Full text data of SRP14
SRP14
[Confidence: low (only semi-automatic identification from reviews)]
Signal recognition particle 14 kDa protein; SRP14 (18 kDa Alu RNA-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Signal recognition particle 14 kDa protein; SRP14 (18 kDa Alu RNA-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P37108
ID SRP14_HUMAN Reviewed; 136 AA.
AC P37108; B5BUF5; Q6B0K5; Q96Q14;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT present in more than 20-fold excess over SRP in primate cells and
RT exists primarily free but also in complex with small cytoplasmic Alu
RT RNAs.";
RL Mol. Biol. Cell 6:471-484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8196634;
RA Chang D.-Y., Nelson B., Bilyeu T., Hsu K., Darlington G.J.,
RA 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
RT in 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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon adenocarcinoma, and Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Murray L.,
RA Brunton V.G., 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.,
RA Buerckstuemmer T., 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 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-107 IN COMPLEX WITH SRP9,
RP 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).
CC -!- FUNCTION: Signal-recognition-particle assembly has a crucial role
CC in targeting secretory proteins to the rough endoplasmic reticulum
CC membrane. SRP9 together with SRP14 and the Alu portion of the SRP
CC RNA, constitutes the elongation arrest domain of SRP. The complex
CC of SRP9 and SRP14 is required for SRP RNA binding.
CC -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC SRP19, SRP14 and SRP9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SRP14 family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle
CC entry;
CC URL="http://en.wikipedia.org/wiki/Signal_recognition_particle";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A56062; A56062.
DR PIR; S34196; S34196.
DR RefSeq; NP_003125.3; NM_003134.4.
DR UniGene; Hs.533732; -.
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 PDBsum; 1E8O; -.
DR PDBsum; 1E8S; -.
DR PDBsum; 1RY1; -.
DR ProteinModelPortal; P37108; -.
DR SMR; P37108; 2-95.
DR DIP; DIP-6152N; -.
DR IntAct; P37108; 8.
DR MINT; MINT-1413971; -.
DR STRING; 9606.ENSP00000267884; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P37108; -.
DR DMDM; 116242801; -.
DR SWISS-2DPAGE; P37108; -.
DR PaxDb; P37108; -.
DR PeptideAtlas; P37108; -.
DR PRIDE; P37108; -.
DR DNASU; 6727; -.
DR Ensembl; ENST00000267884; ENSP00000267884; ENSG00000140319.
DR GeneID; 6727; -.
DR KEGG; hsa:6727; -.
DR UCSC; uc001zkq.2; human.
DR CTD; 6727; -.
DR GeneCards; GC15M040327; -.
DR HGNC; HGNC:11299; SRP14.
DR MIM; 600708; gene.
DR neXtProt; NX_P37108; -.
DR PharmGKB; PA36123; -.
DR eggNOG; NOG237715; -.
DR HOGENOM; HOG000184883; -.
DR HOVERGEN; HBG057435; -.
DR InParanoid; P37108; -.
DR KO; K03104; -.
DR OMA; IKFQMAY; -.
DR OrthoDB; EOG7BP854; -.
DR PhylomeDB; P37108; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SRP14; human.
DR EvolutionaryTrace; P37108; -.
DR GenomeRNAi; 6727; -.
DR NextBio; 26240; -.
DR PRO; PR:P37108; -.
DR ArrayExpress; P37108; -.
DR Bgee; P37108; -.
DR CleanEx; HS_SRP14; -.
DR Genevestigator; P37108; -.
DR GO; GO:0005829; C:cytosol; 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:0042493; P:response to drug; IDA:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
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 ProDom; PD009170; Signal_recog_particle_SRP14; 1.
DR SUPFAM; SSF54762; SSF54762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Polymorphism; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 136 Signal recognition particle 14 kDa
FT protein.
FT /FTId=PRO_0000135189.
FT COMPBIAS 108 136 Ala/Thr-rich.
FT VARIANT 51 51 P -> S (in dbSNP:rs1802601).
FT /FTId=VAR_028057.
FT VARIANT 68 68 S -> I (in dbSNP:rs1802600).
FT /FTId=VAR_028058.
FT VARIANT 124 124 P -> A (in dbSNP:rs7535).
FT /FTId=VAR_028059.
FT VARIANT 125 125 T -> A (in dbSNP:rs16924476).
FT /FTId=VAR_028060.
FT VARIANT 127 127 A -> T (in dbSNP:rs16924521).
FT /FTId=VAR_028061.
FT VARIANT 130 130 T -> A (in dbSNP:rs4814).
