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ELAV-like protein 4 (Hu-antigen D) (HuD) (Paraneoplastic encephalomyelitis antigen HuD)

 ELAV4_HUMAN             Reviewed;         380 AA.
P26378; B1APY6; B1APY7; B7Z4G7; Q8IYD4; Q96J74; Q96J75; Q9UD24;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
28-FEB-2018, entry version 164.
RecName: Full=ELAV-like protein 4;
AltName: Full=Hu-antigen D;
Short=HuD;
AltName: Full=Paraneoplastic encephalomyelitis antigen HuD;
Name=ELAVL4; Synonyms=HUD, PNEM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT SER-270.
TISSUE=Brain;
PubMed=1655278; DOI=10.1016/0092-8674(91)90184-Z;
Szabo A., Dalmau J., Manley G., Rosenfeld M., Wong E., Henson J.,
Posner J.B., Furneaux H.M.;
"HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding
domains and is homologous to Elav and Sex-lethal.";
Cell 67:325-333(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT
SER-270.
TISSUE=Neuroblastoma;
PubMed=12209604; DOI=10.1002/ijc.10550;
Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S.,
Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.;
"Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes
identified by autologous antibody screening of a pediatric
neuroblastoma library.";
Int. J. Cancer 100:669-677(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
GLY-166 AND THR-356.
TISSUE=Hypothalamus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 240-279 (ISOFORM 1), FUNCTION,
ALTERNATIVE SPLICING, AND VARIANT SER-270.
PubMed=7898713; DOI=10.1212/WNL.45.3.544;
Liu J., Dalmau J., Szabo A., Rosenfeld M., Huber J., Furneaux H.;
"Paraneoplastic encephalomyelitis antigens bind to the AU-rich
elements of mRNA.";
Neurology 45:544-550(1995).
[8]
FUNCTION, AND RNA-BINDING.
PubMed=10710437; DOI=10.1093/nar/28.7.e20;
King P.H.;
"RNA-binding analyses of HuC and HuD with the VEGF and c-myc 3'-
untranslated regions using a novel ELISA-based assay.";
Nucleic Acids Res. 28:E20-E20(2000).
[9]
METHYLATION AT ARG-243.
PubMed=16508003; DOI=10.1128/MCB.26.6.2273-2285.2006;
Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H.,
Yachi K., Kubo T., Yoshikawa H., Tohyama M.;
"CARM1 regulates proliferation of PC12 cells by methylating HuD.";
Mol. Cell. Biol. 26:2273-2285(2006).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 44-210 IN COMPLEX WITH RNA.
PubMed=11175903; DOI=10.1038/84131;
Wang X., Tanaka Hall T.M.;
"Structural basis for recognition of AU-rich element RNA by the HuD
protein.";
Nat. Struct. Biol. 8:141-145(2001).
-!- FUNCTION: 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. {ECO:0000250,
ECO:0000269|PubMed:10710437, ECO:0000269|PubMed:7898713}.
-!- SUBUNIT: Component of a TAU mRNP complex, at least composed of
IGF2BP1, ELAVL4 and G3BP. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=HUD1PRO;
IsoId=P26378-1; Sequence=Displayed;
Name=2; Synonyms=HUD1;
IsoId=P26378-2; Sequence=VSP_005791;
Name=3; Synonyms=HUD4;
IsoId=P26378-3; Sequence=VSP_014150, VSP_005791;
Name=4; Synonyms=HUD3;
IsoId=P26378-4; Sequence=VSP_037608, VSP_005791;
Name=5;
IsoId=P26378-5; Sequence=VSP_043450, VSP_005791;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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EMBL; M62843; AAA58396.1; -; mRNA.
EMBL; AY033995; AAK57538.1; -; mRNA.
EMBL; AY033996; AAK57539.1; -; mRNA.
EMBL; AY033997; AAK57540.1; -; mRNA.
EMBL; AY033998; AAK57541.1; -; mRNA.
EMBL; AK297338; BAH12553.1; -; mRNA.
EMBL; AL583843; CAI14634.1; -; Genomic_DNA.
EMBL; AL592182; CAI14634.1; JOINED; Genomic_DNA.
EMBL; AL583843; CAI14635.1; -; Genomic_DNA.
