AEBP1_HUMAN - dbPTM
AEBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AEBP1_HUMAN
UniProt AC Q8IUX7
Protein Name Adipocyte enhancer-binding protein 1
Gene Name AEBP1
Organism Homo sapiens (Human).
Sequence Length 1158
Subcellular Localization Isoform 1: Secreted .
Isoform 2: Cytoplasm . Nucleus .
Protein Description May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor..
Protein Sequence MAAVRGAPLLSCLLALLALCPGGRPQTVLTDDEIEEFLEGFLSELEPEPREDDVEAPPPPEPTPRVRKAQAGGKPGKRPGTAAEVPPEKTKDKGKKGKKDKGPKVPKESLEGSPRPPKKGKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPPSGKRPPILAPSETLEWPLPPPPSPGPEELPQEGGAPLSNNWQNPGEETHVEAREHQPEPEEETEQPTLDYNDQIEREDYEDFEYIRRQKQPRPPPSRRRRPERVWPEPPEEKAPAPAPEERIEPPVKPLLPPLPPDYGDGYVIPNYDDMDYYFGPPPPQKPDAERQTDEEKEELKKPKKEDSSPKEETDKWAVEKGKDHKEPRKGEELEEEWTPTEKVKCPPIGMESHRIEDNQIRASSMLRHGLGAQRGRLNMQTGATEDDYYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGCSVAPVYSYYAQNEVVATDDLDFRHHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCREYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWVPYRVPNNNLPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTQEQLLAAAMAAARGEDEDEVSEAQETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGMGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHESELPREWENNKEALLTFMEQVHRGIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTPSAKTCNVDYDIGATQCNFILARSNWKRIREIMAMNGNRPIPHIDPSRPMTPQQRRLQQRRLQHRLRLRAQMRLRRLNATTTLGPHTVPPTLPPAPATTLSTTIEPWGLIPPTTAGWEESETETYTEVVTEFGTEVEPEFGTKVEPEFETQLEPEFETQLEPEFEEEEEEEKEEEIATGQAFPFTTVETYTVNFGDF
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
95AcetylationEKTKDKGKKGKKDKG
HHCCCCCCCCCCCCC		65.187265039
96AcetylationKTKDKGKKGKKDKGP
HCCCCCCCCCCCCCC		82.007265049
109PhosphorylationGPKVPKESLEGSPRP
CCCCCHHHCCCCCCC		37.5423312004
113PhosphorylationPKESLEGSPRPPKKG
CHHHCCCCCCCCCCC		14.3669467865
134AcetylationATKKPKEKPPKATKK
CCCCCCCCCCCCCCC		73.147978621
137AcetylationKPKEKPPKATKKPKE
CCCCCCCCCCCCCCC		76.777978631
145AcetylationATKKPKEKPPKATKK
CCCCCCCCCCCCCCC		73.147978641
148AcetylationKPKEKPPKATKKPKE
CCCCCCCCCCCCCCC		76.777978651
156AcetylationATKKPKEKPPKATKK
CCCCCCCCCCCCCCC		73.147978661
159AcetylationKPKEKPPKATKKPPS
CCCCCCCCCCCCCCC		76.777978671
176O-linked_GlycosylationRPPILAPSETLEWPL
CCCCCCCCCCCCCCC		37.29OGP
188O-linked_GlycosylationWPLPPPPSPGPEELP
CCCCCCCCCCCCCCC		48.54OGP
203O-linked_GlycosylationQEGGAPLSNNWQNPG
CCCCCCCCCCCCCCC		27.36OGP
228O-linked_GlycosylationQPEPEEETEQPTLDY
CCCCCCCCCCCCCCC		43.11OGP
228PhosphorylationQPEPEEETEQPTLDY
CCCCCCCCCCCCCCC		43.11113325363
232PhosphorylationEEETEQPTLDYNDQI
CCCCCCCCCCCCCCC		31.77113325369
232O-linked_GlycosylationEEETEQPTLDYNDQI
CCCCCCCCCCCCCCC		31.77OGP
347PhosphorylationKKPKKEDSSPKEETD
HCCCCCCCCCCHHHH		50.0226657352
404PhosphorylationDNQIRASSMLRHGLG
CCCHHHHHHHHHCCC		22.3519664995
429PhosphorylationGATEDDYYDGAWCAE
CCCCCCCCCCCEECC		18.2023872183
523PhosphorylationVARFIRIYPLTWNGS
HHHEEEEEEECCCCC		5.1524260401
526PhosphorylationFIRIYPLTWNGSLCM
EEEEEEECCCCCCCC		16.6324260401
528N-linked_GlycosylationRIYPLTWNGSLCMRL
EEEEECCCCCCCCEE		25.5819159218
530PhosphorylationYPLTWNGSLCMRLEV
EEECCCCCCCCEEEE		18.3824260401
575UbiquitinationKDMRQLMKVVNEECP
HHHHHHHHHHHCCCC		52.18-
592UbiquitinationTRTYSLGKSSRGLKI
EEEEECCCCCCCCEE		51.02-
598AcetylationGKSSRGLKIYAMEIS
CCCCCCCEEEEEEEC		36.1720167786
716UbiquitinationLWGAEERKWVPYRVP
CCCCCCCCCCCCCCC		56.68-
884PhosphorylationCDKFPHESELPREWE
CCCCCCCCCCCCCHH		41.2020860994
894UbiquitinationPREWENNKEALLTFM
CCCHHCCHHHHHHHH		56.8129967540
922N-linked_GlycosylationEQGIPIANATISVSG
CCCCEECCEEEEEEC		38.0319159218
1083O-linked_GlycosylationAGWEESETETYTEVV
CCCCCCCCEEEEEHH		42.79OGP
1087O-linked_GlycosylationESETETYTEVVTEFG
CCCCEEEEEHHHCCC		29.71OGP
1091O-linked_GlycosylationETYTEVVTEFGTEVE
EEEEEHHHCCCCEEC		30.67OGP
1095O-linked_GlycosylationEVVTEFGTEVEPEFG
EHHHCCCCEECCCCC		42.02OGP
1146O-linked_GlycosylationTGQAFPFTTVETYTV
HCCCCCCEEEEEEEE		30.12OGP
1147O-linked_GlycosylationGQAFPFTTVETYTVN
CCCCCCEEEEEEEEE		19.41OGP
1152O-linked_GlycosylationFTTVETYTVNFGDF-
CEEEEEEEEECCCC-		19.18OGP
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 AEBP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AEBP1_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 AEBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AEBP1_HUMAN !!
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 AEBP1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-922, AND MASSSPECTROMETRY.

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