RBM12_HUMAN
ID RBM12_HUMAN Reviewed; 932 AA.
AC Q9NTZ6; B3KRU2; E1P5R6; O94865; Q8N3B1; Q9H196;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=RNA-binding protein 12;
DE AltName: Full=RNA-binding motif protein 12;
DE AltName: Full=SH3/WW domain anchor protein in the nucleus;
DE Short=SWAN;
GN Name=RBM12; Synonyms=KIAA0765; ORFNames=HRIHFB2091;
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=Leukemia;
RX PubMed=11435693; DOI=10.1159/000056908;
RA Stover C.M., Gradl G., Jentsch I., Speicher M.R., Wieser R.,
RA Schwaeble W.J.;
RT "cDNA cloning, chromosomal assignment, and genomic structure of a human
RT gene encoding a novel member of the RBM family.";
RL Cytogenet. Cell Genet. 92:225-230(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Huang C.-H.;
RT "Identification of SWAN as a novel hnRNP-like adaptor protein with multiple
RT domains and broadly expressed in mammalian tissues.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-932.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 557-932, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-422 AND SER-424, AND
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-375; SER-422;
RP SER-424 AND SER-525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP INVOLVEMENT IN CPCMR.
RX PubMed=24678003; DOI=10.1002/ajmg.a.36498;
RA Johansson S., Berland S., Gradek G.A., Bongers E., de Leeuw N., Pfundt R.,
RA Fannemel M., Roedningen O., Brendehaug A., Haukanes B.I., Hovland R.,
RA Helland G., Houge G.;
RT "Haploinsufficiency of MEIS2 is associated with orofacial clefting and
RT learning disability.";
RL Am. J. Med. Genet. A 164A:1622-1626(2014).
RN [19]
RP INVOLVEMENT IN SCZD19, AND VARIANT SCZD19 793-GLY--GLY-932 DEL.
RX PubMed=28628109; DOI=10.1038/ng.3894;
RA Steinberg S., Gudmundsdottir S., Sveinbjornsson G., Suvisaari J.,
RA Paunio T., Torniainen-Holm M., Frigge M.L., Jonsdottir G.A.,
RA Huttenlocher J., Arnarsdottir S., Ingimarsson O., Haraldsson M.,
RA Tyrfingsson T., Thorgeirsson T.E., Kong A., Norddahl G.L.,
RA Gudbjartsson D.F., Sigurdsson E., Stefansson H., Stefansson K.;
RT "Truncating mutations in RBM12 are associated with psychosis.";
RL Nat. Genet. 49:1251-1254(2017).
RN [20]
RP STRUCTURE BY NMR OF 290-638.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domains in RNA-binding protein 12.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- INTERACTION:
CC Q9NTZ6; Q96CV9: OPTN; NbExp=6; IntAct=EBI-310707, EBI-748974;
CC Q9NTZ6; P55345: PRMT2; NbExp=3; IntAct=EBI-310707, EBI-78458;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}.
CC -!- DISEASE: Schizophrenia 19 (SCZD19) [MIM:617629]: A complex,
CC multifactorial psychotic disorder or group of disorders characterized
CC by disturbances in the form and content of thought (e.g. delusions,
CC hallucinations), in mood (e.g. inappropriate affect), in sense of self
CC and relationship to the external world (e.g. loss of ego boundaries,
CC withdrawal), and in behavior (e.g bizarre or apparently purposeless
CC behavior). Although it affects emotions, it is distinguished from mood
CC disorders in which such disturbances are primary. Similarly, there may
CC be mild impairment of cognitive function, and it is distinguished from
CC the dementias in which disturbed cognitive function is considered
CC primary. Some patients manifest schizophrenic as well as bipolar
CC disorder symptoms and are often given the diagnosis of schizoaffective
CC disorder. {ECO:0000269|PubMed:28628109}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34485.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ289772; CAC20441.1; -; mRNA.
DR EMBL; AF345332; AAL83752.1; -; mRNA.
DR EMBL; AF345335; AAL83755.1; -; Genomic_DNA.
DR EMBL; AF393214; AAM73682.1; -; mRNA.
DR EMBL; AB018308; BAA34485.2; ALT_INIT; mRNA.
DR EMBL; AK092239; BAG52504.1; -; mRNA.
DR EMBL; AL109827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76182.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76184.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76188.1; -; Genomic_DNA.
DR EMBL; BC012787; AAH12787.1; -; mRNA.
DR EMBL; BC013981; AAH13981.1; -; mRNA.
DR EMBL; AL834472; CAD39131.1; -; mRNA.
DR EMBL; AB015336; BAA34794.1; -; mRNA.
