ANR28_MOUSE - dbPTM
ANR28_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR28_MOUSE
UniProt AC Q505D1
Protein Name Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
Gene Name Ankrd28
Organism Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence MAFLKLRDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYVLKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSATSVDANPAVVDNHGYTALHWACYNGHETCVELLLEQDVFQKIDGNAFSPLHCAVINDNEGAAEMLIDSLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSQNAQVNSADSTGKTPLMMAAENGQTNTVEMLVSSASADLTLQDKSKNTALHLACGKGHETSALLILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSSSPLTSLTFNAINRYTNTSKTVSFEALPIMRNEASSYCSFNNIGGEQEYLYTDVDELNDSDSETY
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
84PhosphorylationPLHRAVASCSEEAVQ
HHHHHHHCCCHHHHH
16.1617203969
308PhosphorylationMKSKDGKTPLHMTAL
CCCCCCCCCCHHEEE
36.2922871156
313PhosphorylationGKTPLHMTALHGRFS
CCCCCHHEEECCCCC
18.4722871156
528PhosphorylationLQLIASETPLDVLME
HHHHHCCCCCHHHHH
27.0221183079
671PhosphorylationGHTDCVYSLLNKGAN
CCCHHHHHHHHCCCC
13.1429899451
1007PhosphorylationINRYTNTSKTVSFEA
HHCCCCCCCEEEEEE
28.53-
1008UbiquitinationNRYTNTSKTVSFEAL
HCCCCCCCEEEEEEE
51.4022790023
1009PhosphorylationRYTNTSKTVSFEALP
CCCCCCCEEEEEEEC
22.5822324799
1009O-linked_GlycosylationRYTNTSKTVSFEALP
CCCCCCCEEEEEEEC
22.5855410887
1011PhosphorylationTNTSKTVSFEALPIM
CCCCCEEEEEEECCC
23.7023527152

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 ANR28_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR28_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPP6_HUMANPPP6Cphysical
26496610
ARHG2_HUMANARHGEF2physical
26496610
NGAP_HUMANRASAL2physical
26496610
PP6R2_HUMANPPP6R2physical
26496610
PP6R1_HUMANPPP6R1physical
26496610
PP6R3_HUMANPPP6R3physical
26496610
KDEL1_HUMANKDELC1physical
26496610
ANR52_HUMANANKRD52physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANR28_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND MASSSPECTROMETRY.

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