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Protein

Protein LSM14 homolog A

Gene

Lsm14a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs.By similarity

GO - Molecular functioni

  • double-stranded DNA binding Source: MGI
  • double-stranded RNA binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • single-stranded RNA binding Source: MGI

GO - Biological processi

  • cytoplasmic mRNA processing body assembly Source: UniProtKB
  • defense response to virus Source: MGI
  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of type I interferon-mediated signaling pathway Source: MGI
  • regulation of translation Source: UniProtKB-KW
  • RIG-I signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor, Ribonucleoprotein

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein LSM14 homolog A
Alternative name(s):
Protein FAM61A
RNA-associated protein 55A
Short name:
mRAP55A
Gene namesi
Name:Lsm14a
Synonyms:Fam61a, Rap55a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914320. Lsm14a.

Subcellular locationi

  • Cytoplasm By similarity
  • CytoplasmP-body By similarity

  • Note: Targeted to stress granules (SGs) in response to cellular stress.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 462461Protein LSM14 homolog APRO_0000187091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei194 – 1941PhosphothreonineBy similarity
Modified residuei216 – 2161PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K2F8.
MaxQBiQ8K2F8.
PaxDbiQ8K2F8.
PRIDEiQ8K2F8.

PTM databases

iPTMnetiQ8K2F8.
PhosphoSiteiQ8K2F8.

Expressioni

Gene expression databases

BgeeiQ8K2F8.
CleanExiMM_LSM14A.
ExpressionAtlasiQ8K2F8. baseline and differential.
GenevisibleiQ8K2F8. MM.

Interactioni

Subunit structurei

Component of a ribonucleoprotein (RNP) complex.By similarity

Protein-protein interaction databases

BioGridi211917. 5 interactions.
IntActiQ8K2F8. 5 interactions.
STRINGi10090.ENSMUSP00000082723.

Structurei

3D structure databases

ProteinModelPortaliQ8K2F8.
SMRiQ8K2F8. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini283 – 31937DFDFPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 37617FFD boxAdd
BLAST
Motifi379 – 39921TFG boxAdd
BLAST

Domaini

The LSM14 domain and the RGG repeats are required for accumulation in P-bodies, and the region containing the FDF motif is responsible for cytoplasmic retention.By similarity

Sequence similaritiesi

Belongs to the LSM14 family.Curated
Contains 1 DFDF domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1073. Eukaryota.
ENOG41122RA. LUCA.
GeneTreeiENSGT00390000004174.
HOGENOMiHOG000231251.
HOVERGENiHBG054326.
InParanoidiQ8K2F8.
KOiK18749.
OMAiFGAVGVX.
OrthoDBiEOG72C519.
PhylomeDBiQ8K2F8.
TreeFamiTF313514.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025761. FFD_box.
IPR025609. Lsm14_N.
IPR010920. LSM_dom.
IPR025768. TFG_box.
[Graphical view]
PfamiPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
PROSITEiPS51512. DFDF. 1 hit.
PS51513. FFD. 1 hit.
PS51536. TFG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8K2F8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP
60 70 80 90 100
TDRPIPPRDE VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS
110 120 130 140 150
SSSSFQSVGS YGPFGRMPAY SQFSPSTLVG QQFGAVGVAG NSLTSFGTEA
160 170 180 190 200
SNSGTLSQSN AVGSAFTQDT RSVKPQLAQG RSSPQLDPLR KSPTMEQAVQ
210 220 230 240 250
TASAHLPAPA PVGRRSPVPA RPLPPTSQKA IDNQEHRRAE VHKVPRPENE
260 270 280 290 300
QLRNDKRQVV PGVPSAPRRG RGGHRGGRGR FGIRRDGPMK FEKDFDFESA
310 320 330 340 350
NAQFNKEEID REFHNKLKLK EDKLEKQEKP VNGEDKGDSG VDTQNSEGNA
360 370 380 390 400
DEEDPLGPNC YYDKTKSFFD NISCDDNRER RPTWAEERRL NAETFGIPLR
410 420 430 440 450
PNRGRGGYRG RGGLGFRGGR GRGSGRGGTF TAPRGFRAGF RGARGGREFA
460
DFEYRKTTAF GP
Length:462
Mass (Da):50,546
Last modified:October 1, 2002 - v1
Checksum:iB2554A73B96C473B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031521 mRNA. Translation: AAH31521.1.
AK003611 mRNA. Translation: BAB22889.1.
CCDSiCCDS21140.1.
RefSeqiNP_080224.1. NM_025948.2.
UniGeneiMm.276503.

Genome annotation databases

EnsembliENSMUST00000085585; ENSMUSP00000082723; ENSMUSG00000066568.
GeneIDi67070.
KEGGimmu:67070.
UCSCiuc009gjd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031521 mRNA. Translation: AAH31521.1.
AK003611 mRNA. Translation: BAB22889.1.
CCDSiCCDS21140.1.
RefSeqiNP_080224.1. NM_025948.2.
UniGeneiMm.276503.

3D structure databases

ProteinModelPortaliQ8K2F8.
SMRiQ8K2F8. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211917. 5 interactions.
IntActiQ8K2F8. 5 interactions.
STRINGi10090.ENSMUSP00000082723.

PTM databases

iPTMnetiQ8K2F8.
PhosphoSiteiQ8K2F8.

Proteomic databases

EPDiQ8K2F8.
MaxQBiQ8K2F8.
PaxDbiQ8K2F8.
PRIDEiQ8K2F8.

Protocols and materials databases

DNASUi67070.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085585; ENSMUSP00000082723; ENSMUSG00000066568.
GeneIDi67070.
KEGGimmu:67070.
UCSCiuc009gjd.1. mouse.

Organism-specific databases

CTDi26065.
MGIiMGI:1914320. Lsm14a.

Phylogenomic databases

eggNOGiKOG1073. Eukaryota.
ENOG41122RA. LUCA.
GeneTreeiENSGT00390000004174.
HOGENOMiHOG000231251.
HOVERGENiHBG054326.
InParanoidiQ8K2F8.
KOiK18749.
OMAiFGAVGVX.
OrthoDBiEOG72C519.
PhylomeDBiQ8K2F8.
TreeFamiTF313514.

Miscellaneous databases

PROiQ8K2F8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2F8.
CleanExiMM_LSM14A.
ExpressionAtlasiQ8K2F8. baseline and differential.
GenevisibleiQ8K2F8. MM.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025761. FFD_box.
IPR025609. Lsm14_N.
IPR010920. LSM_dom.
IPR025768. TFG_box.
[Graphical view]
PfamiPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
PROSITEiPS51512. DFDF. 1 hit.
PS51513. FFD. 1 hit.
PS51536. TFG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-462.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "RAP55: insights into an evolutionarily conserved protein family."
    Marnef A., Sommerville J., Ladomery M.R.
    Int. J. Biochem. Cell Biol. 41:977-981(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiLS14A_MOUSE
AccessioniPrimary (citable) accession number: Q8K2F8
Secondary accession number(s): Q9CTG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.