SRP72_HUMAN
ID SRP72_HUMAN Reviewed; 671 AA.
AC O76094; G5E9Z8; Q7Z3C0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Signal recognition particle subunit SRP72;
DE Short=SRP72;
DE AltName: Full=Signal recognition particle 72 kDa protein;
GN Name=SRP72;
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 1).
RA Gowda K., Zwieb C.;
RT "Protein SRP72 sequence of human signal recognition particle.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Utz P.J., Hottelet M., Miller I.J., Anderson P.;
RT "Sequence of human signal recognition particle (SRP) 72.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophageal carcinoma;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP PROTEIN SEQUENCE OF 2-20; 63-84; 113-121; 148-163; 242-275; 288-297;
RP 302-324; 326-350; 357-376; 465-475; 480-498; 516-531 AND 601-617, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP SUBUNIT, AND INTERACTION WITH SRP68.
RX PubMed=16672232; DOI=10.1110/ps.051861406;
RA Iakhiaeva E., Bhuiyan S.H., Yin J., Zwieb C.;
RT "Protein SRP68 of human signal recognition particle: identification of the
RT RNA and SRP72 binding domains.";
RL Protein Sci. 15:1290-1302(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, 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 [12]
RP FUNCTION, RNA BINDING, AND MUTAGENESIS OF 553-LYS--LYS-558;
RP 555-LYS-LYS-556; 577-TRP-LEU-578; PRO-579; MET-580; 579-PRO-MET-580;
RP 581-ARG-GLU-582; 583-ARG-SER-584; 585-TYR-TYR-589; 587-ARG-GLY-588 AND
RP 589-ARG-LYS-590.
RX PubMed=21073748; DOI=10.1186/1471-2199-11-83;
RA Iakhiaeva E., Iakhiaev A., Zwieb C.;
RT "Identification of amino acid residues in protein SRP72 required for
RT binding to a kinked 5e motif of the human signal recognition particle
RT RNA.";
RL BMC Mol. Biol. 11:83-83(2010).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618; SER-630 AND SER-635, AND
RP IDENTIFICATION BY 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-391, 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
RN [21] {ECO:0007744|PDB:5WRV, ECO:0007744|PDB:5WRW}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-163 IN COMPLEX WITH SRP68
RP MUTANT 608-GLU--610-LYS, SUBUNIT, INTERACTION WITH SRP68, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 11-VAL--ASP-44; ASP-44; VAL-45; VAL-53;
RP TYR-86; 113-GLU--VAL-131; 132-TRP--VAL-165 AND 136-VAL-ARG-137.
RX PubMed=28369529; DOI=10.1093/jmcb/mjx010;
RA Gao Y., Zhang Q., Lang Y., Liu Y., Dong X., Chen Z., Tian W., Tang J.,
RA Wu W., Tong Y., Chen Z.;
RT "Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis
RT of protein translocation.";
RL Fen Zi Xi Bao Sheng Wu Xue Bao 9:220-230(2017).
RN [22] {ECO:0007744|PDB:5M72, ECO:0007744|PDB:5M73}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 10-166 OF MUTANT LEU-31 AND
RP LEU-65 AND OF 513-662 IN COMPLEX WITH SRP68; SRP19 AND 7SL RNA, RNA
RP BINDING, SUBUNIT, INTERACTION WITH SRP68, AND MUTAGENESIS OF ILE-56.
RX PubMed=27899666; DOI=10.1093/nar/gkw1124;
RA Becker M.M., Lapouge K., Segnitz B., Wild K., Sinning I.;
RT "Structures of human SRP72 complexes provide insights into SRP RNA
RT remodeling and ribosome interaction.";
RL Nucleic Acids Res. 45:470-481(2017).
RN [23] {ECO:0007744|PDB:7NFX}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF SIGNAL RECOGNITION
RP PARTICLE IN COMPLEX WITH RIBOSOME NASCENT CHAIN COMPLEX AND THE SRP
RP RECEPTOR.
