RBM27_HUMAN
ID RBM27_HUMAN Reviewed; 1060 AA.
AC Q9P2N5; Q8IYW9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=RNA-binding protein 27;
DE AltName: Full=RNA-binding motif protein 27;
GN Name=RBM27; Synonyms=KIAA1311;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-1060.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 665-1060.
RC TISSUE=Cervix;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1020, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447 AND SER-1012, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, 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 [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-455, 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle. Note=Incorporated
CC into the nuclear speckles and to speckles proximal to the nuclear
CC periphery. Also localizes to punctate structures in the cytoplasm
CC termed cytospeckles (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RRM domain mediates integration into cytospeckles.
CC {ECO:0000250}.
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DR EMBL; AC091959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037732; BAA92549.1; -; mRNA.
DR EMBL; BC033524; AAH33524.1; -; mRNA.
DR CCDS; CCDS43378.1; -.
DR RefSeq; NP_061862.1; NM_018989.1.
DR AlphaFoldDB; Q9P2N5; -.
DR SMR; Q9P2N5; -.
DR BioGRID; 119955; 112.
DR IntAct; Q9P2N5; 39.
DR MINT; Q9P2N5; -.
DR STRING; 9606.ENSP00000265271; -.
DR CarbonylDB; Q9P2N5; -.
DR GlyConnect; 2897; 1 O-Linked glycan (2 sites).
DR GlyGen; Q9P2N5; 11 sites, 2 O-linked glycans (11 sites).
DR iPTMnet; Q9P2N5; -.
DR PhosphoSitePlus; Q9P2N5; -.
DR BioMuta; RBM27; -.
DR DMDM; 124021005; -.
DR EPD; Q9P2N5; -.
DR jPOST; Q9P2N5; -.
DR MassIVE; Q9P2N5; -.
DR MaxQB; Q9P2N5; -.
DR PaxDb; Q9P2N5; -.
DR PeptideAtlas; Q9P2N5; -.
DR PRIDE; Q9P2N5; -.
DR ProteomicsDB; 83858; -.
DR Antibodypedia; 27561; 37 antibodies from 10 providers.
DR DNASU; 54439; -.
DR Ensembl; ENST00000265271.7; ENSP00000265271.5; ENSG00000091009.8.
DR GeneID; 54439; -.
DR KEGG; hsa:54439; -.
DR MANE-Select; ENST00000265271.7; ENSP00000265271.5; NM_018989.2; NP_061862.1.
DR UCSC; uc003lnz.5; human.
DR CTD; 54439; -.
DR DisGeNET; 54439; -.
DR GeneCards; RBM27; -.
DR HGNC; HGNC:29243; RBM27.
DR HPA; ENSG00000091009; Low tissue specificity.
DR neXtProt; NX_Q9P2N5; -.
DR OpenTargets; ENSG00000091009; -.
DR PharmGKB; PA134925458; -.
DR VEuPathDB; HostDB:ENSG00000091009; -.
DR eggNOG; KOG2135; Eukaryota.
DR GeneTree; ENSGT00510000046929; -.
DR HOGENOM; CLU_006190_0_0_1; -.
DR InParanoid; Q9P2N5; -.
DR OMA; CPMEHGL; -.
DR OrthoDB; 741871at2759; -.
DR PhylomeDB; Q9P2N5; -.
DR TreeFam; TF319253; -.
DR PathwayCommons; Q9P2N5; -.
DR SignaLink; Q9P2N5; -.
DR BioGRID-ORCS; 54439; 59 hits in 1084 CRISPR screens.
DR ChiTaRS; RBM27; human.
DR GenomeRNAi; 54439; -.
DR Pharos; Q9P2N5; Tdark.
DR PRO; PR:Q9P2N5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9P2N5; protein.
DR Bgee; ENSG00000091009; Expressed in caput epididymis and 192 other tissues.
DR Genevisible; Q9P2N5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; PTHR14398; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1060
FT /note="RNA-binding protein 27"
FT /id="PRO_0000273044"
FT DOMAIN 600..674
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 273..301
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 91..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..886
FT /evidence="ECO:0000255"
FT COMPBIAS 166..181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 455
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SFM8"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 1060 AA; 118718 MW; 9DACF8B155187456 CRC64;
MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
TSGFVDKLFE SLYTKNYLPL LEPVKPEPKP LVQEKEEIKE EVFQEPAEEE RDGRKKKYPS
PQKTRSESSE RRTREKKRED GKWRDYDRYY ERNELYREKY DWRRGRSKSR SKSRGLSRSR
SRSRGRSKDR DPNRNVEHRE RSKFKSERND LESSYVPVSA PPPNSSEQYS SGAQSIPSTV
TVIAPAHHSE NTTESWSNYY NNHSSSNSFG RNLPPKRRCR DYDERGFCVL GDLCQFDHGN
DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG MLMPPMPGPG PGPGPGPGPG PGPGPGPGHS
MRLPVPQGHG QPPPSVVLPI PRPPITQSSL INSRDQPGTS AVPNLASVGT RLPPPLPQNL
LYTVSERQPM YSREHGAAAS ERLQLGTPPP LLAARLVPPR NLMGSSIGYH TSVSSPTPLV
PDTYEPDGYN PEAPSITSSG RSQYRQFFSR TQTQRPNLIG LTSGDMDVNP RAANIVIQTE
PPVPVSINSN ITRVVLEPDS RKRAMSGLEG PLTKKPWLGK QGNNNQNKPG FLRKNQYTNT
KLEVKKIPQE LNNITKLNEH FSKFGTIVNI QVAFKGDPEA ALIQYLTNEE ARKAISSTEA
VLNNRFIRVL WHRENNEQPT LQSSAQLLLQ QQQTLSHLSQ QHHHLPQHLH QQQVLVAQSA
PSTVHGGIQK MMSKPQTSGA YVLNKVPVKH RLGHAGGNQS DASHLLNQSG GAGEDCQIFS
TPGHPKMIYS SSNLKTPSKL CSGSKSHDVQ EVLKKKQEAM KLQQDMRKKR QEVLEKQIEC
QKMLISKLEK NKNMKPEERA NIMKTLKELG EKISQLKDEL KTSSAVSTPS KVKTKTEAQK
ELLDTELDLH KRLSSGEDTT ELRKKLSQLQ VEAARLGILP VGRGKTMSSQ GRGRGRGRGG
RGRGSLNHMV VDHRPKALTV GGFIEEEKED LLQHFSTANQ GPKFKDRRLQ ISWHKPKVPS
ISTETEEEEV KEEETETSDL FLPDDDDEDE DEYESRSWRR
