PDIA6_HUMAN - dbPTM
PDIA6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDIA6_HUMAN
UniProt AC Q15084
Protein Name Protein disulfide-isomerase A6
Gene Name PDIA6
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization Endoplasmic reticulum lumen . Cell membrane . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545).
Protein Description May function as a chaperone that inhibits aggregation of misfolded proteins. [PubMed: 12204115 Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling]
Protein Sequence MALLVLGLVSCTFFLAVNGLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKDVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFPTIVEREPWDGRDGELPVEDDIDLSDVELDDLGKDEL
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
7 (in isoform 3)Phosphorylation-19.2926552605
9 (in isoform 3)Phosphorylation-4.1326552605
18 (in isoform 3)Phosphorylation-29.1926552605
19 (in isoform 3)Phosphorylation-21.2826552605
20 (in isoform 3)Phosphorylation-2.9426552605
21 (in isoform 3)Phosphorylation-14.1226552605
22PhosphorylationLAVNGLYSSSDDVIE
HHHCCCCCCCCCEEE		28.549058200
25 (in isoform 5)Phosphorylation-57.03-
28 (in isoform 3)Phosphorylation-4.6426552605
30 (in isoform 3)Phosphorylation-6.1626552605
66MethylationQRLTPEWKKAATALK
HHCCHHHHHHHHHHH		30.76115974771
66AcetylationQRLTPEWKKAATALK
HHCCHHHHHHHHHHH		30.7625953088
73AcetylationKKAATALKDVVKVGA
HHHHHHHHHHEEECC		46.1127452117
73UbiquitinationKKAATALKDVVKVGA
HHHHHHHHHHEEECC		46.11-
77 (in isoform 1)Ubiquitination-34.5021890473
77UbiquitinationTALKDVVKVGAVDAD
HHHHHHEEECCEECC		34.5021906983
85AcetylationVGAVDADKHHSLGGQ
ECCEECCCCCCCCCC		44.9626822725
85UbiquitinationVGAVDADKHHSLGGQ
ECCEECCCCCCCCCC		44.96-
88PhosphorylationVDADKHHSLGGQYGV
EECCCCCCCCCCCCC		28.5528152594
93PhosphorylationHHSLGGQYGVQGFPT
CCCCCCCCCCCCCCE		23.6528152594
100PhosphorylationYGVQGFPTIKIFGSN
CCCCCCCEEEEECCC		32.4228152594
102UbiquitinationVQGFPTIKIFGSNKN
CCCCCEEEEECCCCC		34.17-
102AcetylationVQGFPTIKIFGSNKN
CCCCCEEEEECCCCC		34.1790461
108UbiquitinationIKIFGSNKNRPEDYQ
EEEECCCCCCCCCCC		56.9121890473
108 (in isoform 1)Ubiquitination-56.9121890473
108UbiquitinationIKIFGSNKNRPEDYQ
EEEECCCCCCCCCCC		56.9121890473
108UbiquitinationIKIFGSNKNRPEDYQ
EEEECCCCCCCCCCC		56.9121890473
119PhosphorylationEDYQGGRTGEAIVDA
CCCCCCCHHHHHHHH		42.5221712546
125UbiquitinationRTGEAIVDAALSALR
CHHHHHHHHHHHHHH		21.73-
129PhosphorylationAIVDAALSALRQLVK
HHHHHHHHHHHHHHH		22.1128857561
129 (in isoform 2)Ubiquitination-22.1121890473
142MethylationVKDRLGGRSGGYSSG
HHHHHCCCCCCCCCC		30.26115486875
147PhosphorylationGGRSGGYSSGKQGRS
CCCCCCCCCCCCCCC		35.5724719451
148PhosphorylationGRSGGYSSGKQGRSD
CCCCCCCCCCCCCCC		41.3426546556
150UbiquitinationSGGYSSGKQGRSDSS
