AKAP8_MOUSE - dbPTM
AKAP8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKAP8_MOUSE
UniProt AC Q9DBR0
Protein Name A-kinase anchor protein 8
Gene Name Akap8
Organism Mus musculus (Mouse).
Sequence Length 687
Subcellular Localization Nucleus matrix . Nucleus, nucleolus . Cytoplasm . Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis (By similarity). Localizes specifically to the vicinity of the meiotic spindle in metaphase II oo
Protein Description Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (By similarity). Specifically involved in recruitment of CAPD2 to, and condensation of maternal but not paternal chromosomes. [PubMed: 12082153 May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression]
Protein Sequence MEQGYGGYGAWSAGPANTQGTYGSGMTSWQGYENYNYYNAQNTSVPAGTPYSYGPASWEATKTNDGGLAAGSPAMHVASFAPEPCTDNSDSLIAKINQRLDMLSKEGGRGGISSGGEGVQDRDSSFRFQPYESYDARPCIPEHNPYRPGYGYDYDFDLGTDRNGSFGGTFNDCRDPAPERGSLDGFLRGRGQGRFQDRSNSSTFIRSDPFMPPSASEPLSTTWNELNYMGGRGLGGPSTSRPPPSLFSQSMAPDYSMMGMQGVGGFGGTMPYGCGRSQTRIRDWPRRRGFERFGPDNMGRKRKQFPLYEEPDAKLARADSDGDLSENDDGAGDLRSGDEEFRGEDDLCDSRKQRGEKEDEDEDVKKRREKQRRRDRMRDRAADRIQFACSVCKFRSFEDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIINRNKKIEKRRQELLEKESPKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQHQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNKHIVKMLEKYLKGEDPFVNETADLETEGDENVGEEKEETPEEVAAEVLAEVITAAVKAVEGEGEPAAAHSDVLTEVEGPVDTAEASSDPHTEKLLEEQTCEAASETRSIEDKTRGEAAEARNEAAMPTADAGSTLPVIAIPGIMEDELEQTGAEAKDIPTE
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
63PhosphorylationASWEATKTNDGGLAA
CCCEEEECCCCCCCC		33.9025619855
72PhosphorylationDGGLAAGSPAMHVAS
CCCCCCCCCCEEEHH		12.5421082442
79PhosphorylationSPAMHVASFAPEPCT
CCCEEEHHCCCCCCC		22.3525619855
109Asymmetric dimethylarginineMLSKEGGRGGISSGG
HHHHCCCCCCCCCCC		51.53-
109MethylationMLSKEGGRGGISSGG
HHHHCCCCCCCCCCC		51.5324129315
113PhosphorylationEGGRGGISSGGEGVQ
CCCCCCCCCCCCCCC		26.6329472430
114PhosphorylationGGRGGISSGGEGVQD
CCCCCCCCCCCCCCC		49.2328066266
124PhosphorylationEGVQDRDSSFRFQPY
CCCCCCCCCCCCCCC		32.0728066266
125PhosphorylationGVQDRDSSFRFQPYE
CCCCCCCCCCCCCCC		25.4028066266
188MethylationGSLDGFLRGRGQGRF
CCCCHHHCCCCCCCC		30.42-
190MethylationLDGFLRGRGQGRFQD
CCHHHCCCCCCCCCC		28.03-
199PhosphorylationQGRFQDRSNSSTFIR
CCCCCCCCCCCCEEE		49.7225266776
201PhosphorylationRFQDRSNSSTFIRSD
CCCCCCCCCCEEECC		31.81103260605
202PhosphorylationFQDRSNSSTFIRSDP
CCCCCCCCCEEECCC		31.4228066266
203PhosphorylationQDRSNSSTFIRSDPF
CCCCCCCCEEECCCC		23.9328066266
232MethylationELNYMGGRGLGGPST
HHHCCCCCCCCCCCC		31.2824129315
276MethylationTMPYGCGRSQTRIRD
CCCCCCCCCCHHCCC		29.6624129315
286DimethylationTRIRDWPRRRGFERF
HHCCCCCCCCCCHHH		36.35-