RX PubMed=34020957; DOI=10.1126/sciadv.abg0942;
RA Lee J.H., Jomaa A., Jomaa A., Chung S., Hwang Fu Y.H., Qian R., Sun X.,
RA Hsieh H.H., Chandrasekar S., Bi X., Mattei S., Boehringer D., Weiss S.,
RA Ban N., Shan S.O.;
RT "Receptor compaction and GTPase rearrangement drive SRP-mediated
RT cotranslational protein translocation into the ER.";
RL Sci. Adv. 7:942-942(2021).
RN [24]
RP VARIANT BMFS1 HIS-207, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
RP VARIANT BMFS1 HIS-207.
RX PubMed=22541560; DOI=10.1016/j.ajhg.2012.03.020;
RA Kirwan M., Walne A.J., Plagnol V., Velangi M., Ho A., Hossain U.,
RA Vulliamy T., Dokal I.;
RT "Exome sequencing identifies autosomal-dominant SRP72 mutations associated
RT with familial aplasia and myelodysplasia.";
RL Am. J. Hum. Genet. 90:888-892(2012).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC (PubMed:34020957). The SRP complex interacts with the signal sequence
CC in nascent secretory and membrane proteins and directs them to the
CC membrane of the ER (PubMed:34020957). The SRP complex targets the
CC ribosome-nascent chain complex to the SRP receptor (SR), which is
CC anchored in the ER, where SR compaction and GTPase rearrangement drive
CC cotranslational protein translocation into the ER (PubMed:34020957).
CC Binds the signal recognition particle RNA (7SL RNA) in presence of
CC SRP68 (PubMed:27899666, PubMed:21073748). Can bind 7SL RNA with low
CC affinity (PubMed:27899666, PubMed:21073748). The SRP complex possibly
CC participates in the elongation arrest function (By similarity).
CC {ECO:0000250|UniProtKB:P38688, ECO:0000269|PubMed:21073748,
CC ECO:0000269|PubMed:27899666, ECO:0000269|PubMed:34020957}.
CC -!- SUBUNIT: Heterodimer with SRP68 (PubMed:16672232, PubMed:28369529,
CC PubMed:27899666). SRP68-SRP72 heterodimer formation is stabilized by
CC the presence of 7SL RNA (By similarity). Component of a signal
CC recognition particle (SRP) complex that consists of a 7SL RNA molecule
CC of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC SRP19, SRP14 and SRP9 (By similarity). Within the SRP complex,
CC interacts (via N-terminus) with SRP68 (via C-terminus)
CC (PubMed:16672232, PubMed:28369529, PubMed:27899666).
CC {ECO:0000250|UniProtKB:P33731, ECO:0000269|PubMed:16672232,
CC ECO:0000269|PubMed:27899666, ECO:0000269|PubMed:28369529}.
CC -!- INTERACTION:
CC O76094; Q9UHB9: SRP68; NbExp=5; IntAct=EBI-1058850, EBI-1048560;
CC O76094; O00204: SULT2B1; NbExp=3; IntAct=EBI-1058850, EBI-749441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22541560}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:22541560,
CC ECO:0000269|PubMed:28369529}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O76094-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O76094-2; Sequence=VSP_045576;
CC -!- DISEASE: Bone marrow failure syndrome 1 (BMFS1) [MIM:614675]: An
CC autosomal dominant disease characterized by aplastic anemia and
CC myelodysplasia resulting from bone marrow failure. Aplastic anemia is a
CC form of anemia in which the bone marrow fails to produce adequate
CC numbers of peripheral blood elements. Myelodysplasia is a clonal
CC hematopoietic stem cell disorder in which immature cells in the bone
CC marrow become malformed and dysfunctional.
CC {ECO:0000269|PubMed:22541560}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SRP72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97950.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle entry;
CC URL="https://en.wikipedia.org/wiki/Signal_recognition_particle";
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DR EMBL; AF077019; AAC27324.1; -; mRNA.
DR EMBL; AF069765; AAC97490.1; -; mRNA.
DR EMBL; BX537991; CAD97950.1; ALT_SEQ; mRNA.
DR EMBL; AC114766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05498.1; -; Genomic_DNA.
DR CCDS; CCDS3506.1; -. [O76094-1]
DR CCDS; CCDS58898.1; -. [O76094-2]
DR RefSeq; NP_001254651.1; NM_001267722.1. [O76094-2]
DR RefSeq; NP_008878.3; NM_006947.3. [O76094-1]
DR PDB; 5M72; X-ray; 1.60 A; A=10-166.
