PP6R1_HUMAN - dbPTM
PP6R1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP6R1_HUMAN
UniProt AC Q9UPN7
Protein Name Serine/threonine-protein phosphatase 6 regulatory subunit 1
Gene Name PPP6R1
Organism Homo sapiens (Human).
Sequence Length 881
Subcellular Localization Cytoplasm .
Protein Description Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha..
Protein Sequence MFWKFDLHTSSHLDTLLEREDLSLPELLDEEDVLQECKVVNRKLLDFLLQPPHLQAMVAWVTQEPPDSGEERLRYKYPSVACEILTSDVPQINDALGADESLLNRLYGFLQSTGSLNPLLASFFSKVMGILINRKTDQLVSFLRKKDDFVDLLLQHIGTSAIMDLLLRLLTCVERPQLRQDVVNWLNEEKIVQRLIEQIHPSKDENQHSNASQSLCDIIRLSREQMIQVQDSPEPDQLLATLEKQETIEQLLSNMFEGEQSQSVIVSGIQVLLTLLEPRRPRSESVTVNSFFSSVDGQLELLAQGALESTVSSVGALHALRPRLSCFHQLLLEPPKLEPLQMTWGMLAPPLGNTRLHVVKLLASALSANDAALTHELLALDVPNTMLDLFFHYVFNNFLHAQVEGCVSTMLSLGPPPDSSPETPIQNPVVKHLLQQCRLVERILTSWEENDRVQCAGGPRKGYMGHLTRVAGALVQNTEKGPNAEQLRQLLKELPSEQQEQWEAFVSGPLAETNKKNMVDLVNTHHLHSSSDDEDDRLKEFNFPEEAVLQQAFMDFQMQRMTSAFIDHFGFNDEEFGEQEESVNAPFDKTANITFSLNADDENPNANLLEICYKDRIQQFDDDEEEEDEEEAQGSGESDGEDGAWQGSQLARGARLGQPPGVRSGGSTDSEDEEEEDEEEEEDEEGIGCAARGGATPLSYPSPGPQPPGPSWTATFDPVPTDAPTSPRVSGEEELHTGPPAPQGPLSVPQGLPTQSLASPPARDALQLRSQDPTPPSAPQEATEGSKVTEPSAPCQALVSIGDLQATFHGIRSAPSSSDSATRDPSTSVPASGAHQPPQTTEGEKSPEPLGLPQSQSAQALTPPPIPNGSAPEGPASPGSQ
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
38UbiquitinationEDVLQECKVVNRKLL
HHHHHHCHHHCHHHH		48.7629967540
76UbiquitinationGEERLRYKYPSVACE
CCHHHHHCCCHHHHH		44.2221963094
135UbiquitinationMGILINRKTDQLVSF
HHHHHCCCHHHHHHH		52.5521906983
190UbiquitinationVNWLNEEKIVQRLIE
HHHHCHHHHHHHHHH		41.831906983
197 (in isoform 1)Ubiquitination-48.3421906983
203UbiquitinationIEQIHPSKDENQHSN
HHHHCCCCCCCCCCC		73.7921963094
232PhosphorylationQMIQVQDSPEPDQLL
HCCCCCCCCCHHHHH		17.67-
241PhosphorylationEPDQLLATLEKQETI
CHHHHHHHHHHHHHH		35.1024719451
252 (in isoform 1)Ubiquitination-3.3021906983
412PhosphorylationGCVSTMLSLGPPPDS
HHHHHHHHCCCCCCC		22.0626074081
419PhosphorylationSLGPPPDSSPETPIQ
HCCCCCCCCCCCCCC		54.2726074081
420PhosphorylationLGPPPDSSPETPIQN
CCCCCCCCCCCCCCC		33.8526074081
423PhosphorylationPPDSSPETPIQNPVV
CCCCCCCCCCCCHHH		29.1326074081
461UbiquitinationQCAGGPRKGYMGHLT
ECCCCCCCCHHHHHH		58.4922505724
463PhosphorylationAGGPRKGYMGHLTRV
CCCCCCCHHHHHHHH		11.7122210691
468PhosphorylationKGYMGHLTRVAGALV
CCHHHHHHHHHHHHH		19.88-
480UbiquitinationALVQNTEKGPNAEQL
HHHHCCCCCCCHHHH		77.0921906983
480AcetylationALVQNTEKGPNAEQL
HHHHCCCCCCCHHHH		77.0925953088
