dbPTM

PP6R2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP6R2_HUMAN
UniProt AC	O75170
Protein Name	Serine/threonine-protein phosphatase 6 regulatory subunit 2
Gene Name	PPP6R2
Organism	Homo sapiens (Human).
Sequence Length	966
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	MFWKFDLNTTSHVDKLLDKEHVTLQELMDEDDILQECKAQNQKLLDFLCRQQCMEELVSLITQDPPLDMEEKVRFKYPNTACELLTCDVPQISDRLGGDESLLSLLYDFLDHEPPLNPLLASFFSKTIGNLIARKTEQVITFLKKKDKFISLVLKHIGTSALMDLLLRLVSCVEPAGLRQDVLHWLNEEKVIQRLVELIHPSQDEDRQSNASQTLCDIVRLGRDQGSQLQEALEPDPLLTALESQDCVEQLLKNMFDGDRTESCLVSGTQVLLTLLETRRVGTEGLVDSFSQGLERSYAVSSSVLHGIEPRLKDFHQLLLNPPKKKAILTTIGVLEEPLGNARLHGARLMAALLHTNTPSINQELCRLNTMDLLLDLFFKYTWNNFLHFQVELCIAAILSHAAREERTEASGSESRVEPPHENGNRSLETPQPAASLPDNTMVTHLFQKCCLVQRILEAWEANDHTQAAGGMRRGNMGHLTRIANAVVQNLERGPVQTHISEVIRGLPADCRGRWESFVEETLTETNRRNTVDLVSTHHLHSSSEDEDIEGAFPNELSLQQAFSDYQIQQMTANFVDQFGFNDEEFADQDDNINAPFDRIAEINFNIDADEDSPSAALFEACCSDRIQPFDDDEDEDIWEDSDTRCAARVMARPRFGAPHASESCSKNGPERGGQDGKASLEAHRDAPGAGAPPAPGKKEAPPVEGDSEGAMWTAVFDEPANSTPTAPGVVRDVGSSVWAAGTSAPEEKGWAKFTDFQPFCCSESGPRCSSPVDTECSHAEGSRSQGPEKASQASYFAVSPASPCAWNVCVTRKAPLLASDSSSSGGSHSEDGDQKAASAMDAVSRGPGREAPPLPTVARTEEAVGRVGCADSRLLSPACPAPKEVTAAPAVAVPPEATVAITTALSKAGPAIPTPAVSSALAVAVPLGPIMAVTAAPAMVATLGTVTKDGKTDAPPEGAALNGPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	FWKFDLNTTSHVDKL CCCCCCCCCHHHHHH	36.65	28555341
10	Phosphorylation	WKFDLNTTSHVDKLL CCCCCCCCHHHHHHH	18.76	25159151
15	Ubiquitination	NTTSHVDKLLDKEHV CCCHHHHHHHCCCCC	50.27	29967540
19	Ubiquitination	HVDKLLDKEHVTLQE HHHHHHCCCCCCHHH	50.09	29967540
38	Ubiquitination	DDILQECKAQNQKLL HHHHHHHHHHHHHHH	52.86	29967540
76	Ubiquitination	MEEKVRFKYPNTACE HHHHHCCCCCCHHHH	49.59	-
136	Phosphorylation	GNLIARKTEQVITFL HHHHHHCHHHHHHHH	26.54	23403867
141	Phosphorylation	RKTEQVITFLKKKDK HCHHHHHHHHHHHHH	24.86	23403867
145	Ubiquitination	QVITFLKKKDKFISL HHHHHHHHHHHHHHH	69.24	-
151	Phosphorylation	KKKDKFISLVLKHIG HHHHHHHHHHHHHHC	18.63	29083192
261	Phosphorylation	NMFDGDRTESCLVSG HHCCCCCHHHCEECH	36.67	-
263	Phosphorylation	FDGDRTESCLVSGTQ CCCCCHHHCEECHHH	16.49	-
269	Phosphorylation	ESCLVSGTQVLLTLL HHCEECHHHHHHHHH	14.16	-
274	Phosphorylation	SGTQVLLTLLETRRV CHHHHHHHHHHHCCC	25.74	-
278	Phosphorylation	VLLTLLETRRVGTEG HHHHHHHHCCCCCCC	24.60	-
283	Phosphorylation	LETRRVGTEGLVDSF HHHCCCCCCCHHHHH	24.83	23403867
289	Phosphorylation	GTEGLVDSFSQGLER CCCCHHHHHHHHHHH	21.22	19664994
291	Phosphorylation	EGLVDSFSQGLERSY CCHHHHHHHHHHHHH	27.56	29255136
292	Phosphorylation	GLVDSFSQGLERSYA CHHHHHHHHHHHHHH	59.48	32142685
297	Phosphorylation	FSQGLERSYAVSSSV HHHHHHHHHHHHHHH	14.20	27080861
