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Protein

Signal recognition particle 14 kDa protein

Gene

SRP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • 7S RNA binding Source: ProtInc
  • endoplasmic reticulum signal peptide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • cotranslational protein targeting to membrane Source: ProtInc
  • gene expression Source: Reactome
  • protein targeting to ER Source: UniProtKB
  • response to drug Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.

Protein family/group databases

TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle 14 kDa protein
Short name:
SRP14
Alternative name(s):
18 kDa Alu RNA-binding protein
Gene namesi
Name:SRP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11299. SRP14.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
  • signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36123.

Polymorphism and mutation databases

BioMutaiSRP14.
DMDMi116242801.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 136135Signal recognition particle 14 kDa proteinPRO_0000135189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP37108.
MaxQBiP37108.
PaxDbiP37108.
PeptideAtlasiP37108.
PRIDEiP37108.
TopDownProteomicsiP37108.

2D gel databases

SWISS-2DPAGEP37108.

PTM databases

iPTMnetiP37108.
PhosphoSiteiP37108.

Expressioni

Gene expression databases

BgeeiP37108.
CleanExiHS_SRP14.
ExpressionAtlasiP37108. baseline and differential.
GenevisibleiP37108. HS.

Interactioni

Subunit structurei

Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9.1 Publication

Protein-protein interaction databases

BioGridi112605. 71 interactions.
DIPiDIP-6152N.
IntActiP37108. 16 interactions.
MINTiMINT-1413971.
STRINGi9606.ENSP00000267884.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi6 – 1914Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 327Combined sources
Beta strandi53 – 7220Combined sources
Turni73 – 753Combined sources
Helixi76 – 9015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8OX-ray3.20B/D2-107[»]
1E8SX-ray4.00B2-107[»]
1RY1electron microscopy12.00D2-107[»]
4UYJX-ray3.35B/D1-107[»]
4UYKX-ray3.22B1-107[»]
5AOXX-ray2.04B/E2-95[»]
ProteinModelPortaliP37108.
SMRiP37108. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37108.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 13629Ala/Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the SRP14 family.Curated

Phylogenomic databases

eggNOGiKOG1761. Eukaryota.
ENOG4111PSF. LUCA.
GeneTreeiENSGT00390000008496.
HOGENOMiHOG000184883.
HOVERGENiHBG057435.
InParanoidiP37108.
OMAiEEIEYRC.
OrthoDBiEOG7BP854.
PhylomeDBiP37108.
TreeFamiTF106247.

Family and domain databases

Gene3Di3.30.720.10. 1 hit.
InterProiIPR003210. Signal_recog_particle_SRP14.
IPR009018. Signal_recog_particle_SRP9/14.
[Graphical view]
PfamiPF02290. SRP14. 1 hit.
[Graphical view]
ProDomiPD009170. Signal_recog_particle_SRP14. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54762. SSF54762. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLESEQFL TELTRLFQKC RTSGSVYITL KKYDGRTKPI PKKGTVEGFE
60 70 80 90 100
PADNKCLLRA TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK
110 120 130
NKTKKTKAAA AAAAAAPAAA ATAPTTAATT AATAAQ
Length:136
Mass (Da):14,570
Last modified:October 17, 2006 - v2
Checksum:i2B5B2D1D62AF5E8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291T → A in BAB69067 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511P → S.
Corresponds to variant rs1802601 [ dbSNP | Ensembl ].
VAR_028057
Natural varianti68 – 681S → I.
Corresponds to variant rs1802600 [ dbSNP | Ensembl ].
VAR_028058
Natural varianti124 – 1241P → A.6 Publications
Corresponds to variant rs7535 [ dbSNP | Ensembl ].
VAR_028059
Natural varianti125 – 1251T → A.
Corresponds to variant rs200831083 [ dbSNP | Ensembl ].
VAR_028060
Natural varianti127 – 1271A → T.
Corresponds to variant rs16924521 [ dbSNP | Ensembl ].
VAR_028061
Natural varianti130 – 1301T → A.
Corresponds to variant rs4814 [ dbSNP | Ensembl ].
VAR_028062

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73459 mRNA. Translation: CAA51838.1.
U07857 mRNA. Translation: AAA59066.1.
AB061546 mRNA. Translation: BAB69067.1.
AB451391 mRNA. Translation: BAG70205.1.
AC025168 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92390.1.
BC035495 mRNA. Translation: AAH35495.1.
BC071716 mRNA. Translation: AAH71716.1.
BC100031 mRNA. Translation: AAI00032.1.
CCDSiCCDS42017.1.
PIRiA56062.
S34196.
RefSeqiNP_003125.3. NM_003134.5.
UniGeneiHs.533732.

