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P98175

- RBM10_HUMAN

UniProt

P98175 - RBM10_HUMAN

Protein

RNA-binding protein 10

Gene

RBM10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri212 – 24231RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri759 – 78426C2H2-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein complex binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: Ensembl
    2. mRNA processing Source: UniProtKB-KW
    3. negative regulation of cell proliferation Source: Ensembl
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. positive regulation of smooth muscle cell apoptotic process Source: Ensembl
    6. RNA splicing Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA-binding protein 10
    Alternative name(s):
    G patch domain-containing protein 9
    RNA-binding motif protein 10
    RNA-binding protein S1-1
    Short name:
    S1-1
    Gene namesi
    Name:RBM10
    Synonyms:DXS8237E, GPATC9, GPATCH9, KIAA0122
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9896. RBM10.

    Subcellular locationi

    Nucleus 1 Publication
    Note: In the extranucleolar nucleoplasm constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, the nuclear bodies enlarge and decrease in number. They occur closely adjacent to nuclear speckles or IGCs (interchromatin granule clusters) but coincide with TIDRs (transcription-inactivation-dependent RNA domains).

    GO - Cellular componenti

    1. nucleus Source: LIFEdb

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    TARP syndrome (TARPS) [MIM:311900]: A disorder characterized by the Robin sequence (micrognathia, glossoptosis and cleft palate), talipes equinovarus and cardiac defects.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi311900. phenotype.
    Orphaneti2886. TARP syndrome.
    PharmGKBiPA34259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 930930RNA-binding protein 10PRO_0000081767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611Phosphoserine1 Publication
    Modified residuei89 – 891Phosphoserine1 Publication
    Modified residuei383 – 3831N6-acetyllysine1 Publication
    Modified residuei718 – 7181Phosphoserine2 Publications
    Modified residuei723 – 7231Phosphoserine4 Publications
    Modified residuei733 – 7331Phosphoserine2 Publications
    Modified residuei736 – 7361Phosphoserine3 Publications
    Modified residuei738 – 7381Phosphoserine3 Publications
    Modified residuei781 – 7811Phosphoserine1 Publication
    Modified residuei797 – 7971Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP98175.
    PaxDbiP98175.
    PRIDEiP98175.

    PTM databases

    PhosphoSiteiP98175.

    Expressioni

    Gene expression databases

    BgeeiP98175.
    CleanExiHS_RBM10.
    GenevestigatoriP98175.

    Organism-specific databases

    HPAiHPA034972.

    Interactioni

    Subunit structurei

    Associates with the spliceosome. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-721525,EBI-721525
    DHX15O431432EBI-721525,EBI-1237044
    DHX38Q926202EBI-721525,EBI-1043041
    GPKOWQ929172EBI-721525,EBI-746309
    IKQ131232EBI-721525,EBI-713456
    PRPF19Q9UMS42EBI-721525,EBI-395746
    SF3A1Q154592EBI-721525,EBI-1054743
    SF3B4Q154272EBI-721525,EBI-348469
    SNRPCP092342EBI-721525,EBI-766589
    SUGP1Q8IWZ82EBI-721525,EBI-2691671
    U2AF2P263682EBI-721525,EBI-742339
    U2SURPO150422EBI-721525,EBI-310697

    Protein-protein interaction databases

    BioGridi113869. 52 interactions.
    IntActiP98175. 40 interactions.
    MINTiMINT-2864879.
    STRINGi9606.ENSP00000366829.