492UbiquitinationEQLRQLLKELPSEQQ
HHHHHHHHHCCHHHH		66.8421906983
513PhosphorylationVSGPLAETNKKNMVD
HHCCCHHCCCCCHHH		46.8926074081
515UbiquitinationGPLAETNKKNMVDLV
CCCHHCCCCCHHHHH		53.6029967540
516UbiquitinationPLAETNKKNMVDLVN
CCHHCCCCCHHHHHH		52.9623503661
524PhosphorylationNMVDLVNTHHLHSSS
CHHHHHHHCCCCCCC		11.8223401153
529PhosphorylationVNTHHLHSSSDDEDD
HHHCCCCCCCCCCCH		37.5929255136
530PhosphorylationNTHHLHSSSDDEDDR
HHCCCCCCCCCCCHH		27.3429255136
531PhosphorylationTHHLHSSSDDEDDRL
HCCCCCCCCCCCHHH		52.6929255136
542 (in isoform 1)Ubiquitination-53.2921906983
554 (in isoform 1)Ubiquitination-5.9021906983
577 (in isoform 1)Ubiquitination-38.6721906983
635PhosphorylationDEEEAQGSGESDGED
HHHHHCCCCCCCCCC		27.5726503892
638PhosphorylationEAQGSGESDGEDGAW
HHCCCCCCCCCCCCC		55.2126503892
648PhosphorylationEDGAWQGSQLARGAR
CCCCCCHHHHHHCCC		13.6128176443
664PhosphorylationGQPPGVRSGGSTDSE
CCCCCCCCCCCCCCC		45.1321712546
667PhosphorylationPGVRSGGSTDSEDEE
CCCCCCCCCCCCCCH		32.3521712546
668PhosphorylationGVRSGGSTDSEDEEE
CCCCCCCCCCCCCHH		46.9821712546
670PhosphorylationRSGGSTDSEDEEEED
CCCCCCCCCCCHHHH		47.2221712546
696PhosphorylationCAARGGATPLSYPSP
CCCCCCCCCCCCCCC		28.2126552605
699PhosphorylationRGGATPLSYPSPGPQ
CCCCCCCCCCCCCCC		35.8826552605
700PhosphorylationGGATPLSYPSPGPQP
CCCCCCCCCCCCCCC		18.5326552605
702PhosphorylationATPLSYPSPGPQPPG
CCCCCCCCCCCCCCC		33.9728176443
711PhosphorylationGPQPPGPSWTATFDP
CCCCCCCCCEEEECC		42.8728450419
713PhosphorylationQPPGPSWTATFDPVP
CCCCCCCEEEECCCC		21.8428450419
715PhosphorylationPGPSWTATFDPVPTD
CCCCCEEEECCCCCC		22.6125106551
721PhosphorylationATFDPVPTDAPTSPR
EEECCCCCCCCCCCC		45.0630206219
725PhosphorylationPVPTDAPTSPRVSGE
CCCCCCCCCCCCCCC		53.7528176443
726PhosphorylationVPTDAPTSPRVSGEE
CCCCCCCCCCCCCCC		15.0628176443
730PhosphorylationAPTSPRVSGEEELHT
CCCCCCCCCCCCCCC		41.5926552605
737PhosphorylationSGEEELHTGPPAPQG
CCCCCCCCCCCCCCC		65.1026552605
747PhosphorylationPAPQGPLSVPQGLPT
CCCCCCCCCCCCCCC		34.5826552605
754PhosphorylationSVPQGLPTQSLASPP
CCCCCCCCCCCCCCC		35.5128176443
756PhosphorylationPQGLPTQSLASPPAR
CCCCCCCCCCCCCHH		28.5123401153
759PhosphorylationLPTQSLASPPARDAL
CCCCCCCCCCHHHHH		36.3929255136
770PhosphorylationRDALQLRSQDPTPPS
HHHHHHHCCCCCCCC		47.7529970186
774PhosphorylationQLRSQDPTPPSAPQE
HHHCCCCCCCCCCCC		57.0021815630
789PhosphorylationATEGSKVTEPSAPCQ
CCCCCCCCCCCCCCC		46.0125693802
792PhosphorylationGSKVTEPSAPCQALV
