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Protein Page:
HuR (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
HuR Involved in 3'-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR 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. 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, EIF2C1 and EIF2C2. Ubiquitous. Belongs to the RRM elav family. Note: This description may include information from UniProtKB.
Protein type: RNA binding protein
Cellular Component: nucleoplasm; cytoplasm; cytosol; nucleus
Molecular Function: mRNA binding; protein binding; RNA binding; double-stranded RNA binding; nucleotide binding; AU-rich element binding; protein kinase binding
Biological Process: positive regulation of translation; RNA metabolic process; multicellular organismal development; mRNA stabilization; gene expression; mRNA metabolic process
Reference #:  Q15717 (UniProtKB)
Alt. Names/Synonyms: ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R); ELAV-like protein 1; ELAV1; ELAVL1; embryonic lethal, abnormal vision, drosophila, homolog-like 1; Hu antigen R; Hu-antigen R; Hua; HUR; MelG
Gene Symbols: ELAVL1
Molecular weight: 36,092 Da
Basal Isoelectric point: 9.23  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HuR

Protein Structure Not Found.


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Sites Implicated In
carcinogenesis, altered: S318‑p
cell cycle regulation: S242‑p, S318‑p
cell growth, altered: S242‑p
cell motility, altered: S221‑p, S318‑p
RNA stability, altered: S88‑p, S100‑p, T118‑p, S158‑p, S221‑p
translation, altered: S158‑p, S221‑p
intracellular localization: T118‑p, S158‑p, Y200‑p, S221‑p, S242‑p, S318‑p
molecular association, regulation: T118‑p, S158‑p, S221‑p, S242‑p, S318‑p
phosphorylation: S158‑p, S221‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S2-p ______MsNGYEDHM
0 4 Y26-p RTNLIVNyLPQNMtQ
0 2 T32-p NyLPQNMtQDELRSL
0 14 K50-u IGEVESAkLIRDkVA
0 8 K55-u SAkLIRDkVAGHSLG
1 3 Y63-p VAGHSLGyGFVNyVT
1 1 Y68-p LGyGFVNyVTAkDAE
0 14 K72-u FVNyVTAkDAERAIN
0 2 T80-p DAERAINtLNGLRLQ
2 0 S88-p LNGLRLQsKTIkVSY
0 2 K92-u RLQsKTIkVSYARPS
2 2 S100-p VSYARPSsEVIkDAN
0 2 K104-u RPSsEVIkDANLyIS
0 5 Y109-p VIkDANLyISGLPRT
4 3 T118-p SGLPRTMtQkDVEDM
0 4 K120-u LPRTMtQkDVEDMFS
3 0 S158-p FIRFDKRsEAEEAIT
1 0 K182-u SSEPITVkFAANPNQ
0 20 K191-u AANPNQNkNVALLsQ
0 9 S197-p NkNVALLsQLyHsPA
1 247 Y200-p VALLsQLyHsPArrF
5 84 S202-p LLsQLyHsPArrFGG
0 1 R205-m1 QLyHsPArrFGGPVH
0 10 R206-m1 LyHsPArrFGGPVHH
0 1 R206 LyHsPArRFGGPVHH
1 0 R217-m PVHHQAQrFrFsPMG
0 16 R217-m1 PVHHQAQrFrFsPMG
0 6 R217-m2 PVHHQAQrFrFsPMG
0 3 R219-m1 HHQAQrFrFsPMGVD
8 0 S221-p QAQrFrFsPMGVDHM
1 0 S242-p NVPGNASsGWCIFIY
0 4 K283-u IRDFNTNkCKGFGFV
1 0 S304-p EAAMAIAsLNGYRLG
1 9 K313-u NGYRLGDkILQVsFk
7 1 S318-p GDkILQVsFkTNkSH
0 39 K320-u kILQVsFkTNkSHk_
0 2 K323-u QVsFkTNkSHk____
1 0 K326-u FkTNkSHk_______
  mouse

 
S2 ______MSNGYEDHM
Y26 RTNLIVNYLPQNMTQ
T32 NYLPQNMTQEELRSL
K50-u IGEVESAkLIRDkVA
K55-u SAkLIRDkVAGHSLG
Y63 VAGHSLGYGFVNYVT
Y68 LGYGFVNYVTAkDAE
K72-u FVNYVTAkDAERAIS
T80-p DAERAIStLNGLRLQ
S88 LNGLRLQSKTIkVSY
K92-u RLQSKTIkVSYARPS
S100 VSYARPSSEVIkDAN
K104-u RPSSEVIkDANLYIS
Y109 VIkDANLYISGLPRT
T118 SGLPRTMTQkDVEDM
K120-u LPRTMTQkDVEDMFS
S158 FIRFDKRSEAEEAIT
K182 SSEPITVKFAANPNQ
K191-u AANPNQNkNMALLSQ
S197 NkNMALLSQLyHsPA
Y200-p MALLSQLyHsPARrF
S202-p LLSQLyHsPARrFGG
R205 QLyHsPARrFGGPVH
R206-m1 LyHsPARrFGGPVHH
R206-m2 LyHsPARrFGGPVHH
R217 PVHHQAQRFrFSPMG
R217-m1 PVHHQAQrFrFSPMG
R217-m2 PVHHQAQrFrFSPMG
R219-m1 HHQAQrFrFSPMGVD
S221 QAQrFrFSPMGVDHM
S242 NVPGNASSGWCIFIY
K283-u IRDFNTNkCKGFGFV
S304 EAAMAIASLNGYRLG
K313 NGYRLGDKILQVsFk
S318-p GDKILQVsFkTNkSH
K320-u KILQVsFkTNkSHK_
K323-u QVsFkTNkSHK____
K326 FkTNkSHK_______
  rat

 
S2 ______MSNGYEDHM
Y26 RTNLIVNYLPQNMTQ
T32 NYLPQNMTQEELRSL
K50 IGEVESAKLIRDKVA
K55 SAKLIRDKVAGHSLG
Y63 VAGHSLGYGFVNYVT
Y68 LGYGFVNYVTAKDAE
K72 FVNYVTAKDAERAIS
T80 DAERAISTLNGLRLQ
S88 LNGLRLQSKTIKVSY
K92 RLQSKTIKVSYARPS
S100 VSYARPSSEVIKDAN
K104 RPSSEVIKDANLYIS
Y109 VIKDANLYISGLPRT
T118 SGLPRTMTQKDVEDM
K120 LPRTMTQKDVEDMFS
S158 FIRFDKRSEAEEAIT
K182 SSEPITVKFAANPNQ
K191 AANPNQNKNMALLSQ
S197 NKNMALLSQLYHSPA
Y200 MALLSQLYHSPARrF
S202 LLSQLYHSPARrFGG
R205 QLYHSPARrFGGPVH
R206-m1 LYHSPARrFGGPVHH
R206 LYHSPARRFGGPVHH
R217 PVHHQAQRFRFSPMG
R217-m1 PVHHQAQrFRFSPMG
R217 PVHHQAQRFRFSPMG
R219 HHQAQrFRFSPMGVD
S221 QAQrFRFSPMGVDHM
S242 NVPGNASSGWCIFIY
K283 IRDFNTNKCKGFGFV
S304 EAAMAIASLNGYRLG
K313 NGYRLGDKILQVSFK
S318 GDKILQVSFKTNKSH
K320 KILQVSFKTNKSHK_
K323 QVSFKTNKSHK____
K326 FKTNKSHK_______
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