DR PDB; 5M73; X-ray; 3.40 A; D/H=513-662.
DR PDB; 5WRV; X-ray; 1.70 A; B=1-163.
DR PDB; 5WRW; X-ray; 2.91 A; A/B/C/D/E/F=1-163.
DR PDB; 7NFX; EM; 3.20 A; z=1-671.
DR PDBsum; 5M72; -.
DR PDBsum; 5M73; -.
DR PDBsum; 5WRV; -.
DR PDBsum; 5WRW; -.
DR PDBsum; 7NFX; -.
DR AlphaFoldDB; O76094; -.
DR SMR; O76094; -.
DR BioGRID; 112609; 173.
DR IntAct; O76094; 57.
DR MINT; O76094; -.
DR STRING; 9606.ENSP00000342181; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; O76094; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O76094; -.
DR MetOSite; O76094; -.
DR PhosphoSitePlus; O76094; -.
DR SwissPalm; O76094; -.
DR BioMuta; SRP72; -.
DR EPD; O76094; -.
DR jPOST; O76094; -.
DR MassIVE; O76094; -.
DR MaxQB; O76094; -.
DR PaxDb; O76094; -.
DR PeptideAtlas; O76094; -.
DR PRIDE; O76094; -.
DR ProteomicsDB; 34096; -.
DR ProteomicsDB; 50412; -. [O76094-1]
DR Antibodypedia; 24034; 93 antibodies from 24 providers.
DR DNASU; 6731; -.
DR Ensembl; ENST00000510663.6; ENSP00000424576.1; ENSG00000174780.17. [O76094-2]
DR Ensembl; ENST00000642900.1; ENSP00000495128.1; ENSG00000174780.17. [O76094-1]
DR GeneID; 6731; -.
DR KEGG; hsa:6731; -.
DR MANE-Select; ENST00000642900.1; ENSP00000495128.1; NM_006947.4; NP_008878.3.
DR UCSC; uc010ihe.4; human. [O76094-1]
DR CTD; 6731; -.
DR DisGeNET; 6731; -.
DR GeneCards; SRP72; -.
DR HGNC; HGNC:11303; SRP72.
DR HPA; ENSG00000174780; Low tissue specificity.
DR MalaCards; SRP72; -.
DR MIM; 602122; gene.
DR MIM; 614675; phenotype.
DR neXtProt; NX_O76094; -.
DR OpenTargets; ENSG00000174780; -.
DR Orphanet; 314399; Autosomal dominant aplasia and myelodysplasia.
DR PharmGKB; PA36127; -.
DR VEuPathDB; HostDB:ENSG00000174780; -.
DR eggNOG; KOG2376; Eukaryota.
DR GeneTree; ENSGT00390000013264; -.
DR HOGENOM; CLU_013808_1_0_1; -.
DR InParanoid; O76094; -.
DR OMA; NDMKVLA; -.
DR PhylomeDB; O76094; -.
DR TreeFam; TF106250; -.
DR PathwayCommons; O76094; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; O76094; -.
DR SIGNOR; O76094; -.
DR BioGRID-ORCS; 6731; 599 hits in 1098 CRISPR screens.
DR ChiTaRS; SRP72; human.
DR GenomeRNAi; 6731; -.
DR Pharos; O76094; Tbio.
DR PRO; PR:O76094; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O76094; protein.
DR Bgee; ENSG00000174780; Expressed in pylorus and 214 other tissues.
DR ExpressionAtlas; O76094; baseline and differential.
DR Genevisible; O76094; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0048500; C:signal recognition particle; IDA:CAFA.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
DR GO; GO:0008312; F:7S RNA binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005047; F:signal recognition particle binding; IPI:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; IPI:CAFA.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR InterPro; IPR026270; SRP72.
DR InterPro; IPR031545; SRP_TPR-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14094; PTHR14094; 1.
DR Pfam; PF08492; SRP72; 1.