EMBL; AL592182; CAI14635.1; JOINED; Genomic_DNA.
EMBL; AL583843; CAI14636.1; -; Genomic_DNA.
EMBL; AL592182; CAI14636.1; JOINED; Genomic_DNA.
EMBL; AL583843; CAI14637.1; -; Genomic_DNA.
EMBL; AL592182; CAI14637.1; JOINED; Genomic_DNA.
EMBL; AL592182; CAI15788.1; -; Genomic_DNA.
EMBL; AL583843; CAI15788.1; JOINED; Genomic_DNA.
EMBL; AL592182; CAI15789.1; -; Genomic_DNA.
EMBL; AL583843; CAI15789.1; JOINED; Genomic_DNA.
EMBL; AL592182; CAI15790.1; -; Genomic_DNA.
EMBL; AL583843; CAI15790.1; JOINED; Genomic_DNA.
EMBL; AL592182; CAI15791.1; -; Genomic_DNA.
EMBL; AL583843; CAI15791.1; JOINED; Genomic_DNA.
EMBL; AL645730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06845.1; -; Genomic_DNA.
EMBL; BC036071; AAH36071.1; -; mRNA.
CCDS; CCDS44138.1; -. [P26378-4]
CCDS; CCDS44140.1; -. [P26378-2]
CCDS; CCDS53315.1; -. [P26378-5]
CCDS; CCDS553.1; -. [P26378-1]
PIR; A40348; A40348.
RefSeq; NP_001138246.1; NM_001144774.2. [P26378-2]
RefSeq; NP_001138247.2; NM_001144775.2.
RefSeq; NP_001138248.1; NM_001144776.2. [P26378-4]
RefSeq; NP_001138249.1; NM_001144777.2. [P26378-5]
RefSeq; NP_001281277.1; NM_001294348.1.
RefSeq; NP_068771.2; NM_021952.4. [P26378-1]
UniGene; Hs.213050; -.
PDB; 1FXL; X-ray; 1.80 A; A=44-210.
PDB; 1G2E; X-ray; 2.30 A; A=44-210.
PDBsum; 1FXL; -.
PDBsum; 1G2E; -.
ProteinModelPortal; P26378; -.
SMR; P26378; -.
BioGrid; 108311; 17.
IntAct; P26378; 2.
STRING; 9606.ENSP00000349594; -.
iPTMnet; P26378; -.
PhosphoSitePlus; P26378; -.
BioMuta; ELAVL4; -.
DMDM; 223590202; -.
MaxQB; P26378; -.
PaxDb; P26378; -.
PeptideAtlas; P26378; -.
PRIDE; P26378; -.
Ensembl; ENST00000371823; ENSP00000360888; ENSG00000162374. [P26378-1]
Ensembl; ENST00000371824; ENSP00000360889; ENSG00000162374. [P26378-2]
Ensembl; ENST00000371827; ENSP00000360892; ENSG00000162374. [P26378-4]
Ensembl; ENST00000448907; ENSP00000399939; ENSG00000162374. [P26378-5]
GeneID; 1996; -.
KEGG; hsa:1996; -.
UCSC; uc001cry.3; human. [P26378-1]
CTD; 1996; -.
DisGeNET; 1996; -.
EuPathDB; HostDB:ENSG00000162374.16; -.
GeneCards; ELAVL4; -.
HGNC; HGNC:3315; ELAVL4.
HPA; CAB004442; -.
MIM; 168360; gene.
neXtProt; NX_P26378; -.
OpenTargets; ENSG00000162374; -.
PharmGKB; PA27743; -.
eggNOG; KOG0145; Eukaryota.
eggNOG; ENOG410XP7S; LUCA.
GeneTree; ENSGT00760000118913; -.
HOGENOM; HOG000231162; -.
HOVERGEN; HBG002295; -.
InParanoid; P26378; -.
KO; K13208; -.
PhylomeDB; P26378; -.
TreeFam; TF313377; -.
ChiTaRS; ELAVL4; human.
EvolutionaryTrace; P26378; -.
GeneWiki; HuD_(protein); -.
GenomeRNAi; 1996; -.
PRO; PR:P26378; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162374; -.
CleanEx; HS_ELAVL4; -.
ExpressionAtlas; P26378; baseline and differential.
