SRBD1_HUMAN
ID SRBD1_HUMAN Reviewed; 995 AA.
AC Q8N5C6; Q53T56; Q96TA4; Q9NW11;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=S1 RNA-binding domain-containing protein 1;
GN Name=SRBD1;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861 AND SER-964, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134; LYS-185 AND LYS-955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134 AND LYS-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-134; LYS-166; LYS-167;
RP LYS-183 AND LYS-185, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N5C6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5C6-2; Sequence=VSP_024461;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14821.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK001241; BAA91577.1; -; mRNA.
DR EMBL; AK056536; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC012072; AAY14821.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC008179; AAK52078.1; -; Genomic_DNA.
DR EMBL; BC032538; AAH32538.1; -; mRNA.
DR CCDS; CCDS1823.1; -. [Q8N5C6-1]
DR RefSeq; NP_060549.4; NM_018079.4. [Q8N5C6-1]
DR AlphaFoldDB; Q8N5C6; -.
DR SMR; Q8N5C6; -.
DR BioGRID; 120439; 112.
DR IntAct; Q8N5C6; 32.
DR MINT; Q8N5C6; -.
DR STRING; 9606.ENSP00000263736; -.
DR iPTMnet; Q8N5C6; -.
DR PhosphoSitePlus; Q8N5C6; -.
DR BioMuta; SRBD1; -.
DR DMDM; 145566960; -.
DR EPD; Q8N5C6; -.
DR jPOST; Q8N5C6; -.
DR MassIVE; Q8N5C6; -.
DR MaxQB; Q8N5C6; -.
DR PaxDb; Q8N5C6; -.
DR PeptideAtlas; Q8N5C6; -.
DR PRIDE; Q8N5C6; -.
DR ProteomicsDB; 72030; -. [Q8N5C6-1]
DR ProteomicsDB; 72031; -. [Q8N5C6-2]
DR Antibodypedia; 29937; 123 antibodies from 24 providers.
DR DNASU; 55133; -.
DR Ensembl; ENST00000263736.5; ENSP00000263736.4; ENSG00000068784.13. [Q8N5C6-1]
DR GeneID; 55133; -.
DR KEGG; hsa:55133; -.
DR MANE-Select; ENST00000263736.5; ENSP00000263736.4; NM_018079.5; NP_060549.4.
DR UCSC; uc002rus.4; human. [Q8N5C6-1]
DR CTD; 55133; -.
DR DisGeNET; 55133; -.
DR GeneCards; SRBD1; -.
DR HGNC; HGNC:25521; SRBD1.
DR HPA; ENSG00000068784; Low tissue specificity.
DR neXtProt; NX_Q8N5C6; -.
DR OpenTargets; ENSG00000068784; -.
DR PharmGKB; PA144596269; -.
DR VEuPathDB; HostDB:ENSG00000068784; -.
DR eggNOG; KOG1857; Eukaryota.
DR GeneTree; ENSGT00510000047850; -.
DR HOGENOM; CLU_009833_1_0_1; -.
DR InParanoid; Q8N5C6; -.
DR OMA; RWAWRTR; -.
DR OrthoDB; 56990at2759; -.
DR PhylomeDB; Q8N5C6; -.
DR TreeFam; TF313600; -.
DR PathwayCommons; Q8N5C6; -.
DR SignaLink; Q8N5C6; -.
DR BioGRID-ORCS; 55133; 743 hits in 1090 CRISPR screens.
DR ChiTaRS; SRBD1; human.
DR GenomeRNAi; 55133; -.
DR Pharos; Q8N5C6; Tbio.
DR PRO; PR:Q8N5C6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8N5C6; protein.
DR Bgee; ENSG00000068784; Expressed in monocyte and 135 other tissues.
DR Genevisible; Q8N5C6; HS.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd05685; S1_Tex; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.140; -; 1.
DR InterPro; IPR041692; HHH_9.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044146; S1_Tex.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR018974; Tex-like_N.
DR InterPro; IPR032639; Tex_YqgF.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR Pfam; PF17674; HHH_9; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF09371; Tex_N; 1.
DR Pfam; PF16921; Tex_YqgF; 1.
DR SMART; SM00316; S1; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..995
FT /note="S1 RNA-binding domain-containing protein 1"
FT /id="PRO_0000284357"
FT DOMAIN 919..992
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..288
FT /evidence="ECO:0000255"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 955
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024461"
FT VARIANT 361
FT /note="T -> M (in dbSNP:rs6544834)"
FT /id="VAR_056995"
FT VARIANT 798
FT /note="V -> F (in dbSNP:rs3755073)"
FT /id="VAR_056996"
FT VARIANT 811
FT /note="K -> R (in dbSNP:rs3755072)"
FT /id="VAR_056997"
FT CONFLICT 597
FT /note="N -> S (in Ref. 1; BAA91577)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="S -> G (in Ref. 1; AK056536)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="S -> P (in Ref. 1; BAA91577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 111776 MW; BB286FB734708C55 CRC64;
MSSLPRRAKV QVQDVVLKDE FSSFSELSSA SEEDDKEDSA WEPQKKVPRS RKQPPPKESK
PKRMPRVKKN APQISDGSEV VVVKEELNSS VAIADTALED RKNKLDTVQT LKTAKTKQKC
AAQPHTVRRT KKLKVEEETS KASNLEGESN SSETPSTSTV WGGTCKKEEN DDDFTFGQSA
LKKIKTETYP QGQPVKFPAN ANSTKEEVEM NWDMVQVLSE RTNIEPWVCA NIIRLFNDDN
TIPFIIRYRK ELINNLDADS LREVQQTLEE LRAVAKKVHS TIQKIKKEGK MSECLLKAML
NCKTFEELEH VSAPYKTGSK GTKAQRARQL GLEGAARALL EKPGELSLLS YIRPDVKGLS
TLQDIEIGVQ HILADMIAKD KDTLDFIRNL CQKRHVCIQS SLAKVSSKKV NEKDVDKFLL
YQHFSCNIRN IHHHQILAIN RGENLKVLTV KVNISDGVKD EFCRWCIQNR WRPRSFARPE
LMKILYNSLN DSFKRLIYPL LCREFRAKLT SDAEKESVMM FGRNLRQLLL TSPVPGRTLM
GVDPGYKHGC KLAIISPTSQ ILHTDVVYLH CGQGFREAEK IKTLLLNFNC STVVIGNGTA
CRETEAYFAD LIMKNYFAPL DVVYCIVSEA GASIYSVSPE ANKEMPGLDP NLRSAVSIAR
RVQDPLAELV KIEPKHIGVG MYQHDVSQTL LKATLDSVVE ECVSFVGVDI NICSEVLLRH
IAGLNANRAK NIIEWREKNG PFINREQLKK VKGLGPKSFQ QCAGFIRINQ DYIRTFCSQQ
TETSGQIQGV AVTSSADVEV TNEKQGKKKS KTAVNVLLKP NPLDQTCIHP ESYDIAMRFL
SSIGGTLYEV GKPEMQQKIN SFLEKEGMEK IAERLQTTVH TLQVIIDGLS QPESFDFRTD
FDKPDFKRSI VCLEDLQIGT VLTGKVENAT LFGIFVDIGV GKSGLIPIRN VTEAKLSKTK
KRRSLGLGPG ERVEVQVLNI DIPRSRITLD LIRVL