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Q8BHS3

- RBM22_MOUSE

UniProt

Q8BHS3 - RBM22_MOUSE

Protein

Pre-mRNA-splicing factor RBM22

Gene

Rbm22

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. nucleocytoplasmic transporter activity Source: UniProtKB
    3. nucleotide binding Source: InterPro
    4. pre-mRNA binding Source: UniProtKB
    5. snRNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to drug Source: UniProtKB
    2. mRNA cis splicing, via spliceosome Source: UniProtKB
    3. positive regulation of intracellular protein transport Source: UniProtKB
    4. positive regulation of RNA splicing Source: UniProtKB
    5. protein import into nucleus, translocation Source: Ensembl

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transport

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-mRNA-splicing factor RBM22
    Alternative name(s):
    RNA-binding motif protein 22
    Gene namesi
    Name:Rbm22
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1914060. Rbm22.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity
    Note: Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol By similarity.By similarity

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 420419Pre-mRNA-splicing factor RBM22PRO_0000250548Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei212 – 2121N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BHS3.
    PaxDbiQ8BHS3.
    PRIDEiQ8BHS3.

    PTM databases

    PhosphoSiteiQ8BHS3.

    Expressioni

    Gene expression databases

    BgeeiQ8BHS3.
    CleanExiMM_RBM22.
    GenevestigatoriQ8BHS3.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8BHS3. 1 interaction.
    MINTiMINT-4110604.
    STRINGi10090.ENSMUSP00000025506.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BHS3.
    SMRiQ8BHS3. Positions 165-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini232 – 30574RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi327 – 40781Pro-richAdd
    BLAST

    Domaini

    The C-terminus RRM domain and the zinc finger motif are necessary for RNA-binding.By similarity

    Sequence similaritiesi

    Belongs to the SLT11 family.Curated
    Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG277760.
    GeneTreeiENSGT00390000002792.
    HOGENOMiHOG000171086.
    HOVERGENiHBG083475.
    InParanoidiQ8BHS3.
    KOiK12872.
    OMAiHSRYGNG.
    OrthoDBiEOG7K0ZCH.
    TreeFamiTF314284.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR000571. Znf_CCCH.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    SM00356. ZnF_C3H1. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BHS3-1 [UniParc]FASTAAdd to Basket

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    MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR    50
    PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG 100
    LSFKDDMPKS DVNKEYYTQN MEREISNSDG TRPVGMLGKA TSTSDMLLKL 150
    ARTTPYYKRN RPHICSFWVK GECKRGEECP YRHEKPTDPD DPLADQNIKD 200
    RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG DTITETDLRN 250
    HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV 300
    KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF 350
    NLPPSGPPAV VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI 400
    HYPSQDPQRM GAHAGKHSSP 420
    Length:420
    Mass (Da):46,896
    Last modified:March 1, 2003 - v1
    Checksum:iA82549D8CC88C7D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711G → R in BAE39585. (PubMed:16141072)Curated
    Sequence conflicti339 – 3391P → L in BAB31220. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018452 mRNA. Translation: BAB31220.1.
    AK045116 mRNA. Translation: BAC32229.1.
    AK150271 mRNA. Translation: BAE29427.1.
    AK151758 mRNA. Translation: BAE30665.1.
    AK152252 mRNA. Translation: BAE31073.1.
    AK166600 mRNA. Translation: BAE38885.1.
    AK167509 mRNA. Translation: BAE39585.1.
    AK168919 mRNA. Translation: BAE40732.1.
    BC080205 mRNA. Translation: AAH80205.1.
    CCDSiCCDS29272.1.
    RefSeqiNP_080052.1. NM_025776.2.
    UniGeneiMm.275106.

    Genome annotation databases

    EnsembliENSMUST00000025506; ENSMUSP00000025506; ENSMUSG00000024604.
    GeneIDi66810.
    KEGGimmu:66810.
    UCSCiuc008fal.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018452 mRNA. Translation: BAB31220.1 .
    AK045116 mRNA. Translation: BAC32229.1 .
    AK150271 mRNA. Translation: BAE29427.1 .
    AK151758 mRNA. Translation: BAE30665.1 .
    AK152252 mRNA. Translation: BAE31073.1 .
    AK166600 mRNA. Translation: BAE38885.1 .
    AK167509 mRNA. Translation: BAE39585.1 .
    AK168919 mRNA. Translation: BAE40732.1 .
    BC080205 mRNA. Translation: AAH80205.1 .
    CCDSi CCDS29272.1.
    RefSeqi NP_080052.1. NM_025776.2.
    UniGenei Mm.275106.

    3D structure databases

    ProteinModelPortali Q8BHS3.
    SMRi Q8BHS3. Positions 165-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BHS3. 1 interaction.
    MINTi MINT-4110604.
    STRINGi 10090.ENSMUSP00000025506.

    PTM databases

    PhosphoSitei Q8BHS3.

    Proteomic databases

    MaxQBi Q8BHS3.
    PaxDbi Q8BHS3.
    PRIDEi Q8BHS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025506 ; ENSMUSP00000025506 ; ENSMUSG00000024604 .
    GeneIDi 66810.
    KEGGi mmu:66810.
    UCSCi uc008fal.1. mouse.

    Organism-specific databases

    CTDi 55696.
    MGIi MGI:1914060. Rbm22.

    Phylogenomic databases

    eggNOGi NOG277760.
    GeneTreei ENSGT00390000002792.
    HOGENOMi HOG000171086.
    HOVERGENi HBG083475.
    InParanoidi Q8BHS3.
    KOi K12872.
    OMAi HSRYGNG.
    OrthoDBi EOG7K0ZCH.
    TreeFami TF314284.

    Miscellaneous databases

    ChiTaRSi RBM22. mouse.
    NextBioi 322703.
    PROi Q8BHS3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BHS3.
    CleanExi MM_RBM22.
    Genevestigatori Q8BHS3.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR000571. Znf_CCCH.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    SM00356. ZnF_C3H1. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Heart, Lung and Placenta.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRBM22_MOUSE
    AccessioniPrimary (citable) accession number: Q8BHS3
    Secondary accession number(s): Q3TJB0, Q9CXA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3