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Protein

ELAV-like protein 1

Gene

Elavl1

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

Functioni

RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro. With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA.2 Publications

GO - Molecular functioni

GO - Biological processi

  • 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  • mRNA stabilization Source: UniProtKB
  • positive regulation of translation Source: MGI
  • regulation of stem cell maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_274491. HuR stabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
ELAV-like protein 1
Alternative name(s):
Elav-like generic protein
Hu-antigen R
Short name:
HuR
MelG
Gene namesi
Name:Elavl1
Synonyms:Elra, Hua
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1100851. Elavl1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Translocates into the cytoplasm following phosphorylation by MAPKAPK2.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 326325ELAV-like protein 1PRO_0000081578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei202 – 2021PhosphoserineBy similarity
Modified residuei217 – 2171Omega-N-methylated arginine; by CARM11 Publication

Post-translational modificationi

Phosphorylated by MAPKAPK2.By similarity
Methylated at Arg-217 by CARM1 in T-cells in response to LPS challenge.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP70372.
PaxDbiP70372.
PRIDEiP70372.

PTM databases

PhosphoSiteiP70372.

Expressioni

Gene expression databases

BgeeiP70372.
ExpressionAtlasiP70372. baseline and differential.
GenevestigatoriP70372.

Interactioni

Subunit structurei

Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with ANP32A (By similarity). Interact with ZNF385A; the interaction is indirect and mRNA-dependent and may regulate p53/TP53 expression. Interacts with IGF2BP2 and IGF2BP3 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Grb7Q031607EBI-6877056,EBI-7100053
Tia1Q80ZW72EBI-6877056,EBI-7809240

Protein-protein interaction databases

BioGridi200482. 4 interactions.
DIPiDIP-46480N.
IntActiP70372. 7 interactions.
MINTiMINT-4094207.
STRINGi10090.ENSMUSP00000096549.

Structurei

3D structure databases

ProteinModelPortaliP70372.
SMRiP70372. Positions 18-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini106 – 18681RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 32279RRM 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RRM elav family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiP70372.
KOiK13088.
OMAiRFGGPLH.
OrthoDBiEOG77T14R.
TreeFamiTF313377.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNGYEDHMA EDCRDDIGRT NLIVNYLPQN MTQEELRSLF SSIGEVESAK
60 70 80 90 100
LIRDKVAGHS LGYGFVNYVT AKDAERAIST LNGLRLQSKT IKVSYARPSS
110 120 130 140 150
EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA
160 170 180 190 200
FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNMALLSQLY
210 220 230 240 250
HSPARRFGGP VHHQAQRFRF SPMGVDHMSG ISGVNVPGNA SSGWCIFIYN
260 270 280 290 300
LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
310 320
AIASLNGYRL GDKILQVSFK TNKSHK
Length:326
Mass (Da):36,169
Last modified:July 27, 2011 - v2
Checksum:i74A98DEE5B921AF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31N → G in AAB17967 (PubMed:9763509).Curated
Sequence conflicti15 – 151D → G in AAB17967 (PubMed:9763509).Curated
Sequence conflicti168 – 1681N → I in AAB17967 (PubMed:9763509).Curated
Sequence conflicti168 – 1681N → I in AAA96941 (PubMed:7753842).Curated
Sequence conflicti298 – 2981A → S in AAB17967 (PubMed:9763509).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65735 mRNA. Translation: AAB17967.1.
AK080365 mRNA. Translation: BAC37892.1.
CH466566 Genomic DNA. Translation: EDL21996.1.
CH466566 Genomic DNA. Translation: EDL21997.1.
U17595 mRNA. Translation: AAA96941.1.
CCDSiCCDS22084.1.
PIRiI49144.
RefSeqiNP_034615.2. NM_010485.3.
XP_006508761.1. XM_006508698.2.
UniGeneiMm.119162.

Genome annotation databases

EnsembliENSMUST00000098950; ENSMUSP00000096549; ENSMUSG00000040028.
GeneIDi15568.
KEGGimmu:15568.
UCSCiuc009kts.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65735 mRNA. Translation: AAB17967.1.
AK080365 mRNA. Translation: BAC37892.1.
CH466566 Genomic DNA. Translation: EDL21996.1.
CH466566 Genomic DNA. Translation: EDL21997.1.
U17595 mRNA. Translation: AAA96941.1.
CCDSiCCDS22084.1.
PIRiI49144.
RefSeqiNP_034615.2. NM_010485.3.
XP_006508761.1. XM_006508698.2.
UniGeneiMm.119162.

3D structure databases

ProteinModelPortaliP70372.
SMRiP70372. Positions 18-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200482. 4 interactions.
DIPiDIP-46480N.
IntActiP70372. 7 interactions.
MINTiMINT-4094207.
STRINGi10090.ENSMUSP00000096549.

PTM databases

PhosphoSiteiP70372.

Proteomic databases

MaxQBiP70372.
PaxDbiP70372.
PRIDEiP70372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098950; ENSMUSP00000096549; ENSMUSG00000040028.
GeneIDi15568.
KEGGimmu:15568.
UCSCiuc009kts.1. mouse.

Organism-specific databases

CTDi1994.
MGIiMGI:1100851. Elavl1.

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiP70372.
KOiK13088.
OMAiRFGGPLH.
OrthoDBiEOG77T14R.
TreeFamiTF313377.

Enzyme and pathway databases

ReactomeiREACT_274491. HuR stabilizes mRNA.

Miscellaneous databases

ChiTaRSiElavl1. mouse.
NextBioi288542.
PROiP70372.
SOURCEiSearch...

Gene expression databases

BgeeiP70372.
ExpressionAtlasiP70372. baseline and differential.
GenevestigatoriP70372.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ELAV protein HuA (HuR) can redistribute between nucleus and cytoplasm and is upregulated during serum stimulation and T cell activation."
    Atasoy U., Watson J., Patel D., Keene J.D.
    J. Cell Sci. 111:3145-3156(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Spleen.
  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].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "A conserved family of elav-like genes in vertebrates."
    Good P.J.
    Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-292.
    Tissue: Brain.
  5. "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase."
    Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A.
    J. Biol. Chem. 277:44623-44630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-217.
  6. "Cooperative role of the RNA-binding proteins Hzf and HuR in p53 activation."
    Nakamura H., Kawagishi H., Watanabe A., Sugimoto K., Maruyama M., Sugimoto M.
    Mol. Cell. Biol. 31:1997-2009(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA LOCALIZATION, INTERACTION WITH ZNF385A, RNA-BINDING.
  7. "N-methyladenosine modification destabilizes developmental regulators in embryonic stem cells."
    Wang Y., Li Y., Toth J.I., Petroski M.D., Zhang Z., Zhao J.C.
    Nat. Cell Biol. 16:191-198(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.

Entry informationi

Entry nameiELAV1_MOUSE
AccessioniPrimary (citable) accession number: P70372
Secondary accession number(s): Q60745, Q78QY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 128 of the entry and version 2 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

External Data

Dasty 3

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 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.