SRP68_HUMAN
ID SRP68_HUMAN Reviewed; 627 AA.
AC Q9UHB9; B3KUU5; B3KWY7; G3V1U4; Q8NCJ4; Q8WUK2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Signal recognition particle subunit SRP68;
DE Short=SRP68;
DE AltName: Full=Signal recognition particle 68 kDa protein;
GN Name=SRP68;
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), AND SUBCELLULAR LOCATION.
RX PubMed=10618370; DOI=10.1073/pnas.97.1.55;
RA Politz J.C., Yarovoi S., Kilroy S.M., Gowda K., Zwieb C., Pederson T.;
RT "Signal recognition particle components in the nucleolus.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:55-60(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Liver, Mammary gland, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
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 [6]
RP FUNCTION, RNA BINDING, SUBUNIT, INTERACTION WITH SRP72, AND DOMAIN.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-452, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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 [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
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 [15]
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 [16] {ECO:0007744|PDB:4P3E, ECO:0007744|PDB:4P3F}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 47-254 IN COMPLEX WITH SRP19 AND
RP 7SL RNA.
RX PubMed=24700861; DOI=10.1126/science.1249094;
RA Grotwinkel J.T., Wild K., Segnitz B., Sinning I.;
RT "SRP RNA remodeling by SRP68 explains its role in protein translocation.";
RL Science 344:101-104(2014).
RN [17] {ECO:0007744|PDB:5WRV}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 509-614 OF MUTANT
RP 608-GLU--610-LYS IN COMPLEX WITH SRP78, SUBUNIT, INTERACTION WITH SRP72,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-590 AND GLN-609.
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 [18] {ECO:0007744|PDB:5M72, ECO:0007744|PDB:5M73}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 60-254 AND 546-614 IN COMPLEX
RP WITH SRP72; SRP19 AND 7SL RNA, RNA BINDING, SUBUNIT, INTERACTION WITH
RP SRP72, AND MUTAGENESIS OF TYR-86; ASP-592; VAL-598 AND PHE-600.
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 [19] {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, AND FUNCTION.
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).
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), SRP72 binds to
CC this complex subsequently (PubMed:16672232, PubMed:27899666). The SRP
CC complex possibly participates in the elongation arrest function (By
CC similarity). {ECO:0000250|UniProtKB:P38687,
CC ECO:0000269|PubMed:16672232, ECO:0000269|PubMed:27899666,
CC ECO:0000269|PubMed:34020957}.
CC -!- SUBUNIT: Heterodimer with SRP72 (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 C-terminus) with SRP72 (via N-terminus)
CC (PubMed:16672232, PubMed:28369529, PubMed:27899666).
CC {ECO:0000250|UniProtKB:Q00004, ECO:0000269|PubMed:16672232,
CC ECO:0000269|PubMed:27899666, ECO:0000269|PubMed:28369529}.
CC -!- INTERACTION:
CC Q9UHB9; P09132: SRP19; NbExp=2; IntAct=EBI-1048560, EBI-2680090;
CC Q9UHB9; O76094: SRP72; NbExp=5; IntAct=EBI-1048560, EBI-1058850;
CC Q9UHB9-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12210563, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10618370}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10618370}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:28369529}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UHB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHB9-2; Sequence=VSP_008347;
CC Name=3;
CC IsoId=Q9UHB9-3; Sequence=VSP_045132;
CC Name=4;
CC IsoId=Q9UHB9-4; Sequence=VSP_046944;
CC -!- DOMAIN: The N-terminus is required for RNA-binding.
CC {ECO:0000269|PubMed:16672232}.
CC -!- SIMILARITY: Belongs to the SRP68 family. {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; AF195951; AAF24308.1; -; mRNA.
DR EMBL; AK074698; BAC11145.1; -; mRNA.
DR EMBL; AK097962; BAG53557.1; -; mRNA.
DR EMBL; AK126258; BAG54299.1; -; mRNA.
DR EMBL; AC040980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89360.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89362.1; -; Genomic_DNA.
DR EMBL; BC020238; AAH20238.1; -; mRNA.
DR CCDS; CCDS11738.1; -. [Q9UHB9-1]
DR CCDS; CCDS58600.1; -. [Q9UHB9-3]
DR CCDS; CCDS58601.1; -. [Q9UHB9-4]
DR RefSeq; NP_001247431.1; NM_001260502.1. [Q9UHB9-4]
DR RefSeq; NP_001247432.1; NM_001260503.1. [Q9UHB9-3]
DR RefSeq; NP_055045.2; NM_014230.3. [Q9UHB9-1]
DR PDB; 4P3E; X-ray; 3.50 A; C=47-254.