CCCCCCCCCCCCCCC		52.07-
154 (in isoform 2)Ubiquitination-48.98-
156UbiquitinationGKQGRSDSSSKKDVI
CCCCCCCCCCCCCEE		37.44-
156PhosphorylationGKQGRSDSSSKKDVI
CCCCCCCCCCCCCEE		37.4426091039
157PhosphorylationKQGRSDSSSKKDVIE
CCCCCCCCCCCCEEE		51.6823186163
158PhosphorylationQGRSDSSSKKDVIEL
CCCCCCCCCCCEEEC		47.9123917254
160UbiquitinationRSDSSSKKDVIELTD
CCCCCCCCCEEECCC		60.2121890473
160 (in isoform 2)Ubiquitination-60.2121890473
160UbiquitinationRSDSSSKKDVIELTD
CCCCCCCCCEEECCC		60.21-
160UbiquitinationRSDSSSKKDVIELTD
CCCCCCCCCEEECCC		60.2121890473
166PhosphorylationKKDVIELTDDSFDKN
CCCEEECCCCCCCCC		25.6023186163
208UbiquitinationAAAASEVKEQTKGKV
HHHHHHHHHHHCCCE		39.80-
216UbiquitinationEQTKGKVKLAAVDAT
HHHCCCEEEEEEHHH		35.57-
230PhosphorylationTVNQVLASRYGIRGF
HHHHHHHHHHCCCCC		23.1329802988
239PhosphorylationYGIRGFPTIKIFQKG
HCCCCCCEEEEEECC		32.42-
241UbiquitinationIRGFPTIKIFQKGES
CCCCCEEEEEECCCC		39.6921890473
241AcetylationIRGFPTIKIFQKGES
CCCCCEEEEEECCCC		39.6990465
241UbiquitinationIRGFPTIKIFQKGES
CCCCCEEEEEECCCC		39.6921890473
241UbiquitinationIRGFPTIKIFQKGES
CCCCCEEEEEECCCC		39.6921890473
241 (in isoform 1)Ubiquitination-39.6921890473
245UbiquitinationPTIKIFQKGESPVDY
CEEEEEECCCCCCCC		54.6321890473
245UbiquitinationPTIKIFQKGESPVDY
CEEEEEECCCCCCCC		54.6321890473
245 (in isoform 1)Ubiquitination-54.6321890473
245AcetylationPTIKIFQKGESPVDY
CEEEEEECCCCCCCC		54.6326822725
245UbiquitinationPTIKIFQKGESPVDY
CEEEEEECCCCCCCC		54.6321890473
248PhosphorylationKIFQKGESPVDYDGG
EEEECCCCCCCCCCC		38.6024719451
252PhosphorylationKGESPVDYDGGRTRS
CCCCCCCCCCCCCHH		19.40-
257PhosphorylationVDYDGGRTRSDIVSR
CCCCCCCCHHHHHHH		37.4926437602
259PhosphorylationYDGGRTRSDIVSRAL
CCCCCCHHHHHHHHH		30.9526437602
264UbiquitinationTRSDIVSRALDLFSD
CHHHHHHHHHHHHCC		28.42-
268 (in isoform 2)Ubiquitination-4.62-
270PhosphorylationSRALDLFSDNAPPPE
HHHHHHHCCCCCCHH		36.93-
288UbiquitinationIINEDIAKRTCEEHQ
HHCHHHHHCCCHHHC		48.88-
289UbiquitinationINEDIAKRTCEEHQL
HCHHHHHCCCHHHCH		35.27-
293UbiquitinationIAKRTCEEHQLCVVA
HHHCCCHHHCHHHEE		38.80-
293 (in isoform 2)Ubiquitination-38.8021890473
293UbiquitinationIAKRTCEEHQLCVVA
HHHCCCHHHCHHHEE		38.8021890473
293UbiquitinationIAKRTCEEHQLCVVA
HHHCCCHHHCHHHEE		38.8021890473
297UbiquitinationTCEEHQLCVVAVLPH
CCHHHCHHHEEHHHH		1.5421890473
297 (in isoform 2)Ubiquitination-1.5421890473
297UbiquitinationTCEEHQLCVVAVLPH
CCHHHCHHHEEHHHH		1.5421890473
315PhosphorylationTGAAGRNSYLEVLLK
CCCCCCCHHHHHHHH		29.7228152594
316PhosphorylationGAAGRNSYLEVLLKL
CCCCCCHHHHHHHHH		15.4928152594
368MalonylationAINARKMKFALLKGS
HHHHHHHCEEHHHCC		30.4426320211
368UbiquitinationAINARKMKFALLKGS
HHHHHHHCEEHHHCC		30.4421890473
368 (in isoform 1)Ubiquitination-30.4421890473
