SRP09_HUMAN
ID SRP09_HUMAN Reviewed; 86 AA.
AC P49458; A8K0N0; Q6NVX0; Q8WTW0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Signal recognition particle 9 kDa protein;
DE Short=SRP9;
GN Name=SRP9;
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).
RX PubMed=7730321; DOI=10.1074/jbc.270.17.10179;
RA Hsu K., Chang D.-Y., Maraia R.J.;
RT "Human signal recognition particle (SRP) Alu-associated protein also binds
RT Alu interspersed repeat sequence RNAs. Characterization of human SRP9.";
RL J. Biol. Chem. 270:10179-10186(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lee W.K., Sohn Y.-W., Kim H.;
RT "Molecular cloning of a novel isoform of human signal recognition particle
RT 9 kda (SRP9i).";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
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 [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] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, and 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 PROTEIN SEQUENCE OF 2-12 AND 17-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, 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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-86 IN COMPLEX WITH SRP14,
RP FUNCTION, AND SUBUNIT.
RX PubMed=11089964; DOI=10.1038/35041507;
RA Weichenrieder O., Wild K., Strub K., Cusack S.;
RT "Structure and assembly of the Alu domain of the mammalian signal
RT recognition particle.";
RL Nature 408:167-173(2000).
RN [13] {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).
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 (By similarity). SRP9 together with SRP14 and the Alu portion of the
CC SRP RNA, constitutes the elongation arrest domain of SRP
CC (PubMed:11089964). The complex of SRP9 and SRP14 is required for SRP
CC RNA binding (By similarity). {ECO:0000250|UniProtKB:P21262,
CC ECO:0000269|PubMed:11089964}.
CC -!- SUBUNIT: Heterodimer with SRP14; binds RNA as heterodimer (By
CC similarity). Component of a signal recognition particle complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:11089964).
CC {ECO:0000250|UniProtKB:P21262, ECO:0000269|PubMed:11089964}.
CC -!- INTERACTION:
CC P49458; P35609: ACTN2; NbExp=3; IntAct=EBI-350743, EBI-77797;
CC P49458; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-350743, EBI-12143631;
CC P49458; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-350743, EBI-21529239;
CC P49458; Q8N488: RYBP; NbExp=3; IntAct=EBI-350743, EBI-752324;
CC P49458; P37108: SRP14; NbExp=8; IntAct=EBI-350743, EBI-353399;
CC P49458-1; P37108: SRP14; NbExp=2; IntAct=EBI-15490029, EBI-353399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49458-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49458-2; Sequence=VSP_041270;
CC -!- SIMILARITY: Belongs to the SRP9 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; U20998; AAA70170.1; -; mRNA.
DR EMBL; EF488978; ABP02070.1; -; mRNA.
DR EMBL; AK289595; BAF82284.1; -; mRNA.
DR EMBL; CH471066; EAW50106.1; -; Genomic_DNA.
DR EMBL; CH471098; EAW69750.1; -; Genomic_DNA.
DR EMBL; CH471098; EAW69751.1; -; Genomic_DNA.
DR EMBL; BC008443; AAH08443.1; -; mRNA.
DR EMBL; BC067845; AAH67845.1; -; mRNA.
DR EMBL; BC021995; AAH21995.1; -; mRNA.
DR EMBL; BC015094; AAH15094.1; -; mRNA.
DR EMBL; BC022415; AAH22415.1; -; mRNA.
DR EMBL; BC066957; AAH66957.1; -; mRNA.
DR CCDS; CCDS1546.1; -. [P49458-1]
DR CCDS; CCDS44323.1; -. [P49458-2]
DR PIR; A57292; A57292.
DR RefSeq; NP_001123912.1; NM_001130440.1. [P49458-2]
DR RefSeq; NP_003124.1; NM_003133.5. [P49458-1]
DR PDB; 1E8O; X-ray; 3.20 A; A/C=2-86.
DR PDB; 1E8S; X-ray; 4.00 A; A=2-86.
DR PDB; 1RY1; EM; 12.00 A; C=2-86.
DR PDB; 4UYJ; X-ray; 3.35 A; A/C=1-85.
DR PDB; 4UYK; X-ray; 3.22 A; A=1-85.
DR PDB; 5AOX; X-ray; 2.04 A; A/D=2-86.
DR PDB; 7NFX; EM; 3.20 A; w=1-86.
DR PDBsum; 1E8O; -.
DR PDBsum; 1E8S; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 4UYJ; -.
DR PDBsum; 4UYK; -.
DR PDBsum; 5AOX; -.
DR PDBsum; 7NFX; -.
DR AlphaFoldDB; P49458; -.
DR SMR; P49458; -.
DR BioGRID; 112604; 148.
