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Database: UniProt
Entry: P09132
LinkDB: P09132
Original site: P09132 
ID   SRP19_HUMAN             Reviewed;         144 AA.
AC   P09132; B2R4E9; D6RCQ5; Q05D77; Q96FG6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 3.
DT   29-SEP-2021, entry version 208.
DE   RecName: Full=Signal recognition particle 19 kDa protein;
DE            Short=SRP19;
GN   Name=SRP19;
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 PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=2460823; DOI=10.1093/nar/16.20.9431;
RA   Lingelbach K., Zwieb C., Webb J.R., Marshallsaz C., Hoben P., Walter P.,
RA   Dobberstein B.;
RT   "Isolation and characterization of a cDNA clone encoding the 19 kDa protein
RT   of signal recognition particle (SRP): expression and binding to 7SL RNA.";
RL   Nucleic Acids Res. 16:9431-9442(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Erythroblast;
RA   Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.;
RT   "Gene expression in human erythroid precursor cells.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   THR-4.
RC   TISSUE=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   [7]
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   [8]
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   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-128.
RX   PubMed=11641499; DOI=10.1126/science.1063839;
RA   Wild K., Sinning I., Cusack S.;
RT   "Crystal structure of an early protein-RNA assembly complex of the signal
RT   recognition particle.";
RL   Science 294:598-601(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-120 IN COMPLEX WITH SRP54 AND
RP   7SL RNA.
RX   PubMed=12244299; DOI=10.1038/nsb843;
RA   Kuglstatter A., Oubridge C., Nagai K.;
RT   "Induced structural changes of 7SL RNA during the assembly of human signal
RT   recognition particle.";
RL   Nat. Struct. Biol. 9:740-744(2002).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-120 IN COMPLEX WITH 7SL RNA.
RX   PubMed=20179341; DOI=10.1107/s0907444910000879;
RA   Wild K., Bange G., Bozkurt G., Segnitz B., Hendricks A., Sinning I.;
RT   "Structural insights into the assembly of the human and archaeal signal
RT   recognition particles.";
RL   Acta Crystallogr. D 66:295-303(2010).
CC   -!- FUNCTION: Signal-recognition-particle assembly, binds directly to 7S
CC       RNA and mediates binding of the 54 kDa subunit of the SRP.
CC   -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of
CC       300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19,
CC       SRP14 and SRP9. {ECO:0000269|PubMed:12244299,
CC       ECO:0000269|PubMed:20179341}.
CC   -!- INTERACTION:
CC       P09132; Q9UHB9: SRP68; NbExp=2; IntAct=EBI-2680090, EBI-1048560;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P09132-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P09132-2; Sequence=VSP_042540;
CC       Name=3;
CC         IsoId=P09132-3; Sequence=VSP_044524;
CC   -!- SIMILARITY: Belongs to the SRP19 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; X12791; CAA31280.1; -; mRNA.
DR   EMBL; BU661702; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK311803; BAG34746.1; -; mRNA.
DR   EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471086; EAW48999.1; -; Genomic_DNA.
DR   EMBL; CH471086; EAW49000.1; -; Genomic_DNA.
DR   EMBL; BC010947; AAH10947.1; -; mRNA.
DR   EMBL; BC017830; AAH17830.1; -; mRNA.
DR   CCDS; CCDS4108.1; -. [P09132-1]
DR   CCDS; CCDS56375.1; -. [P09132-2]
DR   CCDS; CCDS56376.1; -. [P09132-3]
DR   PIR; S01700; S01700.
DR   RefSeq; NP_001191122.1; NM_001204193.1. [P09132-2]
DR   RefSeq; NP_001191123.1; NM_001204194.1.
DR   RefSeq; NP_001191125.1; NM_001204196.1. [P09132-3]
DR   RefSeq; NP_003126.1; NM_003135.2. [P09132-1]
DR   PDB; 1JID; X-ray; 1.80 A; A=1-120.
DR   PDB; 1MFQ; X-ray; 3.10 A; B=14-120.
DR   PDB; 1RY1; EM; 12.00 A; B=14-120.
DR   PDB; 2J37; EM; 8.00 A; B=14-120.
DR   PDB; 3KTV; X-ray; 3.80 A; B/D=1-120.
DR   PDB; 4P3E; X-ray; 3.50 A; B=1-120.
DR   PDB; 5M73; X-ray; 3.40 A; B/F=11-118.
DR   PDB; 7NFX; EM; 3.20 A; q=1-144.
DR   PDBsum; 1JID; -.
DR   PDBsum; 1MFQ; -.
DR   PDBsum; 1RY1; -.
DR   PDBsum; 2J37; -.
DR   PDBsum; 3KTV; -.
DR   PDBsum; 4P3E; -.
DR   PDBsum; 5M73; -.
