AT2A3_HUMAN - dbPTM
AT2A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT2A3_HUMAN
UniProt AC Q93084
Protein Name Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
Gene Name ATP2A3
Organism Homo sapiens (Human).
Sequence Length 1043
Subcellular Localization Nucleus membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . Sarcoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction..
Protein Sequence MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMRKEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPTSREQILAKIRDWGSGSDTLRCLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGMLDPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVAGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAIGVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDNPLFAGIDCEVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVTPLSGRQWVVVLQISLPVILLDEALKYLSRNHMHACLYPGLLRTVSQAWSRQPLTTSWTPDHTGRNEPEVSAGNRVESPVCTSD
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
1Acetylation-------MEAAHLLP
-------CCHHHHHC		36.3012665801
17PhosphorylationADVLRHFSVTAEGGL
HHHHHHEEEECCCCC		16.6625849741
19PhosphorylationVLRHFSVTAEGGLSP
HHHHEEEECCCCCCH		20.1423312004
25PhosphorylationVTAEGGLSPAQVTGA
EECCCCCCHHHHCCC		22.8227251275
30PhosphorylationGLSPAQVTGARERYG
CCCHHHHCCCHHHCC		17.0323312004
120UbiquitinationESAIEALKEYEPEMG
HHHHHHHHHHCHHHH		66.36-
120 (in isoform 5)Ubiquitination-66.36-
122NitrationAIEALKEYEPEMGKV
HHHHHHHHCHHHHCH		34.89-
128UbiquitinationEYEPEMGKVIRSDRK
HHCHHHHCHHCCCCC		32.93-
128 (in isoform 5)Ubiquitination-32.93-
158UbiquitinationVEVAVGDKVPADLRL
EEEECCCCCCCCEEE		44.16-
158 (in isoform 5)Ubiquitination-44.16-
169UbiquitinationDLRLIEIKSTTLRVD
CEEEEEEECCEEEEE		29.03-
169 (in isoform 5)Ubiquitination-29.03-
178PhosphorylationTTLRVDQSILTGESV
CEEEEECHHHCCCCE		18.3320068231
189UbiquitinationGESVSVTKHTEAIPD
CCCEEEEECCCCCCC		46.50-
189 (in isoform 5)Ubiquitination-46.50-
204UbiquitinationPRAVNQDKKNMLFSG
CCCCCCCCCCCCCCC		35.96-
204 (in isoform 5)Ubiquitination-35.96-
205UbiquitinationRAVNQDKKNMLFSGT
CCCCCCCCCCCCCCC		56.74-
205 (in isoform 5)Ubiquitination-56.74-
234UbiquitinationGLHTELGKIRSQMAA
CHHHHHHHHHHHHHC		47.79-
234 (in isoform 5)Ubiquitination-47.79-
252UbiquitinationERTPLQRKLDEFGRQ
CCCHHHHHHHHHHHH		47.53-
252 (in isoform 5)Ubiquitination-47.53-
294NitrationSWLRGAVYYFKIAVA
CCHHHHHHHHHHHHH		11.58-
295NitrationWLRGAVYYFKIAVAL
CHHHHHHHHHHHHHH		7.56-
335PhosphorylationRKNAIVRSLPSVETL
HHCCHHHCCCCCCCC		33.4622210691
338PhosphorylationAIVRSLPSVETLGCT
CHHHCCCCCCCCCCC		37.5726437602
341PhosphorylationRSLPSVETLGCTSVI
HCCCCCCCCCCCEEE		26.7122210691
345PhosphorylationSVETLGCTSVICSDK
CCCCCCCCEEEEECC		24.9928348404
346PhosphorylationVETLGCTSVICSDKT
CCCCCCCEEEEECCC		17.3526437602
350PhosphorylationGCTSVICSDKTGTLT
