ATP9A_HUMAN - dbPTM
ATP9A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATP9A_HUMAN
UniProt AC O75110
Protein Name Probable phospholipid-transporting ATPase IIA
Gene Name ATP9A
Organism Homo sapiens (Human).
Sequence Length 1047
Subcellular Localization Early endosome membrane
Multi-pass membrane protein . Recycling endosome . Golgi apparatus, trans-Golgi network membrane . Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.
Protein Description
Protein Sequence MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIREAVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFTREDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEVNCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSWVIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDEVQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTDQAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQIFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLVVAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVRPTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLTCAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSAALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKSEVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTSLILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVITLVSCLPLYVLKYLRRRFSPPSYSKLTS
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
2Acetylation------MTDNIPLQP
------CCCCCCCCC		49.4022814378
14"N6,N6-dimethyllysine"LQPVRQKKRMDSRPR
CCCCCCCCCCCCCCC		44.62-
14MethylationLQPVRQKKRMDSRPR
CCCCCCCCCCCCCCC		44.6223644510
24S-palmitoylationDSRPRAGCCEWLRCC
CCCCCCCCCHHHHHC		1.5329575903
25S-palmitoylationSRPRAGCCEWLRCCG
CCCCCCCCHHHHHCC		4.0429575903
48UbiquitinationVWLGHPEKRDQRYPR
EECCCHHHCCCCCCC		66.7721890473
48 (in isoform 2)Ubiquitination-66.7721890473
48 (in isoform 1)Ubiquitination-66.7721890473
128PhosphorylationAVEEIRCYVRDKEVN
HHHHHHEEECCCCCH		6.67-
181UbiquitinationIFLRTSEKNGSCFLR
EEEEECCCCCEEEEE		67.39-
196PhosphorylationTDQLDGETDWKLRLP
ECCCCCCCCEEEEEC		53.3325003641
199UbiquitinationLDGETDWKLRLPVAC
CCCCCCEEEEECCEE		26.92-
282PhosphorylationYTGRELRSVMNTSNP
ECCHHHHHHHHCCCC		38.04-
326 (in isoform 2)Ubiquitination-21.51-
346PhosphorylationFSNIIPISLRVNLDM
HCCCCCEEEEEECCC		12.55-
358PhosphorylationLDMGKIVYSWVIRRD
CCCCCEEEEEEEECC		10.5726074081
359PhosphorylationDMGKIVYSWVIRRDS
CCCCEEEEEEEECCC		12.1726074081
366PhosphorylationSWVIRRDSKIPGTVV
EEEEECCCCCCCEEE		30.5823927012
367UbiquitinationWVIRRDSKIPGTVVR
EEEECCCCCCCEEEE		58.15-
371PhosphorylationRDSKIPGTVVRSSTI
CCCCCCCEEEECCCC		15.52-
375PhosphorylationIPGTVVRSSTIPEQL
CCCEEEECCCCCHHH		21.8923312004
376PhosphorylationPGTVVRSSTIPEQLG
CCEEEECCCCCHHHC		21.5723312004
377PhosphorylationGTVVRSSTIPEQLGR
CEEEECCCCCHHHCC		41.6223312004
386PhosphorylationPEQLGRISYLLTDKT
CHHHCCCEEEEECCC		14.36-
390PhosphorylationGRISYLLTDKTGTLT
CCCEEEEECCCCCCC		32.62-
392UbiquitinationISYLLTDKTGTLTQN
CEEEEECCCCCCCCC		43.55-
404UbiquitinationTQNEMIFKRLHLGTV
CCCHHHHHHHCHHHH		43.03-
410PhosphorylationFKRLHLGTVAYGLDS
HHHHCHHHHHHCCCC		14.3426074081
413PhosphorylationLHLGTVAYGLDSMDE
HCHHHHHHCCCCHHH		17.5526074081
417PhosphorylationTVAYGLDSMDEVQSH
HHHHCCCCHHHHHHH		32.9326074081
447UbiquitinationKGPTLTTKVRRTMSS
CCCCHHHHHHHHHHH		28.63-
486UbiquitinationTDQAEAEKQYEDSCR
CCHHHHHHHHHHCCE		66.29-
488PhosphorylationQAEAEKQYEDSCRVY
HHHHHHHHHHCCEEE		32.5425884760
545PhosphorylationILQIFPFTYESKRMG
EEEEECCEECCCCCE		26.98-
604UbiquitinationRVLVVAKKSLAEEQY
HHEEEECCCHHHHHH		40.75-
622UbiquitinationEARYVQAKLSVHDRS
HHHHHHHHHHHHCCC		24.97-
629PhosphorylationKLSVHDRSLKVATVI
HHHHHCCCHHHHHHH		38.3029514088
638PhosphorylationKVATVIESLEMEMEL
HHHHHHHHHHHHHHH		20.64-
680UbiquitinationVWMLTGDKLETATCT
EEEEECCCCCEEEEE		49.95-
765UbiquitinationCRCAPTQKAQIVRLL
ECCCCCCHHHHHHHH		44.74-
778UbiquitinationLLQERTGKLTCAVGD
HHHHHHCCCEEEECC		39.76-
790 (in isoform 2)Ubiquitination-4.92-
805UbiquitinationCGVGVEGKEGKQASL
CCCCCCCCCCCHHHH		50.19-
808AcetylationGVEGKEGKQASLAAD
CCCCCCCCHHHHHCC		43.7230587101
811PhosphorylationGKEGKQASLAADFSI
CCCCCHHHHHCCCEE		18.95-
822AcetylationDFSITQFKHLGRLLM
CCEEEHHHHHCCEEE		28.2730587107
899UbiquitinationLVLDKDVKSEVAMLY
HHHCCCHHHHHHHHC		51.54-
900PhosphorylationVLDKDVKSEVAMLYP
HHCCCHHHHHHHHCH		36.8329083192
906PhosphorylationKSEVAMLYPELYKDL
HHHHHHHCHHHHHHH		4.9929083192
910PhosphorylationAMLYPELYKDLLKGR
HHHCHHHHHHHHCCC		10.7829083192
911UbiquitinationMLYPELYKDLLKGRP
HHCHHHHHHHHCCCC		55.30-
1044UbiquitinationFSPPSYSKLTS----
CCCCCHHHCCC----		47.77-
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 ATP9A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATP9A_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 ATP9A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP3_HUMANABCC3physical
26344197
ACADM_HUMANACADMphysical
26344197
AT2B4_HUMANATP2B4physical
26344197
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 ATP9A_HUMAN

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Related Literatures of Post-Translational Modification

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