    Structurei

    Secondary structure

    1
    930
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi130 – 1345
    Helixi142 – 15211
    Beta strandi161 – 1633
    Beta strandi165 – 1673
    Beta strandi171 – 1777
    Helixi181 – 1899
    Turni190 – 1934
    Beta strandi194 – 1974
    Beta strandi200 – 2056
    Beta strandi301 – 3044
    Helixi314 – 3207
    Helixi321 – 3233
    Turni328 – 3303
    Beta strandi337 – 3426
    Beta strandi346 – 3494
    Helixi354 – 36310
    Helixi372 – 3743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LXINMR-A128-218[»]
    2M2BNMR-A277-408[»]
    ProteinModelPortaliP98175.
    SMRiP98175. Positions 128-218, 277-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 20981RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 38485RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini858 – 90447G-patchPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi80 – 878Poly-Arg
    Compositional biasi113 – 12513Poly-GluAdd
    BLAST
    Compositional biasi561 – 60747Tyr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 G-patch domain.PROSITE-ProRule annotation
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri212 – 24231RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri759 – 78426C2H2-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290849.
    HOVERGENiHBG000318.
    InParanoidiP98175.
    KOiK13094.
    OMAiKGDPAGT.
    OrthoDBiEOG7NSB1M.
    PhylomeDBiP98175.
    TreeFamiTF315789.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    4.10.1060.10. 1 hit.
    InterProiIPR000467. G_patch_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF01585. G-patch. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    SMARTiSM00443. G_patch. 1 hit.
    SM00360. RRM. 2 hits.
    SM00355. ZnF_C2H2. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    PROSITEiPS50174. G_PATCH. 1 hit.
    PS50102. RRM. 2 hits.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P98175-1) [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

    MEYERRGGRG DRTGRYGATD RSQDDGGENR SRDHDYRDMD YRSYPREYGS    50
    QEGKHDYDDS SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG 100
    DYRDQDYRTE QGEEEEEEED EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ 150
    SHGVQAREVR LMRNKSSGQS RGFAFVEFSH LQDATRWMEA NQHSLNILGQ 200
    KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK SEAEQKLPLG 250
    TRLDQQTLPL GGRELSQGLL PLPQPYQAQG VLASQALSQG SEPSSENAND 300
    TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL 350
    STIVEAAQLL QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRISAA 400
    SVASTAIAAA QWAISQASQG GEGTWATSEE PPVDYSYYQQ DEGYGNSQGT 450
    ESSLYAHGYL KGTKGPGITG TKGDPTGAGP EASLEPGADS VSMQAFSRAQ 500
    PGAAPGIYQQ SAEASSSQGT AANSQSYTIM SPAVLKSELQ SPTHPSSALP 550
    PATSPTAQES YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA 600
    QSQQYLYWDG ERRTYVPALE QSADGHKETG APSKEGKEKK EKHKTKTAQQ 650
    IAKDMERWAR SLNKQKENFK NSFQPISSLR DDERRESATA DAGYAILEKK 700
    GALAERQHTS MDLPKLASDD RPSPPRGLVA AYSGESDSEE EQERGGPERE 750
    EKLTDWQKLA CLLCRRQFPS KEALIRHQQL SGLHKQNLEI HRRAHLSENE 800
    LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG ISTASVDFEQ 850
    PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG 900
    ARGSSYGVTS TESYKETLHK TMVTRFNEAQ 930
    Length:930
    Mass (Da):103,533
    Last modified:December 16, 2008 - v3
    Checksum:i472E68F085CA5744
    GO
    Isoform 2 (identifier: P98175-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         354-354: Missing.

    Show »
    Length:929
    Mass (Da):103,433
    Checksum:i43D8E086250E441B
    GO
    Isoform 3 (identifier: P98175-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-144: Missing.

    Show »
    Length:853
    Mass (Da):94,469
    Checksum:iBF5689F0C926EDA8
    GO
    Isoform 4 (identifier: P98175-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-144: Missing.
         354-354: Missing.

