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P26378

- ELAV4_HUMAN

UniProt

P26378 - ELAV4_HUMAN

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Protein
ELAV-like protein 4
Gene
ELAVL4, HUD, PNEM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. mRNA processing Source: ProtInc
Complete GO annotation...

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 4
PRO_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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP26378.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 12479RRM 1
Add
BLAST
Domaini132 – 21281RRM 2
Add
BLAST
Domaini297 – 37579RRM 3
Add
BLAST

Sequence similaritiesi

Belongs to the RRM elav family.

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.
VSP_037608
Alternative sequencei1 – 33MVM → MRLKNQ in isoform 5.
VSP_043450
Alternative sequencei1 – 22MV → MRLLLLREIVINESRNCSF in isoform 3.
VSP_014150
Alternative sequencei259 – 27214Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_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]
CCDS44139.1. [P26378-3]
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 ]
CCDS44139.1. [P26378-3 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 138 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

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