RBM7_HUMAN
ID RBM7_HUMAN Reviewed; 266 AA.
AC Q9Y580; B2R6K8; Q9NUT4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=RNA-binding protein 7 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 7 {ECO:0000312|HGNC:HGNC:9904};
GN Name=RBM7 {ECO:0000312|HGNC:HGNC:9904};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=12634307; DOI=10.1002/j.1939-4640.2003.tb02664.x;
RA Guo T.B., Boros L.G., Chan K.C., Hikim A.P., Hudson A.P., Swerdloff R.S.,
RA Mitchell A.P., Salameh W.A.;
RT "Spermatogenetic expression of RNA-binding motif protein 7, a protein that
RT interacts with splicing factors.";
RL J. Androl. 24:204-214(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH ZCCHC8.
RX PubMed=16263084; DOI=10.1016/j.bbrc.2005.10.090;
RA Gustafson M.P., Welcker M., Hwang H.C., Clurman B.E.;
RT "Zcchc8 is a glycogen synthase kinase-3 substrate that interacts with RNA-
RT binding proteins.";
RL Biochem. Biophys. Res. Commun. 338:1359-1367(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21855801; DOI=10.1016/j.molcel.2011.06.028;
RA Lubas M., Christensen M.S., Kristiansen M.S., Domanski M., Falkenby L.G.,
RA Lykke-Andersen S., Andersen J.S., Dziembowski A., Jensen T.H.;
RT "Interaction profiling identifies the human nuclear exosome targeting
RT complex.";
RL Mol. Cell 43:624-637(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION, MUTAGENESIS OF SER-136
RP AND SER-204, AND FUNCTION.
RX PubMed=25189701; DOI=10.1101/gad.246272.114;
RA Blasius M., Wagner S.A., Choudhary C., Bartek J., Jackson S.P.;
RT "A quantitative 14-3-3 interaction screen connects the nuclear exosome
RT targeting complex to the DNA damage response.";
RL Genes Dev. 28:1977-1982(2014).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION.
RX PubMed=25578728; DOI=10.1016/j.celrep.2014.12.026;
RA Lubas M., Andersen P.R., Schein A., Dziembowski A., Kudla G., Jensen T.H.;
RT "The human nuclear exosome targeting complex is loaded onto newly
RT synthesized RNA to direct early ribonucleolysis.";
RL Cell Rep. 10:178-192(2015).
RN [14]
RP ACETYLATION AT GLY-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [15]
RP PHOSPHORYLATION AT SER-136, MUTAGENESIS OF SER-136, AND FUNCTION.
RX PubMed=25525152; DOI=10.1261/rna.048090.114;
RA Tiedje C., Lubas M., Tehrani M., Menon M.B., Ronkina N., Rousseau S.,
RA Cohen P., Kotlyarov A., Gaestel M.;
RT "p38MAPK/MK2-mediated phosphorylation of RBM7 regulates the human nuclear
RT exosome targeting complex.";
RL RNA 21:262-278(2015).
RN [16]
RP SUBUNIT, INTERACTION WITH MTREX AND ZCCHC8, AND FUNCTION.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
RN [17]
RP MUTAGENESIS OF LYS-50; PHE-52 AND PHE-54, FUNCTION, AND INTERACTION WITH
RP MEPCE AND LARP7.
RX PubMed=30824372; DOI=10.1016/j.molcel.2019.01.033;
RA Bugai A., Quaresma A.J.C., Friedel C.C., Lenasi T., Duester R.,
RA Sibley C.R., Fujinaga K., Kukanja P., Hennig T., Blasius M., Geyer M.,
RA Ule J., Doelken L., Barboric M.;
RT "P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response
RT to Genotoxic Stress.";
RL Mol. Cell 74:254-267(2019).
RN [18]
RP VARIANT ARG-79.