Genome annotation databases

EnsembliENST00000267884; ENSP00000267884; ENSG00000140319.
GeneIDi6727.
UCSCiuc001zkq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Signal recognition particle entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73459 mRNA. Translation: CAA51838.1.
U07857 mRNA. Translation: AAA59066.1.
AB061546 mRNA. Translation: BAB69067.1.
AB451391 mRNA. Translation: BAG70205.1.
AC025168 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92390.1.
BC035495 mRNA. Translation: AAH35495.1.
BC071716 mRNA. Translation: AAH71716.1.
BC100031 mRNA. Translation: AAI00032.1.
CCDSiCCDS42017.1.
PIRiA56062.
S34196.
RefSeqiNP_003125.3. NM_003134.5.
UniGeneiHs.533732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8OX-ray3.20B/D2-107[»]
1E8SX-ray4.00B2-107[»]
1RY1electron microscopy12.00D2-107[»]
4UYJX-ray3.35B/D1-107[»]
4UYKX-ray3.22B1-107[»]
5AOXX-ray2.04B/E2-95[»]
ProteinModelPortaliP37108.
SMRiP37108. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112605. 71 interactions.
DIPiDIP-6152N.
IntActiP37108. 16 interactions.
MINTiMINT-1413971.
STRINGi9606.ENSP00000267884.

Protein family/group databases

TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

iPTMnetiP37108.
PhosphoSiteiP37108.

Polymorphism and mutation databases

BioMutaiSRP14.
DMDMi116242801.

2D gel databases

SWISS-2DPAGEP37108.

Proteomic databases

EPDiP37108.
MaxQBiP37108.
PaxDbiP37108.
PeptideAtlasiP37108.
PRIDEiP37108.
TopDownProteomicsiP37108.

Protocols and materials databases

DNASUi6727.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267884; ENSP00000267884; ENSG00000140319.
GeneIDi6727.
UCSCiuc001zkq.3. human.

Organism-specific databases

CTDi6727.
GeneCardsiSRP14.
HGNCiHGNC:11299. SRP14.
MIMi600708. gene.
neXtProtiNX_P37108.
PharmGKBiPA36123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1761. Eukaryota.
ENOG4111PSF. LUCA.
GeneTreeiENSGT00390000008496.
HOGENOMiHOG000184883.
HOVERGENiHBG057435.
InParanoidiP37108.
OMAiEEIEYRC.
OrthoDBiEOG7BP854.
PhylomeDBiP37108.
TreeFamiTF106247.

Enzyme and pathway databases

ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiSRP14. human.
EvolutionaryTraceiP37108.
GenomeRNAii6727.
NextBioi26240.
PROiP37108.
SOURCEiSearch...

Gene expression databases

BgeeiP37108.
CleanExiHS_SRP14.
ExpressionAtlasiP37108. baseline and differential.
GenevisibleiP37108. HS.

Family and domain databases

Gene3Di3.30.720.10. 1 hit.
InterProiIPR003210. Signal_recog_particle_SRP14.
IPR009018. Signal_recog_particle_SRP9/14.
[Graphical view]
PfamiPF02290. SRP14. 1 hit.
[Graphical view]
ProDomiPD009170. Signal_recog_particle_SRP14. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54762. SSF54762. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Bovia F., Fornallaz M., Leffers H., Strub K.
    Mol. Biol. Cell 6:471-484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-124.
  2. "A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNA."
    Chang D.-Y., Nelson B., Bilyeu T., Hsu K., Darlington G.J., Maraia R.J.
    Mol. Cell. Biol. 14:3949-3959(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A novel gene encoding signal recognition particle 14kD is upregulated in the acute morphine dependent SH-SY5Y cells."
    Wang H., Gao X., Huang Y., Han J.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-124.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    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.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-124.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    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.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-124.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-124.
    Tissue: Cervix, Prostate and Uterus.
  8. Cited for: PROTEIN SEQUENCE OF 2-15; 22-31; 79-88 AND 108-136, VARIANT ALA-124, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Colon adenocarcinoma and Hepatoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure and assembly of the Alu domain of the mammalian signal recognition particle."
    Weichenrieder O., Wild K., Strub K., Cusack S.
    Nature 408:167-173(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-107 IN COMPLEX WITH SRP9, SUBUNIT.

Entry informationi

Entry nameiSRP14_HUMAN
AccessioniPrimary (citable) accession number: P37108
Secondary accession number(s): B5BUF5, Q6B0K5, Q96Q14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: May 11, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.