RBMS1_HUMAN
ID RBMS1_HUMAN Reviewed; 406 AA.
AC P29558; Q14869; Q15433; Q53P46; Q53QX8; Q53RG6; Q8WV20;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=RNA-binding motif, single-stranded-interacting protein 1;
DE AltName: Full=Single-stranded DNA-binding protein MSSP-1;
DE AltName: Full=Suppressor of CDC2 with RNA-binding motif 2;
GN Name=RBMS1; Synonyms=C2orf12, MSSP, MSSP1, SCR2;
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] (ISOFORM 2).
RX PubMed=8041632; DOI=10.1093/nar/22.13.2687;
RA Kanaoka Y., Nojima H.;
RT "SCR: novel human suppressors of cdc2/cdc13 mutants of Schizosaccharomyces
RT pombe harbour motifs for RNA binding proteins.";
RL Nucleic Acids Res. 22:2687-2693(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=7838710; DOI=10.1093/nar/22.25.5576;
RA Takai T., Nishita Y., Iguchi-Ariga S.M.M., Ariga H.;
RT "Molecular cloning of MSSP-2, a c-myc gene single-strand binding protein:
RT characterization of binding specificity and DNA replication activity.";
RL Nucleic Acids Res. 22:5576-5581(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Muscle;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 26-406 (ISOFORM 1).
RX PubMed=8134115;
RA Negishi Y., Nishita Y., Saegusa Y., Kakizaki I., Galli I., Kihara F.,
RA Tamai K., Miyajima N., Iguchi-Ariga S.M.M., Ariga H.;
RT "Identification and cDNA cloning of single-stranded DNA binding proteins
RT that interact with the region upstream of the human c-myc gene.";
RL Oncogene 9:1133-1143(1994).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208, 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=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 [8]
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 [9]
RP STRUCTURE BY NMR OF 121-223.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in RNA binding motif, single-stranded-
RT interacting protein 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Single-stranded DNA binding protein that interacts with the
CC region upstream of the MYC gene. Binds specifically to the DNA sequence
CC motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
CC -!- INTERACTION:
CC P29558; Q12800: TFCP2; NbExp=3; IntAct=EBI-5462600, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P29558-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29558-2; Sequence=VSP_011930;
CC Name=4; Synonyms=MSSP-2;
CC IsoId=P29558-4; Sequence=VSP_037790, VSP_037791;
CC -!- TISSUE SPECIFICITY: Highest amounts are found in placenta, lung and
CC heart.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels during the G1 to S
CC transition of the cell cycle.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX93095.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA45923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA45923.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA54628.1; Type=Erroneous translation; Note=Wrong coding sequence.; Evidence={ECO:0000305};
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DR EMBL; D28482; BAA05841.1; -; mRNA.
DR EMBL; X77494; CAA54628.1; ALT_SEQ; mRNA.
DR EMBL; AC092153; AAX93095.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC104598; AAX93183.1; -; Genomic_DNA.
DR EMBL; AC131754; AAY15005.1; -; Genomic_DNA.
DR EMBL; BC012992; AAH12992.1; -; mRNA.
DR EMBL; BC012993; AAH12993.1; -; mRNA.
DR EMBL; BC018951; AAH18951.1; -; mRNA.
DR EMBL; X64652; CAA45923.1; ALT_SEQ; mRNA.
DR CCDS; CCDS2213.1; -. [P29558-1]
DR PIR; I38042; I38042.
DR PIR; S19873; S19873.
DR PIR; S47659; S47659.
DR PIR; S53612; S53612.
DR RefSeq; NP_002888.1; NM_002897.4. [P29558-2]
DR RefSeq; NP_058520.1; NM_016836.3. [P29558-1]
DR PDB; 1X5O; NMR; -; A=123-223.
DR PDB; 6M75; X-ray; 2.57 A; A=62-223.
DR PDB; 7C36; NMR; -; A=62-223.
DR PDBsum; 1X5O; -.
DR PDBsum; 6M75; -.
DR PDBsum; 7C36; -.
DR AlphaFoldDB; P29558; -.
DR SMR; P29558; -.
DR BioGRID; 111872; 190.
DR IntAct; P29558; 22.
DR MINT; P29558; -.
DR STRING; 9606.ENSP00000294904; -.
DR GlyGen; P29558; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29558; -.
DR MetOSite; P29558; -.
DR PhosphoSitePlus; P29558; -.
DR BioMuta; RBMS1; -.