298	Phosphorylation	SQGLERSYAVSSSVL HHHHHHHHHHHHHHH	19.76	27080861
301	Phosphorylation	LERSYAVSSSVLHGI HHHHHHHHHHHHCCC	14.55	27080861
302	Phosphorylation	ERSYAVSSSVLHGIE HHHHHHHHHHHCCCC	20.19	27080861
303	Phosphorylation	RSYAVSSSVLHGIEP HHHHHHHHHHCCCCC	22.61	27080861
370	Phosphorylation	QELCRLNTMDLLLDL HHHHHHHHHHHHHHH	19.36	22210691
427	Phosphorylation	PHENGNRSLETPQPA CCCCCCCCCCCCCCC	34.26	28192239
430	Phosphorylation	NGNRSLETPQPAASL CCCCCCCCCCCCCCC	32.30	29978859
436	Phosphorylation	ETPQPAASLPDNTMV CCCCCCCCCCCCHHH	42.41	27080861
449	Ubiquitination	MVTHLFQKCCLVQRI HHHHHHHHHHHHHHH	21.41	-
498	Phosphorylation	LERGPVQTHISEVIR HHHCCCCHHHHHHHC	22.78	25332170
501	Phosphorylation	GPVQTHISEVIRGLP CCCCHHHHHHHCCCC	20.43	25332170
536	Phosphorylation	RNTVDLVSTHHLHSS CCCEEEEEECCCCCC	29.35	24275569
542	Phosphorylation	VSTHHLHSSSEDEDI EEECCCCCCCCCCCC	41.75	24275569
543	Phosphorylation	STHHLHSSSEDEDIE EECCCCCCCCCCCCC	27.31	24275569
544	Phosphorylation	THHLHSSSEDEDIEG ECCCCCCCCCCCCCC	52.67	24275569
662	Phosphorylation	RFGAPHASESCSKNG CCCCCCCCCCCCCCC	27.32	26552605
664	Phosphorylation	GAPHASESCSKNGPE CCCCCCCCCCCCCCC	22.61	26552605
666	Phosphorylation	PHASESCSKNGPERG CCCCCCCCCCCCCCC	38.13	27251275
667	Acetylation	HASESCSKNGPERGG CCCCCCCCCCCCCCC	70.96	25953088
680	Phosphorylation	GGQDGKASLEAHRDA CCCCCCHHHHHCCCC	30.17	28555341
698	Acetylation	GAPPAPGKKEAPPVE CCCCCCCCCCCCCCC	46.51	25953088
722	Ubiquitination	AVFDEPANSTPTAPG EEECCCCCCCCCCCC	58.07	29967540
723	Phosphorylation	VFDEPANSTPTAPGV EECCCCCCCCCCCCE	37.56	27251275
723	Ubiquitination	VFDEPANSTPTAPGV EECCCCCCCCCCCCE	37.56	29967540
724	Phosphorylation	FDEPANSTPTAPGVV ECCCCCCCCCCCCEE	25.19	27251275
736	Phosphorylation	GVVRDVGSSVWAAGT CEEEECCCCCCCCCC	22.90	25693802
737	Phosphorylation	VVRDVGSSVWAAGTS EEEECCCCCCCCCCC	18.75	25693802
739 (in isoform 6)	Phosphorylation	-	5.15	25106551
742 (in isoform 6)	Phosphorylation	-	16.68	25159151
744	Phosphorylation	SVWAAGTSAPEEKGW CCCCCCCCCCCCCCC	40.69	19369195
745	Phosphorylation	VWAAGTSAPEEKGWA CCCCCCCCCCCCCCC	18.50	33259812
749	Ubiquitination	GTSAPEEKGWAKFTD CCCCCCCCCCCCCCC	59.08	29967540
755	Phosphorylation	EKGWAKFTDFQPFCC CCCCCCCCCCCCEEE	34.89	28111955
763	Phosphorylation	DFQPFCCSESGPRCS CCCCEEECCCCCCCC	35.66	26074081
765	Phosphorylation	QPFCCSESGPRCSSP CCEEECCCCCCCCCC	37.49	26074081
766 (in isoform 4)	Phosphorylation	-	15.04	25106551
767 (in isoform 2)	Phosphorylation	-	43.30	25106551
767 (in isoform 3)	Phosphorylation	-	43.30	25106551
769 (in isoform 4)	Phosphorylation	-	5.48	25159151
770	Phosphorylation	SESGPRCSSPVDTEC CCCCCCCCCCCCCCC	38.67	29255136
770 (in isoform 2)	Phosphorylation	-	38.67	25159151