DR PDB; 4P3F; X-ray; 1.70 A; A/B=47-254.
DR PDB; 5M72; X-ray; 1.60 A; B=546-614.
DR PDB; 5M73; X-ray; 3.40 A; C/G=60-254.
DR PDB; 5WRV; X-ray; 1.70 A; A=509-614.
DR PDB; 7NFX; EM; 3.20 A; u=1-627.
DR PDB; 7QWQ; EM; 2.83 A; v=1-627.
DR PDBsum; 4P3E; -.
DR PDBsum; 4P3F; -.
DR PDBsum; 5M72; -.
DR PDBsum; 5M73; -.
DR PDBsum; 5WRV; -.
DR PDBsum; 7NFX; -.
DR PDBsum; 7QWQ; -.
DR AlphaFoldDB; Q9UHB9; -.
DR SMR; Q9UHB9; -.
DR BioGRID; 112608; 171.
DR DIP; DIP-50905N; -.
DR IntAct; Q9UHB9; 60.
DR MINT; Q9UHB9; -.
DR STRING; 9606.ENSP00000312066; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; Q9UHB9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHB9; -.
DR PhosphoSitePlus; Q9UHB9; -.
DR SwissPalm; Q9UHB9; -.
DR BioMuta; SRP68; -.
DR DMDM; 37154869; -.
DR EPD; Q9UHB9; -.
DR jPOST; Q9UHB9; -.
DR MassIVE; Q9UHB9; -.
DR MaxQB; Q9UHB9; -.
DR PaxDb; Q9UHB9; -.
DR PeptideAtlas; Q9UHB9; -.
DR PRIDE; Q9UHB9; -.
DR ProteomicsDB; 32444; -.
DR ProteomicsDB; 3735; -.
DR ProteomicsDB; 84303; -. [Q9UHB9-1]
DR ProteomicsDB; 84304; -. [Q9UHB9-2]
DR Antibodypedia; 19656; 141 antibodies from 24 providers.
DR DNASU; 6730; -.
DR Ensembl; ENST00000307877.7; ENSP00000312066.1; ENSG00000167881.15. [Q9UHB9-1]
DR Ensembl; ENST00000539137.5; ENSP00000446136.1; ENSG00000167881.15. [Q9UHB9-4]
DR Ensembl; ENST00000602720.5; ENSP00000473613.1; ENSG00000167881.15. [Q9UHB9-3]
DR GeneID; 6730; -.
DR KEGG; hsa:6730; -.
DR MANE-Select; ENST00000307877.7; ENSP00000312066.1; NM_014230.4; NP_055045.2.
DR UCSC; uc002jqj.3; human. [Q9UHB9-1]
DR CTD; 6730; -.
DR DisGeNET; 6730; -.
DR GeneCards; SRP68; -.
DR HGNC; HGNC:11302; SRP68.
DR HPA; ENSG00000167881; Tissue enhanced (brain).
DR MIM; 604858; gene.
DR neXtProt; NX_Q9UHB9; -.
DR OpenTargets; ENSG00000167881; -.
DR PharmGKB; PA36126; -.
DR VEuPathDB; HostDB:ENSG00000167881; -.
DR eggNOG; KOG2460; Eukaryota.
DR GeneTree; ENSGT00390000011856; -.
DR HOGENOM; CLU_084496_0_0_1; -.
DR InParanoid; Q9UHB9; -.
DR OMA; DERFIHI; -.
DR OrthoDB; 1019762at2759; -.
DR PhylomeDB; Q9UHB9; -.
DR TreeFam; TF105779; -.
DR PathwayCommons; Q9UHB9; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; Q9UHB9; -.
DR SIGNOR; Q9UHB9; -.
DR BioGRID-ORCS; 6730; 625 hits in 1088 CRISPR screens.
DR ChiTaRS; SRP68; human.
DR GenomeRNAi; 6730; -.
DR Pharos; Q9UHB9; Tbio.
DR PRO; PR:Q9UHB9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UHB9; protein.
DR Bgee; ENSG00000167881; Expressed in tibialis anterior and 182 other tissues.