    Show »
    Length:852
    Mass (Da):94,370
    Checksum:iBB39E0CAC9B4A8A3
    GO

    Sequence cautioni

    The sequence AAB33572.1 differs from that shown. Reason: Frameshift at position 696.
    The sequence CAB70731.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAA09471.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB70731.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti499 – 4991A → P in BAA09471. (PubMed:8590280)Curated
    Sequence conflicti672 – 6721S → T in CAB70731. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti396 – 3961R → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035486

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 14477Missing in isoform 3 and isoform 4. 2 PublicationsVSP_036173Add
    BLAST
    Alternative sequencei354 – 3541Missing in isoform 2 and isoform 4. 2 PublicationsVSP_036035

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50912 mRNA. Translation: BAA09471.1. Different initiation.
    AK292758 mRNA. Translation: BAF85447.1.
    AL137421 mRNA. Translation: CAB70731.1. Sequence problems.
    AL513366 Genomic DNA. Translation: CAI41700.1.
    CH471164 Genomic DNA. Translation: EAW59284.1.
    CH471164 Genomic DNA. Translation: EAW59285.1.
    CH471164 Genomic DNA. Translation: EAW59287.1.
    CH471164 Genomic DNA. Translation: EAW59283.1.
    BC003089 mRNA. Translation: AAH03089.1.
    BC004181 mRNA. Translation: AAH04181.1.
    BC008733 mRNA. Translation: AAH08733.1.
    BC024153 mRNA. Translation: AAH24153.1.
    U35373 mRNA. Translation: AAB33572.1. Frameshift.
    CCDSiCCDS14274.1. [P98175-1]
    CCDS55407.1. [P98175-4]
    CCDS56600.1. [P98175-3]
    RefSeqiNP_001191395.1. NM_001204466.1. [P98175-3]
    NP_001191396.1. NM_001204467.1. [P98175-2]
    NP_005667.2. NM_005676.4. [P98175-1]
    NP_690595.1. NM_152856.2. [P98175-4]
    UniGeneiHs.401509.

    Genome annotation databases

    EnsembliENST00000329236; ENSP00000328848; ENSG00000182872. [P98175-4]
    ENST00000345781; ENSP00000329659; ENSG00000182872. [P98175-3]
    ENST00000377604; ENSP00000366829; ENSG00000182872. [P98175-1]
    GeneIDi8241.
    KEGGihsa:8241.
    UCSCiuc004dhf.3. human. [P98175-1]
    uc004dhg.3. human. [P98175-4]
    uc004dhh.3. human. [P98175-2]
    uc010nhq.3. human. [P98175-3]

    Polymorphism databases

    DMDMi218512116.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50912 mRNA. Translation: BAA09471.1 . Different initiation.
    AK292758 mRNA. Translation: BAF85447.1 .
    AL137421 mRNA. Translation: CAB70731.1 . Sequence problems.
    AL513366 Genomic DNA. Translation: CAI41700.1 .
    CH471164 Genomic DNA. Translation: EAW59284.1 .
    CH471164 Genomic DNA. Translation: EAW59285.1 .
    CH471164 Genomic DNA. Translation: EAW59287.1 .
    CH471164 Genomic DNA. Translation: EAW59283.1 .
    BC003089 mRNA. Translation: AAH03089.1 .
    BC004181 mRNA. Translation: AAH04181.1 .
    BC008733 mRNA. Translation: AAH08733.1 .
    BC024153 mRNA. Translation: AAH24153.1 .
    U35373 mRNA. Translation: AAB33572.1 . Frameshift.
    CCDSi CCDS14274.1. [P98175-1 ]
    CCDS55407.1. [P98175-4 ]
    CCDS56600.1. [P98175-3 ]
    RefSeqi NP_001191395.1. NM_001204466.1. [P98175-3 ]
    NP_001191396.1. NM_001204467.1. [P98175-2 ]
    NP_005667.2. NM_005676.4. [P98175-1 ]
    NP_690595.1. NM_152856.2. [P98175-4 ]
    UniGenei Hs.401509.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LXI NMR - A 128-218 [» ]
    2M2B NMR - A 277-408 [» ]
    ProteinModelPortali P98175.
    SMRi P98175. Positions 128-218, 277-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113869. 52 interactions.
    IntActi P98175. 40 interactions.
    MINTi MINT-2864879.
    STRINGi 9606.ENSP00000366829.

