AT131_HUMAN - dbPTM
AT131_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT131_HUMAN
UniProt AC Q9HD20
Protein Name Manganese-transporting ATPase 13A1
Gene Name ATP13A1
Organism Homo sapiens (Human).
Sequence Length 1204
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis..
Protein Sequence MAAAAAVGNAVPCGARPCGVRPDGQPKPGPQPRALLAAGPALIANGDELVAAVWPYRRLALLRRLTVLPFAGLLYPAWLGAAAAGCWGWGSSWVQIPEAALLVLATICLAHALTVLSGHWSVHAHCALTCTPEYDPSKATFVKVVPTPNNGSTELVALHRNEGEDGLEVLSFEFQKIKYSYDALEKKQFLPVAFPVGNAFSYYQSNRGFQEDSEIRAAEKKFGSNKAEMVVPDFSELFKERATAPFFVFQVFCVGLWCLDEYWYYSVFTLSMLVAFEASLVQQQMRNMSEIRKMGNKPHMIQVYRSRKWRPIASDEIVPGDIVSIGRSPQENLVPCDVLLLRGRCIVDEAMLTGESVPQMKEPIEDLSPDRVLDLQADSRLHVIFGGTKVVQHIPPQKATTGLKPVDSGCVAYVLRTGFNTSQGKLLRTILFGVKRVTANNLETFIFILFLLVFAIAAAAYVWIEGTKDPSRNRYKLFLECTLILTSVVPPELPIELSLAVNTSLIALAKLYMYCTEPFRIPFAGKVEVCCFDKTGTLTSDSLVVRGVAGLRDGKEVTPVSSIPVETHRALASCHSLMQLDDGTLVGDPLEKAMLTAVDWTLTKDEKVFPRSIKTQGLKIHQRFHFASALKRMSVLASYEKLGSTDLCYIAAVKGAPETLHSMFSQCPPDYHHIHTEISREGARVLALGYKELGHLTHQQAREVKREALECSLKFVGFIVVSCPLKADSKAVIREIQNASHRVVMITGDNPLTACHVAQELHFIEKAHTLILQPPSEKGRQCEWRSIDGSIVLPLARGSPKALALEYALCLTGDGLAHLQATDPQQLLRLIPHVQVFARVAPKQKEFVITSLKELGYVTLMCGDGTNDVGALKHADVGVALLANAPERVVERRRRPRDSPTLSNSGIRATSRTAKQRSGLPPSEEQPTSQRDRLSQVLRDLEDESTPIVKLGDASIAAPFTSKLSSIQCICHVIKQGRCTLVTTLQMFKILALNALILAYSQSVLYLEGVKFSDFQATLQGLLLAGCFLFISRSKPLKTLSRERPLPNIFNLYTILTVMLQFFVHFLSLVYLYREAQARSPEKQEQFVDLYKEFEPSLVNSTVYIMAMAMQMATFAINYKGPPFMESLPENKPLVWSLAVSLLAIIGLLLGSSPDFNSQFGLVDIPVEFKLVIAQVLLLDFCLALLADRVLQFFLGTPKLKVPS
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------MAAAAAVGN
------CCCHHHHCC		19.6722223895
25 (in isoform 2)Ubiquitination-50.6621890473
58 (in isoform 2)Ubiquitination-20.6121890473
68 (in isoform 2)Ubiquitination-2.1421890473
69 (in isoform 2)Ubiquitination-16.83-
70UbiquitinationRRLTVLPFAGLLYPA
HHHCHHHCCCCCCHH		8.0221890473
90 (in isoform 3)Ubiquitination-14.0921906983
121 (in isoform 2)Ubiquitination-9.8021890473
137PhosphorylationCTPEYDPSKATFVKV
ECCCCCCCCCEEEEE		31.8321406692
140PhosphorylationEYDPSKATFVKVVPT
CCCCCCCEEEEEEEC		32.4721406692
143UbiquitinationPSKATFVKVVPTPNN
CCCCEEEEEEECCCC		33.0721890473
143 (in isoform 1)Ubiquitination-33.0721890473
147PhosphorylationTFVKVVPTPNNGSTE
EEEEEEECCCCCCCE		27.3421406692
152PhosphorylationVPTPNNGSTELVALH
EECCCCCCCEEEEEE		22.3421406692