RX PubMed=27193168; DOI=10.1093/hmg/ddw149;
RA Giunta M., Edvardson S., Xu Y., Schuelke M., Gomez-Duran A., Boczonadi V.,
RA Elpeleg O., Mueller J.S., Horvath R.;
RT "Altered RNA metabolism due to a homozygous RBM7 mutation in a patient with
RT spinal motor neuropathy.";
RL Hum. Mol. Genet. 25:2985-2996(2016).
RN [19] {ECO:0007744|PDB:2M8H}
RP STRUCTURE BY NMR OF 6-94, DOMAIN, MUTAGENESIS OF PHE-13 AND PHE-52,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25852104; DOI=10.1093/nar/gkv240;
RA Hrossova D., Sikorsky T., Potesil D., Bartosovic M., Pasulka J.,
RA Zdrahal Z., Stefl R., Vanacova S.;
RT "RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end
RT extended forms of snRNAs.";
RL Nucleic Acids Res. 43:4236-4248(2015).
RN [20] {ECO:0007744|PDB:5IQQ}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 1-91.
RX PubMed=27139832; DOI=10.1107/s2053230x16006129;
RA Sofos N., Winkler M.B., Brodersen D.E.;
RT "RRM domain of human RBM7: purification, crystallization and structure
RT determination.";
RL Acta Crystallogr. F 72:397-402(2016).
RN [21] {ECO:0007744|PDB:5LXR, ECO:0007744|PDB:5LXY}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-86 IN COMPLEX WITH ZCCHC8,
RP SUBUNIT, INTERACTION WITH ZCCHC8 AND SF3B2/SAP145, AND MUTAGENESIS OF
RP LEU-25; LEU-29; TYR-65 AND LEU-69.
RX PubMed=27905398; DOI=10.1038/ncomms13573;
RA Falk S., Finogenova K., Melko M., Benda C., Lykke-Andersen S., Jensen T.H.,
RA Conti E.;
RT "Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections
RT to splicing factors.";
RL Nat. Commun. 7:13573-13573(2016).
CC -!- FUNCTION: RNA-binding subunit of the trimeric nuclear exosome targeting
CC (NEXT) complex, a complex that functions as an RNA exosome cofactor
CC that directs a subset of non-coding short-lived RNAs for exosomal
CC degradation (PubMed:25189701, PubMed:25578728, PubMed:25525152,
CC PubMed:25852104, PubMed:27871484). NEXT is involved in surveillance and
CC turnover of aberrant transcripts and non-coding RNAs (PubMed:25189701,
CC PubMed:27871484, PubMed:25852104). Binds preferentially polyuridine
CC sequences and associates with newly synthesized RNAs, including pre-
CC mRNAs and short-lived exosome substrates such as promoter upstream
CC transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products
CC from small nuclear RNAs (snRNAs) (PubMed:25189701, PubMed:25578728,
CC PubMed:25525152, PubMed:25852104). Participates in several biological
CC processes including DNA damage response (DDR) and stress response
CC (PubMed:25525152, PubMed:30824372). During stress response, activation
CC of the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequently
CC the RNA exosome degradation activities, thereby modulating the turnover
CC of non-coding transcriptome (PubMed:25525152). Participates in DNA
CC damage response (DDR), through its interaction with MEPCE and LARP7,
CC the core subunits of 7SK snRNP complex, that release the positive
CC transcription elongation factor b (P-TEFb) complex from the 7SK snRNP.
CC In turn, activation of P-TEFb complex induces the transcription of P-
CC TEFb-dependent DDR genes to promote cell viability (PubMed:30824372).
CC {ECO:0000269|PubMed:25189701, ECO:0000269|PubMed:25525152,
CC ECO:0000269|PubMed:25578728, ECO:0000269|PubMed:25852104,
CC ECO:0000269|PubMed:27871484, ECO:0000269|PubMed:30824372}.