CCCEEEEECCCCCCC		30.9028348404
352UbiquitinationTSVICSDKTGTLTTN
CEEEEECCCCCCCCC		32.34-
352 (in isoform 6)Ubiquitination-32.34-
353PhosphorylationSVICSDKTGTLTTNQ
EEEEECCCCCCCCCC		40.1524719451
357PhosphorylationSDKTGTLTTNQMSVC
ECCCCCCCCCCCCEE		24.4424719451
358PhosphorylationDKTGTLTTNQMSVCR
CCCCCCCCCCCCEEE		26.9422210691
362PhosphorylationTLTTNQMSVCRMFVV
CCCCCCCCEEEEEEE		14.3226437602
364S-nitrosylationTTNQMSVCRMFVVAE
CCCCCCEEEEEEEEE		1.732212679
415PhosphorylationDGLVELATICALCND
CHHHHHHHHHHHHCC		29.25-
427PhosphorylationCNDSALDYNEAKGVY
HCCCCCCHHHHCCHH		18.76-
431UbiquitinationALDYNEAKGVYEKVG
CCCHHHHCCHHHHHH		42.61-
436UbiquitinationEAKGVYEKVGEATET
HHCCHHHHHHHHHHH		37.54-
441PhosphorylationYEKVGEATETALTCL
HHHHHHHHHHHHHHH		29.5729255136
443PhosphorylationKVGEATETALTCLVE
HHHHHHHHHHHHHHH		23.7029255136
446PhosphorylationEATETALTCLVEKMN
HHHHHHHHHHHHHCC		11.0020860994
447GlutathionylationATETALTCLVEKMNV
HHHHHHHHHHHHCCC		4.1022555962
451UbiquitinationALTCLVEKMNVFDTD
HHHHHHHHCCCCCHH		28.44-
476UbiquitinationGACNTVIKQLMRKEF
CHHHHHHHHHHCCCC		32.80-
476 (in isoform 5)Ubiquitination-32.80-
476 (in isoform 6)Ubiquitination-32.80-
481AcetylationVIKQLMRKEFTLEFS
HHHHHHCCCCEEEEE		43.1254357721
481UbiquitinationVIKQLMRKEFTLEFS
HHHHHHCCCCEEEEE		43.12-
481 (in isoform 6)Ubiquitination-43.12-
484PhosphorylationQLMRKEFTLEFSRDR
HHHCCCCEEEEECCC		26.8622673903
488PhosphorylationKEFTLEFSRDRKSMS
CCCEEEEECCCCCCE		24.7221712546
492UbiquitinationLEFSRDRKSMSVYCT
EEEECCCCCCEEEEC		55.59-
492 (in isoform 5)Ubiquitination-55.59-
492 (in isoform 6)Ubiquitination-55.59-
495PhosphorylationSRDRKSMSVYCTPTR
ECCCCCCEEEECCCC		19.6128796482
497PhosphorylationDRKSMSVYCTPTRPH
CCCCCEEEECCCCCC		5.3628796482
498S-nitrosylationRKSMSVYCTPTRPHP
CCCCEEEECCCCCCC		3.262212679
499PhosphorylationKSMSVYCTPTRPHPT
CCCEEEECCCCCCCC		15.2628796482
501PhosphorylationMSVYCTPTRPHPTGQ
CEEEECCCCCCCCCC		38.3828796482
506PhosphorylationTPTRPHPTGQGSKMF
CCCCCCCCCCCCCEE		38.8228796482
510PhosphorylationPHPTGQGSKMFVKGA
CCCCCCCCCEEECCC		17.0428509920
511UbiquitinationHPTGQGSKMFVKGAP
CCCCCCCCEEECCCC		43.09-
511 (in isoform 5)Ubiquitination-43.09-
515UbiquitinationQGSKMFVKGAPESVI
CCCCEEECCCCHHHH		37.78-
515 (in isoform 2)Ubiquitination-37.78-
515 (in isoform 5)Ubiquitination-37.78-
515 (in isoform 6)Ubiquitination-37.78-
526PhosphorylationESVIERCSSVRVGSR
HHHHHHHCCCCCCCC		37.7822210691
527PhosphorylationSVIERCSSVRVGSRT
HHHHHHCCCCCCCCC		19.9822210691
538PhosphorylationGSRTAPLTPTSREQI
CCCCCCCCCCCHHHH		24.3828060719
540PhosphorylationRTAPLTPTSREQILA
CCCCCCCCCHHHHHH		34.8728060719
541PhosphorylationTAPLTPTSREQILAK
CCCCCCCCHHHHHHH		34.7228060719
548UbiquitinationSREQILAKIRDWGSG
CHHHHHHHHHHCCCC		34.52-
548 (in isoform 5)Ubiquitination-34.52-
548 (in isoform 6)Ubiquitination-34.52-
