ANR28_HUMAN - dbPTM
ANR28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR28_HUMAN
UniProt AC O15084
Protein Name Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
Gene Name ANKRD28
Organism Homo sapiens (Human).
Sequence Length 1053
Subcellular Localization Nucleus, nucleoplasm . Seems to be excluded from nucleoli.
Protein Description Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation..
Protein Sequence MAFLKLRDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSSSPLSSLTFNAINRYTNTSKTVSFEALPIMRNEPSSYCSFNNIGGEQEYLYTDVDELNDSDSETY
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
5Ubiquitination---MAFLKLRDQPSL
---CCCCCCCCCCHH		34.71-
29 (in isoform 4)Phosphorylation-10.8628450419
29 (in isoform 1)Phosphorylation-10.8628450419
32 (in isoform 4)Phosphorylation-68.7128450419
32 (in isoform 1)Phosphorylation-68.7128450419
35 (in isoform 4)Phosphorylation-40.9822617229
35 (in isoform 1)Phosphorylation-40.9828450419
41 (in isoform 4)Phosphorylation-68.7528450419
73UbiquitinationRVNAKDSKWLTPLHR
CCCCCCCCCCCHHHH		57.252189047
73AcetylationRVNAKDSKWLTPLHR
CCCCCCCCCCCHHHH		57.2519608861
73 (in isoform 2)Ubiquitination-57.2521890473
73UbiquitinationRVNAKDSKWLTPLHR
CCCCCCCCCCCHHHH		57.2521890473
84PhosphorylationPLHRAVASCSEEAVQ
HHHHHHHCCCHHHHH		16.1625693802
86PhosphorylationHRAVASCSEEAVQVL
HHHHHCCCHHHHHHH		35.6625693802
106UbiquitinationDVNARDKNWQTPLHI
CCCCCCCCCCCHHHH		40.1421890473
106UbiquitinationDVNARDKNWQTPLHI
CCCCCCCCCCCHHHH		40.1421890473
106 (in isoform 1)Ubiquitination-40.1421890473
122GlutathionylationAANKAVKCAEALVPL
HHHHHHHHHHHHHHH		3.1322555962
142PhosphorylationVSDRAGRTALHHAAF
CCCCCCCHHHHHHHH		32.4346164151
171AcetylationANINAFDKKDRRAIH
CCCCCCCHHHHHHHH		50.5523749302
171MalonylationANINAFDKKDRRAIH
CCCCCCCHHHHHHHH		50.5526320211
194PhosphorylationEVVKLLVSHGAEVTC
HHHHHHHHCCCEEEE		19.0322210691
313PhosphorylationGKTPLHMTALHGRFS
CCCCCHHEEECCCCC		18.4724247654
349PhosphorylationPLHIAARYGHELLIN
CEEEEHHHCHHHHHH		20.3629888752
357PhosphorylationGHELLINTLITSGAD
CHHHHHHHHHHCCCC		16.7329888752
360PhosphorylationLLINTLITSGADTAK
HHHHHHHHCCCCHHH		24.9929888752
390UbiquitinationGFSDCCRKLLSSGFD
CCHHHHHHHHHCCCC		39.61-
528PhosphorylationLQLIASETPLDVLME
HHHHHCCCCCHHHHH		27.0225693802
536PhosphorylationPLDVLMETSGTDMLS
CCHHHHHCCCCCCCC		20.6325693802
537PhosphorylationLDVLMETSGTDMLSD
CHHHHHCCCCCCCCC		26.7925693802
539PhosphorylationVLMETSGTDMLSDSD
HHHHCCCCCCCCCCC		20.2925693802
543PhosphorylationTSGTDMLSDSDNRAT
CCCCCCCCCCCCCCC		28.5625693802
545PhosphorylationGTDMLSDSDNRATIS
CCCCCCCCCCCCCCC		33.1525693802
671PhosphorylationGHTDCVYSLLNKGAN
CCCHHHHHHHHCCCC		13.1424719451
688PhosphorylationAKDKWGRTALHRGAV
CCCCCCCHHHHCCCC		29.6326546556
696PhosphorylationALHRGAVTGHEECVD
HHHCCCCCCCHHHHH		32.0846164157
711UbiquitinationALLQHGAKCLLRDSR
HHHHCCCEEEECCCC		29.97-
982PhosphorylationCLALILATMMPVSSS
HHHHHHHHHCCCCCC		15.5720068231
987PhosphorylationLATMMPVSSSSPLSS
HHHHCCCCCCCCHHH		20.7325159151
988PhosphorylationATMMPVSSSSPLSSL
HHHCCCCCCCCHHHC		34.7625627689
989PhosphorylationTMMPVSSSSPLSSLT
HHCCCCCCCCHHHCC		28.5920068231
990PhosphorylationMMPVSSSSPLSSLTF
HCCCCCCCCHHHCCH		31.6329496963
993PhosphorylationVSSSSPLSSLTFNAI
CCCCCCHHHCCHHHH		27.0426074081
994PhosphorylationSSSSPLSSLTFNAIN
CCCCCHHHCCHHHHH		38.8326074081
996PhosphorylationSSPLSSLTFNAINRY
CCCHHHCCHHHHHHC		19.4526074081
