AT132_HUMAN - dbPTM
AT132_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT132_HUMAN
UniProt AC Q9NQ11
Protein Name Cation-transporting ATPase 13A2
Gene Name ATP13A2 {ECO:0000312|HGNC:HGNC:30213}
Organism Homo sapiens (Human).
Sequence Length 1180
Subcellular Localization Membrane
Multi-pass membrane protein. Lysosome . Lysosome membrane .
Protein Description ATPase that plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity. [PubMed: 22186024 Required for a proper lysosomal and mitochondrial maintenance]
Protein Sequence MSADSSPLVGSTPTGYGTLTIGTSIDPLSSSVSSVRLSGYCGSPWRVIGYHVVVWMMAGIPLLLFRWKPLWGVRLRLRPCNLAHAETLVIEIRDKEDSSWQLFTVQVQTEAIGEGSLEPSPQSQAEDGRSQAAVGAVPEGAWKDTAQLHKSEEAVSVGQKRVLRYYLFQGQRYIWIETQQAFYQVSLLDHGRSCDDVHRSRHGLSLQDQMVRKAIYGPNVISIPVKSYPQLLVDEALNPYYGFQAFSIALWLADHYYWYALCIFLISSISICLSLYKTRKQSQTLRDMVKLSMRVCVCRPGGEEEWVDSSELVPGDCLVLPQEGGLMPCDAALVAGECMVNESSLTGESIPVLKTALPEGLGPYCAETHRRHTLFCGTLILQARAYVGPHVLAVVTRTGFCTAKGGLVSSILHPRPINFKFYKHSMKFVAALSVLALLGTIYSIFILYRNRVPLNEIVIRALDLVTVVVPPALPAAMTVCTLYAQSRLRRQGIFCIHPLRINLGGKLQLVCFDKTGTLTEDGLDVMGVVPLKGQAFLPLVPEPRRLPVGPLLRALATCHALSRLQDTPVGDPMDLKMVESTGWVLEEEPAADSAFGTQVLAVMRPPLWEPQLQAMEEPPVPVSVLHRFPFSSALQRMSVVVAWPGATQPEAYVKGSPELVAGLCNPETVPTDFAQMLQSYTAAGYRVVALASKPLPTVPSLEAAQQLTRDTVEGDLSLLGLLVMRNLLKPQTTPVIQALRRTRIRAVMVTGDNLQTAVTVARGCGMVAPQEHLIIVHATHPERGQPASLEFLPMESPTAVNGVKDPDQAASYTVEPDPRSRHLALSGPTFGIIVKHFPKLLPKVLVQGTVFARMAPEQKTELVCELQKLQYCVGMCGDGANDCGALKAADVGISLSQAEASVVSPFTSSMASIECVPMVIREGRCSLDTSFSVFKYMALYSLTQFISVLILYTINTNLGDLQFLAIDLVITTTVAVLMSRTGPALVLGRVRPPGALLSVPVLSSLLLQMVLVTGVQLGGYFLTLAQPWFVPLNRTVAAPDNLPNYENTVVFSLSSFQYLILAAAVSKGAPFRRPLYTNVPFLVALALLSSVLVGLVLVPGLLQGPLALRNITDTGFKLLLLGLVTLNFVGAFMLESVLDQCLPACLRRLRPKRASKKRFKQLERELAEQPWPPLPAGPLR
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
6Phosphorylation--MSADSSPLVGSTP
--CCCCCCCCCCCCC		23.8519690332
11PhosphorylationDSSPLVGSTPTGYGT
CCCCCCCCCCCCCEE		24.5919690332
12PhosphorylationSSPLVGSTPTGYGTL
CCCCCCCCCCCCEEE		20.9519690332
14PhosphorylationPLVGSTPTGYGTLTI
CCCCCCCCCCEEEEE		43.0219690332
16PhosphorylationVGSTPTGYGTLTIGT
CCCCCCCCEEEEECC		14.9319690332
18PhosphorylationSTPTGYGTLTIGTSI
CCCCCCEEEEECCCC		16.5519690332
23PhosphorylationYGTLTIGTSIDPLSS
CEEEEECCCCCCCCC		20.7519690332
24PhosphorylationGTLTIGTSIDPLSSS
EEEEECCCCCCCCCC		21.5619690332
29PhosphorylationGTSIDPLSSSVSSVR
CCCCCCCCCCCCEEE		26.4219690332
30PhosphorylationTSIDPLSSSVSSVRL
CCCCCCCCCCCEEEE		42.3019690332
34PhosphorylationPLSSSVSSVRLSGYC
