Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70372

- ELAV1_MOUSE

UniProt

P70372 - ELAV1_MOUSE

Protein

ELAV-like protein 1

Gene

Elavl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. AU-rich element binding Source: UniProtKB
    2. double-stranded RNA binding Source: MGI
    3. mRNA 3'-UTR AU-rich region binding Source: MGI
    4. mRNA 3'-UTR binding Source: UniProtKB
    5. nucleotide binding Source: InterPro
    6. protein binding Source: IntAct
    7. RNA binding Source: UniProtKB

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
    2. mRNA stabilization Source: UniProtKB
    3. positive regulation of translation Source: MGI
    4. regulation of stem cell maintenance Source: UniProtKB
    5. regulation of translation Source: MGI

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198691. 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: 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

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: MGI

    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

    ArrayExpressiP70372.
    BgeeiP70372.
    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.
    GeneTreeiENSGT00560000077064.
    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

    MSNGYEDHMA EDCRDDIGRT NLIVNYLPQN MTQEELRSLF SSIGEVESAK    50
    LIRDKVAGHS LGYGFVNYVT AKDAERAIST LNGLRLQSKT IKVSYARPSS 100
    EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA 150
    FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNMALLSQLY 200
    HSPARRFGGP VHHQAQRFRF SPMGVDHMSG ISGVNVPGNA SSGWCIFIYN 250
    LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM 300
    AIASLNGYRL GDKILQVSFK TNKSHK 326
    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:
    EMBL
    GenBank
    DDBJ
    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_006508698.1.
    UniGeneiMm.119162.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS22084.1.
    PIRi I49144.
    RefSeqi NP_034615.2. NM_010485.3.
    XP_006508761.1. XM_006508698.1.
    UniGenei Mm.119162.

    3D structure databases

    ProteinModelPortali P70372.
    SMRi P70372. Positions 18-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200482. 4 interactions.
    DIPi DIP-46480N.
    IntActi P70372. 7 interactions.
    MINTi MINT-4094207.
    STRINGi 10090.ENSMUSP00000096549.

    PTM databases

    PhosphoSitei P70372.

    Proteomic databases

    MaxQBi P70372.
    PaxDbi P70372.
    PRIDEi P70372.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098950 ; ENSMUSP00000096549 ; ENSMUSG00000040028 .
    GeneIDi 15568.
    KEGGi mmu:15568.
    UCSCi uc009kts.1. mouse.

    Organism-specific databases

    CTDi 1994.
    MGIi MGI:1100851. Elavl1.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00560000077064.
    HOGENOMi HOG000231162.
    HOVERGENi HBG002295.
    InParanoidi P70372.
    KOi K13088.
    OMAi RFGGPLH.
    OrthoDBi EOG77T14R.
    TreeFami TF313377.

    Enzyme and pathway databases

    Reactomei REACT_198691. HuR stabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi ELAVL1. mouse.
    NextBioi 288542.
    PROi P70372.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70372.
    Bgeei P70372.
    Genevestigatori P70372.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR006548. ELAD_HUD_SF.
    IPR002343. Hud_Sxl_RNA.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    [Graphical view ]
    PRINTSi PR00961. HUDSXLRNA.
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01661. ELAV_HUD_SF. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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