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)

P26378

- ELAV4_HUMAN

UniProt

P26378 - ELAV4_HUMAN

Protein

ELAV-like protein 4

Gene

ELAVL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR By similarity. Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA.By similarity2 Publications

    GO - Molecular functioni

    1. AU-rich element binding Source: UniProtKB
    2. mRNA 3'-UTR binding Source: ProtInc
    3. nucleotide binding Source: InterPro
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. mRNA processing Source: ProtInc
    2. RNA processing Source: ProtInc

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ELAV-like protein 4
    Alternative name(s):
    Hu-antigen D
    Short name:
    HuD
    Paraneoplastic encephalomyelitis antigen HuD
    Gene namesi
    Name:ELAVL4
    Synonyms:HUD, PNEM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3315. ELAVL4.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27743.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380ELAV-like protein 4PRO_0000081583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei243 – 2431Omega-N-methylated arginine; by CARM11 Publication

    Post-translational modificationi

    Methylation at Arg-243 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state. Methylation is inhibited by NGF, which facilitates neurite outgrowth By similarity.By similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP26378.
    PRIDEiP26378.

    PTM databases

    PhosphoSiteiP26378.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    ArrayExpressiP26378.
    BgeeiP26378.
    CleanExiHS_ELAVL4.
    GenevestigatoriP26378.

    Organism-specific databases

    HPAiCAB004442.

    Interactioni

    Subunit structurei

    Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP.By similarity

    Protein-protein interaction databases

    BioGridi108311. 5 interactions.
    IntActiP26378. 2 interactions.
    MINTiMINT-1471928.
    STRINGi9606.ENSP00000349594.

    Structurei

    Secondary structure

    1
    380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 527
    Helixi59 – 679
    Beta strandi72 – 798
    Turni81 – 833
    Beta strandi86 – 9611
    Helixi97 – 10711
    Beta strandi118 – 1214
    Helixi127 – 1293
    Beta strandi133 – 1386
    Helixi145 – 1528
    Helixi153 – 1553
    Beta strandi158 – 1658
    Turni167 – 1693
    Beta strandi172 – 18211
    Helixi183 – 19311
    Beta strandi206 – 2094

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FXLX-ray1.80A44-210[»]
    1G2EX-ray2.30A44-210[»]
    ProteinModelPortaliP26378.
    SMRiP26378. Positions 44-258, 296-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26378.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 12479RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 21281RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini297 – 37579RRM 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.
    KOiK13208.
    OrthoDBiEOG77T14R.
    PhylomeDBiP26378.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26378-1) [UniParc]FASTAAdd to Basket

    Also known as: HUD1PRO

    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

    MVMIISTMEP QVSNGPTSNT SNGPSSNNRN CPSPMQTGAT TDDSKTNLIV    50
    NYLPQNMTQE EFRSLFGSIG EIESCKLVRD KITGQSLGYG FVNYIDPKDA 100
    EKAINTLNGL RLQTKTIKVS YARPSSASIR DANLYVSGLP KTMTQKELEQ 150
    LFSQYGRIIT SRILVDQVTG VSRGVGFIRF DKRIEAEEAI KGLNGQKPSG 200
    ATEPITVKFA NNPSQKSSQA LLSQLYQSPN RRYPGPLHHQ AQRFRLDNLL 250
    NMAYGVKRLM SGPVPPSACP PRFSPITIDG MTSLVGMNIP GHTGTGWCIF 300
    VYNLSPDSDE SVLWQLFGPF GAVNNVKVIR DFNTNKCKGF GFVTMTNYDE 350
    AAMAIASLNG YRLGDRVLQV SFKTNKAHKS 380
    Length:380
    Mass (Da):41,770
    Last modified:February 10, 2009 - v2
    Checksum:i80E82D40FA5A05DE
    GO
    Isoform 2 (identifier: P26378-2) [UniParc]FASTAAdd to Basket

    Also known as: HUD1

    The sequence of this isoform differs from the canonical sequence as follows:
         259-272: Missing.

    Show »
    Length:366
    Mass (Da):40,379
    Checksum:i9BB102A0AD7495F1
    GO
    Isoform 3 (identifier: P26378-3) [UniParc]FASTAAdd to Basket

    Also known as: HUD4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MV → MRLLLLREIVINESRNCSF
         259-272: Missing.

    Show »
    Length:383
    Mass (Da):42,437
    Checksum:i4FA0B4DC38E805A2
    GO
    Isoform 4 (identifier: P26378-4) [UniParc]FASTAAdd to Basket

    Also known as: HUD3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MVM → MEQ
         259-272: Missing.

