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Signal recognition particle 14 kDa protein (SRP14) (18 kDa Alu RNA-binding protein)

 SRP14_HUMAN             Reviewed;         136 AA.
P37108; B5BUF5; Q6B0K5; Q96Q14;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
23-MAY-2018, entry version 178.
RecName: Full=Signal recognition particle 14 kDa protein;
Short=SRP14;
AltName: Full=18 kDa Alu RNA-binding protein;
Name=SRP14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-124.
PubMed=7542942; DOI=10.1091/mbc.6.4.471;
Bovia F., Fornallaz M., Leffers H., Strub K.;
"The SRP9/14 subunit of the signal recognition particle (SRP) is
present in more than 20-fold excess over SRP in primate cells and
exists primarily free but also in complex with small cytoplasmic Alu
RNAs.";
Mol. Biol. Cell 6:471-484(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8196634; DOI=10.1128/MCB.14.6.3949;
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.";
Mol. Cell. Biol. 14:3949-3959(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-124.
Wang H., Gao X., Huang Y., Han J.;
"A novel gene encoding signal recognition particle 14kD is upregulated
in the acute morphine dependent SH-SY5Y cells.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-124.
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-124.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-124.
TISSUE=Cervix, Prostate, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-15; 22-31; 79-88 AND 108-136, VARIANT ALA-124,
CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma, Colon adenocarcinoma, and Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Murray L.,
Brunton V.G., Frame M.C., Calvo F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-107 IN COMPLEX WITH SRP9,
AND SUBUNIT.
PubMed=11089964; DOI=10.1038/35041507;
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).
-!- FUNCTION: Signal-recognition-particle assembly has a crucial role
in targeting secretory proteins to the rough endoplasmic reticulum
membrane. SRP9 together with SRP14 and the Alu portion of the SRP
RNA, constitutes the elongation arrest domain of SRP. The complex
of SRP9 and SRP14 is required for SRP RNA binding.
-!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
SRP19, SRP14 and SRP9. {ECO:0000269|PubMed:11089964}.
-!- INTERACTION:
P49458-1:SRP9; NbExp=2; IntAct=EBI-353399, EBI-15490029;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the SRP14 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle
entry;
URL="https://en.wikipedia.org/wiki/Signal_recognition_particle";
-----------------------------------------------------------------------
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EMBL; X73459; CAA51838.1; -; mRNA.
EMBL; U07857; AAA59066.1; -; mRNA.
EMBL; AB061546; BAB69067.1; -; mRNA.
EMBL; AB451391; BAG70205.1; -; mRNA.
EMBL; AC025168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471125; EAW92390.1; -; Genomic_DNA.
EMBL; BC035495; AAH35495.1; -; mRNA.
EMBL; BC071716; AAH71716.1; -; mRNA.
EMBL; BC100031; AAI00032.1; -; mRNA.
CCDS; CCDS42017.1; -.
PIR; A56062; A56062.
PIR; S34196; S34196.
RefSeq; NP_003125.3; NM_003134.5.
UniGene; Hs.533732; -.
PDB; 1E8O; X-ray; 3.20 A; B/D=2-107.
PDB; 1E8S; X-ray; 4.00 A; B=2-107.
PDB; 1RY1; EM; 12.00 A; D=2-107.
PDB; 4UYJ; X-ray; 3.35 A; B/D=1-107.
PDB; 4UYK; X-ray; 3.22 A; B=1-107.
PDB; 5AOX; X-ray; 2.04 A; B/E=2-95.
PDBsum; 1E8O; -.
PDBsum; 1E8S; -.
PDBsum; 1RY1; -.
PDBsum; 4UYJ; -.
PDBsum; 4UYK; -.
PDBsum; 5AOX; -.
ProteinModelPortal; P37108; -.
SMR; P37108; -.
BioGrid; 112605; 79.
CORUM; P37108; -.
DIP; DIP-6152N; -.
IntAct; P37108; 23.
MINT; P37108; -.
STRING; 9606.ENSP00000267884; -.
TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
iPTMnet; P37108; -.
PhosphoSitePlus; P37108; -.
SwissPalm; P37108; -.
BioMuta; SRP14; -.
