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Protein

ELAV-like protein 4

Gene

ELAVL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.By similarity2 Publications

GO - Molecular functioni

  • AU-rich element binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: ProtInc
  • nucleotide binding Source: InterPro
  • RNA binding Source: ProtInc

GO - Biological processi

  • mRNA processing Source: ProtInc
  • RNA 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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3315. ELAVL4.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27743.

Polymorphism and mutation databases

BioMutaiELAVL4.
DMDMi223590202.

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

BgeeiP26378.
CleanExiHS_ELAVL4.
ExpressionAtlasiP26378. baseline and differential.
GenevisibleiP26378. HS.

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. 6 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 – 527Combined sources
Helixi59 – 679Combined sources
Beta strandi72 – 798Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 9611Combined sources
Helixi97 – 10711Combined sources
Beta strandi118 – 1214Combined sources
Helixi127 – 1293Combined sources
Beta strandi133 – 1386Combined sources
Helixi145 – 1528Combined sources
Helixi153 – 1553Combined sources
Beta strandi158 – 1658Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 18211Combined sources
Helixi183 – 19311Combined sources
Beta strandi206 – 2094Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiP26378.
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. AlignAdd to basket

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

        10         20         30         40         50
MVMIISTMEP QVSNGPTSNT SNGPSSNNRN CPSPMQTGAT TDDSKTNLIV
60 70 80 90 100
NYLPQNMTQE EFRSLFGSIG EIESCKLVRD KITGQSLGYG FVNYIDPKDA
110 120 130 140 150
EKAINTLNGL RLQTKTIKVS YARPSSASIR DANLYVSGLP KTMTQKELEQ
160 170 180 190 200
LFSQYGRIIT SRILVDQVTG VSRGVGFIRF DKRIEAEEAI KGLNGQKPSG
210 220 230 240 250
ATEPITVKFA NNPSQKSSQA LLSQLYQSPN RRYPGPLHHQ AQRFRLDNLL
260 270 280 290 300
NMAYGVKRLM SGPVPPSACP PRFSPITIDG MTSLVGMNIP GHTGTGWCIF
310 320 330 340 350
VYNLSPDSDE SVLWQLFGPF GAVNNVKVIR DFNTNKCKGF GFVTMTNYDE
360 370 380
AAMAIASLNG YRLGDRVLQV SFKTNKAHKS
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:
EMBLi
GenBanki
DDBJi
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_001144774.2. [P26378-2]
NP_001138247.2. NM_001144775.2.
NP_001138248.1. NM_001144776.2. [P26378-4]
NP_001138249.1. NM_001144777.2. [P26378-5]
NP_001281277.1. NM_001294348.1.
NP_068771.2. NM_021952.4. [P26378-1]
UniGeneiHs.213050.

Genome annotation databases

EnsembliENST00000371823; ENSP00000360888; ENSG00000162374. [P26378-1]
ENST00000371824; ENSP00000360889; ENSG00000162374. [P26378-2]
ENST00000371827; ENSP00000360892; ENSG00000162374. [P26378-4]
ENST00000448907; ENSP00000399939; ENSG00000162374. [P26378-5]
ENST00000625794; ENSP00000485759; ENSG00000162374. [P26378-3]
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001144774.2. [P26378-2]
NP_001138247.2. NM_001144775.2.
NP_001138248.1. NM_001144776.2. [P26378-4]
NP_001138249.1. NM_001144777.2. [P26378-5]
NP_001281277.1. NM_001294348.1.
NP_068771.2. NM_021952.4. [P26378-1]
UniGeneiHs.213050.

3D structure databases

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

Protein-protein interaction databases

BioGridi108311. 6 interactions.
IntActiP26378. 2 interactions.
MINTiMINT-1471928.
STRINGi9606.ENSP00000349594.

PTM databases

PhosphoSiteiP26378.

Polymorphism and mutation databases

BioMutaiELAVL4.
DMDMi223590202.

Proteomic databases

PaxDbiP26378.
PRIDEiP26378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371823; ENSP00000360888; ENSG00000162374. [P26378-1]
ENST00000371824; ENSP00000360889; ENSG00000162374. [P26378-2]
ENST00000371827; ENSP00000360892; ENSG00000162374. [P26378-4]
ENST00000448907; ENSP00000399939; ENSG00000162374. [P26378-5]
ENST00000625794; ENSP00000485759; ENSG00000162374. [P26378-3]
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]

Organism-specific databases

CTDi1996.
GeneCardsiGC01P050513.
HGNCiHGNC:3315. ELAVL4.
HPAiCAB004442.
MIMi168360. gene.
neXtProtiNX_P26378.
PharmGKBiPA27743.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiP26378.
KOiK13208.
OrthoDBiEOG77T14R.
PhylomeDBiP26378.
TreeFamiTF313377.

Miscellaneous databases

ChiTaRSiELAVL4. human.
EvolutionaryTraceiP26378.
GeneWikiiHuD_(protein).
GenomeRNAii1996.
NextBioi8073.
PROiP26378.
SOURCEiSearch...

Gene expression databases

BgeeiP26378.
CleanExiHS_ELAVL4.
ExpressionAtlasiP26378. baseline and differential.
GenevisibleiP26378. HS.

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. "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: June 24, 2015
This is version 145 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

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.