Q9BWF3 (RBM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBM4
Synonyms:	RBM4A

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	364 AA.
Sequence status	Complete.
Protein existence	Evidence 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 EIF2C2-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 EIF2C1. Interacts with EIF2C2; the interaction occurs under both cell proliferation and differentiation conditions and in a RNA- and phosphorylation-independent manner. Interacts with DDX5; the interaction occurs in a RNA-independent manner. Ref.7 Ref.11 Ref.13 Ref.14 Ref.18 Ref.23
Subcellular location	Nucleus. Nucleus › nucleolus. 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 process	Differentiation RNA-mediated gene silencing mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	IRES-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 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 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 stress-activated MAPK cascade Inferred from direct assay Ref.13. Source: UniProtKB
Cellular_component	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
Molecular_function	mRNA 3'-UTR binding Inferred from sequence or structural similarity. Source: UniProtKB miRNA binding Inferred from direct assay Ref.18. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro pre-mRNA intronic pyrimidine-rich binding Inferred from direct assay Ref.8Ref.12. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

RNA-binding protein 4

PRO_0000081754

Regions

Domain

2 – 72

71

RRM 1

Domain

78 – 148

71

RRM 2

Zinc finger

160 – 177

18

CCHC-type

Region

196 – 364

169

Interaction with TNPO3

Compositional bias

233 – 239

7

Poly-Ala

Compositional bias

282 – 295

14

Poly-Ala

Amino acid modifications

Modified residue

309

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

139 – 177

39

KRMHV…KECPI → EPPSLGRGLNTRLCAENGWI SKRRGLVKITAVGWLVMKK in isoform 2.

VSP_013414

Alternative sequence

139 – 143

5

KRMHV → GMCVG in isoform 3.

VSP_013413

Alternative sequence

140 – 364

225

RMHVQ…RYSAF → ITPVTEGYCCCNKGHTYIFK NCNLILESRKSRRC in isoform 4.

VSP_044493

Alternative sequence

144 – 364

221

Missing in isoform 3.

VSP_013415

Alternative sequence

178 – 364

187

Missing in isoform 2.

VSP_013416

Experimental info

Mutagenesis

37

1

Y → A: Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115. Ref.7

Mutagenesis

39

1

F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115. Ref.7

Mutagenesis

113

1

Y → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115. Ref.7

Mutagenesis

115

1

F → A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113. Ref.7

Mutagenesis

309

1

S → 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 conflict

52

1

I → M in BAG64902. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

364

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

15 – 23

9

Beta strand

28 – 34

7

Beta strand

37 – 44

8

Helix

45 – 55

11

Beta strand

66 – 68

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 3EA1C80D4C9122A2	FASTA	364	40,314
	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
	Isoform 2 [UniParc]. Checksum: D139DCDF1C9FEF5B	FASTA	177	20,044
	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 AEDAVEAIRG LDNTEFQGEP PSLGRGLNTR LCAENGWISK RRGLVKITAV GWLVMKK
	Isoform 3 [UniParc]. Checksum: 6067E91D4167261A	FASTA	143	16,173
	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 AEDAVEAIRG LDNTEFQGGM CVG
	Isoform 4 [UniParc]. Checksum: A6868F2823CD17B1	FASTA	173	19,788
	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 AEDAVEAIRG LDNTEFQGKI TPVTEGYCCC NKGHTYIFKN CNLILESRKS RRC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 EIF2C1 AND EIF2C2.
[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 EIF2C2, 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.

IPI

IPI00003704.
IPI00556034.
IPI00908491.
IPI00940890.

RefSeq

NP_001185772.1. NM_001198843.1.
NP_001185773.1. NM_001198844.1.
NP_002887.2. NM_002896.3.

UniGene

Hs.523822.
Hs.728823.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DNQ	NMR	-	A	1-77	[»]

ProteinModelPortal

Q9BWF3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44199N.

IntAct

Q9BWF3. 2 interactions.

MINT

MINT-1187795.

STRING

9606.ENSP00000309166.

PTM databases

PhosphoSite

Q9BWF3.

Polymorphism databases

DMDM

62511089.

Proteomic databases

PaxDb

Q9BWF3.

PRIDE

Q9BWF3.

Protocols and materials databases

DNASU

5936.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310092; ENSP00000309166; ENSG00000173933.
ENST00000396053; ENSP00000413497; ENSG00000173933.
ENST00000398692; ENSP00000381680; ENSG00000173933.
ENST00000408993; ENSP00000386561; ENSG00000173933.
ENST00000409406; ENSP00000386894; ENSG00000173933.
ENST00000483858; ENSP00000435821; ENSG00000173933.
ENST00000530235; ENSP00000432150; ENSG00000173933.
ENST00000532968; ENSP00000432020; ENSG00000173933.

GeneID

5936.

KEGG

hsa:5936.

UCSC

uc001oiv.3. human.
uc001oiw.2. human.
uc001oix.2. human.

Organism-specific databases

CTD

5936.

GeneCards

GC11P066406.

HGNC

HGNC:9901. RBM4.

MIM

602571. gene.

neXtProt

NX_Q9BWF3.

PharmGKB

PA34266.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG294108.

HOGENOM

HOG000026790.

HOVERGEN

HBG062217.

KO

K13187.

OMA

IPTIDTC.

OrthoDB

EOG4NP74W.

Gene expression databases

ArrayExpress

Q9BWF3.

Bgee

Q9BWF3.

CleanEx

HS_RBM4.

Genevestigator

Q9BWF3.

GermOnline

ENSG00000173933. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.
4.10.60.10. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
PF00098. zf-CCHC. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RBM4. human.

EvolutionaryTrace

Q9BWF3.

GenomeRNAi

5936.

NextBio

23140.

SOURCE

Search...

Entry information

Entry name

RBM4_HUMAN

Accession

Primary (citable) accession number: Q9BWF3
Secondary accession number(s): B3KUN0 , B4E1U0, E7EQS3, O02916, Q4VC48, Q6P1P2, Q8WU85

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 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.