CCCCCCCEEEECCCC		14.7619690332
68UbiquitinationPLLLFRWKPLWGVRL
CEEEHHCCCCCCCEE		26.4421890473
68UbiquitinationPLLLFRWKPLWGVRL
CEEEHHCCCCCCCEE		26.4421890473
68UbiquitinationPLLLFRWKPLWGVRL
CEEEHHCCCCCCCEE		26.4421890473
68 (in isoform 1)Ubiquitination-26.4421890473
143UbiquitinationAVPEGAWKDTAQLHK
CCCCCCCCCHHHHCC		44.6721890473
143 (in isoform 2)Ubiquitination-44.6721890473
143UbiquitinationAVPEGAWKDTAQLHK
CCCCCCCCCHHHHCC		44.6721890473
143UbiquitinationAVPEGAWKDTAQLHK
CCCCCCCCCHHHHCC		44.6721890473
143 (in isoform 1)Ubiquitination-44.6721890473
145PhosphorylationPEGAWKDTAQLHKSE
CCCCCCCHHHHCCCH		16.7523403867
150UbiquitinationKDTAQLHKSEEAVSV
CCHHHHCCCHHHHHH		69.0621906983
150 (in isoform 1)Ubiquitination-69.0621890473
151PhosphorylationDTAQLHKSEEAVSVG
CHHHHCCCHHHHHHC		29.8925159151
160UbiquitinationEAVSVGQKRVLRYYL
HHHHHCHHHHHHHEE		38.25-
165PhosphorylationGQKRVLRYYLFQGQR
CHHHHHHHEECCCCE		10.60-
205PhosphorylationHRSRHGLSLQDQMVR
HHHCCCCCHHHHHHH		28.6923917254
213UbiquitinationLQDQMVRKAIYGPNV
HHHHHHHHHHHCCCE		27.94-
216PhosphorylationQMVRKAIYGPNVISI
HHHHHHHHCCCEEEE		31.2423917254
222PhosphorylationIYGPNVISIPVKSYP
HHCCCEEEEECCCCC		19.2923917254
282PhosphorylationLYKTRKQSQTLRDMV
HHHHHHCCHHHHHHH		28.3229457462
284PhosphorylationKTRKQSQTLRDMVKL
HHHHCCHHHHHHHHH		29.0729457462
422PhosphorylationRPINFKFYKHSMKFV
CCCCCCCHHHHHHHH		14.3722210691
425PhosphorylationNFKFYKHSMKFVAAL
CCCCHHHHHHHHHHH		21.3722210691
433PhosphorylationMKFVAALSVLALLGT
HHHHHHHHHHHHHHH		15.4522210691
527 (in isoform 2)Ubiquitination-19.67-
532UbiquitinationVMGVVPLKGQAFLPL
EEEEEECCCCEEECC		42.79-
688 (in isoform 2)Ubiquitination-2.4021890473
692PhosphorylationYRVVALASKPLPTVP
CEEEEEECCCCCCCC		35.3424719451
693 (in isoform 1)Ubiquitination-44.9921890473
693UbiquitinationRVVALASKPLPTVPS
EEEEEECCCCCCCCC		44.9921906983
729UbiquitinationLVMRNLLKPQTTPVI
HHHHHCCCCCCHHHH		37.94-
804UbiquitinationPTAVNGVKDPDQAAS
CCCCCCCCCHHHHHC		66.0121906983
804 (in isoform 1)Ubiquitination-66.0121890473
805 (in isoform 2)Phosphorylation-49.9922468782
838UbiquitinationGIIVKHFPKLLPKVL
EEHHHHHHHHHCHHH		26.5521890473
839UbiquitinationIIVKHFPKLLPKVLV
EHHHHHHHHHCHHHH		62.81-
843UbiquitinationHFPKLLPKVLVQGTV
HHHHHHCHHHHCCEE		48.4421890473
843 (in isoform 1)Ubiquitination-48.4421890473
859UbiquitinationARMAPEQKTELVCEL
EEECCCHHHHHHHHH		42.16-
868UbiquitinationELVCELQKLQYCVGM
HHHHHHHHHHHHHCC		50.62-
1033N-linked_GlycosylationQPWFVPLNRTVAAPD
CCCEEECCCEEECCC		31.3526134396