    PTM databases

    PhosphoSitei P98175.

    Polymorphism databases

    DMDMi 218512116.

    Proteomic databases

    MaxQBi P98175.
    PaxDbi P98175.
    PRIDEi P98175.

    Protocols and materials databases

    DNASUi 8241.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329236 ; ENSP00000328848 ; ENSG00000182872 . [P98175-4 ]
    ENST00000345781 ; ENSP00000329659 ; ENSG00000182872 . [P98175-3 ]
    ENST00000377604 ; ENSP00000366829 ; ENSG00000182872 . [P98175-1 ]
    GeneIDi 8241.
    KEGGi hsa:8241.
    UCSCi uc004dhf.3. human. [P98175-1 ]
    uc004dhg.3. human. [P98175-4 ]
    uc004dhh.3. human. [P98175-2 ]
    uc010nhq.3. human. [P98175-3 ]

    Organism-specific databases

    CTDi 8241.
    GeneCardsi GC0XP047004.
    HGNCi HGNC:9896. RBM10.
    HPAi HPA034972.
    MIMi 300080. gene.
    311900. phenotype.
    neXtProti NX_P98175.
    Orphaneti 2886. TARP syndrome.
    PharmGKBi PA34259.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290849.
    HOVERGENi HBG000318.
    InParanoidi P98175.
    KOi K13094.
    OMAi KGDPAGT.
    OrthoDBi EOG7NSB1M.
    PhylomeDBi P98175.
    TreeFami TF315789.

    Miscellaneous databases

    ChiTaRSi RBM10. human.
    GeneWikii RBM10.
    GenomeRNAii 8241.
    NextBioi 30996.
    PROi P98175.
    SOURCEi Search...

    Gene expression databases

    Bgeei P98175.
    CleanExi HS_RBM10.
    Genevestigatori P98175.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    4.10.1060.10. 1 hit.
    InterProi IPR000467. G_patch_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF01585. G-patch. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    SMARTi SM00443. G_patch. 1 hit.
    SM00360. RRM. 2 hits.
    SM00355. ZnF_C2H2. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50174. G_PATCH. 1 hit.
    PS50102. RRM. 2 hits.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    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] (ISOFORM 3).
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 AND 4).
      Tissue: Brain, Lung, Muscle and Placenta.
    7. "A novel gene, DXS8237E, lies within 20 kb upstream of UBE1 in Xp11.23 and has a different X inactivation status."
      Coleman M.P., Ambrose H.J., Carrel L., Nemeth A.H., Willard H.F., Davies K.E.
      Genomics 31:135-138(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 544-930.
      Tissue: Fetal brain.
    8. "Large-scale proteomic analysis of the human spliceosome."
      Rappsilber J., Ryder U., Lamond A.I., Mann M.
      Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-723; SER-733; SER-736 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736; SER-738 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Massively parallel sequencing of exons on the X chromosome identifies RBM10 as the gene that causes a syndromic form of cleft palate."
      Johnston J.J., Teer J.K., Cherukuri P.F., Hansen N.F., Loftus S.K., Chong K., Mullikin J.C., Biesecker L.G.
      Am. J. Hum. Genet. 86:743-748(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN TARPS.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-718; SER-723; SER-738; SER-781 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718; SER-723; SER-736 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
      Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
      Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
    21. "S1-1 nuclear domains: characterization and dynamics as a function of transcriptional activity."
      Inoue A., Tsugawa K., Tokunaga K., Takahashi K.P., Uni S., Kimura M., Nishio K., Yamamoto N., Honda K., Watanabe T., Yamane H., Tani T.
      Biol. Cell 100:523-535(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-396.

    Entry informationi

    Entry nameiRBM10_HUMAN
    AccessioniPrimary (citable) accession number: P98175
    Secondary accession number(s): C4AM81
    , Q14136, Q5JRR2, Q9BTE4, Q9BTX0, Q9NTB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3