AT133_HUMAN - dbPTM
AT133_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT133_HUMAN
UniProt AC Q9H7F0
Protein Name Probable cation-transporting ATPase 13A3
Gene Name ATP13A3
Organism Homo sapiens (Human).
Sequence Length 1226
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MDREERKTINQGQEDEMEIYGYNLSRWKLAIVSLGVICSGGFLLLLLYWMPEWRVKATCVRAAIKDCEVVLLRTTDEFKMWFCAKIRVLSLETYPVSSPKSMSNKLSNGHAVCLIENPTEENRHRISKYSQTESQQIRYFTHHSVKYFWNDTIHNFDFLKGLDEGVSCTSIYEKHSAGLTKGMHAYRKLLYGVNEIAVKVPSVFKLLIKEVLNPFYIFQLFSVILWSTDEYYYYALAIVVMSIVSIVSSLYSIRKQYVMLHDMVATHSTVRVSVCRVNEEIEEIFSTDLVPGDVMVIPLNGTIMPCDAVLINGTCIVNESMLTGESVPVTKTNLPNPSVDVKGIGDELYNPETHKRHTLFCGTTVIQTRFYTGELVKAIVVRTGFSTSKGQLVRSILYPKPTDFKLYRDAYLFLLCLVAVAGIGFIYTIINSILNEVQVGVIIIESLDIITITVPPALPAAMTAGIVYAQRRLKKIGIFCISPQRINICGQLNLVCFDKTGTLTEDGLDLWGIQRVENARFLSPEENVCNEMLVKSQFVACMATCHSLTKIEGVLSGDPLDLKMFEAIGWILEEATEEETALHNRIMPTVVRPPKQLLPESTPAGNQEMELFELPATYEIGIVRQFPFSSALQRMSVVARVLGDRKMDAYMKGAPEAIAGLCKPETVPVDFQNVLEDFTKQGFRVIALAHRKLESKLTWHKVQNISRDAIENNMDFMGLIIMQNKLKQETPAVLEDLHKANIRTVMVTGDSMLTAVSVARDCGMILPQDKVIIAEALPPKDGKVAKINWHYADSLTQCSHPSAIDPEAIPVKLVHDSLEDLQMTRYHFAMNGKSFSVILEHFQDLVPKLMLHGTVFARMAPDQKTQLIEALQNVDYFVGMCGDGANDCGALKRAHGGISLSELEASVASPFTSKTPSISCVPNLIREGRAALITSFCVFKFMALYSIIQYFSVTLLYSILSNLGDFQFLFIDLAIILVVVFTMSLNPAWKELVAQRPPSGLISGALLFSVLSQIIICIGFQSLGFFWVKQQPWYEVWHPKSDACNTTGSGFWNSSHVDNETELDEHNIQNYENTTVFFISSFQYLIVAIAFSKGKPFRQPCYKNYFFVFSVIFLYIFILFIMLYPVASVDQVLQIVCVPYQWRVTMLIIVLVNAFVSITVEESVDRWGKCCLPWALGCRKKTPKAKYMYLAQELLVDPEWPPKPQTTTEAKALVKENGSCQIITIT
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
8PhosphorylationMDREERKTINQGQED
CCHHHHHCCCCCCCC		31.2318452278
33PhosphorylationRWKLAIVSLGVICSG
HHHEEHHHHHCCCCH		17.1928111955
39PhosphorylationVSLGVICSGGFLLLL
HHHHCCCCHHHHHHH		30.7228111955
65UbiquitinationTCVRAAIKDCEVVLL
HHHHHHHCCCEEEEE		52.15-
65 (in isoform 2)Ubiquitination-52.1521906983
74PhosphorylationCEVVLLRTTDEFKMW
CEEEEEEECHHHHHH		38.2722210691
75PhosphorylationEVVLLRTTDEFKMWF
EEEEEEECHHHHHHH		27.3922210691
78 (in isoform 2)Ubiquitination-7.9621906983
85AcetylationFKMWFCAKIRVLSLE
HHHHHEEEEEEEEEE		32.0220167786
90PhosphorylationCAKIRVLSLETYPVS
EEEEEEEEEEECCCC		22.69-
93PhosphorylationIRVLSLETYPVSSPK
EEEEEEEECCCCCCC		38.1228450419
94PhosphorylationRVLSLETYPVSSPKS
EEEEEEECCCCCCCH		7.7130108239
97PhosphorylationSLETYPVSSPKSMSN
EEEECCCCCCCHHHC		36.1030266825
98PhosphorylationLETYPVSSPKSMSNK
EEECCCCCCCHHHCC		36.2630266825
100 (in isoform 1)Ubiquitination-61.8221906983
100UbiquitinationTYPVSSPKSMSNKLS
ECCCCCCCHHHCCCC		61.8221906983
100 (in isoform 2)Ubiquitination-61.8221906983
103PhosphorylationVSSPKSMSNKLSNGH
CCCCCHHHCCCCCCE		37.5930108239
107PhosphorylationKSMSNKLSNGHAVCL
CHHHCCCCCCEEEEE		42.2330108239
112 (in isoform 2)Ubiquitination-1.9621906983
127PhosphorylationEENRHRISKYSQTES
HHHCHHHHCCCCCHH		26.0428450419
128 (in isoform 1)Ubiquitination-46.6921906983
128UbiquitinationENRHRISKYSQTESQ
HHCHHHHCCCCCHHH		46.6921906983
129PhosphorylationNRHRISKYSQTESQQ
HCHHHHCCCCCHHHH		10.1430108239
130PhosphorylationRHRISKYSQTESQQI
CHHHHCCCCCHHHHH		34.0728450419
132PhosphorylationRISKYSQTESQQIRY
HHHCCCCCHHHHHHH		31.5028450419
134PhosphorylationSKYSQTESQQIRYFT
HCCCCCHHHHHHHHH		30.6730108239
139PhosphorylationTESQQIRYFTHHSVK
CHHHHHHHHHHHCHH		17.9227642862
144PhosphorylationIRYFTHHSVKYFWND
HHHHHHHCHHHHCCC		16.8227642862
160UbiquitinationIHNFDFLKGLDEGVS
CCCCHHHCCCCCCCC		58.37-
174UbiquitinationSCTSIYEKHSAGLTK
CCCHHHHHHCCCCCC		26.36-
