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Q9BWF3 (RBM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein 4
Alternative name(s):
Lark homolog
Short name=hLark
RNA-binding motif protein 4
RNA-binding motif protein 4a
Gene names
Name:RBM4
Synonyms:RBM4A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.22 Ref.23

Subunit structure

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. Ref.7 Ref.11 Ref.13 Ref.14 Ref.18 Ref.23

Subcellular location

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. Ref.7 Ref.10 Ref.11 Ref.13 Ref.16 Ref.18

Tissue specificity

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. Ref.7 Ref.8 Ref.12 Ref.16

Developmental stage

Found to be expressed in fetal brain. Down-regulated in fetal Down syndrome (DS) brain. Ref.6

Post-translational modification

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. Ref.13

Sequence similarities

Contains 1 CCHC-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
RNA-mediated gene silencing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processIRES-dependent translational initiation

Inferred from direct assay Ref.13. Source: UniProtKB

RNA processing

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

cap-independent translational initiation

Inferred from direct assay Ref.13. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

circadian regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of translation in response to stress

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of translation involved in gene silencing by miRNA

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of translational initiation

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of muscle cell differentiation

Inferred from direct assay Ref.22. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from direct assay Ref.7Ref.8Ref.12Ref.11Ref.22. Source: UniProtKB

regulation of nucleocytoplasmic transport

Inferred from direct assay Ref.7Ref.13. Source: UniProtKB

response to arsenic-containing substance

Inferred from direct assay Ref.13. Source: UniProtKB

stress-activated MAPK cascade

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.7Ref.12Ref.10Ref.13. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.7Ref.10. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.7Ref.10. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.12Ref.10Ref.13. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.19. Source: UniProtKB

mRNA 3'-UTR binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA binding

Inferred from direct assay Ref.22. Source: UniProtKB

miRNA binding

Inferred from direct assay Ref.18. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

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

pre-mRNA intronic binding

Inferred from direct assay Ref.8. Source: UniProtKB

pre-mRNA intronic pyrimidine-rich binding

Inferred from direct assay Ref.8Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.11Ref.13Ref.18Ref.23. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BWF3-1)

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: Q9BWF3-2)

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.
Isoform 3 (identifier: Q9BWF3-3)

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.
Isoform 4 (identifier: Q9BWF3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     140-364: RMHVQLSTSR...YADRARYSAF → ITPVTEGYCCCNKGHTYIFKNCNLILESRKSRRC
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364RNA-binding protein 4
PRO_0000081754

Regions

Domain2 – 7271RRM 1
Domain78 – 14871RRM 2
Zinc finger160 – 17718CCHC-type
Region196 – 364169Interaction with TNPO3
Compositional bias233 – 2397Poly-Ala
Compositional bias282 – 29514Poly-Ala

Amino acid modifications

Modified residue3091Phosphoserine Ref.13

Natural variations

Alternative sequence139 – 17739KRMHV…KECPI → EPPSLGRGLNTRLCAENGWI SKRRGLVKITAVGWLVMKK in isoform 2.
VSP_013414
Alternative sequence139 – 1435KRMHV → GMCVG in isoform 3.
VSP_013413
Alternative sequence140 – 364225RMHVQ…RYSAF → ITPVTEGYCCCNKGHTYIFK NCNLILESRKSRRC in isoform 4.
VSP_044493
Alternative sequence144 – 364221Missing in isoform 3.
VSP_013415
Alternative sequence178 – 364187Missing in isoform 2.
VSP_013416

Experimental info

Mutagenesis371Y → A: Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115. Ref.7
Mutagenesis391F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115. Ref.7
Mutagenesis1131Y → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115. Ref.7
Mutagenesis1151F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113. Ref.7
Mutagenesis3091S → 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. Ref.13 Ref.18 Ref.22
Sequence conflict521I → M in BAG64902. Ref.2

Secondary structure

............ 364
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 3EA1C80D4C9122A2

FASTA36440,314
        10         20         30         40         50         60 
MVKLFIGNLP REATEQEIRS LFEQYGKVLE CDIIKNYGFV HIEDKTAAED AIRNLHHYKL 

        70         80         90        100        110        120 
HGVNINVEAS KNKSKTSTKL HVGNISPTCT NKELRAKFEE YGPVIECDIV KDYAFVHMER 

