RBM14_PONAB
ID RBM14_PONAB Reviewed; 669 AA.
AC Q5RC41;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=RNA-binding protein 14;
DE AltName: Full=RNA-binding motif protein 14;
GN Name=RBM14;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a nuclear receptor coactivator, enhancing
CC transcription through other coactivators such as NCOA6 and CITED1.
CC Regulates centriole biogenesis by suppressing the formation of aberrant
CC centriolar protein complexes in the cytoplasm and thus preserving
CC mitotic spindle integrity. Prevents the formation of the STIL-CENPJ
CC complex (which can induce the formation of aberrant centriolar protein
CC complexes) by interfering with the interaction of STIL with CENPJ.
CC Plays a role in the regulation of DNA virus-mediated innate immune
CC response by assembling into the HDP-RNP complex, a complex that serves
CC as a platform for IRF3 phosphorylation and subsequent innate immune
CC response activation through the cGAS-STING pathway.
CC {ECO:0000250|UniProtKB:Q96PK6}.
CC -!- SUBUNIT: Interacts with NCOA6, CITED1 and XRCC5/KU86. Interacts with
CC SS18. Interacts with STIL and interferes with its interaction with
CC CENPJ. Interacts with gamma-tubulin. Part of the HDP-RNP complex
CC composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins
CC (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA.
CC {ECO:0000250|UniProtKB:Q96PK6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PK6}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q96PK6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96PK6}. Note=In punctate subnuclear structures
CC often located adjacent to splicing speckles, called paraspeckles.
CC Cytoplasmic localization is crucial for its function in suppressing the
CC formation of aberrant centriolar protein complexes.
CC {ECO:0000250|UniProtKB:Q96PK6}.
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DR EMBL; CR858440; CAH90669.1; -; mRNA.
DR RefSeq; NP_001125363.1; NM_001131891.2.
DR AlphaFoldDB; Q5RC41; -.
DR SMR; Q5RC41; -.
DR STRING; 9601.ENSPPYP00000003492; -.
DR GeneID; 100172266; -.
DR KEGG; pon:100172266; -.
DR CTD; 10432; -.
DR eggNOG; ENOG502R6FF; Eukaryota.
DR InParanoid; Q5RC41; -.
DR OrthoDB; 1563362at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd12608; RRM1_CoAA; 1.
DR CDD; cd12609; RRM2_CoAA; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034506; RBM14_RRM1.
DR InterPro; IPR034507; RBM14_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..669
FT /note="RNA-binding protein 14"
FT /id="PRO_0000081776"
FT DOMAIN 1..73
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 79..149
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 147..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..354
FT /note="TRBP-interacting domain; interaction with STIL"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT REGION 566..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 164
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C2Q3"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
SQ SEQUENCE 669 AA; 69466 MW; 4CE6E555BA6981ED CRC64;
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR AIEALHGHEL
RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME
KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG
FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ
PSVSLGAAYR AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS
SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA
AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYNAQPSASY NAQSAPYAAQ
QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASM
GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPHRTQS SASLAASYAA QQHPQAAASY
RGQPGNAYDG AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ
MHSGYQRRM
