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   10-JUN-2026, entry version 209.
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:21073748, PubMed:27899666). Can bind 7SL RNA with low
CC       affinity (PubMed:21073748, PubMed:27899666). 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:27899666,
CC       PubMed:28369529). 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:27899666, PubMed:28369529).
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=9; 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_001267722.2. [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   PDB; 8QVW; EM; 3.00 A; B=1-671.
DR   PDB; 8QVX; EM; 2.70 A; B=1-671.
DR   PDBsum; 5M72; -.
DR   PDBsum; 5M73; -.
DR   PDBsum; 5WRV; -.
DR   PDBsum; 5WRW; -.
DR   PDBsum; 7NFX; -.
DR   PDBsum; 8QVW; -.
DR   PDBsum; 8QVX; -.
DR   AlphaFoldDB; O76094; -.
DR   EMDB; EMD-12303; -.
DR   EMDB; EMD-18674; -.
DR   EMDB; EMD-18677; -.
DR   SMR; O76094; -.
DR   BioGRID; 112609; 372.
DR   ComplexPortal; CPX-2652; Signal recognition particle.
DR   FunCoup; O76094; 2262.
DR   IntAct; O76094; 256.
DR   MINT; O76094; -.
DR   NDEx; IQUERY-CP-SRP72; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000495128; -.
DR   ChEMBL; CHEMBL6066168; -.
DR   TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR   GlyCosmos; O76094; 1 site, 1 glycan.
DR   GlyGen; O76094; 4 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; O76094; -.
DR   MetOSite; O76094; -.
DR   PhosphoSitePlus; O76094; -.
DR   SwissPalm; O76094; -.
DR   BioMuta; SRP72; -.
DR   jPOST; O76094; -.
DR   MassIVE; O76094; -.
DR   PaxDb; 9606-ENSP00000495128; -.
DR   PeptideAtlas; O76094; -.
DR   ProteomicsDB; 34096; -.
DR   ProteomicsDB; 50412; -. [O76094-1]
DR   Pumba; O76094; -.
DR   Antibodypedia; 24034; 99 antibodies from 26 providers.
DR   DNASU; 6731; -.
DR   Ensembl; ENST00000510663.6; ENSP00000424576.1; ENSG00000174780.18. [O76094-2]
DR   Ensembl; ENST00000642900.1; ENSP00000495128.1; ENSG00000174780.18. [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   AGR; HGNC:11303; -.
DR   ClinPGx; PA36127; -.
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   OpenTargets; ENSG00000174780; -.
DR   Orphanet; 314399; Autosomal dominant aplasia and myelodysplasia.
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   OrthoDB; 5421607at2759; -.
DR   PAN-GO; O76094; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; O76094; -.
DR   PathwayCommons; O76094; -.
DR   Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   SignaLink; O76094; -.
DR   SIGNOR; O76094; -.
DR   Agora; ENSG00000174780; -.
DR   BioGRID-ORCS; 6731; 618 hits in 1178 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   CD-CODE; DEE660B4; Stress granule.
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 216 other cell types or tissues.
DR   ExpressionAtlas; O76094; baseline and differential.
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   GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; NAS:ComplexPortal.
DR   FunFam; 1.25.40.10:FF:000062; Signal recognition particle subunit SRP72; 1.
DR   FunFam; 1.25.40.10:FF:000133; Signal recognition particle subunit SRP72; 1.
DR   FunFam; 1.25.40.10:FF:000369; Signal recognition particle subunit SRP72; 1.
DR   FunFam; 1.25.40.10:FF:000847; Signal recognition particle subunit SRP72; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR   InterPro; IPR026270; SRP72.
DR   InterPro; IPR031545; SRP72_TPR-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR14094; SIGNAL RECOGNITION PARTICLE 72; 1.
DR   PANTHER; PTHR14094:SF9; SIGNAL RECOGNITION PARTICLE SUBUNIT SRP72; 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; TPR-like; 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; Proteomics identification;
KW   Reference proteome; Repeat; Ribonucleoprotein; Signal recognition particle;
KW   TPR repeat; 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        552..562
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..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   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:8QVX"
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           176..189
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           193..211
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           223..239
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           261..274
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           279..289
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           300..316
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           320..333
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           341..350
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           355..367
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           372..382
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           389..397
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           406..418
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           422..439
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           444..460
FT                   /evidence="ECO:0007829|PDB:8QVX"
FT   HELIX           563..566
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   TURN            567..570
FT                   /evidence="ECO:0007829|PDB:5M73"
FT   STRAND          576..578
FT                   /evidence="ECO:0007829|PDB:7NFX"
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
//