554PhosphorylationAKIRDWGSGSDTLRC
HHHHHCCCCHHHHHH		30.7628122231
556PhosphorylationIRDWGSGSDTLRCLA
HHHCCCCHHHHHHHH		29.1728348404
558PhosphorylationDWGSGSDTLRCLALA
HCCCCHHHHHHHHHH		20.1428122231
573UbiquitinationTRDAPPRKEDMELDD
CCCCCCCHHHCCHHH		64.93-
573 (in isoform 5)Ubiquitination-64.93-
629UbiquitinationVMITGDNKGTAVAIC
EEEECCCHHHHHHHH		63.48-
629 (in isoform 5)Ubiquitination-63.48-
629 (in isoform 6)Ubiquitination-63.48-
651UbiquitinationDTEDVAGKAYTGREF
CCHHCCCCCCCCCCC		28.6021906983
651 (in isoform 1)Ubiquitination-28.6021906983
651 (in isoform 2)Ubiquitination-28.6021906983
651 (in isoform 3)Ubiquitination-28.6021906983
651 (in isoform 4)Ubiquitination-28.6021906983
651 (in isoform 5)Ubiquitination-28.6021906983
651 (in isoform 6)Ubiquitination-28.6021906983
654PhosphorylationDVAGKAYTGREFDDL
HCCCCCCCCCCCCCC		34.3223186163
662PhosphorylationGREFDDLSPEQQRQA
CCCCCCCCHHHHHHH		33.1323401153
684UbiquitinationARVEPAHKSRIVENL
HHCCHHHHHHHHHHH		43.46-
712UbiquitinationVNDAPALKKAEIGIA
CCCCHHHHHCCCEEE		52.632190698
712 (in isoform 1)Ubiquitination-52.6321906983
712 (in isoform 2)Ubiquitination-52.6321906983
712 (in isoform 3)Ubiquitination-52.6321906983
712 (in isoform 4)Ubiquitination-52.6321906983
712 (in isoform 5)Ubiquitination-52.6321906983
712 (in isoform 6)Ubiquitination-52.6321906983
713UbiquitinationNDAPALKKAEIGIAM
CCCHHHHHCCCEEEE		52.69-
713 (in isoform 1)Ubiquitination-52.6921906983
713 (in isoform 2)Ubiquitination-52.6921906983
713 (in isoform 3)Ubiquitination-52.6921906983
713 (in isoform 4)Ubiquitination-52.6921906983
713 (in isoform 5)Ubiquitination-52.6921906983
713 (in isoform 6)Ubiquitination-52.6921906983
729PhosphorylationSGTAVAKSAAEMVLS
CCHHHHHHHHHHHHC		23.9930278072
736PhosphorylationSAAEMVLSDDNFASI
HHHHHHHCCCCHHHH		31.3530278072
742PhosphorylationLSDDNFASIVAAVEE
HCCCCHHHHHHHHHH		17.2930278072
755PhosphorylationEEGRAIYSNMKQFIR
HHHHHHHHCHHHHHH		25.0821712546
758UbiquitinationRAIYSNMKQFIRYLI
HHHHHCHHHHHHHHH		46.43-
758 (in isoform 5)Ubiquitination-46.43-
823PhosphorylationIMEKLPRSPREALIS
HHHHCCCCHHHHHHH		26.7728355574
875UbiquitinationYQLRNFLKCSEDNPL
HHHHHHHHCCCCCCC		31.42-
921PhosphorylationNSVSENQSLLRMPPW
CCCCCCCCHHCCCCC		40.7424719451
1005PhosphorylationPGLLRTVSQAWSRQP
HHHHHHHHHHHHCCC		17.3623312004
1014 (in isoform 1)O-linked_Glycosylation-26.0129351928
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 AT2A3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT2A3_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 AT2A3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL2_HUMANBCL2physical
9788433
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 AT2A3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-14, AND ACETYLATION AT MET-1.

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