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Q9NW64

- RBM22_HUMAN

UniProt

Q9NW64 - RBM22_HUMAN

Protein

Pre-mRNA-splicing factor RBM22

Gene

RBM22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.3 Publications

    Regions

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

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. nucleocytoplasmic transporter activity Source: UniProtKB
    4. nucleotide binding Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. pre-mRNA binding Source: UniProtKB
    7. snRNA binding Source: UniProtKB

    GO - Biological processi

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

    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
    Zinc finger CCCH domain-containing protein 16
    Gene namesi
    Name:RBM22
    Synonyms:ZC3H16
    ORF Names:199G4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:25503. RBM22.

    Subcellular locationi

    Nucleus. Cytoplasm
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701K → R: Accumulates in speckle-like structures. 1 Publication
    Mutagenesisi324 – 3241K → R: Accumulates in speckle-like structures. 1 Publication

    Organism-specific databases

    PharmGKBiPA134982384.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 420419Pre-mRNA-splicing factor RBM22PRO_0000250546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei212 – 2121N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NW64.
    PaxDbiQ9NW64.
    PRIDEiQ9NW64.

    PTM databases

    PhosphoSiteiQ9NW64.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NW64.
    BgeeiQ9NW64.
    CleanExiHS_RBM22.
    GenevestigatoriQ9NW64.

    Organism-specific databases

    HPAiHPA001634.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRNPP041561EBI-2602260,EBI-977302

    Protein-protein interaction databases

    BioGridi120821. 15 interactions.
    IntActiQ9NW64. 11 interactions.
    MINTiMINT-2819539.
    STRINGi9606.ENSP00000199814.

    Structurei

    Secondary structure

    1
    420
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi234 – 2374
    Turni240 – 2423
    Helixi245 – 2539
    Beta strandi258 – 2647
    Helixi265 – 2673
    Beta strandi269 – 2768
    Helixi277 – 2859
    Turni286 – 2905
    Beta strandi300 – 3023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YTCNMR-A227-304[»]
    ProteinModelPortaliQ9NW64.
    SMRiQ9NW64. Positions 165-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NW64.

    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.
    HOGENOMiHOG000171086.
    HOVERGENiHBG083475.
    InParanoidiQ9NW64.
    KOiK12872.
    OMAiHSRYGNG.
    OrthoDBiEOG7K0ZCH.
    PhylomeDBiQ9NW64.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NW64-1) [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

    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:October 1, 2000 - v1
    Checksum:iA82549D8CC88C7D0
    GO
    Isoform 2 (identifier: Q9NW64-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-91: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:371
    Mass (Da):41,152
    Checksum:iCD43CE9BAD03CE15
    GO

    Sequence cautioni

    The sequence AAC99998.1 differs from that shown. Reason: Chimera.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei43 – 9149Missing in isoform 2. 1 PublicationVSP_036832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136933 mRNA. Translation: CAB66867.1.
    AK001152 mRNA. Translation: BAA91521.1.
    AK297019 mRNA. Translation: BAG59551.1.
    AC008453 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61711.1.
    BC003402 mRNA. Translation: AAH03402.1.
    U39402 mRNA. Translation: AAC99998.1. Sequence problems.
    CCDSiCCDS34278.1. [Q9NW64-1]
    RefSeqiNP_060517.1. NM_018047.2. [Q9NW64-1]
    UniGeneiHs.713564.

    Genome annotation databases

    EnsembliENST00000199814; ENSP00000199814; ENSG00000086589. [Q9NW64-1]
    ENST00000447771; ENSP00000412118; ENSG00000086589. [Q9NW64-2]
    GeneIDi55696.
    KEGGihsa:55696.
    UCSCiuc003lst.3. human. [Q9NW64-1]

    Polymorphism databases

    DMDMi74762758.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136933 mRNA. Translation: CAB66867.1 .
    AK001152 mRNA. Translation: BAA91521.1 .
    AK297019 mRNA. Translation: BAG59551.1 .
    AC008453 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61711.1 .
    BC003402 mRNA. Translation: AAH03402.1 .
    U39402 mRNA. Translation: AAC99998.1 . Sequence problems.
    CCDSi CCDS34278.1. [Q9NW64-1 ]
    RefSeqi NP_060517.1. NM_018047.2. [Q9NW64-1 ]
    UniGenei Hs.713564.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YTC NMR - A 227-304 [» ]
    ProteinModelPortali Q9NW64.
    SMRi Q9NW64. Positions 165-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120821. 15 interactions.
    IntActi Q9NW64. 11 interactions.
    MINTi MINT-2819539.
    STRINGi 9606.ENSP00000199814.

    PTM databases

    PhosphoSitei Q9NW64.

    Polymorphism databases

    DMDMi 74762758.

    Proteomic databases

    MaxQBi Q9NW64.
    PaxDbi Q9NW64.
    PRIDEi Q9NW64.

    Protocols and materials databases

    DNASUi 55696.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000199814 ; ENSP00000199814 ; ENSG00000086589 . [Q9NW64-1 ]
    ENST00000447771 ; ENSP00000412118 ; ENSG00000086589 . [Q9NW64-2 ]
    GeneIDi 55696.
    KEGGi hsa:55696.
    UCSCi uc003lst.3. human. [Q9NW64-1 ]

    Organism-specific databases

    CTDi 55696.
    GeneCardsi GC05M150050.
    HGNCi HGNC:25503. RBM22.
    HPAi HPA001634.
    MIMi 612430. gene.
    neXtProti NX_Q9NW64.
    PharmGKBi PA134982384.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277760.
    HOGENOMi HOG000171086.
    HOVERGENi HBG083475.
    InParanoidi Q9NW64.
    KOi K12872.
    OMAi HSRYGNG.
    OrthoDBi EOG7K0ZCH.
    PhylomeDBi Q9NW64.
    TreeFami TF314284.

    Miscellaneous databases

    EvolutionaryTracei Q9NW64.
    GeneWikii RBM22.
    GenomeRNAii 55696.
    NextBioi 60521.
    PROi Q9NW64.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NW64.
    Bgeei Q9NW64.
    CleanExi HS_RBM22.
    Genevestigatori Q9NW64.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    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 2).
      Tissue: Mammary gland and Umbilical cord blood.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Placenta.
    6. "Transcriptional map of the Treacher Collins candidate gene region."
      Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
      Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-420.
      Tissue: Brain.
    7. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    8. "Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22."
      Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M., Webb S.E., Miller A.L., Krebs J.
      Biochim. Biophys. Acta 1763:1335-1343(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "The influence of calcium signaling on the regulation of alternative splicing."
      Krebs J.
      Biochim. Biophys. Acta 1793:979-984(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-170 AND LYS-324.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
      Janowicz A., Michalak M., Krebs J.
      Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre."
      Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P., Luhrmann R.
      EMBO J. 31:1591-1604(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Solution structure of RNA binding domain in pre-mRNA-splicing factor RBM22."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 227-304.

    Entry informationi

    Entry nameiRBM22_HUMAN
    AccessioniPrimary (citable) accession number: Q9NW64
    Secondary accession number(s): A6NDM5, B4DLI9, O95607
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 124 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 5
      Human chromosome 5: 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