368UbiquitinationAINARKMKFALLKGS
HHHHHHHCEEHHHCC		30.44-
368UbiquitinationAINARKMKFALLKGS
HHHHHHHCEEHHHCC		30.4421890473
373UbiquitinationKMKFALLKGSFSEQG
HHCEEHHHCCCCHHH		54.05-
375PhosphorylationKFALLKGSFSEQGIN
CEEHHHCCCCHHHHH		24.8221712546
377PhosphorylationALLKGSFSEQGINEF
EHHHCCCCHHHHHHH		30.6128348404
392MethylationLRELSFGRGSTAPVG
HHHHHCCCCCCCCCC		33.60115486883
394PhosphorylationELSFGRGSTAPVGGG
HHHCCCCCCCCCCCC		21.7521130716
395PhosphorylationLSFGRGSTAPVGGGA
HHCCCCCCCCCCCCC		37.4929449344
409MethylationAFPTIVEREPWDGRD
CCCCEEEECCCCCCC		44.37115486891
416UbiquitinationREPWDGRDGELPVED
ECCCCCCCCCCCCCC		61.52-
420 (in isoform 2)Ubiquitination-24.1321890473
420UbiquitinationDGRDGELPVEDDIDL
CCCCCCCCCCCCCCC		24.1321890473
420UbiquitinationDGRDGELPVEDDIDL
CCCCCCCCCCCCCCC		24.1321890473
428PhosphorylationVEDDIDLSDVELDDL
CCCCCCCCCCCHHHC		35.5429255136
480 (in isoform 2)Phosphorylation-21406692
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
22SPhosphorylationKinaseCSNK2A1P68400
GPS
156SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
428SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDIA6_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 PDIA6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SERPH_HUMANSERPINH1physical
22939629
TXNL1_HUMANTXNL1physical
22939629
TPIS_HUMANTPI1physical
22939629
ARPC4_HUMANARPC4physical
22863883
NRDC_HUMANNRD1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
UGDH_HUMANUGDHphysical
22863883
VWA1_HUMANVWA1physical
26186194
PLSI_HUMANPLS1physical
26186194
KLH24_HUMANKLHL24physical
26186194
C102A_HUMANCCDC102Aphysical
26186194
TRXR1_HUMANTXNRD1physical
26186194
BTBD9_HUMANBTBD9physical
26186194
HNRLL_HUMANHNRNPLLphysical
26186194
ISCA1_HUMANISCA1physical
26186194
ZHX3_HUMANZHX3physical
26186194
JMJD8_HUMANJMJD8physical
26186194
ACO13_HUMANACOT13physical
26344197
CALX_HUMANCANXphysical
26344197
CCAR2_HUMANCCAR2physical
26344197
DNJC3_HUMANDNAJC3physical
26344197
GLRX3_HUMANGLRX3physical
26344197
LMAN2_HUMANLMAN2physical
26344197
RPN1_HUMANRPN1physical
26344197
VWA1_HUMANVWA1physical
28514442
JMJD8_HUMANJMJD8physical
28514442
BTBD9_HUMANBTBD9physical
28514442
TRXR1_HUMANTXNRD1physical
28514442
ISCA1_HUMANISCA1physical
28514442
KLH24_HUMANKLHL24physical
28514442
PLSI_HUMANPLS1physical
28514442
ZHX3_HUMANZHX3physical
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 PDIA6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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-428, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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-428, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.

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