DR CCDS; CCDS13261.1; -.
DR RefSeq; NP_001185767.1; NM_001198838.1.
DR RefSeq; NP_001185769.1; NM_001198840.1.
DR RefSeq; NP_006038.2; NM_006047.5.
DR RefSeq; NP_690051.1; NM_152838.3.
DR PDB; 1WEL; NMR; -; A=412-522.
DR PDB; 2CPY; NMR; -; A=536-636.
DR PDB; 2DNN; NMR; -; A=295-390.
DR PDB; 2EK1; X-ray; 2.00 A; A/B/C/D/E/F/G/H=848-929.
DR PDB; 2EK6; X-ray; 2.38 A; A/B/C/D=848-929.
DR PDBsum; 1WEL; -.
DR PDBsum; 2CPY; -.
DR PDBsum; 2DNN; -.
DR PDBsum; 2EK1; -.
DR PDBsum; 2EK6; -.
DR AlphaFoldDB; Q9NTZ6; -.
DR SMR; Q9NTZ6; -.
DR BioGRID; 115440; 96.
DR IntAct; Q9NTZ6; 30.
DR MINT; Q9NTZ6; -.
DR STRING; 9606.ENSP00000363228; -.
DR GlyGen; Q9NTZ6; 11 sites, 2 O-linked glycans (11 sites).
DR iPTMnet; Q9NTZ6; -.
DR MetOSite; Q9NTZ6; -.
DR PhosphoSitePlus; Q9NTZ6; -.
DR BioMuta; RBM12; -.
DR DMDM; 30173387; -.
DR EPD; Q9NTZ6; -.
DR jPOST; Q9NTZ6; -.
DR MassIVE; Q9NTZ6; -.
DR MaxQB; Q9NTZ6; -.
DR PaxDb; Q9NTZ6; -.
DR PeptideAtlas; Q9NTZ6; -.
DR PRIDE; Q9NTZ6; -.
DR ProteomicsDB; 82646; -.
DR Antibodypedia; 35036; 156 antibodies from 22 providers.
DR DNASU; 10137; -.
DR Ensembl; ENST00000359646.1; ENSP00000352668.1; ENSG00000244462.8.
DR Ensembl; ENST00000374104.7; ENSP00000363217.3; ENSG00000244462.8.
DR Ensembl; ENST00000374114.8; ENSP00000363228.3; ENSG00000244462.8.
DR GeneID; 10137; -.
DR KEGG; hsa:10137; -.
DR MANE-Select; ENST00000374114.8; ENSP00000363228.3; NM_006047.6; NP_006038.2.
DR UCSC; uc002xdq.4; human.
DR CTD; 10137; -.
DR DisGeNET; 10137; -.
DR GeneCards; RBM12; -.
DR HGNC; HGNC:9898; RBM12.
DR HPA; ENSG00000244462; Low tissue specificity.
DR MalaCards; RBM12; -.
DR MIM; 607179; gene.
DR MIM; 617629; phenotype.
DR neXtProt; NX_Q9NTZ6; -.
DR OpenTargets; ENSG00000244462; -.
DR PharmGKB; PA34261; -.
DR VEuPathDB; HostDB:ENSG00000244462; -.
DR eggNOG; KOG4307; Eukaryota.
DR GeneTree; ENSGT00940000160611; -.
DR HOGENOM; CLU_004368_1_0_1; -.
DR InParanoid; Q9NTZ6; -.
DR OMA; PFSCSEV; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q9NTZ6; -.
DR TreeFam; TF331899; -.
DR PathwayCommons; Q9NTZ6; -.
DR SignaLink; Q9NTZ6; -.
DR BioGRID-ORCS; 10137; 66 hits in 1090 CRISPR screens.
DR EvolutionaryTrace; Q9NTZ6; -.
DR GeneWiki; RBM12; -.
DR GenomeRNAi; 10137; -.
DR Pharos; Q9NTZ6; Tbio.
DR PRO; PR:Q9NTZ6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NTZ6; protein.
DR Bgee; ENSG00000244462; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; Q9NTZ6; baseline and differential.
DR Genevisible; Q9NTZ6; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR CDD; cd12745; RRM1_RBM12; 1.
DR CDD; cd12747; RRM2_RBM12; 1.
DR CDD; cd12512; RRM3_RBM12; 1.
DR CDD; cd12749; RRM4_RBM12; 1.
DR CDD; cd12751; RRM5_RBM12; 1.
DR Gene3D; 3.30.70.330; -; 5.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034591; RBM12_RRM1.
DR InterPro; IPR034594; RBM12_RRM2.
