ELAV2_HUMAN - dbPTM
ELAV2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELAV2_HUMAN
UniProt AC Q12926
Protein Name ELAV-like protein 2
Gene Name ELAVL2
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization
Protein Description Binds RNA. Seems to recognize a GAAA motif. Can bind to its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR..
Protein Sequence METQLSNGPTCNNTANGPTTINNNCSSPVDSGNTEDSKTNLIVNYLPQNMTQEELKSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGISRGVGFIRFDKRIEAEEAIKGLNGQKPPGATEPITVKFANNPSQKTNQAILSQLYQSPNRRYPGPLAQQAQRFRLDNLLNMAYGVKRFSPMTIDGMTSLAGINIPGHPGTGWCIFVYNLAPDADESILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKTHKA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--METQLSNGPTCNN
--CCCCCCCCCCCCC
29.8922210691
10PhosphorylationTQLSNGPTCNNTANG
CCCCCCCCCCCCCCC
29.3028348404
14PhosphorylationNGPTCNNTANGPTTI
CCCCCCCCCCCCCEE
13.9128348404
19PhosphorylationNNTANGPTTINNNCS
CCCCCCCCEECCCCC
41.5322210691
20PhosphorylationNTANGPTTINNNCSS
CCCCCCCEECCCCCC
25.4922210691
26PhosphorylationTTINNNCSSPVDSGN
CEECCCCCCCCCCCC
39.5428348404
27PhosphorylationTINNNCSSPVDSGNT
EECCCCCCCCCCCCC
31.0128348404
51PhosphorylationNYLPQNMTQEELKSL
ECCCCCCCHHHHHHH
40.14-
74 (in isoform 2)Ubiquitination-31.4421890473
74UbiquitinationSCKLVRDKITGQSLG
HCEEECCCCCCCCCC
31.44-
74 (in isoform 1)Ubiquitination-31.4421890473
95UbiquitinationIDPKDAEKAINTLNG
CCHHHHHHHHHHHHC
57.18-
95 (in isoform 1)Ubiquitination-57.1821890473
95 (in isoform 2)Ubiquitination-57.1821890473
99PhosphorylationDAEKAINTLNGLRLQ
HHHHHHHHHHCCEEE
18.58-
111UbiquitinationRLQTKTIKVSYARPS
EEEEEEEEEEEECCC
30.29-
113PhosphorylationQTKTIKVSYARPSSA
EEEEEEEEEECCCCC
14.2024117733
114PhosphorylationTKTIKVSYARPSSAS
EEEEEEEEECCCCCC
15.04-
118PhosphorylationKVSYARPSSASIRDA
EEEEECCCCCCCCCC
32.7424117733
119PhosphorylationVSYARPSSASIRDAN
EEEECCCCCCCCCCC
28.8124117733
121PhosphorylationYARPSSASIRDANLY
EECCCCCCCCCCCEE
21.8024117733
135PhosphorylationYVSGLPKTMTQKELE
EECCCCCCCCHHHHH
24.4230631047
137PhosphorylationSGLPKTMTQKELEQL
CCCCCCCCHHHHHHH
41.5430622161
146PhosphorylationKELEQLFSQYGRIIT
HHHHHHHHHHHHHHH
30.9630622161
148PhosphorylationLEQLFSQYGRIITSR
HHHHHHHHHHHHHHH
13.7430622161
153PhosphorylationSQYGRIITSRILVDQ
HHHHHHHHHHHHHHH
15.0224719451
154PhosphorylationQYGRIITSRILVDQV
HHHHHHHHHHHHHHH
13.6024719451
162PhosphorylationRILVDQVTGISRGVG
HHHHHHHHCCCCCCC
24.1421406692
165PhosphorylationVDQVTGISRGVGFIR
HHHHHCCCCCCCEEE
25.0724719451
209UbiquitinationFANNPSQKTNQAILS
ECCCCCHHHHHHHHH
54.502189047
209 (in isoform 1)Ubiquitination-54.5021890473
209 (in isoform 2)Ubiquitination-54.5021890473
216PhosphorylationKTNQAILSQLYQSPN
HHHHHHHHHHHCCCC
16.4221406692
219PhosphorylationQAILSQLYQSPNRRY
HHHHHHHHCCCCCCC
10.1721406692
221PhosphorylationILSQLYQSPNRRYPG
HHHHHHCCCCCCCCC
15.587972035
315UbiquitinationIRDFNTNKCKGFGFV
EEECCCCCCCCEEEE
34.97-
323PhosphorylationCKGFGFVTMTNYDEA
CCCEEEEEECCHHHH
18.93-
336PhosphorylationEAAMAIASLNGYRLG
HHHHHHHHHCCCCCC
19.0922468782

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ELAV2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELAV2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ELAV2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROAA_HUMANHNRNPABphysical