DR Pfam; PF17004; SRP_TPR_like; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PIRSF; PIRSF038922; SRP72; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Signal recognition particle; TPR repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..671
FT /note="Signal recognition particle subunit SRP72"
FT /id="PRO_0000135234"
FT REPEAT 11..44
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 109..142
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 226..259
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 406..439
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 447..480
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REGION 9..163
FT /note="Required for interaction with SRP68"
FT /evidence="ECO:0000269|PubMed:16672232,
FT ECO:0000269|PubMed:28369529"
FT REGION 379..509
FT /note="Required for the interaction with the SRP68/7SL RNA
FT complex"
FT /evidence="ECO:0000250|UniProtKB:P33731"
FT REGION 532..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..617
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:21073748"
FT COMPBIAS 564..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 215..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045576"
FT VARIANT 207
FT /note="R -> H (in BMFS1; affects protein localization to
FT ER; dbSNP:rs387907189)"
FT /evidence="ECO:0000269|PubMed:22541560"
FT /id="VAR_068522"
FT MUTAGEN 11..44
FT /note="Missing: Loss of interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 44
FT /note="D->E: Reduced interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 45
FT /note="V->I: Reduced interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 53
FT /note="V->I: Reduced interaction with SRP68. Diminished
FT localization to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 56
FT /note="I->A: Loss of interaction with SRP72; when
FT associated with A-598 in SRP68."
FT /evidence="ECO:0000269|PubMed:27899666"
FT MUTAGEN 86
FT /note="Y->C: Loss of interaction with SRP68. Diminished
FT localization to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 113..131
FT /note="Missing: Loss of interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 132..165
FT /note="Missing: Loss of interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 136..137
FT /note="VR->AA: Stronger interaction with SRP68."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 553..558
FT /note="KKKKKK->AAAAAA: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 555..556
FT /note="KK->AA: Diminished RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 577..578
FT /note="WL->AA: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 579..580
FT /note="PM->AA: Diminished RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 579
FT /note="P->A: Strongly reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 580
FT /note="M->A: Does not affect RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 581..582
FT /note="RE->AA: Diminished RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 583..584
FT /note="RS->AA: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 585..586
FT /note="YY->AA: Diminished RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 587..588
FT /note="RG->AA: No impact on RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT MUTAGEN 589..590
FT /note="RK->AA: No impact on RNA binding."
FT /evidence="ECO:0000269|PubMed:21073748"
FT CONFLICT 23
FT /note="Q -> R (in Ref. 3; CAD97950)"
FT /evidence="ECO:0000305"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:5M73"
FT TURN 567..570
FT /evidence="ECO:0007829|PDB:5M73"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:5M73"
FT HELIX 590..602
FT /evidence="ECO:0007829|PDB:5M73"
SQ SEQUENCE 671 AA; 74606 MW; CC0BA17AC52E3613 CRC64;
MASGGSGGVS VPALWSEVNR YGQNGDFTRA LKTVNKILQI NKDDVTALHC KVVCLIQNGS
FKEALNVINT HTKVLANNSL SFEKAYCEYR LNRIENALKT IESANQQTDK LKELYGQVLY
RLERYDECLA VYRDLVRNSQ DDYDEERKTN LSAVVAAQSN WEKVVPENLG LQEGTHELCY
NTACALIGQG QLNQAMKILQ KAEDLCRRSL SEDTDGTEED PQAELAIIHG QMAYILQLQG
RTEEALQLYN QIIKLKPTDV GLLAVIANNI ITINKDQNVF DSKKKVKLTN AEGVEFKLSK
KQLQAIEFNK ALLAMYTNQA EQCRKISASL QSQSPEHLLP VLIQAAQLCR EKQHTKAIEL
LQEFSDQHPE NAAEIKLTMA QLKISQGNIS KACLILRSIE ELKHKPGMVS ALVTMYSHEE
DIDSAIEVFT QAIQWYQNHQ PKSPAHLSLI REAANFKLKY GRKKEAISDL QQLWKQNPKD
IHTLAQLISA YSLVDPEKAK ALSKHLPSSD SMSLKVDVEA LENSAGATYI RKKGGKVTGD
SQPKEQGQGD LKKKKKKKKG KLPKNYDPKV TPDPERWLPM RERSYYRGRK KGKKKDQIGK
GTQGATAGAS SELDASKTVS SPPTSPRPGS AATVSASTSN IIPPRHQKPA GAPATKKKQQ
QKKKKGGKGG W