770 (in isoform 3)	Phosphorylation	-	38.67	25159151
771	Phosphorylation	ESGPRCSSPVDTECS CCCCCCCCCCCCCCC	32.35	23401153
775	Phosphorylation	RCSSPVDTECSHAEG CCCCCCCCCCCCCCC	38.84	23403867
778	Phosphorylation	SPVDTECSHAEGSRS CCCCCCCCCCCCCCC	21.35	28111955
783	Phosphorylation	ECSHAEGSRSQGPEK CCCCCCCCCCCCCCH	21.92	24702127
785	Phosphorylation	SHAEGSRSQGPEKAS CCCCCCCCCCCCHHH	40.98	-
793 (in isoform 5)	Phosphorylation	-	38.91	25106551
796 (in isoform 5)	Phosphorylation	-	9.89	25159151
820	Phosphorylation	RKAPLLASDSSSSGG CCCCEECCCCCCCCC	37.69	30576142
822	Phosphorylation	APLLASDSSSSGGSH CCEECCCCCCCCCCC	29.62	23186163
823	Phosphorylation	PLLASDSSSSGGSHS CEECCCCCCCCCCCC	33.25	30576142
824	Phosphorylation	LLASDSSSSGGSHSE EECCCCCCCCCCCCC	36.63	23186163
825	Phosphorylation	LASDSSSSGGSHSED ECCCCCCCCCCCCCC	49.47	30576142
828	Phosphorylation	DSSSSGGSHSEDGDQ CCCCCCCCCCCCCCH	27.62	9734811
830	Phosphorylation	SSSGGSHSEDGDQKA CCCCCCCCCCCCHHH	38.80	30576142
839	Phosphorylation	DGDQKAASAMDAVSR CCCHHHHHHHHHHHC	29.05	30576142
843	Phosphorylation	KAASAMDAVSRGPGR HHHHHHHHHHCCCCC	6.52	32142685
844	Phosphorylation	AASAMDAVSRGPGRE HHHHHHHHHCCCCCC	3.32	32142685
845	Phosphorylation	ASAMDAVSRGPGREA HHHHHHHHCCCCCCC	32.99	24670416
870	Phosphorylation	EAVGRVGCADSRLLS HHHCCCCCCCHHCCC	3.30	32142685
873	Phosphorylation	GRVGCADSRLLSPAC CCCCCCCHHCCCCCC	13.30	28555341
877	Phosphorylation	CADSRLLSPACPAPK CCCHHCCCCCCCCCC	18.29	28985074
882 (in isoform 2)	Phosphorylation	-	27.90	22210691
886 (in isoform 2)	Phosphorylation	-	5.72	26552605
887	O-linked_Glycosylation	CPAPKEVTAAPAVAV CCCCCCCCCCCCEEC	20.42	28657654
887	Phosphorylation	CPAPKEVTAAPAVAV CCCCCCCCCCCCEEC	20.42	22210691
887 (in isoform 2)	Phosphorylation	-	20.42	26552605
899	O-linked_Glycosylation	VAVPPEATVAITTAL EECCHHHHHHHHHHH	14.60	28657654
902 (in isoform 2)	Phosphorylation	-	2.82	26552605
903	O-linked_Glycosylation	PEATVAITTALSKAG HHHHHHHHHHHHHCC	9.04	28657654
904	O-linked_Glycosylation	EATVAITTALSKAGP HHHHHHHHHHHHCCC	21.35	28657654
907	O-linked_Glycosylation	VAITTALSKAGPAIP HHHHHHHHHCCCCCC	20.28	28657654
910 (in isoform 2)	Phosphorylation	-	18.86	26552605
913 (in isoform 2)	Phosphorylation	-	4.37	26552605
915	Phosphorylation	KAGPAIPTPAVSSAL HCCCCCCCHHHHHHH	20.12	24043423
915 (in isoform 2)	Phosphorylation	-	20.12	22210691
919	O-linked_Glycosylation	AIPTPAVSSALAVAV CCCCHHHHHHHHHHC	16.40	28657654
919	Phosphorylation	AIPTPAVSSALAVAV CCCCHHHHHHHHHHC	16.40	24043423
920	O-linked_Glycosylation	IPTPAVSSALAVAVP CCCHHHHHHHHHHCC	22.24	28657654
920	Phosphorylation	IPTPAVSSALAVAVP CCCHHHHHHHHHHCC	22.24	24043423
935	Phosphorylation	LGPIMAVTAAPAMVA CCCHHHHHHHHHHHH	13.94	24043423
