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Protein

ELAV-like protein 1

Gene

ELAVL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 kinase binding Source: UniProtKB
  9. RNA binding Source: UniProtKB

GO - Biological processi

  1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  2. gene expression Source: Reactome
  3. mRNA stabilization Source: UniProtKB
  4. multicellular organismal development Source: ProtInc
  5. positive regulation of translation Source: MGI
  6. regulation of stem cell maintenance Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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 – 21Phosphoserine1 Publication
Modified residuei202 – 2021Phosphoserine4 Publications
Modified residuei217 – 2171Omega-N-methylated arginine; by CARM11 Publication

Post-translational modificationi

Phosphorylated by MAPKAPK2.1 Publication
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

BgeeiQ15717.
CleanExiHS_ELAVL1.
ExpressionAtlasiQ15717. baseline and differential.
GenevestigatoriQ15717.

Organism-specific databases

HPAiCAB005256.
HPA046298.

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. 1756 interactions.
DIPiDIP-31291N.
IntActiQ15717. 37 interactions.
MINTiMINT-5001300.
STRINGi9606.ENSP00000385269.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ15717.
KOiK13088.
OMAiRFGGPLH.
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. AlignAdd to basket

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

        10         20         30         40         50
MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK
60 70 80 90 100
LIRDKVAGHS LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS
110 120 130 140 150
EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA
160 170 180 190 200
FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNVALLSQLY
210 220 230 240 250
HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA SSGWCIFIYN
260 270 280 290 300
LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
310 320
AIASLNGYRL GDKILQVSFK TNKSHK
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:
EMBLi
GenBanki
DDBJi
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. [Q15717-1]
RefSeqiNP_001410.2. NM_001419.2. [Q15717-1]
UniGeneiHs.184492.
Hs.713744.

Genome annotation databases

EnsembliENST00000351593; ENSP00000264073; ENSG00000066044. [Q15717-1]
ENST00000407627; ENSP00000385269; ENSG00000066044. [Q15717-1]
ENST00000596459; ENSP00000472197; ENSG00000066044. [Q15717-1]
GeneIDi1994.
KEGGihsa:1994.
UCSCiuc002mjb.3. human. [Q15717-1]

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:
EMBLi
GenBanki
DDBJi
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. [Q15717-1]
RefSeqiNP_001410.2. NM_001419.2. [Q15717-1]
UniGeneiHs.184492.
Hs.713744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi108309. 1756 interactions.
DIPiDIP-31291N.
IntActiQ15717. 37 interactions.
MINTiMINT-5001300.
STRINGi9606.ENSP00000385269.

Chemistry

BindingDBiQ15717.
ChEMBLiCHEMBL1250379.

PTM databases

PhosphoSiteiQ15717.

Polymorphism databases

DMDMi20981691.

Proteomic databases

MaxQBiQ15717.
PaxDbiQ15717.
PeptideAtlasiQ15717.
PRIDEiQ15717.

Protocols and materials databases

DNASUi1994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351593; ENSP00000264073; ENSG00000066044. [Q15717-1]
ENST00000407627; ENSP00000385269; ENSG00000066044. [Q15717-1]
ENST00000596459; ENSP00000472197; ENSG00000066044. [Q15717-1]
GeneIDi1994.
KEGGihsa:1994.
UCSCiuc002mjb.3. human. [Q15717-1]

Organism-specific databases

CTDi1994.
GeneCardsiGC19M008023.
HGNCiHGNC:3312. ELAVL1.
HPAiCAB005256.
HPA046298.
MIMi603466. gene.
neXtProtiNX_Q15717.
PharmGKBiPA27740.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ15717.
KOiK13088.
OMAiRFGGPLH.
OrthoDBiEOG77T14R.
PhylomeDBiQ15717.
TreeFamiTF313377.

Enzyme and pathway databases

ReactomeiREACT_25218. HuR stabilizes mRNA.

Miscellaneous databases

EvolutionaryTraceiQ15717.
GeneWikiiELAVL1.
GenomeRNAii1994.
NextBioi35475416.
PROiQ15717.
SOURCEiSearch...

Gene expression databases

BgeeiQ15717.
CleanExiHS_ELAVL1.
ExpressionAtlasiQ15717. baseline and differential.
GenevestigatoriQ15717.

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. "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: March 4, 2015
This is version 155 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

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.