CCCCCCCCCCCCEEE		38.3125693802
800PhosphorylationAPCQALVSIGDLQAT
CCCCEEEEHHHHHHE		23.0025693802
816PhosphorylationHGIRSAPSSSDSATR
ECHHCCCCCCCCCCC		42.0428555341
817PhosphorylationGIRSAPSSSDSATRD
CHHCCCCCCCCCCCC		36.79-
846PhosphorylationQTTEGEKSPEPLGLP
CCCCCCCCCCCCCCC		30.14-
857PhosphorylationLGLPQSQSAQALTPP
CCCCCCCCCCCCCCC		27.8228270605
862PhosphorylationSQSAQALTPPPIPNG
CCCCCCCCCCCCCCC		36.4425159151
870PhosphorylationPPPIPNGSAPEGPAS
CCCCCCCCCCCCCCC		47.4928270605
877PhosphorylationSAPEGPASPGSQ---
CCCCCCCCCCCC---		32.6925159151
880PhosphorylationEGPASPGSQ------
CCCCCCCCC------		35.7826074081
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 PP6R1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP6R1_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 PP6R1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRKDC_HUMANPRKDCphysical
20065038
UBP10_HUMANUSP10physical
24255178
ACD11_HUMANACAD11physical
24255178
ACSL3_HUMANACSL3physical
24255178
AL3A2_HUMANALDH3A2physical
24255178
ANR28_HUMANANKRD28physical
24255178
ANR44_HUMANANKRD44physical
24255178
ANR52_HUMANANKRD52physical
24255178
ARHG2_HUMANARHGEF2physical
24255178
CNOT1_HUMANCNOT1physical
24255178
CNO10_HUMANCNOT10physical
24255178
TF3C4_HUMANGTF3C4physical
24255178
ECHA_HUMANHADHAphysical
24255178
ECHB_HUMANHADHBphysical
24255178
HSP74_HUMANHSPA4physical
24255178
ELP1_HUMANIKBKAPphysical
24255178
ILVBL_HUMANILVBLphysical
24255178
C2CD5_HUMANC2CD5physical
24255178
KNTC1_HUMANKNTC1physical
24255178
PDCD2_HUMANPDCD2physical
24255178
PFD2_HUMANPFDN2physical
24255178
PFD5_HUMANPFDN5physical
24255178
PFD6_HUMANPFDN6physical
24255178
PPP6_HUMANPPP6Cphysical
24255178
PP6R2_HUMANPPP6R2physical
24255178
SGPL1_HUMANSGPL1physical
24255178
SRPRA_HUMANSRPRphysical
24255178
SRPRB_HUMANSRPRBphysical
24255178
TTF2_HUMANTTF2physical
24255178
AGO1_HUMANAGO1physical
24778252
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 PP6R1_HUMAN

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Related Literatures of Post-Translational Modification
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-635; SER-638; SER-702;SER-726 AND SER-759, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, 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-635; SER-638; SER-664;SER-667; THR-668; SER-670 AND SER-759, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASSSPECTROMETRY.

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