FT /FTId=VAR_028062.
FT CONFLICT 129 129 T -> A (in Ref. 3; BAB69067).
FT HELIX 6 20
FT TURN 21 23
FT STRAND 26 33
FT STRAND 55 72
FT TURN 73 75
FT HELIX 76 90
SQ SEQUENCE 136 AA; 14570 MW; 2B5B2D1D62AF5E8E CRC64;
MVLLESEQFL TELTRLFQKC RTSGSVYITL KKYDGRTKPI PKKGTVEGFE PADNKCLLRA
TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKTKKTKAAA AAAAAAPAAA
ATAPTTAATT AATAAQ
//
ID SRP14_HUMAN Reviewed; 136 AA.
AC P37108; B5BUF5; Q6B0K5; Q96Q14;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT present in more than 20-fold excess over SRP in primate cells and
RT exists primarily free but also in complex with small cytoplasmic Alu
RT RNAs.";
RL Mol. Biol. Cell 6:471-484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8196634;
RA Chang D.-Y., Nelson B., Bilyeu T., Hsu K., Darlington G.J.,
RA 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
RT in 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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon adenocarcinoma, and Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Murray L.,
RA Brunton V.G., 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.,
RA Buerckstuemmer T., 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 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-107 IN COMPLEX WITH SRP9,
RP 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).
CC -!- FUNCTION: Signal-recognition-particle assembly has a crucial role
CC in targeting secretory proteins to the rough endoplasmic reticulum
CC membrane. SRP9 together with SRP14 and the Alu portion of the SRP
CC RNA, constitutes the elongation arrest domain of SRP. The complex
CC of SRP9 and SRP14 is required for SRP RNA binding.
CC -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC SRP19, SRP14 and SRP9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SRP14 family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle
CC entry;
CC URL="http://en.wikipedia.org/wiki/Signal_recognition_particle";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A56062; A56062.
DR PIR; S34196; S34196.
DR RefSeq; NP_003125.3; NM_003134.4.
DR UniGene; Hs.533732; -.
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 PDBsum; 1E8O; -.
DR PDBsum; 1E8S; -.
DR PDBsum; 1RY1; -.
DR ProteinModelPortal; P37108; -.
DR SMR; P37108; 2-95.
DR DIP; DIP-6152N; -.
DR IntAct; P37108; 8.
DR MINT; MINT-1413971; -.
DR STRING; 9606.ENSP00000267884; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P37108; -.
DR DMDM; 116242801; -.
DR SWISS-2DPAGE; P37108; -.
DR PaxDb; P37108; -.
DR PeptideAtlas; P37108; -.
DR PRIDE; P37108; -.
DR DNASU; 6727; -.
DR Ensembl; ENST00000267884; ENSP00000267884; ENSG00000140319.
DR GeneID; 6727; -.
DR KEGG; hsa:6727; -.
DR UCSC; uc001zkq.2; human.
DR CTD; 6727; -.
DR GeneCards; GC15M040327; -.
DR HGNC; HGNC:11299; SRP14.
DR MIM; 600708; gene.
DR neXtProt; NX_P37108; -.
DR PharmGKB; PA36123; -.
DR eggNOG; NOG237715; -.
DR HOGENOM; HOG000184883; -.
DR HOVERGEN; HBG057435; -.
DR InParanoid; P37108; -.
DR KO; K03104; -.
DR OMA; IKFQMAY; -.
DR OrthoDB; EOG7BP854; -.
DR PhylomeDB; P37108; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SRP14; human.
DR EvolutionaryTrace; P37108; -.
DR GenomeRNAi; 6727; -.
DR NextBio; 26240; -.
DR PRO; PR:P37108; -.
DR ArrayExpress; P37108; -.
DR Bgee; P37108; -.
DR CleanEx; HS_SRP14; -.
DR Genevestigator; P37108; -.
DR GO; GO:0005829; C:cytosol; 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:0042493; P:response to drug; IDA:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
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 ProDom; PD009170; Signal_recog_particle_SRP14; 1.
DR SUPFAM; SSF54762; SSF54762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Polymorphism; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 136 Signal recognition particle 14 kDa
FT protein.
FT /FTId=PRO_0000135189.
FT COMPBIAS 108 136 Ala/Thr-rich.
FT VARIANT 51 51 P -> S (in dbSNP:rs1802601).
FT /FTId=VAR_028057.
FT VARIANT 68 68 S -> I (in dbSNP:rs1802600).
FT /FTId=VAR_028058.