287DimethylationRIRDWPRRRGFERFG
HCCCCCCCCCCHHHC		38.71-
288DimethylationIRDWPRRRGFERFGP
CCCCCCCCCCHHHCC		56.27-
301AcetylationGPDNMGRKRKQFPLY
CCCCCCCCCCCCCCC		59.217618135
308PhosphorylationKRKQFPLYEEPDAKL
CCCCCCCCCCCCHHH		20.6325159016
320PhosphorylationAKLARADSDGDLSEN
HHHCCCCCCCCCCCC		42.3727087446
325PhosphorylationADSDGDLSENDDGAG
CCCCCCCCCCCCCCC		38.8127087446
336PhosphorylationDGAGDLRSGDEEFRG
CCCCCCCCCCHHHCC		58.8727087446
350PhosphorylationGEDDLCDSRKQRGEK
CCCCCCHHHHHHCCC		40.1425159016
396PhosphorylationCSVCKFRSFEDEEIQ
HHHHCCCCCCHHHHH		35.8026643407
419PhosphorylationKETLRFISTKLPDKT
HHHHHHHHHCCCCHH		19.4423140645
453PhosphorylationQELLEKESPKPKPDP
HHHHHHCCCCCCCCC		49.6526824392
521AcetylationKTSLHVAKSVLNNKH
HHHHHHHHHHHCCHH		39.7522826441
547PhosphorylationEDPFVNETADLETEG
CCCCCCCCCCCCCCC		21.9225619855
552PhosphorylationNETADLETEGDENVG
CCCCCCCCCCCCCCC		53.1925521595
565PhosphorylationVGEEKEETPEEVAAE
CCCCCCCCHHHHHHH		36.7727180971
596PhosphorylationGEPAAAHSDVLTEVE
CCCCHHCCCCCEEEE		25.3726745281
600PhosphorylationAAHSDVLTEVEGPVD
HHCCCCCEEEECCCC		37.5226745281
608PhosphorylationEVEGPVDTAEASSDP
EEECCCCHHHHCCCH		26.9921659605
612PhosphorylationPVDTAEASSDPHTEK
CCCHHHHCCCHHHHH		27.1225777480
613PhosphorylationVDTAEASSDPHTEKL
CCHHHHCCCHHHHHH		63.3125777480
617PhosphorylationEASSDPHTEKLLEEQ
HHCCCHHHHHHHHHH		39.9625777480
625PhosphorylationEKLLEEQTCEAASET
HHHHHHHHHHHHHHC		18.6526745281
630PhosphorylationEQTCEAASETRSIED
HHHHHHHHHCCCHHH		46.6926824392
632PhosphorylationTCEAASETRSIEDKT
HHHHHHHCCCHHHHH		27.5026239621
634PhosphorylationEAASETRSIEDKTRG
HHHHHCCCHHHHHHH		37.4425521595
639PhosphorylationTRSIEDKTRGEAAEA
CCCHHHHHHHHHHHH		57.1126160508
659PhosphorylationMPTADAGSTLPVIAI
CCCCCCCCCCCEEEC		28.61-
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 AKAP8_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKAP8_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 AKAP8_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRH3_HUMANHNRNPH3physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
PKP4_HUMANPKP4physical
26496610
FUBP3_HUMANFUBP3physical
26496610
MATR3_HUMANMATR3physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
F120A_HUMANFAM120Aphysical
26496610
MYCBP_HUMANMYCBPphysical
26496610
AKP8L_HUMANAKAP8Lphysical
26496610
YLPM1_HUMANYLPM1physical
26496610
DPY30_HUMANDPY30physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AKAP8_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-325, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-325 ANDSER-336, AND MASS SPECTROMETRY.
"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-320 AND SER-336, ANDMASS SPECTROMETRY.

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