1003PhosphorylationTFNAINRYTNTSKTV
CHHHHHHCCCCCCEE		10.3921712546
1004PhosphorylationFNAINRYTNTSKTVS
HHHHHHCCCCCCEEE		28.8726074081
1006PhosphorylationAINRYTNTSKTVSFE
HHHHCCCCCCEEEEE		24.6526074081
1007PhosphorylationINRYTNTSKTVSFEA
HHHCCCCCCEEEEEE		28.5317023142
1008UbiquitinationNRYTNTSKTVSFEAL
HHCCCCCCEEEEEEE		51.40-
1009PhosphorylationRYTNTSKTVSFEALP
HCCCCCCEEEEEEEC		22.5830266825
1009O-linked_GlycosylationRYTNTSKTVSFEALP
HCCCCCCEEEEEEEC		22.5828657654
1011PhosphorylationTNTSKTVSFEALPIM
CCCCCEEEEEEECCC		23.7029255136
1037PhosphorylationNIGGEQEYLYTDVDE
CCCCCEEEEEECHHH		12.5228348404
1039PhosphorylationGGEQEYLYTDVDELN
CCCEEEEEECHHHCC		10.4528348404
1040PhosphorylationGEQEYLYTDVDELND
CCEEEEEECHHHCCC		27.2728348404
1044PhosphorylationYLYTDVDELNDSDSE
EEEECHHHCCCCCCC		49.6918669648
1048PhosphorylationDVDELNDSDSETY--
CHHHCCCCCCCCC--		41.8018691976
1050PhosphorylationDELNDSDSETY----
HHCCCCCCCCC----		35.4726074081
1052PhosphorylationLNDSDSETY------
CCCCCCCCC------		38.1825841592
1053PhosphorylationNDSDSETY-------
CCCCCCCC-------		16.7125841592
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
1007SPhosphorylationKinaseGSK3AP49840
PSP
1011SPhosphorylationKinaseCAMK2DQ13557
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR28_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 ANR28_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGM2_HUMANTGM2physical
21988832
CSK2B_HUMANCSNK2Bphysical
21988832
UBP10_HUMANUSP10physical
24255178
ACACB_HUMANACACBphysical
24255178
AKP8L_HUMANAKAP8Lphysical
24255178
ANR44_HUMANANKRD44physical
24255178
APC_HUMANAPCphysical
24255178
ARHG2_HUMANARHGEF2physical
24255178
DNJB1_HUMANDNAJB1physical
24255178
EPS8_HUMANEPS8physical
24255178
ABRX2_HUMANFAM175Bphysical
24255178
F193A_HUMANFAM193Aphysical
24255178
FBF1_HUMANFBF1physical
24255178
HECD1_HUMANHECTD1physical
24255178
CE162_HUMANCEP162physical
24255178
KRI1_HUMANKRI1physical
24255178
MAGD1_HUMANMAGED1physical
24255178
MTMR3_HUMANMTMR3physical
24255178
NEK4_HUMANNEK4physical
24255178
NFAC4_HUMANNFATC4physical
24255178
NOTC2_HUMANNOTCH2physical
24255178
PKHG1_HUMANPLEKHG1physical
24255178
NEB1_HUMANPPP1R9Aphysical
24255178
NEB2_HUMANPPP1R9Bphysical
24255178
PPP6_HUMANPPP6Cphysical
24255178
PP6R1_HUMANPPP6R1physical
24255178
PP6R2_HUMANPPP6R2physical
24255178
PP6R3_HUMANPPP6R3physical
24255178
RAD21_HUMANRAD21physical
24255178
RASF8_HUMANRASSF8physical
24255178
RCN2_HUMANRCN2physical
24255178
SDCG3_HUMANSDCCAG3physical
24255178
SC16A_HUMANSEC16Aphysical
24255178
SHKB1_HUMANSHKBP1physical
24255178
SMC1A_HUMANSMC1Aphysical
24255178
SMC3_HUMANSMC3physical
24255178
SNX18_HUMANSNX18physical
24255178
TBK1_HUMANTBK1physical
24255178
TBKB1_HUMANTBKBP1physical
24255178
TRI41_HUMANTRIM41physical
24255178
UBR5_HUMANUBR5physical
24255178
BRCA1_HUMANBRCA1physical
27026398
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 ANR28_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-1011, AND MASSSPECTROMETRY.
"PITK, a PP1 targeting subunit that modulates the phosphorylation ofthe transcriptional regulator hnRNP K.";
Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
Cell. Signal. 18:1769-1778(2006).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1C AND HNRPK,PHOSPHORYLATION AT SER-1007 AND SER-1011, AND MUTAGENESIS OF1007-SER--SER-1011.

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