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Q96PK6

- RBM14_HUMAN

UniProt

Q96PK6 - RBM14_HUMAN

Protein

RNA-binding protein 14

Gene

RBM14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1.

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein binding, bridging Source: UniProtKB
    6. RNA binding Source: UniProtKB
    7. RNA polymerase II transcription cofactor activity Source: UniProtKB

    GO - Biological processi

    1. DNA recombination Source: UniProtKB
    2. DNA repair Source: UniProtKB
    3. DNA replication Source: UniProtKB
    4. glucocorticoid receptor signaling pathway Source: UniProtKB
    5. histone deacetylation Source: UniProtKB
    6. intracellular estrogen receptor signaling pathway Source: UniProtKB
    7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. response to hormone Source: UniProtKB
    9. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA-binding protein 14
    Alternative name(s):
    Paraspeckle protein 2
    Short name:
    PSP2
    RNA-binding motif protein 14
    RRM-containing coactivator activator/modulator
    Synaptotagmin-interacting protein
    Short name:
    SYT-interacting protein
    Gene namesi
    Name:RBM14
    Synonyms:SIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14219. RBM14.

    Subcellular locationi

    Nucleus. Nucleusnucleolus
    Note: In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.

    GO - Cellular componenti

    1. mediator complex Source: UniProtKB
    2. nucleus Source: HPA
    3. ribonucleoprotein complex Source: UniProtKB
    4. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34263.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 669669RNA-binding protein 14PRO_0000081774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei161 – 1611Phosphoserine1 Publication
    Modified residuei164 – 1641N6-acetyllysineBy similarity
    Modified residuei206 – 2061Phosphothreonine6 Publications
    Modified residuei220 – 2201Phosphoserine1 Publication
    Modified residuei256 – 2561Phosphoserine1 Publication
    Modified residuei562 – 5621Phosphoserine1 Publication
    Modified residuei572 – 5721Phosphothreonine1 Publication
    Modified residuei618 – 6181Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96PK6.
    PaxDbiQ96PK6.
    PRIDEiQ96PK6.

    PTM databases

    PhosphoSiteiQ96PK6.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.

    Gene expression databases

    ArrayExpressiQ96PK6.
    BgeeiQ96PK6.
    GenevestigatoriQ96PK6.

    Organism-specific databases

    HPAiHPA006628.

    Interactioni

    Subunit structurei

    Isoform 1 interacts with NCOA6, CITED1 and XRCC5/KU86. Isoform 1 interacts with SS18 isoform 1. Isoform 1 interacts with SS18 isoform 2.2 Publications

    Protein-protein interaction databases

    BioGridi115700. 94 interactions.
    IntActiQ96PK6. 17 interactions.
    MINTiMINT-2798129.
    STRINGi9606.ENSP00000311747.

    Structurei

    Secondary structure

    1
    669
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi81 – 855
    Helixi92 – 10211
    Beta strandi105 – 1106
    Beta strandi115 – 1206
    Helixi122 – 13211
    Beta strandi143 – 1475

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DNPNMR-A77-153[»]
    ProteinModelPortaliQ96PK6.
    SMRiQ96PK6. Positions 2-155.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96PK6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7373RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini79 – 14971RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni307 – 35448TRBP-interacting domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi224 – 569346Ala-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000065673.
    HOVERGENiHBG053180.
    InParanoidiQ96PK6.
    KOiK13189.
    OMAiGSYSEYL.
    OrthoDBiEOG7SFJ0M.
    PhylomeDBiQ96PK6.
    TreeFamiTF320661.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96PK6-1) [UniParc]FASTAAdd to Basket

    Also known as: CoAA

    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

    MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR    50
    AIEALHGHEL RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE 100
    RRGRVIECDV VKDYAFVHME KEADAKAAIA QLNGKEVKGK RINVELSTKG 150
    QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG FSATFDYQQA FGNSTGGFDG 200
    QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ PSVSLGAAYR 250
    AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS 300
    SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA 350
    QAASSYGVRA AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA 400
    SYNAQPSASY NAQSAPYAAQ QAASYSSQPA AYVAQPATAA AYASQPAAYA 450
    AQATTPMAGS YGAQPVVQTQ LNSYGAQASM GLSGSYGAQS AAAATGSYGA 500
    AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY RGQPGNAYDG 550
    AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK 600
    RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG 650
    SYNDYLRAAQ MHSGYQRRM 669
    Length:669
    Mass (Da):69,492
    Last modified:August 30, 2005 - v2
    Checksum:i565C5EF51B6881FD
    GO
    Isoform 2 (identifier: Q96PK6-2) [UniParc]FASTAAdd to Basket

    Also known as: CoAM

    The sequence of this isoform differs from the canonical sequence as follows:
         151-156: QKKGPG → MVPTGV
         157-669: Missing.

