SRP14_HUMAN
ID SRP14_HUMAN Reviewed; 136 AA.
AC P37108; B5BUF5; Q6B0K5; Q96Q14;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Signal recognition particle 14 kDa protein;
DE Short=SRP14;
DE AltName: Full=18 kDa Alu RNA-binding protein;
GN Name=SRP14;
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], AND VARIANT ALA-124.
RX PubMed=7542942; DOI=10.1091/mbc.6.4.471;
RA Bovia F., Fornallaz M., Leffers H., Strub K.;
RT "The SRP9/14 subunit of the signal recognition particle (SRP) is present in
RT more than 20-fold excess over SRP in primate cells and exists primarily
RT free but also in complex with small cytoplasmic Alu RNAs.";
RL Mol. Biol. Cell 6:471-484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8196634; DOI=10.1128/mcb.14.6.3949-3959.1994;
RA Chang D.-Y., Nelson B., Bilyeu T., Hsu K., Darlington G.J., Maraia R.J.;
RT "A human Alu RNA-binding protein whose expression is associated with
RT accumulation of small cytoplasmic Alu RNA.";
RL Mol. Cell. Biol. 14:3949-3959(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-124.
RA Wang H., Gao X., Huang Y., Han J.;
RT "A novel gene encoding signal recognition particle 14kD is upregulated in
RT the acute morphine dependent SH-SY5Y cells.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-124.
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-124.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-124.
RC TISSUE=Cervix, Prostate, and Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-15; 22-31; 79-88 AND 108-136, VARIANT ALA-124,
RP CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon adenocarcinoma, and Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Murray L., Brunton V.G.,
RA Frame M.C., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [9]
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 [10]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, AND IDENTIFICATION BY
RP 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 [13]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP 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 [14]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-107 IN COMPLEX WITH SRP9,
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 [15] {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 (PubMed:11089964). 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 (PubMed:11089964). {ECO:0000269|PubMed:11089964}.
CC -!- SUBUNIT: Heterodimer with SRP9; binds RNA as heterodimer (By
CC similarity). Component of a signal recognition particle (SRP) complex
CC that 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:P16255, ECO:0000269|PubMed:11089964}.
CC -!- INTERACTION:
CC P37108; Q96JC9: EAF1; NbExp=3; IntAct=EBI-353399, EBI-769261;
CC P37108; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-353399, EBI-12023934;
CC P37108; P49458: SRP9; NbExp=8; IntAct=EBI-353399, EBI-350743;
CC P37108; P49458-1: SRP9; NbExp=2; IntAct=EBI-353399, EBI-15490029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SRP14 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; X73459; CAA51838.1; -; mRNA.
DR EMBL; U07857; AAA59066.1; -; mRNA.
DR EMBL; AB061546; BAB69067.1; -; mRNA.
DR EMBL; AB451391; BAG70205.1; -; mRNA.
DR EMBL; AC025168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92390.1; -; Genomic_DNA.
DR EMBL; BC035495; AAH35495.1; -; mRNA.
DR EMBL; BC071716; AAH71716.1; -; mRNA.
DR EMBL; BC100031; AAI00032.1; -; mRNA.
DR CCDS; CCDS42017.1; -.
DR PIR; A56062; A56062.
DR PIR; S34196; S34196.
DR RefSeq; NP_003125.3; NM_003134.5.
DR PDB; 1E8O; X-ray; 3.20 A; B/D=2-107.
DR PDB; 1E8S; X-ray; 4.00 A; B=2-107.
DR PDB; 1RY1; EM; 12.00 A; D=2-107.
DR PDB; 4UYJ; X-ray; 3.35 A; B/D=1-107.
DR PDB; 4UYK; X-ray; 3.22 A; B=1-107.
DR PDB; 5AOX; X-ray; 2.04 A; B/E=2-95.
DR PDB; 7NFX; EM; 3.20 A; t=1-136.
DR PDBsum; 1E8O; -.
DR PDBsum; 1E8S; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 4UYJ; -.
DR PDBsum; 4UYK; -.
DR PDBsum; 5AOX; -.
DR PDBsum; 7NFX; -.
DR AlphaFoldDB; P37108; -.
DR SMR; P37108; -.
DR BioGRID; 112605; 302.
DR CORUM; P37108; -.
DR DIP; DIP-6152N; -.
DR IntAct; P37108; 45.
DR MINT; P37108; -.
