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 27-MAR-2024, entry version 192. 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; P13569: CFTR; NbExp=7; IntAct=EBI-1048560, EBI-349854; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-12303; -. DR EMDB; EMD-14191; -. DR SMR; Q9UHB9; -. DR BioGRID; 112608; 363. DR ComplexPortal; CPX-2652; Signal recognition particle. DR DIP; DIP-50905N; -. DR IntAct; Q9UHB9; 63. 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; 9606-ENSP00000312066; -. DR PeptideAtlas; Q9UHB9; -. DR ProteomicsDB; 32444; -. DR ProteomicsDB; 3735; -. DR ProteomicsDB; 84303; -. [Q9UHB9-1] DR ProteomicsDB; 84304; -. [Q9UHB9-2] DR Pumba; Q9UHB9; -. DR Antibodypedia; 19656; 165 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 AGR; HGNC:11302; -. DR CTD; 6730; -. DR DisGeNET; 6730; -. DR GeneCards; SRP68; -. DR HGNC; HGNC:11302; SRP68. DR HPA; ENSG00000167881; Low tissue specificity. 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; 5477279at2759; -. 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; 654 hits in 1168 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 184 other cell types or tissues. DR ExpressionAtlas; Q9UHB9; baseline and differential. 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; Signal recognition particle, SRP68 subunit, RNA-binding domain; 1. DR InterPro; IPR026258; SRP68. DR InterPro; IPR034652; SRP68-RBD. DR InterPro; IPR038253; SRP68_N_sf. DR PANTHER; PTHR12860; SIGNAL RECOGNITION PARTICLE 68 KDA PROTEIN; 1. DR PANTHER; PTHR12860:SF0; SIGNAL RECOGNITION PARTICLE SUBUNIT SRP68; 1. DR Pfam; PF16969; SRP68; 1. DR PIRSF; PIRSF038995; SRP68; 1. DR Genevisible; Q9UHB9; HS. 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 //