153PhosphorylationPTPNNGSTELVALHR
ECCCCCCCEEEEEEE		34.4321406692
171PhosphorylationEDGLEVLSFEFQKIK
CCCEEEEEEEEEEEC		28.1024719451
176UbiquitinationVLSFEFQKIKYSYDA
EEEEEEEEECEEHHH		46.6221906983
176 (in isoform 1)Ubiquitination-46.6221890473
178UbiquitinationSFEFQKIKYSYDALE
EEEEEEECEEHHHHH		34.87-
179PhosphorylationFEFQKIKYSYDALEK
EEEEEECEEHHHHHH		18.8825884760
180PhosphorylationEFQKIKYSYDALEKK
EEEEECEEHHHHHHC		16.1324719451
181PhosphorylationFQKIKYSYDALEKKQ
EEEECEEHHHHHHCC		11.3525884760
186UbiquitinationYSYDALEKKQFLPVA
EEHHHHHHCCCCCEE		53.3721906983
186 (in isoform 1)Ubiquitination-53.3721890473
187UbiquitinationSYDALEKKQFLPVAF
EHHHHHHCCCCCEEE		36.59-
190 (in isoform 2)Ubiquitination-2.8621890473
201PhosphorylationFPVGNAFSYYQSNRG
EECCCHHHHHHCCCC		22.1126356563
202PhosphorylationPVGNAFSYYQSNRGF
ECCCHHHHHHCCCCC		10.0826356563
203PhosphorylationVGNAFSYYQSNRGFQ
CCCHHHHHHCCCCCC		12.3126356563
203UbiquitinationVGNAFSYYQSNRGFQ
CCCHHHHHHCCCCCC		12.3121890473
205PhosphorylationNAFSYYQSNRGFQED
CHHHHHHCCCCCCCH		16.6326356563
220AcetylationSEIRAAEKKFGSNKA
HHHHHHHHHHCCCCC		48.997308157
223 (in isoform 3)Ubiquitination-38.9121906983
226UbiquitinationEKKFGSNKAEMVVPD
HHHHCCCCCEEECCC		47.63-
239UbiquitinationPDFSELFKERATAPF
CCHHHHHHHHCCCCC		59.9421906983
239 (in isoform 1)Ubiquitination-59.9421890473
287N-linked_GlycosylationLVQQQMRNMSEIRKM
HHHHHHHCHHHHHHH		32.75UniProtKB CARBOHYD
297UbiquitinationEIRKMGNKPHMIQVY
HHHHHCCCCCEEEEE		30.48-
307 (in isoform 2)Ubiquitination-33.2921890473
308UbiquitinationIQVYRSRKWRPIASD
EEEECCCCCCCCCCC		49.1221890473
308 (in isoform 1)Ubiquitination-49.1221890473
328PhosphorylationDIVSIGRSPQENLVP
CEEEECCCCCCCCCC		26.2328258704
361UbiquitinationGESVPQMKEPIEDLS
CCCCCCCCCCHHHCC		55.90-
371MethylationIEDLSPDRVLDLQAD
HHHCCCCCEEEECCC		33.99-
379PhosphorylationVLDLQADSRLHVIFG
EEEECCCCCEEEEEC		39.49-
398MalonylationVQHIPPQKATTGLKP
EECCCCCCCCCCCCC		54.1732601280
404UbiquitinationQKATTGLKPVDSGCV
CCCCCCCCCCCCCCE		44.32-
404MalonylationQKATTGLKPVDSGCV
CCCCCCCCCCCCCCE		44.3232601280
413PhosphorylationVDSGCVAYVLRTGFN
CCCCCEEEEECCCCC		4.6126356563
420N-linked_GlycosylationYVLRTGFNTSQGKLL
EEECCCCCCCHHHHH		39.9216335952
425UbiquitinationGFNTSQGKLLRTILF
CCCCCHHHHHHHHHH		36.3921906983
425 (in isoform 1)Ubiquitination-36.3921890473
435UbiquitinationRTILFGVKRVTANNL