DR DIP; DIP-6151N; -.
DR IntAct; P49458; 63.
DR MINT; P49458; -.
DR STRING; 9606.ENSP00000305230; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR CarbonylDB; P49458; -.
DR GlyGen; P49458; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49458; -.
DR MetOSite; P49458; -.
DR PhosphoSitePlus; P49458; -.
DR SwissPalm; P49458; -.
DR BioMuta; SRP9; -.
DR DMDM; 1351111; -.
DR EPD; P49458; -.
DR jPOST; P49458; -.
DR MassIVE; P49458; -.
DR MaxQB; P49458; -.
DR PaxDb; P49458; -.
DR PeptideAtlas; P49458; -.
DR PRIDE; P49458; -.
DR ProteomicsDB; 56016; -. [P49458-1]
DR ProteomicsDB; 56017; -. [P49458-2]
DR TopDownProteomics; P49458-1; -. [P49458-1]
DR Antibodypedia; 47125; 90 antibodies from 19 providers.
DR DNASU; 6726; -.
DR Ensembl; ENST00000304786.12; ENSP00000305230.7; ENSG00000143742.14. [P49458-1]
DR Ensembl; ENST00000366839.8; ENSP00000355804.4; ENSG00000143742.14. [P49458-2]
DR Ensembl; ENST00000619790.4; ENSP00000485002.1; ENSG00000143742.14. [P49458-2]
DR Ensembl; ENST00000651465.1; ENSP00000498359.1; ENSG00000143742.14. [P49458-2]
DR GeneID; 6726; -.
DR KEGG; hsa:6726; -.
DR MANE-Select; ENST00000304786.12; ENSP00000305230.7; NM_003133.6; NP_003124.1.
DR UCSC; uc001hpg.4; human. [P49458-1]
DR CTD; 6726; -.
DR DisGeNET; 6726; -.
DR GeneCards; SRP9; -.
DR HGNC; HGNC:11304; SRP9.
DR HPA; ENSG00000143742; Low tissue specificity.
DR MIM; 600707; gene.
DR neXtProt; NX_P49458; -.
DR OpenTargets; ENSG00000143742; -.
DR PharmGKB; PA36128; -.
DR VEuPathDB; HostDB:ENSG00000143742; -.
DR eggNOG; KOG3465; Eukaryota.
DR GeneTree; ENSGT00390000018505; -.
DR HOGENOM; CLU_2644400_0_0_1; -.
DR InParanoid; P49458; -.
DR OMA; YINSWEE; -.
DR OrthoDB; 1623953at2759; -.
DR PhylomeDB; P49458; -.
DR TreeFam; TF106246; -.
DR PathwayCommons; P49458; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; P49458; -.
DR BioGRID-ORCS; 6726; 632 hits in 1047 CRISPR screens.
DR ChiTaRS; SRP9; human.
DR EvolutionaryTrace; P49458; -.
DR GenomeRNAi; 6726; -.
DR Pharos; P49458; Tbio.
DR PRO; PR:P49458; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49458; protein.
DR Bgee; ENSG00000143742; Expressed in ganglionic eminence and 103 other tissues.
DR ExpressionAtlas; P49458; baseline and differential.
DR Genevisible; P49458; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005785; C:signal recognition particle receptor complex; TAS:ProtInc.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0005047; F:signal recognition particle binding; TAS:ProtInc.
DR GO; GO:0045900; P:negative regulation of translational elongation; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 3.30.720.10; -; 1.
DR InterPro; IPR008832; Signal_recog_particle_SRP9.
DR InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR InterPro; IPR039914; SRP9.
DR InterPro; IPR039432; SRP9_dom.
DR PANTHER; PTHR12834; PTHR12834; 1.
DR Pfam; PF05486; SRP9-21; 1.
DR PIRSF; PIRSF017029; Signal_recog_particle_SRP9; 1.
DR SUPFAM; SSF54762; SSF54762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Signal recognition particle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..86
FT /note="Signal recognition particle 9 kDa protein"
FT /id="PRO_0000135182"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 48..86
FT /note="CLVYKTDQAQDVKKIEKFHSQLMRLMVAKEARNVTMETE -> RQCLALLLR
FT LQCSGMIIAHCILDLLGSSGPLASAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_041270"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5AOX"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:5AOX"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5AOX"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:5AOX"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4UYK"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4UYK"
FT CONFLICT P49458-2:64
FT /note="I -> M (in Ref. 5; AAH21995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 10112 MW; DB2CA071AF0E6F65 CRC64;
MPQYQTWEEF SRAAEKLYLA DPMKARVVLK YRHSDGNLCV KVTDDLVCLV YKTDQAQDVK
KIEKFHSQLM RLMVAKEARN VTMETE