943	Phosphorylation	AAPAMVATLGTVTKD HHHHHHHHHCEECCC	17.82	24043423
946	Phosphorylation	AMVATLGTVTKDGKT HHHHHHCEECCCCCC	28.28	24043423
948	Phosphorylation	VATLGTVTKDGKTDA HHHHCEECCCCCCCC	24.21	24043423

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
10	T	Phosphorylation	Kinase	PLK1	P53350	PSP
289	S	Phosphorylation	Kinase	PLK1	P53350	PSP
771	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PP6R2_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 PP6R2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRKDC_HUMAN	PRKDC	physical	20065038
A4_HUMAN	APP	physical	21832049
ACSL3_HUMAN	ACSL3	physical	24255178
AIP_HUMAN	AIP	physical	24255178
AL3A2_HUMAN	ALDH3A2	physical	24255178
ANR28_HUMAN	ANKRD28	physical	24255178
ANR44_HUMAN	ANKRD44	physical	24255178
ANR52_HUMAN	ANKRD52	physical	24255178
CYBP_HUMAN	CACYBP	physical	24255178
DPCD_HUMAN	DPCD	physical	24255178
ILVBL_HUMAN	ILVBL	physical	24255178
NUDC_HUMAN	NUDC	physical	24255178
PFD2_HUMAN	PFDN2	physical	24255178
PFD5_HUMAN	PFDN5	physical	24255178
PFD6_HUMAN	PFDN6	physical	24255178
PLK1_HUMAN	PLK1	physical	24255178
PPP6_HUMAN	PPP6C	physical	24255178
PP6R1_HUMAN	PPP6R1	physical	24255178
RUVB2_HUMAN	RUVBL2	physical	24255178
SHLB2_HUMAN	SH3GLB2	physical	24255178
TTC1_HUMAN	TTC1	physical	24255178
WDR92_HUMAN	WDR92	physical	24255178
ANR52_HUMAN	ANKRD52	physical	28514442
ANR28_HUMAN	ANKRD28	physical	28514442
RPOM_HUMAN	POLRMT	physical	28514442
MUL1_HUMAN	MUL1	physical	28514442
AURKA_HUMAN	AURKA	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
S27A2_HUMAN	SLC27A2	physical	28514442
MYO5B_HUMAN	MYO5B	physical	28514442
ACD11_HUMAN	ACAD11	physical	28514442
PPP6_HUMAN	PPP6C	physical	28514442
SCPDL_HUMAN	SCCPDH	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
AP1B1_HUMAN	AP1B1	physical	28514442
PRKDC_HUMAN	PRKDC	physical	28514442
KS6A3_HUMAN	RPS6KA3	physical	28514442
AP2A1_HUMAN	AP2A1	physical	28514442
MYO5A_HUMAN	MYO5A	physical	28514442
AP1G1_HUMAN	AP1G1	physical	28514442
S26A6_HUMAN	SLC26A6	physical	28514442
GDC_HUMAN	SLC25A16	physical	28514442
AP1S2_HUMAN	AP1S2	physical	28514442
TMM43_HUMAN	TMEM43	physical	28514442
EXTL3_HUMAN	EXTL3	physical	28514442
MYO1D_HUMAN	MYO1D	physical	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 PP6R2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-289, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-289 AND SER-770, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"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-289, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-289, AND MASSSPECTROMETRY.	18691976 [Abstract]