    Show »
    Length:366
    Mass (Da):40,406
    Checksum:iB26D48737B9BCACB
    GO
    Isoform 5 (identifier: P26378-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MVM → MRLKNQ
         259-272: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:369
    Mass (Da):40,788
    Checksum:iD4A4DBCC6DF6A4DC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661D → G.1 Publication
    Corresponds to variant rs17853533 [ dbSNP | Ensembl ].
    VAR_058091
    Natural varianti270 – 2701P → S.3 Publications
    Corresponds to variant rs2494876 [ dbSNP | Ensembl ].
    VAR_052204
    Natural varianti356 – 3561A → T.1 Publication
    Corresponds to variant rs17853531 [ dbSNP | Ensembl ].
    VAR_058092

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 33MVM → MEQ in isoform 4. 1 PublicationVSP_037608
    Alternative sequencei1 – 33MVM → MRLKNQ in isoform 5. 1 PublicationVSP_043450
    Alternative sequencei1 – 22MV → MRLLLLREIVINESRNCSF in isoform 3. 1 PublicationVSP_014150
    Alternative sequencei259 – 27214Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_005791Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62843 mRNA. Translation: AAA58396.1.
    AY033995 mRNA. Translation: AAK57538.1.
    AY033996 mRNA. Translation: AAK57539.1.
    AY033997 mRNA. Translation: AAK57540.1.
    AY033998 mRNA. Translation: AAK57541.1.
    AK297338 mRNA. Translation: BAH12553.1.
    AL583843, AL592182 Genomic DNA. Translation: CAI14634.1.
    AL583843, AL592182 Genomic DNA. Translation: CAI14635.1.
    AL583843, AL592182 Genomic DNA. Translation: CAI14636.1.
    AL583843, AL592182 Genomic DNA. Translation: CAI14637.1.
    AL592182, AL583843 Genomic DNA. Translation: CAI15788.1.
    AL592182, AL583843 Genomic DNA. Translation: CAI15789.1.
    AL592182, AL583843 Genomic DNA. Translation: CAI15790.1.
    AL592182, AL583843 Genomic DNA. Translation: CAI15791.1.
    AL645730 Genomic DNA. No translation available.
    AL731870 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06845.1.
    BC036071 mRNA. Translation: AAH36071.1.
    CCDSiCCDS44138.1. [P26378-4]
    CCDS44140.1. [P26378-2]
    CCDS53315.1. [P26378-5]
    CCDS553.1. [P26378-1]
    PIRiA40348.
    RefSeqiNP_001138246.1. NM_001144774.1. [P26378-2]
    NP_001138247.1. NM_001144775.1. [P26378-3]
    NP_001138248.1. NM_001144776.1. [P26378-4]
    NP_001138249.1. NM_001144777.1. [P26378-5]
    NP_068771.2. NM_021952.3. [P26378-1]
    UniGeneiHs.213050.

    Genome annotation databases

    EnsembliENST00000357083; ENSP00000349594; ENSG00000162374. [P26378-3]
    ENST00000371823; ENSP00000360888; ENSG00000162374. [P26378-1]
    ENST00000371824; ENSP00000360889; ENSG00000162374. [P26378-2]
    ENST00000371827; ENSP00000360892; ENSG00000162374. [P26378-4]
    ENST00000448907; ENSP00000399939; ENSG00000162374. [P26378-5]
    GeneIDi1996.
    KEGGihsa:1996.
    UCSCiuc001cry.3. human. [P26378-5]
    uc001crz.3. human. [P26378-4]
    uc001csa.3. human. [P26378-3]
    uc001csb.2. human. [P26378-1]
    uc001csc.3. human. [P26378-2]