DR   PDBsum; 7NFX; -.
DR   SMR; P09132; -.
DR   BioGRID; 112606; 54.
DR   DIP; DIP-41412N; -.
DR   IntAct; P09132; 23.
DR   MINT; P09132; -.
DR   STRING; 9606.ENSP00000424870; -.
DR   ChEMBL; CHEMBL4295704; -.
DR   TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR   GlyGen; P09132; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P09132; -.
DR   PhosphoSitePlus; P09132; -.
DR   SwissPalm; P09132; -.
DR   BioMuta; SRP19; -.
DR   DMDM; 115502457; -.
DR   EPD; P09132; -.
DR   jPOST; P09132; -.
DR   MassIVE; P09132; -.
DR   MaxQB; P09132; -.
DR   PaxDb; P09132; -.
DR   PeptideAtlas; P09132; -.
DR   PRIDE; P09132; -.
DR   ProteomicsDB; 13963; -.
DR   ProteomicsDB; 52203; -. [P09132-1]
DR   ProteomicsDB; 52204; -. [P09132-2]
DR   Antibodypedia; 13558; 178 antibodies.
DR   DNASU; 6728; -.
DR   Ensembl; ENST00000282999; ENSP00000282999; ENSG00000153037. [P09132-2]
DR   Ensembl; ENST00000505459; ENSP00000424870; ENSG00000153037. [P09132-1]
DR   Ensembl; ENST00000515463; ENSP00000425562; ENSG00000153037. [P09132-3]
DR   GeneID; 6728; -.
DR   KEGG; hsa:6728; -.
DR   UCSC; uc003kqb.3; human. [P09132-1]
DR   CTD; 6728; -.
DR   DisGeNET; 6728; -.
DR   GeneCards; SRP19; -.
DR   HGNC; HGNC:11300; SRP19.
DR   HPA; ENSG00000153037; Low tissue specificity.
DR   MIM; 182175; gene.
DR   neXtProt; NX_P09132; -.
DR   OpenTargets; ENSG00000153037; -.
DR   PharmGKB; PA36124; -.
DR   VEuPathDB; HostDB:ENSG00000153037; -.
DR   eggNOG; KOG3198; Eukaryota.
DR   GeneTree; ENSGT00390000004950; -.
DR   HOGENOM; CLU_2621387_0_0_1; -.
DR   InParanoid; P09132; -.
DR   OMA; CVENPTH; -.
DR   OrthoDB; 1552706at2759; -.
DR   PhylomeDB; P09132; -.
DR   TreeFam; TF106248; -.
DR   PathwayCommons; P09132; -.
DR   Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   SIGNOR; P09132; -.
DR   BioGRID-ORCS; 6728; 746 hits in 1023 CRISPR screens.
DR   ChiTaRS; SRP19; human.
DR   EvolutionaryTrace; P09132; -.
DR   GenomeRNAi; 6728; -.
DR   Pharos; P09132; Tbio.
DR   PRO; PR:P09132; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P09132; protein.
DR   Bgee; ENSG00000153037; Expressed in adenohypophysis and 113 other tissues.
DR   ExpressionAtlas; P09132; baseline and differential.
DR   Genevisible; P09132; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
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; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
DR   GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IBA:GO_Central.
DR   DisProt; DP00570; -.
DR   Gene3D; 3.30.56.30; -; 1.
DR   InterPro; IPR002778; Signal_recog_particle_SRP19.
DR   InterPro; IPR036521; SRP19-like_sf.
DR   PANTHER; PTHR17453; PTHR17453; 1.
DR   Pfam; PF01922; SRP19; 1.
DR   SUPFAM; SSF69695; SSF69695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..144
FT                   /note="Signal recognition particle 19 kDa protein"
FT                   /id="PRO_0000135197"
FT   REGION          117..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..144
FT                   /note="Basic region, potentially involved in RNA-binding"
FT   COMPBIAS        120..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         15..144
FT                   /note="FICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNK
FT                   MYSREWNRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGA
FT                   DQSLQQGEGSKKGKGKKKK -> LLKILQLQRFKMYVQQLDLTYFLRKIKCTLENGIVM
FT                   SNTEAESGSSSNRKMGASALYSSHHVSQ (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_044524"
FT   VAR_SEQ         101..144
FT                   /note="RKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK -> HYTL
FT                   SLTSGS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042540"
FT   VARIANT         4
FT                   /note="A -> T (in dbSNP:rs17855423)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027800"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   HELIX           46..55
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:4P3E"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:1MFQ"
FT   HELIX           101..111
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:1JID"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:1MFQ"
SQ   SEQUENCE   144 AA;  16156 MW;  E25F661972338CAE CRC64;
     MACAAARSPA DQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV
     FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ
     KTGGADQSLQ QGEGSKKGKG KKKK
//
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