CC -!- SUBUNIT: Component of the nuclear exosome targeting (NEXT) complex
CC composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding
CC short-lived RNAs for exosomal degradation (PubMed:27905398,
CC PubMed:27871484, PubMed:25189701). Interacts with ZCCHC8 and
CC SF3B2/SAP145 (PubMed:27905398, PubMed:27871484, PubMed:16263084). Binds
CC to MTREX through ZCCHC8 (PubMed:27871484). Interacts with YWHAE and
CC YWHAZ; these interactions are stress-dependent and RBM7 phosphorylation
CC dependent; release RNA from the NEXT complex and may affect RNA
CC targeting to the nuclear RNA exosomome for degradation
CC (PubMed:25189701). Interacts with MEPCE and LARP7, the core subunits of
CC 7SK snRNP; upon genotoxic stress this interaction is enhanced,
CC triggering the release of inactive P-TEFb complex from the core and P-
CC TEFb complex activation (PubMed:30824372).
CC {ECO:0000269|PubMed:16263084, ECO:0000269|PubMed:25189701,
CC ECO:0000269|PubMed:27871484, ECO:0000269|PubMed:27905398,
CC ECO:0000269|PubMed:30824372}.
CC -!- INTERACTION:
CC Q9Y580; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-746903, EBI-347573;
CC Q9Y580; Q96CN4: EVI5L; NbExp=3; IntAct=EBI-746903, EBI-749523;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:21855801, ECO:0000269|PubMed:25852104}. Nucleus
CC {ECO:0000250|UniProtKB:Q9CQT2}. Note=Excluded from the nucleolus.
CC {ECO:0000269|PubMed:21855801}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The RRM domain mediates RNA binding; the RNA must have four
CC nucleotides for efficient binding (PubMed:25852104). Mediates the
CC interaction of NEXT complex with promoter upstream transcripts
CC (PROMPTs) and potentially aberrant forms of other non coding RNAs, such
CC as snRNAs (PubMed:25852104). The RRM domain exhibits specificity for
CC polyuridine sequences (PubMed:25852104). {ECO:0000269|PubMed:25852104}.
CC -!- PTM: Phosphorylated at Ser-136 by MAPK14/p38-alpha-activated
CC MAPKAPK2/MK2; this phosphorylation is stress-dependent; this
CC phosphorylation decreases its RNA-binding capacity therefore affecting
CC RNA nuclear exosome-mediated degradation (PubMed:25525152,
CC PubMed:25189701). This phosphorylation mediates YWHAE and YWHAZ
CC interactions (PubMed:25189701). {ECO:0000269|PubMed:25189701,
CC ECO:0000269|PubMed:25525152}.
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DR EMBL; AF156098; AAD39257.1; -; mRNA.
DR EMBL; AK002015; BAA92036.1; -; mRNA.
DR EMBL; AK312619; BAG35505.1; -; mRNA.
DR EMBL; CH471065; EAW67247.1; -; Genomic_DNA.
DR EMBL; BC034381; AAH34381.1; -; mRNA.
DR CCDS; CCDS8370.1; -.
DR RefSeq; NP_001272974.1; NM_001286045.1.
DR RefSeq; NP_001272975.1; NM_001286046.1.
DR RefSeq; NP_001272976.1; NM_001286047.1.
DR RefSeq; NP_001272977.1; NM_001286048.1.
DR RefSeq; NP_057174.1; NM_016090.3.
DR PDB; 2M8H; NMR; -; A=6-94.
DR PDB; 5IQQ; X-ray; 2.52 A; A/B/C/D/E=1-91.
DR PDB; 5LXR; X-ray; 2.00 A; A=1-86.
DR PDB; 5LXY; X-ray; 2.85 A; A/B/E/G/I/K/M=1-86.
DR PDBsum; 2M8H; -.
DR PDBsum; 5IQQ; -.
DR PDBsum; 5LXR; -.
DR PDBsum; 5LXY; -.
DR AlphaFoldDB; Q9Y580; -.
DR BMRB; Q9Y580; -.
DR SMR; Q9Y580; -.
DR BioGRID; 115478; 132.
DR CORUM; Q9Y580; -.
DR DIP; DIP-48833N; -.
DR IntAct; Q9Y580; 64.
