AAGAB_HUMAN - dbPTM
AAGAB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAGAB_HUMAN
UniProt AC Q6PD74
Protein Name Alpha- and gamma-adaptin-binding protein p34
Gene Name AAGAB
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Cytoplasm, cytosol .
Protein Description May be involved in endocytic recycling of growth factor receptors such as EGFR..
Protein Sequence MAAGVPCALVTSCSSVFSGDQLVQHILGTEDLIVEVTSNDAVRFYPWTIDNKYYSADINLCVVPNKFLVTAEIAESVQAFVVYFDSTQKSGLDSVSSWLPLAKAWLPEVMILVCDRVSEDGINRQKAQEWCIKHGFELVELSPEELPEEDDDFPESTGVKRIVQALNANVWSNVVMKNDRNQGFSLLNSLTGTNHSIGSADPCHPEQPHLPAADSTESLSDHRGGASNTTDAQVDSIVDPMLDLDIQELASLTTGGGDVENFERLFSKLKEMKDKAATLPHEQRKVHAEKVAKAFWMAIGGDRDEIEGLSSDEEH
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
17UbiquitinationVTSCSSVFSGDQLVQ
EECCCCCCCHHHHHH		7.94-
17UbiquitinationVTSCSSVFSGDQLVQ
EECCCCCCCHHHHHH		7.9429967540
51UbiquitinationFYPWTIDNKYYSADI
ECEEEECCCEEECCE		30.31-
51UbiquitinationFYPWTIDNKYYSADI
ECEEEECCCEEECCE		30.3122505724
68UbiquitinationCVVPNKFLVTAEIAE
EEECCCEEEEHHHHH		3.41-
118PhosphorylationILVCDRVSEDGINRQ
EEEECCCCCCCCCHH		30.75113321961
126UbiquitinationEDGINRQKAQEWCIK
CCCCCHHHHHHHHHH		49.1229967540
160UbiquitinationFPESTGVKRIVQALN
CCCCHHHHHHHHHHC		37.4422505724
166UbiquitinationVKRIVQALNANVWSN
HHHHHHHHCCCCHHC		3.30-
166UbiquitinationVKRIVQALNANVWSN
HHHHHHHHCCCCHHC		3.3033845483
172PhosphorylationALNANVWSNVVMKND
HHCCCCHHCEEEECC		18.5718330067
176UbiquitinationNVWSNVVMKNDRNQG
CCHHCEEEECCCCCC		2.6729967540
177UbiquitinationVWSNVVMKNDRNQGF
CHHCEEEECCCCCCC		44.05-
184AcetylationKNDRNQGFSLLNSLT
ECCCCCCCHHHHHHC		3.15-
189PhosphorylationQGFSLLNSLTGTNHS
CCCHHHHHHCCCCCC		27.5528348404
191PhosphorylationFSLLNSLTGTNHSIG
CHHHHHHCCCCCCCC		41.6128348404
193PhosphorylationLLNSLTGTNHSIGSA
HHHHHCCCCCCCCCC		25.2328348404
196PhosphorylationSLTGTNHSIGSADPC
HHCCCCCCCCCCCCC		30.6228348404
199PhosphorylationGTNHSIGSADPCHPE
CCCCCCCCCCCCCCC		28.0328348404
215PhosphorylationPHLPAADSTESLSDH
CCCCCCCCCCCCCCC		29.3729496963
216PhosphorylationHLPAADSTESLSDHR
CCCCCCCCCCCCCCC		30.0929496963
218PhosphorylationPAADSTESLSDHRGG
CCCCCCCCCCCCCCC		33.0128348404
220PhosphorylationADSTESLSDHRGGAS
CCCCCCCCCCCCCCC		40.4228348404
254PhosphorylationQELASLTTGGGDVEN
HHHHHCCCCCCCHHH		38.8446156157
267PhosphorylationENFERLFSKLKEMKD
HHHHHHHHHHHHHHH		41.4924719451
270UbiquitinationERLFSKLKEMKDKAA
HHHHHHHHHHHHHHH		60.54-
275UbiquitinationKLKEMKDKAATLPHE
HHHHHHHHHHCCCHH		34.1133845483
2752-HydroxyisobutyrylationKLKEMKDKAATLPHE
HHHHHHHHHHCCCHH		34.11-
278PhosphorylationEMKDKAATLPHEQRK
HHHHHHHCCCHHHHH		45.7619531485
285UbiquitinationTLPHEQRKVHAEKVA
CCCHHHHHHHHHHHH		37.7629967540
290AcetylationQRKVHAEKVAKAFWM
HHHHHHHHHHHHHHH		48.5625953088
293AcetylationVHAEKVAKAFWMAIG
HHHHHHHHHHHHHHC		47.2922424773
310PhosphorylationRDEIEGLSSDEEH--
HHHHCCCCCCCCC--		46.7522167270
311PhosphorylationDEIEGLSSDEEH---
HHHCCCCCCCCC---		54.8328176443
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 AAGAB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAGAB_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 AAGAB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3C_HUMANEIF3Cphysical
16169070
AP1S3_HUMANAP1S3physical
25416956
AP2S1_HUMANAP2S1physical
26186194
EDRF1_HUMANEDRF1physical
26186194
STX4_HUMANSTX4physical
26186194
AP1S3_HUMANAP1S3physical
26186194
AP1S2_HUMANAP1S2physical
26186194
AP2A1_HUMANAP2A1physical
26186194
AP2A2_HUMANAP2A2physical
26186194
STXB3_HUMANSTXBP3physical
26186194
AP1G1_HUMANAP1G1physical
26186194
ASAH1_HUMANASAH1physical
26186194
AP1G2_HUMANAP1G2physical
26186194
AP1S3_HUMANAP1S3physical
28514442
ASAH1_HUMANASAH1physical
28514442
EDRF1_HUMANEDRF1physical
28514442
AP2A2_HUMANAP2A2physical
28514442
AP2A1_HUMANAP2A1physical
28514442
AP1G1_HUMANAP1G1physical
28514442
STX4_HUMANSTX4physical
28514442
STXB3_HUMANSTXBP3physical
28514442
CCD32_HUMANC15orf57physical
28514442
AP1G2_HUMANAP1G2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
148600Keratoderma, palmoplantar, punctate 1A (PPKP1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AAGAB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-310 AND SER-311, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-311, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-311, ANDMASS SPECTROMETRY.

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