       130        140        150        160        170        180 
AEDAVEAIRG LDNTEFQGKR MHVQLSTSRL RTAPGMGDQS GCYRCGKEGH WSKECPIDRS 

       190        200        210        220        230        240 
GRVADLTEQY NEQYGAVRTP YTMSYGDSLY YNNAYGALDA YYKRCRAARS YEAVAAAAAS 

       250        260        270        280        290        300 
VYNYAEQTLS QLPQVQNTAM ASHLTSTSLD PYDRHLLPTS GAAATAAAAA AAAAAVTAAS 

       310        320        330        340        350        360 
TSYYGRDRSP LRRATAPVPT VGEGYGYGHE SELSQASAAA RNSLYDMARY EREQYADRAR 


YSAF 

« Hide

Isoform 2 [UniParc].

Checksum: D139DCDF1C9FEF5B
Show »

FASTA17720,044
Isoform 3 [UniParc].

Checksum: 6067E91D4167261A
Show »

FASTA14316,173
Isoform 4 [UniParc].

Checksum: A6868F2823CD17B1
Show »

FASTA17319,788

References

« Hide 'large scale' references
[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. 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 1 AND 4).
Tissue: Testis and Trachea.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"The LARK/RBM4a protein is highly expressed in cerebellum as compared to cerebrum."
Pfuhl T., Mamiani A., Durr M., Welter S., Stieber J., Ankara J., Liss M., Dobner T., Schmitt A., Falkai P., Kremmer E., Jung V., Barth S., Grasser F.A.
Neurosci. Lett. 444:11-15(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[17]"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: 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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41676.1. [Q9BWF3-1]
CCDS55776.1. [Q9BWF3-3]
CCDS55777.1. [Q9BWF3-4]
RefSeqNP_001185772.1. NM_001198843.1. [Q9BWF3-3]
NP_001185773.1. NM_001198844.1. [Q9BWF3-4]
NP_002887.2. NM_002896.3. [Q9BWF3-1]
UniGeneHs.523822.
Hs.728823.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNQNMR-A1-77[»]
ProteinModelPortalQ9BWF3.
SMRQ9BWF3. Positions 1-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111871. 56 interactions.
DIPDIP-44199N.
IntActQ9BWF3. 32 interactions.
MINTMINT-1187795.
STRING9606.ENSP00000309166.

PTM databases

PhosphoSiteQ9BWF3.

Polymorphism databases

DMDM62511089.

Proteomic databases

MaxQBQ9BWF3.
PaxDbQ9BWF3.
PRIDEQ9BWF3.

Protocols and materials databases

DNASU5936.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310092; 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]
ENST00000503028; ENSP00000425760; ENSG00000173933. [Q9BWF3-1]
ENST00000530235; ENSP00000432150; ENSG00000173933. [Q9BWF3-3]
ENST00000532968; ENSP00000432020; ENSG00000173933. [Q9BWF3-2]
GeneID5936.
KEGGhsa:5936.
UCSCuc001oiv.3. human. [Q9BWF3-2]
uc001oiw.2. human. [Q9BWF3-1]
uc001oix.2. human. [Q9BWF3-3]
uc010rpj.2. human. [Q9BWF3-4]

Organism-specific databases

CTD5936.
GeneCardsGC11P066394.
HGNCHGNC:9901. RBM4.
MIM602571. gene.
neXtProtNX_Q9BWF3.
PharmGKBPA34266.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294108.
HOGENOMHOG000026790.
HOVERGENHBG062217.
KOK13187.
OrthoDBEOG7SFJ0M.
PhylomeDBQ9BWF3.
TreeFamTF320661.

Gene expression databases

ArrayExpressQ9BWF3.
BgeeQ9BWF3.
CleanExHS_RBM4.
GenevestigatorQ9BWF3.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
4.10.60.10. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM4. human.
EvolutionaryTraceQ9BWF3.
GeneWikiRBM4.
GenomeRNAi5936.
NextBio23140.
PROQ9BWF3.
SOURCESearch...

Entry information

Entry nameRBM4_HUMAN
AccessionPrimary (citable) accession number: Q9BWF3
Secondary accession number(s): B3KUN0 expand/collapse secondary AC list , B4E1U0, E7EQS3, O02916, Q4VC48, Q6P1P2, Q8WU85
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 127 of the entry and version 1 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 11

Human chromosome 11: entries, gene names and cross-references to MIM