FT VARIANT 124 124 P -> A (in dbSNP:rs7535).
FT /FTId=VAR_028059.
FT VARIANT 125 125 T -> A (in dbSNP:rs16924476).
FT /FTId=VAR_028060.
FT VARIANT 127 127 A -> T (in dbSNP:rs16924521).
FT /FTId=VAR_028061.
FT VARIANT 130 130 T -> A (in dbSNP:rs4814).
FT /FTId=VAR_028062.
FT CONFLICT 129 129 T -> A (in Ref. 3; BAB69067).
FT HELIX 6 20
FT TURN 21 23
FT STRAND 26 33
FT STRAND 55 72
FT TURN 73 75
FT HELIX 76 90
SQ SEQUENCE 136 AA; 14570 MW; 2B5B2D1D62AF5E8E CRC64;
MVLLESEQFL TELTRLFQKC RTSGSVYITL KKYDGRTKPI PKKGTVEGFE PADNKCLLRA
TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKTKKTKAAA AAAAAAPAAA
ATAPTTAATT AATAAQ
//
MIM
600708
*RECORD*
*FIELD* NO
600708
*FIELD* TI
*600708 SIGNAL RECOGNITION PARTICLE, 14-KD; SRP14
;;Alu RNA-BINDING PROTEIN, 14-KD SUBUNIT; ALURBP
read more*FIELD* TX
The signal recognition particle (SRP) is a ribonucleoprotein complex
that mediates the targeting of proteins to the endoplasmic reticulum
(ER). The complex consists of a 7S (or 7SL) RNA and 6 different
proteins, SRP9 (600707), SRP14, SRP19 (182175), SRP54 (604857), SRP68
(604858), and SRP72 (602122). The proteins are bound to the 7S RNA as
monomers (SRP19 and SRP54) or heterodimers (SRP9/SRP14 and SRP68/SRP72).
SRP9 and SRP14 constitute the Alu domain of 7S, whereas the other 4
proteins belong to the S domain. SRP has at least 3 distinct functions
that can be associated with the protein subunits: signal recognition,
translational arrest, and ER membrane targeting by interaction with the
docking protein.
Together with SRP9, SRP14 forms a complex that recognizes Alu RNA and
the related 7SL RNA. Chang et al. (1994) cloned the SRP14 cDNA by PCR
with primers based on partial protein sequences obtained from tryptic
peptides and the previously identified mouse nucleotide sequence. The
predicted amino acid sequence was found to be approximately 90% similar
to the mouse homolog. The human sequence is longer at the C terminus and
the predicted protein is 18 kD rather than 14 kD.
For information on a signal recognition particle database, see Larsen et
al. (1998).
Weichenrieder et al. (2000) reported 2 crystal structures of the
heterodimer SRP9/14 bound either to the 5-prime domain or to a construct
containing both 5-prime and 3-prime domains of the SRP RNA.
By somatic cell hybrid analysis, Chang et al. (1994) mapped the SRP14
gene to human chromosome 15q22.
Halic et al. (2004) presented the structure of a targeting complex
consisting of mammalian SRP bound to an active 80S ribosome carrying a
signal sequence. This structure, determined to 12-angstrom resolution by
cryoelectron microscopy, enabled Halic et al. (2004) to generate a
molecular model of SRP in its functional conformation. The model showed
how the S domain of SRP contacts the large ribosomal subunit at the
nascent chain exit site to bind the signal sequence, and that the Alu
domain reaches into the elongation factor-binding site of the ribosome,
explaining its elongation arrest activity.
*FIELD* RF
1. Chang, D. Y.; Nelson, B.; Bilyeu, T.; Hsu, K.; Darlington, G. J.;
Maraia, R. J.: A human Alu RNA-binding protein whose expression is
associated with accumulation of small cytoplasmic Alu RNA. Molec.
Cell. Biol. 14: 3949-3959, 1994.
2. Halic, M.; Becker, T.; Pool, M. R.; Spahn, C. M. T.; Grassucci,
R. A.; Frank, J.; Beckmann, R.: Structure of the signal recognition
particle interacting with the elongation-arrested ribosome. Nature 427:
808-814, 2004.
3. Larsen, N.; Samuelsson, T.; Swieb, C.: The Signal Recognition
Particle Database (SRPDB). Nucleic Acids Res. 26: 177-178, 1998.
4. Weichenrieder, O.; Wild, K.; Strub, K.; Cusack, S.: Structure
and assembly of the Alu domain of the mammalian signal recognition
particle. Nature 408: 167-173, 2000.