20211142
HXC9_HUMANHOXC9physical
20211142
NR2E3_HUMANNR2E3physical
20211142
RFOX2_HUMANRBFOX2physical
20211142
ELAV3_HUMANELAVL3physical
28514442
RMXL1_HUMANRBMXL1physical
28514442
RPC8_HUMANPOLR3Hphysical
28514442
RBM45_HUMANRBM45physical
28514442
PUM2_HUMANPUM2physical
28514442
C19L2_HUMANCWF19L2physical
28514442
HNRC1_HUMANHNRNPCL1physical
28514442
SAFB2_HUMANSAFB2physical
28514442
PRP17_HUMANCDC40physical
28514442
YBOX2_HUMANYBX2physical
28514442
ZC11A_HUMANZC3H11Aphysical
28514442
RALY_HUMANRALYphysical
28514442
GCFC2_HUMANGCFC2physical
28514442
ABC3F_HUMANAPOBEC3Fphysical
28514442
YTDC1_HUMANYTHDC1physical
28514442
CLK2_HUMANCLK2physical
28514442
RBMS2_HUMANRBMS2physical
28514442
CRNL1_HUMANCRNKL1physical
28514442
SYF1_HUMANXAB2physical
28514442
PUM1_HUMANPUM1physical
28514442
CARF_HUMANCDKN2AIPphysical
28514442
PAI2B_HUMANPAIP2Bphysical
28514442
F120A_HUMANFAM120Aphysical
28514442
AQR_HUMANAQRphysical
28514442
SUV3_HUMANSUPV3L1physical
28514442
CASC3_HUMANCASC3physical
28514442
TFP11_HUMANTFIP11physical
28514442
C19L1_HUMANCWF19L1physical
28514442
ABC3B_HUMANAPOBEC3Bphysical
28514442
CCDC9_HUMANCCDC9physical
28514442
DGC14_HUMANDGCR14physical
28514442
SYF2_HUMANSYF2physical
28514442
MOV10_HUMANMOV10physical
28514442
ZC3HE_HUMANZC3H14physical
28514442
PHAX_HUMANPHAXphysical
28514442
SRSF8_HUMANSRSF8physical
28514442
HNRPC_HUMANHNRNPCphysical
28514442
RENT1_HUMANUPF1physical
28514442
CLK3_HUMANCLK3physical
28514442
ZFR_HUMANZFRphysical
28514442
LAR1B_HUMANLARP1Bphysical
28514442
SUGP2_HUMANSUGP2physical
28514442
ATX2_HUMANATXN2physical
28514442
IREB2_HUMANIREB2physical
28514442
ILF2_HUMANILF2physical
28514442
PAIP1_HUMANPAIP1physical
28514442
NCBP3_HUMANC17orf85physical
28514442
RBM22_HUMANRBM22physical
28514442
PININ_HUMANPNNphysical
28514442
STAU2_HUMANSTAU2physical
28514442
ZCH18_HUMANZC3H18physical
28514442
ZN346_HUMANZNF346physical
28514442
HNRL2_HUMANHNRNPUL2physical
28514442
GTPB3_HUMANGTPBP3physical
28514442
ZCHC3_HUMANZCCHC3physical
28514442
IF2B3_HUMANIGF2BP3physical
28514442
ZN326_HUMANZNF326physical
28514442
SAFB1_HUMANSAFBphysical
28514442
SRRT_HUMANSRRTphysical
28514442
HNRPR_HUMANHNRNPRphysical
28514442
CCD12_HUMANCCDC12physical
28514442
PABP4_HUMANPABPC4physical
28514442
ISY1_HUMANISY1physical
28514442
RBMX_HUMANRBMXphysical
28514442
ACINU_HUMANACIN1physical
28514442
RO60_HUMANTROVE2physical
28514442
PRKRA_HUMANPRKRAphysical
28514442
SRSF1_HUMANSRSF1physical
28514442
MKRN2_HUMANMKRN2physical
28514442
IF2B1_HUMANIGF2BP1physical
28514442
TRA2B_HUMANTRA2Bphysical
28514442
SNW1_HUMANSNW1physical
28514442
ALG13_HUMANALG13physical
28514442
PPIE_HUMANPPIEphysical
28514442
PABP1_HUMANPABPC1physical
28514442
MATR3_HUMANMATR3physical
28514442
DKC1_HUMANDKC1physical
28514442
IF2B2_HUMANIGF2BP2physical
28514442
RNPS1_HUMANRNPS1physical
28514442
HNRPL_HUMANHNRNPLphysical
28514442
LARP1_HUMANLARP1physical
28514442
SRRM2_HUMANSRRM2physical
28514442
SRS10_HUMANSRSF10physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
HNRPQ_HUMANSYNCRIPphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELAV2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASSSPECTROMETRY.

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