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Q9BWF3

- RBM4_HUMAN

UniProt

Q9BWF3 - RBM4_HUMAN

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Protein
RNA-binding protein 4
Gene
RBM4, RBM4A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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.6 Publications

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
Complete GO annotation...

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 4
PRO_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.1 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9BWF3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7271RRM 1
Add
BLAST
Domaini78 – 14871RRM 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 364169Interaction with TNPO3
Add
BLAST

Compositional bias

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

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 17739KRMHV…KECPI → EPPSLGRGLNTRLCAENGWI SKRRGLVKITAVGWLVMKK in isoform 2.
VSP_013414Add
BLAST
Alternative sequencei139 – 1435KRMHV → GMCVG in isoform 3.
VSP_013413
Alternative sequencei140 – 364225RMHVQ…RYSAF → ITPVTEGYCCCNKGHTYIFK NCNLILESRKSRRC in isoform 4.
VSP_044493Add
BLAST
Alternative sequencei144 – 364221Missing in isoform 3.
VSP_013415Add
BLAST
Alternative sequencei178 – 364187Missing in isoform 2.
VSP_013416Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521I → M in BAG64902. 1 Publication

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]
ENST00000503028; ENSP00000425760; ENSG00000173933. [Q9BWF3-1]
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 ]
ENST00000503028 ; ENSP00000425760 ; ENSG00000173933 . [Q9BWF3-1 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 127 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

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