    Show »
    Length:156
    Mass (Da):17,117
    Checksum:iBCD4C7DA01982D64
    GO
    Isoform 3 (identifier: Q96PK6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         113-118: DYAFVH → GGMCVG
         119-669: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:118
    Mass (Da):12,894
    Checksum:iCDC3102FDFAF75A5
    GO
    Isoform 4 (identifier: Q96PK6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         113-119: DYAFVHM → GMVPTGV
         120-669: Missing.

    Show »
    Length:119
    Mass (Da):13,031
    Checksum:i9B1DC069EB814F75
    GO
    Isoform 5 (identifier: Q96PK6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         112-339: KDYAFVHMEK...SYGAQGSSLA → KGKRMHVQLS...YADRARYSAF
         340-669: Missing.

    Show »
    Length:339
    Mass (Da):37,035
    Checksum:i3618E2DA670C7E21
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti560 – 5601S → T in AAK77961. (PubMed:11443112)Curated
    Sequence conflicti609 – 6091A → V in BAD96550. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei112 – 339228KDYAF…GSSLA → KGKRMHVQLSTSRLRTAPGM GDQSGCYRCGKEGHWSKECP IDRSGRVADLTEQYNEQYGA VRTPYTMSYGDSLYYNNAYG ALDAYYKRCRAARSYEAVAA AAASVYNYAEQTLSQLPQVQ NTAMASHLTSTSLDPYDRHL LPTSGAAATAAAAAAAAAAV TAASTSYYGRDRSPLRRATA PVPTVGEGYGYGHESELSQA SAAARNSLYDMARYEREQYA DRARYSAF in isoform 5. 1 PublicationVSP_047494Add
    BLAST
    Alternative sequencei113 – 1197DYAFVHM → GMVPTGV in isoform 4. CuratedVSP_047109
    Alternative sequencei113 – 1186DYAFVH → GGMCVG in isoform 3. 2 PublicationsVSP_044641
    Alternative sequencei119 – 669551Missing in isoform 3. 2 PublicationsVSP_044642Add
    BLAST
    Alternative sequencei120 – 669550Missing in isoform 4. CuratedVSP_047110Add
    BLAST
    Alternative sequencei151 – 1566QKKGPG → MVPTGV in isoform 2. 1 PublicationVSP_015078
    Alternative sequencei157 – 669513Missing in isoform 2. 1 PublicationVSP_015079Add
    BLAST
    Alternative sequencei340 – 669330Missing in isoform 5. 1 PublicationVSP_047495Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315632 mRNA. Translation: AAK77961.1.
    AF315633 mRNA. Translation: AAK77962.1.
    DQ294957 mRNA. Translation: ABB99396.1.
    EU287938 mRNA. Translation: ABY74511.1.
    AF080561 mRNA. Translation: AAC64058.1.
    AK021768 mRNA. Translation: BAG51046.1.
    AK222830 mRNA. Translation: BAD96550.1.
    AP001157 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74552.1.
    BC000488 mRNA. Translation: AAH00488.1.
    BE885635 mRNA. No translation available.
    CR749306 mRNA. Translation: CAH18161.1.
    CCDSiCCDS55772.1. [Q96PK6-2]
    CCDS55773.1. [Q96PK6-4]
    CCDS8147.1. [Q96PK6-1]
    RefSeqiNP_001185765.1. NM_001198836.1. [Q96PK6-2]
    NP_001185766.1. NM_001198837.1. [Q96PK6-4]
    NP_001185774.1. NM_001198845.1. [Q96PK6-5]
    NP_001185775.1. NM_001198846.1. [Q96PK6-3]
    NP_006319.1. NM_006328.3. [Q96PK6-1]
    UniGeneiHs.523822.
    Hs.533712.

    Genome annotation databases

    EnsembliENST00000310137; ENSP00000311747; ENSG00000239306. [Q96PK6-1]
    ENST00000393979; ENSP00000377548; ENSG00000239306. [Q96PK6-2]
    ENST00000409738; ENSP00000386995; ENSG00000239306. [Q96PK6-4]
    GeneIDi100526737.
    10432.
    KEGGihsa:100526737.
    hsa:10432.
    UCSCiuc001oit.3. human. [Q96PK6-1]
    uc009yri.3. human. [Q96PK6-2]