DMDM; 116242801; -.
SWISS-2DPAGE; P37108; -.
EPD; P37108; -.
MaxQB; P37108; -.
PaxDb; P37108; -.
PeptideAtlas; P37108; -.
PRIDE; P37108; -.
TopDownProteomics; P37108; -.
DNASU; 6727; -.
Ensembl; ENST00000267884; ENSP00000267884; ENSG00000140319.
GeneID; 6727; -.
KEGG; hsa:6727; -.
UCSC; uc001zkq.3; human.
CTD; 6727; -.
EuPathDB; HostDB:ENSG00000140319.10; -.
GeneCards; SRP14; -.
HGNC; HGNC:11299; SRP14.
HPA; HPA053738; -.
HPA; HPA065118; -.
MIM; 600708; gene.
neXtProt; NX_P37108; -.
OpenTargets; ENSG00000140319; -.
PharmGKB; PA36123; -.
eggNOG; KOG1761; Eukaryota.
eggNOG; ENOG4111PSF; LUCA.
GeneTree; ENSGT00390000008496; -.
HOGENOM; HOG000184883; -.
HOVERGEN; HBG057435; -.
InParanoid; P37108; -.
KO; K03104; -.
OMA; VWLTHKR; -.
OrthoDB; EOG091G1081; -.
PhylomeDB; P37108; -.
TreeFam; TF106247; -.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; SRP14; human.
EvolutionaryTrace; P37108; -.
GenomeRNAi; 6727; -.
PRO; PR:P37108; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140319; -.
CleanEx; HS_SRP14; -.
ExpressionAtlas; P37108; baseline and differential.
Genevisible; P37108; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
GO; GO:0008312; F:7S RNA binding; TAS:ProtInc.
GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
Gene3D; 3.30.720.10; -; 1.
InterPro; IPR003210; Signal_recog_particle_SRP14.
InterPro; IPR009018; Signal_recog_particle_SRP9/14.
PANTHER; PTHR12013; PTHR12013; 1.
Pfam; PF02290; SRP14; 1.
ProDom; PD009170; Signal_recog_particle_SRP14; 1.
SUPFAM; SSF54762; SSF54762; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein;
RNA-binding; Signal recognition particle.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
CHAIN 2 136 Signal recognition particle 14 kDa
protein.
/FTId=PRO_0000135189.
COMPBIAS 108 136 Ala/Thr-rich.
MOD_RES 27 27 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
VARIANT 51 51 P -> S (in dbSNP:rs1802601).
/FTId=VAR_028057.
VARIANT 68 68 S -> I (in dbSNP:rs1802600).
/FTId=VAR_028058.
VARIANT 124 124 P -> A (in dbSNP:rs7535).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19054851,
ECO:0000269|PubMed:7542942,
ECO:0000269|Ref.3, ECO:0000269|Ref.6,
ECO:0000269|Ref.8}.
/FTId=VAR_028059.
VARIANT 125 125 T -> A (in dbSNP:rs200831083).
/FTId=VAR_028060.
VARIANT 127 127 A -> T (in dbSNP:rs16924521).
/FTId=VAR_028061.
VARIANT 130 130 T -> A (in dbSNP:rs4814).
/FTId=VAR_028062.
CONFLICT 129 129 T -> A (in Ref. 3; BAB69067).
{ECO:0000305}.
STRAND 2 4 {ECO:0000244|PDB:4UYJ}.
HELIX 6 19 {ECO:0000244|PDB:5AOX}.
STRAND 21 23 {ECO:0000244|PDB:5AOX}.
STRAND 26 32 {ECO:0000244|PDB:5AOX}.
STRAND 53 72 {ECO:0000244|PDB:5AOX}.
TURN 73 75 {ECO:0000244|PDB:5AOX}.
HELIX 76 90 {ECO:0000244|PDB:5AOX}.
SEQUENCE 136 AA; 14570 MW; 2B5B2D1D62AF5E8E CRC64;
MVLLESEQFL TELTRLFQKC RTSGSVYITL KKYDGRTKPI PKKGTVEGFE PADNKCLLRA
TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKTKKTKAAA AAAAAAPAAA
ATAPTTAATT AATAAQ


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