DR DMDM; 55977783; -.
DR EPD; P29558; -.
DR jPOST; P29558; -.
DR MassIVE; P29558; -.
DR MaxQB; P29558; -.
DR PaxDb; P29558; -.
DR PeptideAtlas; P29558; -.
DR PRIDE; P29558; -.
DR ProteomicsDB; 54586; -. [P29558-1]
DR ProteomicsDB; 54587; -. [P29558-2]
DR ProteomicsDB; 54588; -. [P29558-4]
DR Antibodypedia; 19068; 306 antibodies from 28 providers.
DR DNASU; 5937; -.
DR Ensembl; ENST00000348849.8; ENSP00000294904.6; ENSG00000153250.21. [P29558-1]
DR GeneID; 5937; -.
DR KEGG; hsa:5937; -.
DR MANE-Select; ENST00000348849.8; ENSP00000294904.6; NM_016836.4; NP_058520.1.
DR UCSC; uc002ubo.4; human. [P29558-1]
DR CTD; 5937; -.
DR DisGeNET; 5937; -.
DR GeneCards; RBMS1; -.
DR HGNC; HGNC:9907; RBMS1.
DR HPA; ENSG00000153250; Low tissue specificity.
DR MIM; 602310; gene.
DR neXtProt; NX_P29558; -.
DR OpenTargets; ENSG00000153250; -.
DR PharmGKB; PA34273; -.
DR VEuPathDB; HostDB:ENSG00000153250; -.
DR eggNOG; KOG4733; Eukaryota.
DR GeneTree; ENSGT00940000156082; -.
DR InParanoid; P29558; -.
DR OMA; WEHLSKT; -.
DR OrthoDB; 810893at2759; -.
DR PhylomeDB; P29558; -.
DR TreeFam; TF314644; -.
DR PathwayCommons; P29558; -.
DR SignaLink; P29558; -.
DR BioGRID-ORCS; 5937; 28 hits in 1071 CRISPR screens.
DR ChiTaRS; RBMS1; human.
DR EvolutionaryTrace; P29558; -.
DR GeneWiki; RBMS1; -.
DR GenomeRNAi; 5937; -.
DR Pharos; P29558; Tbio.
DR PRO; PR:P29558; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P29558; protein.
DR Bgee; ENSG00000153250; Expressed in cauda epididymis and 193 other tissues.
DR ExpressionAtlas; P29558; baseline and differential.
DR Genevisible; P29558; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; NAS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; NAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR CDD; cd12470; RRM1_MSSP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR034404; MSSP1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA replication; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..406
FT /note="RNA-binding motif, single-stranded-interacting
FT protein 1"
FT /id="PRO_0000081798"
FT DOMAIN 62..135
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 141..226
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 26..38
FT /note="QSLVPAHPMAPPS -> FGRHSGIPSEKEE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:7838710"
FT /id="VSP_037790"
FT VAR_SEQ 39..406
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:7838710"
FT /id="VSP_037791"
FT VAR_SEQ 250..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8041632"
FT /id="VSP_011930"
FT CONFLICT 132
FT /note="M -> K (in Ref. 5; CAA45923)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="QH -> HD (in Ref. 2; CAA54628)"
FT /evidence="ECO:0000305"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:6M75"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:7C36"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1X5O"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:6M75"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:6M75"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6M75"
SQ SEQUENCE 406 AA; 44505 MW; 97EAAD2B0A5E01C6 CRC64;
MGKVWKQQMY PQYATYYYPQ YLQAKQSLVP AHPMAPPSPS TTSSNNNSSS SSNSGWDQLS
KTNLYIRGLP PHTTDQDLVK LCQPYGKIVS TKAILDKTTN KCKGYGFVDF DSPAAAQKAV
SALKASGVQA QMAKQQEQDP TNLYISNLPL SMDEQELENM LKPFGQVIST RILRDSSGTS
RGVGFARMES TEKCEAVIGH FNGKFIKTPP GVSAPTEPLL CKFADGGQKK RQNPNKYIPN
GRPWHREGEV RLAGMTLTYD PTTAAIQNGF YPSPYSIATN RMITQTSITP YIASPVSAYQ
VQSPSWMQPQ PYILQHPGAV LTPSMEHTMS LQPASMISPL AQQMSHLSLG STGTYMPATS
AMQGAYLPQY AHMQTTAVPV EEASGQQQVA VETSNDHSPY TFQPNK
