP00000435821 ; ENSG00000173933 . [Q9BWF3-2 ]
    ENST00000530235 ; ENSP00000432150 ; ENSG00000173933 . [Q9BWF3-3 ]
    ENST00000532968 ; ENSP00000432020 ; ENSG00000173933 . [Q9BWF3-2 ]
    GeneIDi 5936.
    KEGGi hsa:5936.
    UCSCi uc001oiv.3. human. [Q9BWF3-2 ]
    uc001oiw.2. human. [Q9BWF3-1 ]
    uc001oix.2. human. [Q9BWF3-3 ]
    uc010rpj.2. human. [Q9BWF3-4 ]

    Organism-specific databases

    CTDi 5936.
    GeneCardsi GC11P066394.
    HGNCi HGNC:9901. RBM4.
    MIMi 602571. gene.
    neXtProti NX_Q9BWF3.
    PharmGKBi PA34266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294108.
    HOGENOMi HOG000026790.
    HOVERGENi HBG062217.
    KOi K13187.
    OrthoDBi EOG7SFJ0M.
    PhylomeDBi Q9BWF3.
    TreeFami TF320661.

    Miscellaneous databases

    ChiTaRSi RBM4. human.
    EvolutionaryTracei Q9BWF3.
    GeneWikii RBM4.
    GenomeRNAii 5936.
    NextBioi 23140.
    PROi Q9BWF3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BWF3.
    Bgeei Q9BWF3.
    CleanExi HS_RBM4.
    Genevestigatori Q9BWF3.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel zinc finger-containing RNA-binding protein conserved from fruitflies to humans."
      Jackson F.R., Banfi S., Guffanti A., Rossi E.
      Genomics 41:444-452(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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 1 AND 4).
      Tissue: Testis and Trachea.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Lung, Pancreas and Skin.
    6. "Manifold decreased protein levels of matrin 3, reduced motor protein HMP and hlark in fetal Down's syndrome brain."
      Bernert G., Fountoulakis M., Lubec G.
      Proteomics 2:1752-1757(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    7. "A novel splicing regulator shares a nuclear import pathway with SR proteins."
      Lai M.-C., Kuo H.-W., Chang W.-C., Tarn W.-Y.
      EMBO J. 22:1359-1369(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TNPO3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-37; PHE-39; TYR-113 AND PHE-115.
    8. "Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB."
      Lin J.C., Tarn W.Y.
      Mol. Cell. Biol. 25:10111-10121(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, TISSUE SPECIFICITY.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lark is the splicing factor RBM4 and exhibits unique subnuclear localization properties."
      Markus M.A., Morris B.J.
      DNA Cell Biol. 25:457-464(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "WT1 interacts with the splicing protein RBM4 and regulates its ability to modulate alternative splicing in vivo."
      Markus M.A., Heinrich B., Raitskin O., Adams D.J., Mangs H., Goy C., Ladomery M., Sperling R., Stamm S., Morris B.J.
      Exp. Cell Res. 312:3379-3388(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WT1, SUBCELLULAR LOCATION.
    12. "RBM4 interacts with an intronic element and stimulates tau exon 10 inclusion."
      Kar A., Havlioglu N., Tarn W.Y., Wu J.Y.
      J. Biol. Chem. 281:24479-24488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, TISSUE SPECIFICITY.
    13. "Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
      Lin J.C., Hsu M., Tarn W.Y.
      Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF4A1 AND EIF4G1, PHOSPHORYLATION AT SER-309, ASSOCIATION WITH IRES OF MRNAS, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-309.
    14. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AGO1 AND AGO2.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "RNA-binding motif protein 4 translocates to cytoplasmic granules and suppresses translation via argonaute2 during muscle cell differentiation."
      Lin J.C., Tarn W.Y.
      J. Biol. Chem. 284:34658-34665(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AGO2, MUTAGENESIS OF SER-309, SUBCELLULAR LOCATION.
    19. "Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
      Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
      Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "RBM4 down-regulates PTB and antagonizes its activity in muscle cell-specific alternative splicing."
      Lin J.C., Tarn W.Y.
      J. Cell Biol. 193:509-520(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-309.
    23. "RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site."
      Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S., Wu J.Y.
      Mol. Cell. Biol. 31:1812-1821(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DDX5, RNA-BINDING.
    24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Solution structure of RNA binding domain 1 in RNA-binding protein 30."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-77.

    Entry informationi

    Entry nameiRBM4_HUMAN
    AccessioniPrimary (citable) accession number: Q9BWF3
    Secondary accession number(s): B3KUN0
    , B4E1U0, E7EQS3, O02916, Q4VC48, Q6P1P2, Q8WU85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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