181UbiquitinationKHSAGLTKGMHAYRK
HHCCCCCCHHHHHHH		60.32-
188UbiquitinationKGMHAYRKLLYGVNE
CHHHHHHHHHHCCCH		30.1221906983
188 (in isoform 1)Ubiquitination-30.1221906983
191PhosphorylationHAYRKLLYGVNEIAV
HHHHHHHHCCCHHHC		29.48-
252PhosphorylationSIVSSLYSIRKQYVM
HHHHHHHHHHHHHHH		22.6224719451
342UbiquitinationPNPSVDVKGIGDELY
CCCCCCCCCCCCCCC		40.1121906983
342 (in isoform 1)Ubiquitination-40.1121906983
349PhosphorylationKGIGDELYNPETHKR
CCCCCCCCCCCCCCC		26.99-
355 (in isoform 1)Ubiquitination-53.9821906983
355UbiquitinationLYNPETHKRHTLFCG
CCCCCCCCCCEEEEC		53.9821906983
371PhosphorylationTVIQTRFYTGELVKA
EEEEEEECCCCEEEE		15.5628102081
372PhosphorylationVIQTRFYTGELVKAI
EEEEEECCCCEEEEE		22.8228102081
377 (in isoform 1)Ubiquitination-45.0521906983
377UbiquitinationFYTGELVKAIVVRTG
ECCCCEEEEEEEECC		45.0521906983
389 (in isoform 1)Ubiquitination-51.2521906983
389UbiquitinationRTGFSTSKGQLVRSI
ECCCCCCCCCEEEEE		51.2521906983
450 (in isoform 2)Ubiquitination-1.9721906983
523PhosphorylationVENARFLSPEENVCN
CCCCCCCCCCCCCHH		27.7922817900
556PhosphorylationTKIEGVLSGDPLDLK
HEEECHHCCCCCCHH		38.4523898821
615 (in isoform 2)Ubiquitination-18.5021906983
696UbiquitinationAHRKLESKLTWHKVQ
CCHHHHHCCCHHHCC		40.33-
727UbiquitinationIIMQNKLKQETPAVL
HHHHHHHCCCCHHHH		47.9321906983
727 (in isoform 1)Ubiquitination-47.9321906983
739UbiquitinationAVLEDLHKANIRTVM
HHHHHHHHCCCCEEE		50.88-
744PhosphorylationLHKANIRTVMVTGDS
HHHCCCCEEEECCCH		14.7928270605
748PhosphorylationNIRTVMVTGDSMLTA
CCCEEEECCCHHHHH		19.7128270605
751PhosphorylationTVMVTGDSMLTAVSV
EEEECCCHHHHHHHH		19.6228270605
754PhosphorylationVTGDSMLTAVSVARD
ECCCHHHHHHHHHHH		19.1728270605
757PhosphorylationDSMLTAVSVARDCGM
CHHHHHHHHHHHCCC		13.9528270605
780UbiquitinationIAEALPPKDGKVAKI
EEEECCCCCCCEEEE		76.73-
817PhosphorylationPVKLVHDSLEDLQMT
CEEEECCCHHHHHHH		20.8429255136
824PhosphorylationSLEDLQMTRYHFAMN
CHHHHHHHEEEEHHC		18.3423927012
892UbiquitinationANDCGALKRAHGGIS
HHHHHHHHHHCCCCC		47.182190698
892 (in isoform 1)Ubiquitination-47.1821906983
909PhosphorylationELEASVASPFTSKTP
HHHHHHCCCCCCCCC		20.56-
914UbiquitinationVASPFTSKTPSISCV
HCCCCCCCCCCCCHH		62.49-
1169UbiquitinationESVDRWGKCCLPWAL
CCCHHHHHCHHHHHC		18.15-
1187PhosphorylationKKTPKAKYMYLAQEL
CCCCHHHHHHHHHHH		8.8928270605
1189PhosphorylationTPKAKYMYLAQELLV
CCHHHHHHHHHHHHC		8.8728270605
1206PhosphorylationEWPPKPQTTTEAKAL
CCCCCCCCCHHHHHH		44.1826657352
1207PhosphorylationWPPKPQTTTEAKALV
CCCCCCCCHHHHHHH		19.8628270605
1208PhosphorylationPPKPQTTTEAKALVK
CCCCCCCHHHHHHHH		37.0228270605
1215UbiquitinationTEAKALVKENGSCQI
HHHHHHHHHCCCEEE		46.44-
1219PhosphorylationALVKENGSCQIITIT
HHHHHCCCEEEEEEC		17.9030576142
1224PhosphorylationNGSCQIITIT-----
CCCEEEEEEC-----		21.8628102081
1226PhosphorylationSCQIITIT-------
CEEEEEEC-------		24.7328102081
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 AT133_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT133_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 AT133_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AT133_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 AT133_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, 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-98 AND SER-817, AND MASSSPECTROMETRY.
"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-98 AND SER-817, AND MASSSPECTROMETRY.
"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-817, AND MASSSPECTROMETRY.

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