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Q15717

- ELAV1_HUMAN

UniProt

Q15717 - ELAV1_HUMAN

Protein

ELAV-like protein 1

Gene

ELAVL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    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.1 Publication

    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. mRNA binding Source: ProtInc
    6. nucleotide binding Source: InterPro
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein kinase binding Source: UniProtKB
    10. RNA binding Source: UniProtKB

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. mRNA stabilization Source: UniProtKB
    5. multicellular organismal development Source: ProtInc
    6. positive regulation of translation Source: MGI
    7. regulation of stem cell maintenance Source: UniProtKB
    8. RNA metabolic process Source: Reactome

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_25218. HuR stabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ELAV-like protein 1
    Alternative name(s):
    Hu-antigen R
    Short name:
    HuR
    Gene namesi
    Name:ELAVL1
    Synonyms:HUR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3312. ELAVL1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Translocates into the cytoplasm following phosphorylation by MAPKAPK2.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27740.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 326325ELAV-like protein 1PRO_0000081577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine2 Publications
    Modified residuei202 – 2021Phosphoserine5 Publications
    Modified residuei217 – 2171Omega-N-methylated arginine; by CARM11 Publication

    Post-translational modificationi

    Phosphorylated by MAPKAPK2.5 Publications
    Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15717.
    PaxDbiQ15717.
    PeptideAtlasiQ15717.
    PRIDEiQ15717.

    PTM databases

    PhosphoSiteiQ15717.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ15717.
    BgeeiQ15717.
    CleanExiHS_ELAVL1.
    GenevestigatoriQ15717.

    Organism-specific databases

    HPAiCAB005256.

    Interactioni

    Subunit structurei

    Interacts with ANP32A By similarity. Interact with ZNF385A; the interaction is indirect and mRNA-dependent and may regulate p53/TP53 expression By similarity. 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, AGO1 and AGO2. Interacts with IGF2BP2 and IGF2BP3.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBCP0CG484EBI-374260,EBI-3390054

    Protein-protein interaction databases

    BioGridi108309. 1744 interactions.
    DIPiDIP-31291N.
    IntActiQ15717. 34 interactions.
    MINTiMINT-5001300.
    STRINGi9606.ENSP00000385269.

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 267
    Helixi33 – 419
    Beta strandi46 – 538
    Beta strandi55 – 573
    Beta strandi60 – 7011
    Helixi71 – 8111
    Beta strandi92 – 954
    Helixi101 – 1033
    Beta strandi107 – 1115
    Helixi119 – 1268
    Helixi127 – 1293
    Beta strandi132 – 1398
    Turni141 – 1433
    Beta strandi146 – 15611
    Helixi157 – 16711
    Beta strandi180 – 1834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HI9X-ray2.00A/B/C/D18-99[»]
    4ED5X-ray2.00A/B18-186[»]
    4EGLX-ray2.90A18-186[»]
    4FXVX-ray1.90A/B/C/D20-99[»]
    ProteinModelPortaliQ15717.
    SMRiQ15717. Positions 18-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15717.

    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.
    HOGENOMiHOG000231162.
    HOVERGENiHBG002295.
    InParanoidiQ15717.
    KOiK13088.
    OrthoDBiEOG77T14R.
    PhylomeDBiQ15717.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15717-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK    50
    LIRDKVAGHS LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS 100
    EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA 150
    FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNVALLSQLY 200
    HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA SSGWCIFIYN 250
    LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM 300
    AIASLNGYRL GDKILQVSFK TNKSHK 326
    Length:326
    Mass (Da):36,092
    Last modified:May 15, 2002 - v2
    Checksum:i0B86143805264DEF
    GO
    Isoform 2 (identifier: Q15717-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGSGGRSAQVSTGQRAWLLPCRFLKNTM

    Note: No experimental confirmation available.

    Show »
    Length:353
    Mass (Da):38,996
    Checksum:i3398C72FC8B54012
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801T → A in AAB41913. (PubMed:8626503)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGSGGRSAQVSTGQRAWLLP CRFLKNTM in isoform 2. 1 PublicationVSP_056148

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38175 mRNA. Translation: AAB41913.1.
    BT009793 mRNA. Translation: AAP88795.1.
    AK301013 mRNA. Translation: BAG62630.1.
    AC008975 Genomic DNA. No translation available.
    AC010336 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW68949.1.
    BC003376 mRNA. Translation: AAH03376.1.
    CCDSiCCDS12193.1.
    RefSeqiNP_001410.2. NM_001419.2.
    UniGeneiHs.184492.
    Hs.713744.