HHHHHCCCCCCCCCH		41.34-
4352-HydroxyisobutyrylationRTILFGVKRVTANNL
HHHHHCCCCCCCCCH		41.34-
437 (in isoform 2)Ubiquitination-4.9921890473
438PhosphorylationLFGVKRVTANNLETF
HHCCCCCCCCCHHHH		27.92-
474 (in isoform 2)Ubiquitination-28.93-
534UbiquitinationVEVCCFDKTGTLTSD
EEEEEECCCCCCCCC		28.71-
534AcetylationVEVCCFDKTGTLTSD
EEEEEECCCCCCCCC		28.7126051181
555UbiquitinationVAGLRDGKEVTPVSS
ECCCCCCCEECCCCC		53.9921906983
555 (in isoform 1)Ubiquitination-53.9921890473
558PhosphorylationLRDGKEVTPVSSIPV
CCCCCEECCCCCCCC		21.04-
567PhosphorylationVSSIPVETHRALASC
CCCCCCCHHHHHHHC		19.52-
573PhosphorylationETHRALASCHSLMQL
CHHHHHHHCCCCEEC		17.1427251275
576PhosphorylationRALASCHSLMQLDDG
HHHHHCCCCEECCCC		29.8427251275
592UbiquitinationLVGDPLEKAMLTAVD
CCCCHHHHHHHHHCC		46.94-
603PhosphorylationTAVDWTLTKDEKVFP
HHCCCEECCCCCCCC		29.13-
607UbiquitinationWTLTKDEKVFPRSIK
CEECCCCCCCCCCCC		60.35-
607MalonylationWTLTKDEKVFPRSIK
CEECCCCCCCCCCCC		60.3526320211
614UbiquitinationKVFPRSIKTQGLKIH
CCCCCCCCCCCCCHH		35.72-
631UbiquitinationFHFASALKRMSVLAS
HHHHHHHHHHHHHHH		45.85-
6312-HydroxyisobutyrylationFHFASALKRMSVLAS
HHHHHHHHHHHHHHH		45.85-
638O-linked_GlycosylationKRMSVLASYEKLGST
HHHHHHHHHHHHCCC		29.6629351928
644PhosphorylationASYEKLGSTDLCYIA
HHHHHHCCCCHHHHH		29.2328348404
645PhosphorylationSYEKLGSTDLCYIAA
HHHHHCCCCHHHHHH		31.0627251275
649PhosphorylationLGSTDLCYIAAVKGA
HCCCCHHHHHHHCCC		10.82-
691UbiquitinationRVLALGYKELGHLTH
EEEEECCHHHHCCCH		44.67-
722PhosphorylationFVGFIVVSCPLKADS
EEEEEEEECCCCCCC		10.1020068231
722UbiquitinationFVGFIVVSCPLKADS
EEEEEEEECCCCCCC		10.1021890473
730UbiquitinationCPLKADSKAVIREIQ
CCCCCCCHHHHHHHH		47.41-
730AcetylationCPLKADSKAVIREIQ
CCCCCCCHHHHHHHH		47.4125953088
778AcetylationILQPPSEKGRQCEWR
EECCCCCCCCCCEEE		64.837677967
778UbiquitinationILQPPSEKGRQCEWR
EECCCCCCCCCCEEE		64.83-
832 (in isoform 2)Ubiquitination-26.6221890473
850PhosphorylationKQKEFVITSLKELGY
CCCCEEEEEHHHHCC		23.78-
851PhosphorylationQKEFVITSLKELGYV
CCCEEEEEHHHHCCE		26.73-
855UbiquitinationVITSLKELGYVTLMC
EEEEHHHHCCEEEEE		5.9921890473
857PhosphorylationTSLKELGYVTLMCGD
EEHHHHCCEEEEECC		11.68-
899PhosphorylationRRRRPRDSPTLSNSG
HCCCCCCCCCCCCCC		22.5129255136
901PhosphorylationRRPRDSPTLSNSGIR
CCCCCCCCCCCCCCC		46.9329255136
903PhosphorylationPRDSPTLSNSGIRAT
CCCCCCCCCCCCCCC		31.2829255136
905PhosphorylationDSPTLSNSGIRATSR