DR MINT; Q9Y580; -.
DR STRING; 9606.ENSP00000364639; -.
DR GlyGen; Q9Y580; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y580; -.
DR MetOSite; Q9Y580; -.
DR PhosphoSitePlus; Q9Y580; -.
DR BioMuta; RBM7; -.
DR DMDM; 9978697; -.
DR CPTAC; CPTAC-1365; -.
DR CPTAC; CPTAC-943; -.
DR EPD; Q9Y580; -.
DR jPOST; Q9Y580; -.
DR MassIVE; Q9Y580; -.
DR MaxQB; Q9Y580; -.
DR PaxDb; Q9Y580; -.
DR PeptideAtlas; Q9Y580; -.
DR PRIDE; Q9Y580; -.
DR ProteomicsDB; 86311; -.
DR Antibodypedia; 2822; 117 antibodies from 19 providers.
DR DNASU; 10179; -.
DR Ensembl; ENST00000540163.5; ENSP00000439918.1; ENSG00000076053.12.
DR GeneID; 10179; -.
DR KEGG; hsa:10179; -.
DR UCSC; uc001pov.5; human.
DR CTD; 10179; -.
DR DisGeNET; 10179; -.
DR GeneCards; RBM7; -.
DR HGNC; HGNC:9904; RBM7.
DR HPA; ENSG00000076053; Low tissue specificity.
DR MIM; 612413; gene.
DR neXtProt; NX_Q9Y580; -.
DR OpenTargets; ENSG00000076053; -.
DR PharmGKB; PA34269; -.
DR VEuPathDB; HostDB:ENSG00000076053; -.
DR eggNOG; KOG4454; Eukaryota.
DR GeneTree; ENSGT00870000136493; -.
DR HOGENOM; CLU_087967_0_0_1; -.
DR InParanoid; Q9Y580; -.
DR OrthoDB; 1298240at2759; -.
DR PhylomeDB; Q9Y580; -.
DR TreeFam; TF323596; -.
DR PathwayCommons; Q9Y580; -.
DR SignaLink; Q9Y580; -.
DR SIGNOR; Q9Y580; -.
DR BioGRID-ORCS; 10179; 34 hits in 1046 CRISPR screens.
DR ChiTaRS; RBM7; human.
DR GeneWiki; RBM7; -.
DR GenomeRNAi; 10179; -.
DR Pharos; Q9Y580; Tbio.
DR PRO; PR:Q9Y580; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y580; protein.
DR Bgee; ENSG00000076053; Expressed in cartilage tissue and 198 other tissues.
DR ExpressionAtlas; Q9Y580; baseline and differential.
DR Genevisible; Q9Y580; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0016076; P:snRNA catabolic process; IMP:UniProtKB.
DR CDD; cd12592; RRM_RBM7; 1.
DR DisProt; DP02391; -.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034500; RBM7_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Meiosis; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..266
FT /note="RNA-binding protein 7"
FT /id="PRO_0000081761"
FT DOMAIN 10..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 25..35
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000269|PubMed:27905398,
FT ECO:0007744|PDB:5LXR, ECO:0007744|PDB:5LXY"
FT REGION 59..76
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000269|PubMed:27905398,
FT ECO:0007744|PDB:5LXR, ECO:0007744|PDB:5LXY"
FT REGION 90..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:25489052"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQT2"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQT2"
FT MOD_RES 152
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 79
FT /note="P -> R (found in a patient with a form of spinal
FT muscular atrophy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193168"
FT /id="VAR_082580"
FT MUTAGEN 13
FT /note="F->A: Decreases affinity for RNA binding. Does not
FT affect The NEXT complex assembly. Impairs snRNA binding."
FT /evidence="ECO:0000269|PubMed:25852104"
FT MUTAGEN 25
FT /note="L->E: Impaired interaction with ZCCHC8; when
FT associated with E-29."
FT /evidence="ECO:0000269|PubMed:27905398"
FT MUTAGEN 29
FT /note="L->E: Impaired interaction with ZCCHC8; when
FT associated with E-25."