    Genome annotation databases

    EnsembliENST00000351593; ENSP00000264073; ENSG00000066044.
    ENST00000407627; ENSP00000385269; ENSG00000066044.
    ENST00000596459; ENSP00000472197; ENSG00000066044.
    GeneIDi1994.
    KEGGihsa:1994.
    UCSCiuc002mjb.3. human.

    Polymorphism databases

    DMDMi20981691.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38175 mRNA. Translation: AAB41913.1 .
    BT009793 mRNA. Translation: AAP88795.1 .
    AK301013 mRNA. Translation: BAG62630.1 .
    AC008975 Genomic DNA. No translation available.
    AC010336 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW68949.1 .
    BC003376 mRNA. Translation: AAH03376.1 .
    CCDSi CCDS12193.1.
    RefSeqi NP_001410.2. NM_001419.2.
    UniGenei Hs.184492.
    Hs.713744.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HI9 X-ray 2.00 A/B/C/D 18-99 [» ]
    4ED5 X-ray 2.00 A/B 18-186 [» ]
    4EGL X-ray 2.90 A 18-186 [» ]
    4FXV X-ray 1.90 A/B/C/D 20-99 [» ]
    ProteinModelPortali Q15717.
    SMRi Q15717. Positions 18-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108309. 1744 interactions.
    DIPi DIP-31291N.
    IntActi Q15717. 34 interactions.
    MINTi MINT-5001300.
    STRINGi 9606.ENSP00000385269.

    Chemistry

    BindingDBi Q15717.
    ChEMBLi CHEMBL1250379.

    PTM databases

    PhosphoSitei Q15717.

    Polymorphism databases

    DMDMi 20981691.

    Proteomic databases

    MaxQBi Q15717.
    PaxDbi Q15717.
    PeptideAtlasi Q15717.
    PRIDEi Q15717.

    Protocols and materials databases

    DNASUi 1994.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351593 ; ENSP00000264073 ; ENSG00000066044 .
    ENST00000407627 ; ENSP00000385269 ; ENSG00000066044 .
    ENST00000596459 ; ENSP00000472197 ; ENSG00000066044 .
    GeneIDi 1994.
    KEGGi hsa:1994.
    UCSCi uc002mjb.3. human.

    Organism-specific databases

    CTDi 1994.
    GeneCardsi GC19M008023.
    HGNCi HGNC:3312. ELAVL1.
    HPAi CAB005256.
    MIMi 603466. gene.
    neXtProti NX_Q15717.
    PharmGKBi PA27740.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000231162.
    HOVERGENi HBG002295.
    InParanoidi Q15717.
    KOi K13088.
    OrthoDBi EOG77T14R.
    PhylomeDBi Q15717.
    TreeFami TF313377.

    Enzyme and pathway databases

    Reactomei REACT_25218. HuR stabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei Q15717.
    GeneWikii ELAVL1.
    GenomeRNAii 1994.
    NextBioi 8063.
    PROi Q15717.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15717.
    Bgeei Q15717.
    CleanExi HS_ELAVL1.
    Genevestigatori Q15717.

    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. "Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein."
      Ma W.-J., Cheng S., Campbell C., Wright A., Furneaux H.M.
      J. Biol. Chem. 271:8144-8151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Small intestine.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Cervix.
    7. "Delineation of mRNA export pathways by the use of cell-permeable peptides."
      Gallouzi I.-E., Steitz J.A.
      Science 294:1895-1901(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANP32A.
    8. "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.
    9. "Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2."
      Tran H., Maurer F., Nagamine Y.
      Mol. Cell. Biol. 23:7177-7188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION BY MAPKAPK2.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    12. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
      Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
      Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    16. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    21. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
      Wachter K., Kohn M., Stohr N., Huttelmaier S.
      Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.

    Entry informationi

    Entry nameiELAV1_HUMAN
    AccessioniPrimary (citable) accession number: Q15717
    Secondary accession number(s): B4DVB8, Q53XN6, Q9BTT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 150 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3