ENC1_HUMAN - dbPTM
ENC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENC1_HUMAN
UniProt AC O14682
Protein Name Ectoderm-neural cortex protein 1
Gene Name ENC1
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization Nucleus matrix . Cytoplasm . Cytoplasm, cytoskeleton .
Protein Description Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin-mediated proteasomal degradation mechanism..
Protein Sequence MSVSVHENRKSRASSGSINIYLFHKSSYADSVLTHLNLLRQQRLFTDVLLHAGNRTFPCHRAVLAACSRYFEAMFSGGLKESQDSEVNFDNSIHPEVLELLLDYAYSSRVIINEENAESLLEAGDMLEFQDIRDACAEFLEKNLHPTNCLGMLLLSDAHQCTKLYELSWRMCLSNFQTIRKNEDFLQLPQDMVVQLLSSEELETEDERLVYESAINWISYDLKKRYCYLPELLQTVRLALLPAIYLMENVAMEELITKQRKSKEIVEEAIRCKLKILQNDGVVTSLCARPRKTGHALFLLGGQTFMCDKLYLVDQKAKEIIPKADIPSPRKEFSACAIGCKVYITGGRGSENGVSKDVWVYDTLHEEWSKAAPMLVARFGHGSAELKHCLYVVGGHTAATGCLPASPSVSLKQVEHYDPTINKWTMVAPLREGVSNAAVVSAKLKLFAFGGTSVSHDKLPKVQCYDQCENRWTVPATCPQPWRYTAAAVLGNQIFIMGGDTEFSACSAYKFNSETYQWTKVGDVTAKRMSCHAVASGNKLYVVGGYFGIQRCKTLDCYDPTLDVWNSITTVPYSLIPTAFVSTWKHLPS
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
2Phosphorylation------MSVSVHENR
------CCCCCCCCC		24.0922496350
11PhosphorylationSVHENRKSRASSGSI
CCCCCCCHHCCCCCE		29.8229523821
14PhosphorylationENRKSRASSGSINIY
CCCCHHCCCCCEEEE		33.8422777824
15PhosphorylationNRKSRASSGSINIYL
CCCHHCCCCCEEEEE		35.2622777824
17PhosphorylationKSRASSGSINIYLFH
CHHCCCCCEEEEEEE		17.8929523821
26PhosphorylationNIYLFHKSSYADSVL
EEEEEECHHHHHHHH		21.7328258704
27PhosphorylationIYLFHKSSYADSVLT
EEEEECHHHHHHHHH		29.1928258704
28PhosphorylationYLFHKSSYADSVLTH
EEEECHHHHHHHHHH		22.8628258704
31PhosphorylationHKSSYADSVLTHLNL
ECHHHHHHHHHHHHH		15.7428258704
34PhosphorylationSYADSVLTHLNLLRQ
HHHHHHHHHHHHHHH		23.3528258704
46PhosphorylationLRQQRLFTDVLLHAG
HHHHHHHHHHHHCCC		29.7724719451
70PhosphorylationVLAACSRYFEAMFSG
HHHHHHHHHHHHHCC		6.89-
168PhosphorylationCTKLYELSWRMCLSN
HHHHHHHHHHHHHHC		10.7424719451
213PhosphorylationDERLVYESAINWISY
HHHHHHHHHHHHHCC		19.4326270265
219PhosphorylationESAINWISYDLKKRY
HHHHHHHCCCHHHCC		12.2826270265
220PhosphorylationSAINWISYDLKKRYC
HHHHHHCCCHHHCCC		19.0326270265
245PhosphorylationLALLPAIYLMENVAM
HHHHHHHHHHHHHHH		11.3422817900
263UbiquitinationITKQRKSKEIVEEAI
HHHHHHCHHHHHHHH		55.27-
285PhosphorylationQNDGVVTSLCARPRK
CCCCCEEEEECCCCC		15.1624719451
304PhosphorylationLFLLGGQTFMCDKLY
EEEECCCEECCCEEE		19.3319690332
316UbiquitinationKLYLVDQKAKEIIPK
EEEECCHHHHHHCCC		57.89-
318UbiquitinationYLVDQKAKEIIPKAD
EECCHHHHHHCCCCC		57.38-
331UbiquitinationADIPSPRKEFSACAI
CCCCCCCHHHCCCEE		67.50-
406PhosphorylationATGCLPASPSVSLKQ
CCCCCCCCCCCCHHH		18.7730576142
408PhosphorylationGCLPASPSVSLKQVE
CCCCCCCCCCHHHCE		23.1122617229
410PhosphorylationLPASPSVSLKQVEHY
CCCCCCCCHHHCEEC		33.9026434776
417PhosphorylationSLKQVEHYDPTINKW
CHHHCEECCCCCCEE		15.31-
423UbiquitinationHYDPTINKWTMVAPL
ECCCCCCEEEEEEEC		39.94-
435PhosphorylationAPLREGVSNAAVVSA
EECCCCCCHHHHHHH		31.4417924679
441PhosphorylationVSNAAVVSAKLKLFA
CCHHHHHHHEEEEEE		17.0617924679
443UbiquitinationNAAVVSAKLKLFAFG
HHHHHHHEEEEEEEC		38.3521906983
452PhosphorylationKLFAFGGTSVSHDKL
EEEEECCCCCCCCCC		26.74-
453PhosphorylationLFAFGGTSVSHDKLP
EEEECCCCCCCCCCC		25.54-
455PhosphorylationAFGGTSVSHDKLPKV
EECCCCCCCCCCCCC		26.24-
520UbiquitinationSETYQWTKVGDVTAK
CCEEEEEEECCEEEC		41.0621906983
527UbiquitinationKVGDVTAKRMSCHAV
EECCEEECCCEEEEE		38.9921906983
530PhosphorylationDVTAKRMSCHAVASG
CEEECCCEEEEEEEC		13.5424425749
541PhosphorylationVASGNKLYVVGGYFG
EEECCEEEEECCEEC		8.4924425749
569PhosphorylationLDVWNSITTVPYSLI
CCCHHCCCCCCHHHC		22.8918452278
570PhosphorylationDVWNSITTVPYSLIP
CCHHCCCCCCHHHCC		20.1518452278
573PhosphorylationNSITTVPYSLIPTAF
HCCCCCCHHHCCCHH		16.2718452278
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 ENC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENC1_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 ENC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
15983046
RBX1_HUMANRBX1physical
15983046
ACTB_HUMANACTBphysical
15208678
NF2L2_HUMANNFE2L2physical
20511222
ENC1_HUMANENC1physical
16306221
ENC1_HUMANENC1physical
15983046
SQSTM_HUMANSQSTM1physical
26637326
KLH25_HUMANKLHL25physical
28514442
NUDC3_HUMANNUDCD3physical
28514442
PLIN5_HUMANPLIN5physical
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 ENC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-441, ANDMASS SPECTROMETRY.

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