FT /evidence="ECO:0000269|PubMed:27905398"
FT MUTAGEN 50
FT /note="K->A: Abrogates the interaction with 7SK small
FT nuclear RNA (7SK); when associated with A-52 and A-54. Does
FT not affect interaction between HEXIM1, CDK9 and 7SK small
FT nuclear RNA (7SK); when associated with A-52 and A-54. Does
FT not affect interaction with MEPCE and LARP7; when
FT associated with A-52 and A-54. Decreases induction of P-
FT TEFb-dependent DNA damage response (DDR); when associated
FT with A-52 and A-54."
FT /evidence="ECO:0000269|PubMed:30824372"
FT MUTAGEN 52
FT /note="F->A: Decreases affinity for RNA binding. Abrogates
FT the interaction with 7SK small nuclear RNA (7SK); when
FT associated with A-50 and A-54. Does not affect interaction
FT between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when
FT associated with A-50 and A-54. Does not affect interaction
FT with MEPCE and LARP7; when associated with A-50 and A-54.
FT Decreases induction of P-TEFb-dependent DNA damage response
FT (DDR); when associated with A-50 and A-54."
FT /evidence="ECO:0000269|PubMed:25852104,
FT ECO:0000269|PubMed:30824372"
FT MUTAGEN 54
FT /note="F->A: Abrogates the interaction with 7SK small
FT nuclear RNA (7SK); when associated with A-50 and A-52. Does
FT not affect interaction between HEXIM1, CDK9 and 7SK small
FT nuclear RNA (7SK); when associated with A-50 and A-52. Does
FT not affect interaction with MEPCE and LARP7; when
FT associated with A-50 and A-52. Decreases induction of P-
FT TEFb-dependent DNA damage response (DDR); when associated
FT with A-50 and A-52."
FT /evidence="ECO:0000269|PubMed:30824372"
FT MUTAGEN 65
FT /note="Y->A: Reduced interaction with ZCCHC8, and impaired
FT interaction with SF3B2/SAP145; when associated with E-69."
FT /evidence="ECO:0000269|PubMed:27905398"
FT MUTAGEN 69
FT /note="L->E: Reduced interaction with ZCCHC8, and impaired
FT interaction with SF3B2/SAP145; when associated with A-65."
FT /evidence="ECO:0000269|PubMed:27905398"
FT MUTAGEN 136
FT /note="S->A: Impairs phosphorylation. Impairs
FT phosphorylation; when associated with S-204. Prevents
FT PROMPTs accumulation to >50%."
FT /evidence="ECO:0000269|PubMed:25189701,
FT ECO:0000269|PubMed:25525152"
FT MUTAGEN 204
FT /note="S->A: Impairs phosphorylation. Impairs
FT phosphorylation; when associated with S-136."
FT /evidence="ECO:0000269|PubMed:25189701"
FT CONFLICT 102
FT /note="H -> Y (in Ref. 2; BAA92036)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="P -> PS (in Ref. 2; BAA92036)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:5LXR"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:5LXR"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:5LXR"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5LXR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5IQQ"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5LXR"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:5LXR"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2M8H"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5LXR"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2M8H"
SQ SEQUENCE 266 AA; 30504 MW; 31D344EBFC54B22F CRC64;
MGAAAAEADR TLFVGNLETK VTEELLFELF HQAGPVIKVK IPKDKDGKPK QFAFVNFKHE
VSVPYAMNLL NGIKLYGRPI KIQFRSGSSH APQDVSLSYP QHHVGNSSPT STSPSRYERT
MDNMTSSAQI IQRSFSSPEN FQRQAVMNSA LRQMSYGGKF GSSPLDQSGF SPSVQSHSHS
FNQSSSSQWR QGTPSSQRKV RMNSYPYLAD RHYSREQRYT DHGSDHHYRG KRDDFFYEDR
NHDDWSHDYD NRRDSSRDGK WRSSRH