    Polymorphism databases

    DMDMi73913750.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315632 mRNA. Translation: AAK77961.1 .
    AF315633 mRNA. Translation: AAK77962.1 .
    DQ294957 mRNA. Translation: ABB99396.1 .
    EU287938 mRNA. Translation: ABY74511.1 .
    AF080561 mRNA. Translation: AAC64058.1 .
    AK021768 mRNA. Translation: BAG51046.1 .
    AK222830 mRNA. Translation: BAD96550.1 .
    AP001157 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74552.1 .
    BC000488 mRNA. Translation: AAH00488.1 .
    BE885635 mRNA. No translation available.
    CR749306 mRNA. Translation: CAH18161.1 .
    CCDSi CCDS55772.1. [Q96PK6-2 ]
    CCDS55773.1. [Q96PK6-4 ]
    CCDS8147.1. [Q96PK6-1 ]
    RefSeqi NP_001185765.1. NM_001198836.1. [Q96PK6-2 ]
    NP_001185766.1. NM_001198837.1. [Q96PK6-4 ]
    NP_001185774.1. NM_001198845.1. [Q96PK6-5 ]
    NP_001185775.1. NM_001198846.1. [Q96PK6-3 ]
    NP_006319.1. NM_006328.3. [Q96PK6-1 ]
    UniGenei Hs.523822.
    Hs.533712.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DNP NMR - A 77-153 [» ]
    ProteinModelPortali Q96PK6.
    SMRi Q96PK6. Positions 2-155.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115700. 94 interactions.
    IntActi Q96PK6. 17 interactions.
    MINTi MINT-2798129.
    STRINGi 9606.ENSP00000311747.

    PTM databases

    PhosphoSitei Q96PK6.

    Polymorphism databases

    DMDMi 73913750.

    Proteomic databases

    MaxQBi Q96PK6.
    PaxDbi Q96PK6.
    PRIDEi Q96PK6.

    Protocols and materials databases

    DNASUi 10432.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310137 ; ENSP00000311747 ; ENSG00000239306 . [Q96PK6-1 ]
    ENST00000393979 ; ENSP00000377548 ; ENSG00000239306 . [Q96PK6-2 ]
    ENST00000409738 ; ENSP00000386995 ; ENSG00000239306 . [Q96PK6-4 ]
    GeneIDi 100526737.
    10432.
    KEGGi hsa:100526737.
    hsa:10432.
    UCSCi uc001oit.3. human. [Q96PK6-1 ]
    uc009yri.3. human. [Q96PK6-2 ]

    Organism-specific databases

    CTDi 100526737.
    10432.
    GeneCardsi GC11P066384.
    HGNCi HGNC:14219. RBM14.
    HPAi HPA006628.
    MIMi 612409. gene.
    neXtProti NX_Q96PK6.
    PharmGKBi PA34263.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000065673.
    HOVERGENi HBG053180.
    InParanoidi Q96PK6.
    KOi K13189.
    OMAi GSYSEYL.
    OrthoDBi EOG7SFJ0M.
    PhylomeDBi Q96PK6.
    TreeFami TF320661.

    Miscellaneous databases

    ChiTaRSi RBM14. human.
    RBM14-RBM4. human.
    EvolutionaryTracei Q96PK6.
    GeneWikii RBM14.
    NextBioi 34054915.
    PROi Q96PK6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96PK6.
    Bgeei Q96PK6.
    Genevestigatori Q96PK6.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)."
      Iwasaki T., Chin W.W., Ko L.
      J. Biol. Chem. 276:33375-33383(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, INTERACTION WITH CITED1; NCOA6 AND XRCC5.
    2. "Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation."
      Yang Z., Sui Y., Xiong S., Liour S.S., Phillips A.C., Ko L.
      Nucleic Acids Res. 35:1919-1932(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Functional pre- mRNA trans-splicing of coactivator CoAA and corepressor RBM4 during stem/progenitor cell differentiation."
      Brooks Y.S., Wang G., Yang Z., Smith K.K., Bieberich E., Ko L.
      J. Biol. Chem. 284:18033-18046(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    4. "SIP, a novel protein interacting with SYT."
      Antonson P., Goodwin G.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Synovial sarcoma.
    5. "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 1).
      Tissue: Embryo.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 3).
      Tissue: Leiomyosarcoma and Lung.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-669.
      Tissue: Liver.
    11. Cited for: SUBCELLULAR LOCATION.
    12. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Synovial sarcoma translocation (SYT) encodes a nuclear receptor coactivator."
      Iwasaki T., Koibuchi N., Chin W.W.
      Endocrinology 146:3892-3899(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SS18.
    14. "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 THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    18. "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 THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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].
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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 THR-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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-161; THR-206 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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 THR-206 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    27. "Solution structure of RNA binding domain 2 in RNA-binding protein 14."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 77-153.

    Entry informationi

    Entry nameiRBM14_HUMAN
    AccessioniPrimary (citable) accession number: Q96PK6
    Secondary accession number(s): B0LM41
    , B3KMN4, D6RGD8, O75932, Q2PYN1, Q53GV1, Q68DQ9, Q96PK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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