DR InterPro; IPR034855; RBM12_RRM3.
DR InterPro; IPR034856; RBM12_RRM4.
DR InterPro; IPR034854; RBM12_RRM5.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Schizophrenia.
FT CHAIN 1..932
FT /note="RNA-binding protein 12"
FT /id="PRO_0000081770"
FT DOMAIN 304..379
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 430..507
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 856..932
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 572
FT /note="N -> S (in dbSNP:rs17092928)"
FT /id="VAR_052217"
FT VARIANT 793..932
FT /note="Missing (in SCZD19; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:28628109"
FT /id="VAR_078980"
FT VARIANT 921
FT /note="P -> L (in dbSNP:rs6121012)"
FT /id="VAR_052218"
FT CONFLICT 601
FT /note="S -> T (in Ref. 1; CAC20441)"
FT /evidence="ECO:0000305"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:2DNN"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2DNN"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2DNN"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2DNN"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:2DNN"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:2DNN"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:2DNN"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:2DNN"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2DNN"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:2DNN"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:1WEL"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:1WEL"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:1WEL"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:1WEL"
FT STRAND 468..481
FT /evidence="ECO:0007829|PDB:1WEL"
FT HELIX 482..488
FT /evidence="ECO:0007829|PDB:1WEL"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:1WEL"
FT HELIX 507..521
FT /evidence="ECO:0007829|PDB:1WEL"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:2CPY"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:2CPY"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:2CPY"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:2CPY"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:2CPY"
FT HELIX 595..601
FT /evidence="ECO:0007829|PDB:2CPY"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2CPY"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:2CPY"
FT STRAND 612..619
FT /evidence="ECO:0007829|PDB:2CPY"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:2CPY"
FT STRAND 856..861
FT /evidence="ECO:0007829|PDB:2EK1"
FT HELIX 869..875
FT /evidence="ECO:0007829|PDB:2EK1"
FT TURN 876..880
FT /evidence="ECO:0007829|PDB:2EK1"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:2EK1"
FT STRAND 896..906
FT /evidence="ECO:0007829|PDB:2EK1"
FT HELIX 907..917
FT /evidence="ECO:0007829|PDB:2EK1"
SQ SEQUENCE 932 AA; 97395 MW; 10623E1EBCC93FC5 CRC64;
MAVVIRLQGL PIVAGTMDIR HFFSGLTIPD GGVHIVGGEL GEAFIVFATD EDARLGMMRT
GGTIKGSKVT LLLSSKTEMQ NMIELSRRRF ETANLDIPPA NASRSGPPPS SGMSSRVNLP
TTVSNFNNPS PSVVTATTSV HESNKNIQTF STASVGTAPP NMGASFGSPT FSSTVPSTAS
PMNTVPPPPI PPIPAMPSLP PMPSIPPIPV PPPVPTLPPV PPVPPIPPVP SVPPMTPLPP
MSGMPPLNPP PVAPLPAGMN GSGAPMNLNN NLNPMFLGPL NPVNPIQMNS QSSVKPLPIN
PDDLYVSVHG MPFSAMENDV RDFFHGLRVD AVHLLKDHVG RNNGNGLVKF LSPQDTFEAL
KRNRMLMIQR YVEVSPATER QWVAAGGHIT FKQNMGPSGQ THPPPQTLPR SKSPSGQKRS
RSRSPHEAGF CVYLKGLPFE AENKHVIDFF KKLDIVEDSI YIAYGPNGKA TGEGFVEFRN
EADYKAALCR HKQYMGNRFI QVHPITKKGM LEKIDMIRKR LQNFSYDQRE MILNPEGDVN
SAKVCAHITN IPFSITKMDV LQFLEGIPVD ENAVHVLVDN NGQGLGQALV QFKNEDDARK
SERLHRKKLN GREAFVHVVT LEDMREIEKN PPAQGKKGLK MPVPGNPAVP GMPNAGLPGV
GLPSAGLPGA GLPSTGLPGS AITSAGLPGA GMPSAGIPSA GGEEHAFLTV GSKEANNGPP
FNFPGNFGGS NAFGPPIPPP GLGGGAFGDA RPGMPSVGNS GLPGLGLDVP GFGGGPNNLS
GPSGFGGGPQ NFGNGPGSLG GPPGFGSGPP GLGSAPGHLG GPPAFGPGPG PGPGPGPIHI
GGPPGFASSS GKPGPTVIKV QNMPFTVSID EILDFFYGYQ VIPGSVCLKY NEKGMPTGEA
MVAFESRDEA TAAVIDLNDR PIGSRKVKLV LG