1110N-linked_GlycosylationQGPLALRNITDTGFK
CCCCHHHCCCHHHHH		42.22-
1160UbiquitinationRASKKRFKQLERELA
HHCHHHHHHHHHHHH		58.99-
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 AT132_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT132_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 AT132_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPCS2_HUMANSPCS2physical
22645275
LMAN2_HUMANLMAN2physical
22645275
PDIA6_HUMANPDIA6physical
22645275
SC61B_HUMANSEC61Bphysical
22645275
UB2J2_HUMANUBE2J2physical
22645275
YIF1A_HUMANYIF1Aphysical
22645275
VAMP2_HUMANVAMP2physical
22645275
AAK1_HUMANAAK1physical
22645275
GAK_HUMANGAKphysical
22645275
NRX1B_HUMANNRXN1physical
22645275
NRX1A_HUMANNRXN1physical
22645275
FKBP8_HUMANFKBP8physical
22645275
SYT11_HUMANSYT11physical
22645275
HSP7C_HUMANHSPA8physical
22645275
CXCR4_HUMANCXCR4physical
22645275
ACKR3_HUMANACKR3physical
22645275
ICAM2_HUMANICAM2physical
22645275
PCDBA_HUMANPCDHB10physical
22645275
GASR_HUMANCCKBRphysical
22645275
TSN14_HUMANTSPAN14physical
22645275
NPY1R_HUMANNPY1Rphysical
22645275
PAR1_HUMANF2Rphysical
22645275
LRP6_HUMANLRP6physical
22645275
HDAC6_HUMANHDAC6physical
22645275
BNI3L_HUMANBNIP3Lphysical
22645275
AT5G2_HUMANATP5G2physical
22645275
FUND2_HUMANFUNDC2physical
22645275
HIPK1_HUMANHIPK1physical
22645275
MEX3B_HUMANMEX3Bphysical
22645275
MYCB2_HUMANMYCBP2physical
22645275
OSTC_HUMANOSTCphysical
22645275
WDR5B_HUMANWDR5Bphysical
22645275
DCAF7_HUMANDCAF7physical
22645275
P_HUMANOCA2physical
22645275
PCMD2_HUMANPCMTD2physical
22645275
CYGB_HUMANCYGBphysical
22645275
CO1A1_HUMANCOL1A1physical
22645275
GPR21_HUMANGPR21physical
22645275
F111B_HUMANFAM111Bphysical
22645275
FA8A1_HUMANFAM8A1physical
22645275
F192A_HUMANFAM192Aphysical
22645275
EMC7_HUMANEMC7physical
22645275
ASTER_HUMANWDR83OSphysical
22645275
LAMP1_HUMANLAMP1physical
22768177
RAB5A_HUMANRAB5Aphysical
22768177
RAB7A_HUMANRAB7Aphysical
22768177
RAB9A_HUMANRAB9Aphysical
22768177
Drug and Disease Associations
Kegg Disease
H00057 Parkinson's disease (PD)
H00833 Neurodegeneration with brain iron accumulation (NBIA); Hallervorden-Spatz syndrome; Pantothenate kin
OMIM Disease
606693Kufor-Rakeb syndrome (KRS)
606693Ceroid lipofuscinosis, neuronal, 12 (CLN12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT132_HUMAN

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Related Literatures of Post-Translational Modification

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