DR ExpressionAtlas; Q9UHB9; baseline and differential.
DR Genevisible; Q9UHB9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0005840; C:ribosome; TAS:ProtInc.
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:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005047; F:signal recognition particle binding; IPI:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd15481; SRP68-RBD; 1.
DR Gene3D; 1.10.3450.40; -; 1.
DR InterPro; IPR026258; SRP68.
DR InterPro; IPR034652; SRP68-RBD.
DR InterPro; IPR038253; SRP68_N_sf.
DR PANTHER; PTHR12860; PTHR12860; 1.
DR Pfam; PF16969; SRP68; 1.
DR PIRSF; PIRSF038995; SRP68; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Endoplasmic reticulum; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..627
FT /note="Signal recognition particle subunit SRP68"
FT /id="PRO_0000135227"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..252
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:16672232"
FT REGION 588..610
FT /note="Required for interaction with SRP72"
FT /evidence="ECO:0000269|PubMed:16672232,
FT ECO:0000269|PubMed:28369529"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..339
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045132"
FT VAR_SEQ 84..121
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046944"
FT VAR_SEQ 256..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008347"
FT MUTAGEN 86
FT /note="Y->A: Loss of interaction with SRP72."
FT /evidence="ECO:0000269|PubMed:27899666"
FT MUTAGEN 590
FT /note="F->L: Loss of interaction with SRP72. Diminished
FT localization to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:28369529"
FT MUTAGEN 592
FT /note="D->A: Loss of interaction with SRP72."
FT /evidence="ECO:0000269|PubMed:27899666"
FT MUTAGEN 598
FT /note="V->A: Loss of interaction with SRP72; when
FT associated with A-56 in SRP72."
FT /evidence="ECO:0000269|PubMed:27899666"
FT MUTAGEN 600
FT /note="F->A: Loss of interaction with SRP72."
FT /evidence="ECO:0000269|PubMed:27899666"
FT MUTAGEN 609
FT /note="Q->H: Reduced interaction with SRP72."
FT /evidence="ECO:0000269|PubMed:28369529"
FT CONFLICT 15..19
FT /note="Missing (in Ref. 1; AAF24308)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..29
FT /note="Missing (in Ref. 1; AAF24308)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="E -> K (in Ref. 1; AAF24308)"
FT /evidence="ECO:0000305"
FT CONFLICT 534..535
FT /note="DA -> ES (in Ref. 1; AAF24308)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="K -> E (in Ref. 2; BAG54299)"
FT /evidence="ECO:0000305"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 80..103
FT /evidence="ECO:0007829|PDB:4P3F"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4P3F"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:4P3F"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4P3E"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 204..222
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 227..251
FT /evidence="ECO:0007829|PDB:4P3F"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:5M72"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:5M72"
SQ SEQUENCE 627 AA; 70730 MW; 6EF582892D300B2D CRC64;
MAAEKQVPGG GGGGGSGGGG GSGGGGSGGG RGAGGEENKE NERPSAGSKA NKEFGDSLSL
EILQIIKESQ QQHGLRHGDF QRYRGYCSRR QRRLRKTLNF KMGNRHKFTG KKVTEELLTD
NRYLLLVLMD AERAWSYAMQ LKQEANTEPR KRFHLLSRLR KAVKHAEELE RLCESNRVDA
KTKLEAQAYT AYLSGMLRFE HQEWKAAIEA FNKCKTIYEK LASAFTEEQA VLYNQRVEEI
SPNIRYCAYN IGDQSAINEL MQMRLRSGGT EGLLAEKLEA LITQTRAKQA ATMSEVEWRG
RTVPVKIDKV RIFLLGLADN EAAIVQAESE ETKERLFESM LSECRDAIQV VREELKPDQK
QRDYILEGEP GKVSNLQYLH SYLTYIKLST AIKRNENMAK GLQRALLQQQ PEDDSKRSPR
PQDLIRLYDI ILQNLVELLQ LPGLEEDKAF QKEIGLKTLV FKAYRCFFIA QSYVLVKKWS
EALVLYDRVL KYANEVNSDA GAFKNSLKDL PDVQELITQV RSEKCSLQAA AILDANDAHQ
TETSSSQVKD NKPLVERFET FCLDPSLVTK QANLVHFPPG FQPIPCKPLF FDLALNHVAF
PPLEDKLEQK TKSGLTGYIK GIFGFRS