    Polymorphism databases

    DMDMi223590202.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62843 mRNA. Translation: AAA58396.1 .
    AY033995 mRNA. Translation: AAK57538.1 .
    AY033996 mRNA. Translation: AAK57539.1 .
    AY033997 mRNA. Translation: AAK57540.1 .
    AY033998 mRNA. Translation: AAK57541.1 .
    AK297338 mRNA. Translation: BAH12553.1 .
    AL583843 , AL592182 Genomic DNA. Translation: CAI14634.1 .
    AL583843 , AL592182 Genomic DNA. Translation: CAI14635.1 .
    AL583843 , AL592182 Genomic DNA. Translation: CAI14636.1 .
    AL583843 , AL592182 Genomic DNA. Translation: CAI14637.1 .
    AL592182 , AL583843 Genomic DNA. Translation: CAI15788.1 .
    AL592182 , AL583843 Genomic DNA. Translation: CAI15789.1 .
    AL592182 , AL583843 Genomic DNA. Translation: CAI15790.1 .
    AL592182 , AL583843 Genomic DNA. Translation: CAI15791.1 .
    AL645730 Genomic DNA. No translation available.
    AL731870 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06845.1 .
    BC036071 mRNA. Translation: AAH36071.1 .
    CCDSi CCDS44138.1. [P26378-4 ]
    CCDS44140.1. [P26378-2 ]
    CCDS53315.1. [P26378-5 ]
    CCDS553.1. [P26378-1 ]
    PIRi A40348.
    RefSeqi NP_001138246.1. NM_001144774.1. [P26378-2 ]
    NP_001138247.1. NM_001144775.1. [P26378-3 ]
    NP_001138248.1. NM_001144776.1. [P26378-4 ]
    NP_001138249.1. NM_001144777.1. [P26378-5 ]
    NP_068771.2. NM_021952.3. [P26378-1 ]
    UniGenei Hs.213050.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FXL X-ray 1.80 A 44-210 [» ]
    1G2E X-ray 2.30 A 44-210 [» ]
    ProteinModelPortali P26378.
    SMRi P26378. Positions 44-258, 296-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108311. 5 interactions.
    IntActi P26378. 2 interactions.
    MINTi MINT-1471928.
    STRINGi 9606.ENSP00000349594.

    PTM databases

    PhosphoSitei P26378.

    Polymorphism databases

    DMDMi 223590202.

    Proteomic databases

    PaxDbi P26378.
    PRIDEi P26378.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357083 ; ENSP00000349594 ; ENSG00000162374 . [P26378-3 ]
    ENST00000371823 ; ENSP00000360888 ; ENSG00000162374 . [P26378-1 ]
    ENST00000371824 ; ENSP00000360889 ; ENSG00000162374 . [P26378-2 ]
    ENST00000371827 ; ENSP00000360892 ; ENSG00000162374 . [P26378-4 ]
    ENST00000448907 ; ENSP00000399939 ; ENSG00000162374 . [P26378-5 ]
    GeneIDi 1996.
    KEGGi hsa:1996.
    UCSCi uc001cry.3. human. [P26378-5 ]
    uc001crz.3. human. [P26378-4 ]
    uc001csa.3. human. [P26378-3 ]
    uc001csb.2. human. [P26378-1 ]
    uc001csc.3. human. [P26378-2 ]

    Organism-specific databases

    CTDi 1996.
    GeneCardsi GC01P050513.
    HGNCi HGNC:3315. ELAVL4.
    HPAi CAB004442.
    MIMi 168360. gene.
    neXtProti NX_P26378.
    PharmGKBi PA27743.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000231162.
    HOVERGENi HBG002295.
    KOi K13208.
    OrthoDBi EOG77T14R.
    PhylomeDBi P26378.
    TreeFami TF313377.

    Miscellaneous databases

    EvolutionaryTracei P26378.
    GeneWikii HuD_(protein).
    GenomeRNAii 1996.
    NextBioi 8073.
    PROi P26378.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26378.
    Bgeei P26378.
    CleanExi HS_ELAVL4.
    Genevestigatori P26378.

    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. "HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal."
      Szabo A., Dalmau J., Manley G., Rosenfeld M., Wong E., Henson J., Posner J.B., Furneaux H.M.
      Cell 67:325-333(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT SER-270.
      Tissue: Brain.
    2. "Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes identified by autologous antibody screening of a pediatric neuroblastoma library."
      Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S., Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.
      Int. J. Cancer 100:669-677(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT SER-270.
      Tissue: Neuroblastoma.
    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 5).
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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 2), VARIANTS GLY-166 AND THR-356.
      Tissue: Hypothalamus.
    7. "Paraneoplastic encephalomyelitis antigens bind to the AU-rich elements of mRNA."
      Liu J., Dalmau J., Szabo A., Rosenfeld M., Huber J., Furneaux H.
      Neurology 45:544-550(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 240-279 (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, VARIANT SER-270.
    8. "RNA-binding analyses of HuC and HuD with the VEGF and c-myc 3'-untranslated regions using a novel ELISA-based assay."
      King P.H.
      Nucleic Acids Res. 28:E20-E20(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    9. Cited for: METHYLATION AT ARG-243.
    10. "Structural basis for recognition of AU-rich element RNA by the HuD protein."
      Wang X., Tanaka Hall T.M.
      Nat. Struct. Biol. 8:141-145(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 44-210 IN COMPLEX WITH RNA.

    Entry informationi

    Entry nameiELAV4_HUMAN
    AccessioniPrimary (citable) accession number: P26378
    Secondary accession number(s): B1APY6
    , B1APY7, B7Z4G7, Q8IYD4, Q96J74, Q96J75, Q9UD24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 139 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3