*FIELD* CN
Ada Hamosh - updated: 3/8/2004
Ada Hamosh - updated: 11/8/2000
Paul J. Converse - updated: 4/20/2000
*FIELD* CD
Alan F. Scott: 8/2/1995
*FIELD* ED
tkritzer: 03/09/2004
terry: 3/8/2004
alopez: 11/8/2000
carol: 4/21/2000
carol: 4/20/2000
alopez: 3/9/1999
dkim: 7/30/1998
terry: 6/3/1998
mark: 4/13/1996
mark: 8/2/1995
*RECORD*
*FIELD* NO
600708
*FIELD* TI
*600708 SIGNAL RECOGNITION PARTICLE, 14-KD; SRP14
;;Alu RNA-BINDING PROTEIN, 14-KD SUBUNIT; ALURBP
read more*FIELD* TX
The signal recognition particle (SRP) is a ribonucleoprotein complex
that mediates the targeting of proteins to the endoplasmic reticulum
(ER). The complex consists of a 7S (or 7SL) RNA and 6 different
proteins, SRP9 (600707), SRP14, SRP19 (182175), SRP54 (604857), SRP68
(604858), and SRP72 (602122). The proteins are bound to the 7S RNA as
monomers (SRP19 and SRP54) or heterodimers (SRP9/SRP14 and SRP68/SRP72).
SRP9 and SRP14 constitute the Alu domain of 7S, whereas the other 4
proteins belong to the S domain. SRP has at least 3 distinct functions
that can be associated with the protein subunits: signal recognition,
translational arrest, and ER membrane targeting by interaction with the
docking protein.
Together with SRP9, SRP14 forms a complex that recognizes Alu RNA and
the related 7SL RNA. Chang et al. (1994) cloned the SRP14 cDNA by PCR
with primers based on partial protein sequences obtained from tryptic
peptides and the previously identified mouse nucleotide sequence. The
predicted amino acid sequence was found to be approximately 90% similar
to the mouse homolog. The human sequence is longer at the C terminus and
the predicted protein is 18 kD rather than 14 kD.
For information on a signal recognition particle database, see Larsen et
al. (1998).
Weichenrieder et al. (2000) reported 2 crystal structures of the
heterodimer SRP9/14 bound either to the 5-prime domain or to a construct
containing both 5-prime and 3-prime domains of the SRP RNA.
By somatic cell hybrid analysis, Chang et al. (1994) mapped the SRP14
gene to human chromosome 15q22.
Halic et al. (2004) presented the structure of a targeting complex
consisting of mammalian SRP bound to an active 80S ribosome carrying a
signal sequence. This structure, determined to 12-angstrom resolution by
cryoelectron microscopy, enabled Halic et al. (2004) to generate a
molecular model of SRP in its functional conformation. The model showed
how the S domain of SRP contacts the large ribosomal subunit at the
nascent chain exit site to bind the signal sequence, and that the Alu
domain reaches into the elongation factor-binding site of the ribosome,
explaining its elongation arrest activity.
*FIELD* RF
1. Chang, D. Y.; Nelson, B.; Bilyeu, T.; Hsu, K.; Darlington, G. J.;
Maraia, R. J.: A human Alu RNA-binding protein whose expression is
associated with accumulation of small cytoplasmic Alu RNA. Molec.
Cell. Biol. 14: 3949-3959, 1994.
2. Halic, M.; Becker, T.; Pool, M. R.; Spahn, C. M. T.; Grassucci,
R. A.; Frank, J.; Beckmann, R.: Structure of the signal recognition
particle interacting with the elongation-arrested ribosome. Nature 427:
808-814, 2004.
3. Larsen, N.; Samuelsson, T.; Swieb, C.: The Signal Recognition
Particle Database (SRPDB). Nucleic Acids Res. 26: 177-178, 1998.
4. Weichenrieder, O.; Wild, K.; Strub, K.; Cusack, S.: Structure
and assembly of the Alu domain of the mammalian signal recognition
particle. Nature 408: 167-173, 2000.
*FIELD* CN
Ada Hamosh - updated: 3/8/2004
Ada Hamosh - updated: 11/8/2000
Paul J. Converse - updated: 4/20/2000
*FIELD* CD
Alan F. Scott: 8/2/1995
*FIELD* ED
tkritzer: 03/09/2004
terry: 3/8/2004
alopez: 11/8/2000
carol: 4/21/2000
carol: 4/20/2000
alopez: 3/9/1999
dkim: 7/30/1998
terry: 6/3/1998
mark: 4/13/1996
mark: 8/2/1995