DR STRING; 9606.ENSP00000267884; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; P37108; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P37108; -.
DR MetOSite; P37108; -.
DR PhosphoSitePlus; P37108; -.
DR SwissPalm; P37108; -.
DR BioMuta; SRP14; -.
DR DMDM; 116242801; -.
DR SWISS-2DPAGE; P37108; -.
DR EPD; P37108; -.
DR jPOST; P37108; -.
DR MassIVE; P37108; -.
DR MaxQB; P37108; -.
DR PaxDb; P37108; -.
DR PeptideAtlas; P37108; -.
DR PRIDE; P37108; -.
DR ProteomicsDB; 55263; -.
DR TopDownProteomics; P37108; -.
DR Antibodypedia; 5798; 157 antibodies from 26 providers.
DR DNASU; 6727; -.
DR Ensembl; ENST00000267884.11; ENSP00000267884.6; ENSG00000140319.11.
DR GeneID; 6727; -.
DR KEGG; hsa:6727; -.
DR MANE-Select; ENST00000267884.11; ENSP00000267884.6; NM_003134.6; NP_003125.3.
DR UCSC; uc001zkq.3; human.
DR CTD; 6727; -.
DR GeneCards; SRP14; -.
DR HGNC; HGNC:11299; SRP14.
DR HPA; ENSG00000140319; Low tissue specificity.
DR MIM; 600708; gene.
DR neXtProt; NX_P37108; -.
DR OpenTargets; ENSG00000140319; -.
DR PharmGKB; PA36123; -.
DR VEuPathDB; HostDB:ENSG00000140319; -.
DR eggNOG; KOG1761; Eukaryota.
DR GeneTree; ENSGT00390000008496; -.
DR HOGENOM; CLU_094309_2_1_1; -.
DR InParanoid; P37108; -.
DR OMA; RFNGHNK; -.
DR OrthoDB; 1634105at2759; -.
DR PhylomeDB; P37108; -.
DR TreeFam; TF106247; -.
DR PathwayCommons; P37108; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P37108; -.
DR BioGRID-ORCS; 6727; 533 hits in 1081 CRISPR screens.
DR ChiTaRS; SRP14; human.
DR EvolutionaryTrace; P37108; -.
DR GenomeRNAi; 6727; -.
DR Pharos; P37108; Tbio.
DR PRO; PR:P37108; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P37108; protein.
DR Bgee; ENSG00000140319; Expressed in renal medulla and 215 other tissues.
DR ExpressionAtlas; P37108; baseline and differential.
DR Genevisible; P37108; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
DR GO; GO:0008312; F:7S RNA binding; TAS:ProtInc.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
DR GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 3.30.720.10; -; 1.
DR InterPro; IPR003210; Signal_recog_particle_SRP14.
DR InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR PANTHER; PTHR12013; PTHR12013; 1.
DR Pfam; PF02290; SRP14; 1.
DR SUPFAM; SSF54762; SSF54762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..136
FT /note="Signal recognition particle 14 kDa protein"
FT /id="PRO_0000135189"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 51
FT /note="P -> S (in dbSNP:rs1802601)"
FT /id="VAR_028057"
FT VARIANT 68
FT /note="S -> I (in dbSNP:rs1802600)"
FT /id="VAR_028058"
FT VARIANT 124
FT /note="P -> A (in dbSNP:rs7535)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:19054851, ECO:0000269|PubMed:7542942,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT /id="VAR_028059"
FT VARIANT 125
FT /note="T -> A (in dbSNP:rs200831083)"
FT /id="VAR_028060"
FT VARIANT 127
FT /note="A -> T (in dbSNP:rs16924521)"
FT /id="VAR_028061"
FT VARIANT 130
FT /note="T -> A (in dbSNP:rs4814)"
FT /id="VAR_028062"
FT CONFLICT 129
FT /note="T -> A (in Ref. 3; BAB69067)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:4UYJ"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5AOX"
FT STRAND 53..72
FT /evidence="ECO:0007829|PDB:5AOX"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5AOX"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:5AOX"
SQ SEQUENCE 136 AA; 14570 MW; 2B5B2D1D62AF5E8E CRC64;
MVLLESEQFL TELTRLFQKC RTSGSVYITL KKYDGRTKPI PKKGTVEGFE PADNKCLLRA
TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKTKKTKAAA AAAAAAPAAA
ATAPTTAATT AATAAQ