CCCCCCCCCCCCCCC		32.0229255136
911PhosphorylationNSGIRATSRTAKQRS
CCCCCCCCCCHHHHC		27.0123911959
913PhosphorylationGIRATSRTAKQRSGL
CCCCCCCCHHHHCCC		37.6623911959
918PhosphorylationSRTAKQRSGLPPSEE
CCCHHHHCCCCCCCC		42.0328555341
923PhosphorylationQRSGLPPSEEQPTSQ
HHCCCCCCCCCCCCH		52.4022210691
928PhosphorylationPPSEEQPTSQRDRLS
CCCCCCCCCHHHHHH		36.8722210691
929PhosphorylationPSEEQPTSQRDRLSQ
CCCCCCCCHHHHHHH		29.8722210691
935PhosphorylationTSQRDRLSQVLRDLE
CCHHHHHHHHHHHCC		21.0923401153
945PhosphorylationLRDLEDESTPIVKLG
HHHCCCCCCCCEEEC		52.3725159151
946PhosphorylationRDLEDESTPIVKLGD
HHCCCCCCCCEEECC		18.2626462736
950UbiquitinationDESTPIVKLGDASIA
CCCCCCEEECCCCEE		47.6921906983
950 (in isoform 1)Ubiquitination-47.6921890473
963UbiquitinationIAAPFTSKLSSIQCI
EECCCCCCCCHHHHH		49.70-
965 (in isoform 2)Ubiquitination-29.1821890473
975AcetylationQCICHVIKQGRCTLV
HHHHHHHHCCCCCHH		45.6825953088
1034PhosphorylationCFLFISRSKPLKTLS
HHHHHCCCCCCCCCC		31.6624719451
1038UbiquitinationISRSKPLKTLSRERP
HCCCCCCCCCCCCCC		56.82-
1083UbiquitinationAQARSPEKQEQFVDL
HHCCCHHHHHHHHHH		63.622190698
1083 (in isoform 1)Ubiquitination-63.6221890473
1091PhosphorylationQEQFVDLYKEFEPSL
HHHHHHHHHHHCHHH		12.1921394647
1097PhosphorylationLYKEFEPSLVNSTVY
HHHHHCHHHHHHHHH		37.4424275569
1101PhosphorylationFEPSLVNSTVYIMAM
HCHHHHHHHHHHHHH		16.2724275569
1102PhosphorylationEPSLVNSTVYIMAMA
CHHHHHHHHHHHHHH		16.4824275569
1104PhosphorylationSLVNSTVYIMAMAMQ
HHHHHHHHHHHHHHH		5.7624275569
1197PhosphorylationVLQFFLGTPKLKVPS
HHHHHHCCCCCCCCC		21.2824719451
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 AT131_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT131_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 AT131_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZY11B_HUMANZYG11Bphysical
28514442
VCIP1_HUMANVCPIP1physical
28514442
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 AT131_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-420, AND MASSSPECTROMETRY.
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-899, 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-899, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899 AND THR-901, 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-899, AND MASSSPECTROMETRY.

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