Genevisible; P26378; HS.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; TAS:ProtInc.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
CDD; cd12650; RRM1_Hu; 1.
CDD; cd12656; RRM3_HuD; 1.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR006548; ELAD_HU_SF.
InterPro; IPR034775; ELAV/Hu_RRM1.
InterPro; IPR034918; HuD_RRM3.
InterPro; IPR002343; Hud_Sxl_RNA.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
PRINTS; PR00961; HUDSXLRNA.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding.
CHAIN 1 380 ELAV-like protein 4.
/FTId=PRO_0000081583.
DOMAIN 46 124 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 132 212 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 297 375 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000250|UniProtKB:Q61701}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q61701}.
MOD_RES 243 243 Omega-N-methylated arginine; by CARM1.
{ECO:0000269|PubMed:16508003}.
VAR_SEQ 1 3 MVM -> MEQ (in isoform 4).
{ECO:0000303|PubMed:12209604}.
/FTId=VSP_037608.
VAR_SEQ 1 3 MVM -> MRLKNQ (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043450.
VAR_SEQ 1 2 MV -> MRLLLLREIVINESRNCSF (in isoform 3).
{ECO:0000303|PubMed:12209604}.
/FTId=VSP_014150.
VAR_SEQ 259 272 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:12209604,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1655278}.
/FTId=VSP_005791.
VARIANT 166 166 D -> G (in dbSNP:rs17853533).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058091.
VARIANT 270 270 P -> S (in dbSNP:rs2494876).
{ECO:0000269|PubMed:12209604,
ECO:0000269|PubMed:1655278,
ECO:0000269|PubMed:7898713}.
/FTId=VAR_052204.
VARIANT 356 356 A -> T (in dbSNP:rs17853531).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058092.
STRAND 46 52 {ECO:0000244|PDB:1FXL}.
HELIX 59 67 {ECO:0000244|PDB:1FXL}.
STRAND 72 79 {ECO:0000244|PDB:1FXL}.
TURN 81 83 {ECO:0000244|PDB:1FXL}.
STRAND 86 96 {ECO:0000244|PDB:1FXL}.
HELIX 97 107 {ECO:0000244|PDB:1FXL}.
STRAND 118 121 {ECO:0000244|PDB:1FXL}.
HELIX 127 129 {ECO:0000244|PDB:1FXL}.
STRAND 133 138 {ECO:0000244|PDB:1FXL}.
HELIX 145 152 {ECO:0000244|PDB:1FXL}.
HELIX 153 155 {ECO:0000244|PDB:1FXL}.
STRAND 158 165 {ECO:0000244|PDB:1FXL}.
TURN 167 169 {ECO:0000244|PDB:1FXL}.
STRAND 172 182 {ECO:0000244|PDB:1FXL}.
HELIX 183 193 {ECO:0000244|PDB:1FXL}.
STRAND 206 209 {ECO:0000244|PDB:1FXL}.
SEQUENCE 380 AA; 41770 MW; 80E82D40FA5A05DE CRC64;
MVMIISTMEP QVSNGPTSNT SNGPSSNNRN CPSPMQTGAT TDDSKTNLIV NYLPQNMTQE
EFRSLFGSIG EIESCKLVRD KITGQSLGYG FVNYIDPKDA EKAINTLNGL RLQTKTIKVS
YARPSSASIR DANLYVSGLP KTMTQKELEQ LFSQYGRIIT SRILVDQVTG VSRGVGFIRF
DKRIEAEEAI KGLNGQKPSG ATEPITVKFA NNPSQKSSQA LLSQLYQSPN RRYPGPLHHQ
AQRFRLDNLL NMAYGVKRLM SGPVPPSACP PRFSPITIDG MTSLVGMNIP GHTGTGWCIF
VYNLSPDSDE SVLWQLFGPF GAVNNVKVIR DFNTNKCKGF GFVTMTNYDE AAMAIASLNG
YRLGDRVLQV SFKTNKAHKS


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CSB-EP018267HU Recombinant human Paraneoplastic antigen Ma2 protein Source: E.coli 1mg
CSB-EP018267HU Recombinant human Paraneoplastic antigen Ma2 protein Source: E.coli 200ug


 

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