dbPTM

AKAP8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AKAP8_HUMAN
UniProt AC	O43823
Protein Name	A-kinase anchor protein 8
Gene Name	AKAP8
Organism	Homo sapiens (Human).
Sequence Length	692
Subcellular Localization	Nucleus . Nucleus matrix . Nucleus, nucleolus . Cytoplasm . Associated with the nuclear matrix in interphase and redistributes mostly to chromatin at mitosis. However, mitotic chromatin localization has been questioned. Upon nuclear reassembly at the
Protein Description	Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). [PubMed: 9473338 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]
Protein Sequence	MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEAAKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQDRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARERGSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSPSRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDGTGRKRKQFQLYEEPDTKLARVDSEGDFSENDDAAGDFRSGDEEFKGEDELCDSGRQRGEKEDEDEDVKKRREKQRRRDRTRDRAADRIQFACSVCKFRSFDDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIVNRNKKIEKRRQELMEKETAKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQPQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNRHIVKMLEKYLKGEDPFTSETVDPEMEGDDNLGGEDKKETPEEVAADVLAEVITAAVRAVDGEGAPAPESSGEPAEDEGPTDTAEAGSDPQAEQLLEEQVPCGTAHEKGVPKARSEAAEAGNGAETMAAEAESAQTRVAPAPAAADAEVEQTDAESKDAVPTE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
51	Phosphorylation	SVTTGATYSYGPASW CCCCCCEEEECCHHH	10.20	80839809
53	Phosphorylation	TTGATYSYGPASWEA CCCCEEEECCHHHHH	19.40	80839807
79	Phosphorylation	APAMHMASYGPEPCT CCCCCCHHCCCCCCC	24.05	21945579
80	Phosphorylation	PAMHMASYGPEPCTD CCCCCHHCCCCCCCC	27.45	21945579
86	Phosphorylation	SYGPEPCTDNSDSLI HCCCCCCCCCCHHHH	49.26	21945579
89	Phosphorylation	PEPCTDNSDSLIAKI CCCCCCCCHHHHHHH	31.24	21945579
91	Phosphorylation	PCTDNSDSLIAKINQ CCCCCCHHHHHHHHH	22.84	21945579
95	Acetylation	NSDSLIAKINQRLDM CCHHHHHHHHHHHHH	34.88	26051181
95	Ubiquitination	NSDSLIAKINQRLDM CCHHHHHHHHHHHHH	34.88	29967540
109	Asymmetric dimethylarginine	MMSKEGGRGGSGGGG HHHCCCCCCCCCCCC	58.10	-
109	Methylation	MMSKEGGRGGSGGGG HHHCCCCCCCCCCCC	58.10	-
112	Phosphorylation	KEGGRGGSGGGGEGI CCCCCCCCCCCCCCC	36.77	23401153
124	Phosphorylation	EGIQDRESSFRFQPF CCCCCCCCCCCCCCC	35.35	28555341
136	Phosphorylation	QPFESYDSRPCLPEH CCCCCCCCCCCCCCC	29.86	11664347
146	Phosphorylation	CLPEHNPYRPSYSYD CCCCCCCCCCCCCEE	40.24	80839803
149	Phosphorylation	EHNPYRPSYSYDYEF CCCCCCCCCCEEEEE	20.08	30455651
150	Phosphorylation	HNPYRPSYSYDYEFD CCCCCCCCCEEEEEE	17.58	30814935
152	Phosphorylation	PYRPSYSYDYEFDLG CCCCCCCEEEEEECC	17.82	14733435
154	Phosphorylation	RPSYSYDYEFDLGSD CCCCCEEEEEECCCC	15.40	138797
165	Phosphorylation	LGSDRNGSFGGQYSE CCCCCCCCCCCCCCC	25.02	82900463
170	Phosphorylation	NGSFGGQYSECRDPA CCCCCCCCCCCCCHH	15.09	30835193
182	Phosphorylation	DPARERGSLDGFMRG CHHHHHCCCCHHHCC	29.52	28450419
188	Methylation	GSLDGFMRGRGQGRF CCCCHHHCCCCCCCC	29.42	-
190	Methylation	LDGFMRGRGQGRFQD CCHHHCCCCCCCCCC	24.73	-
194	Methylation	MRGRGQGRFQDRSNP HCCCCCCCCCCCCCC	20.40	-
198	Methylation	GQGRFQDRSNPGTFM CCCCCCCCCCCCCCC	27.79	-
199	Phosphorylation	QGRFQDRSNPGTFMR CCCCCCCCCCCCCCC	56.52	28450419
206	Ubiquitination	SNPGTFMRSDPFVPP CCCCCCCCCCCCCCC	33.44	24816145
207	O-linked_Glycosylation	NPGTFMRSDPFVPPA CCCCCCCCCCCCCCC	37.54	30620550
216	O-linked_Glycosylation	PFVPPAASSEPLSTP CCCCCCCCCCCCCCC	37.02	30620550
217	O-linked_Glycosylation	FVPPAASSEPLSTPW CCCCCCCCCCCCCCH	38.21	30620550
221	O-linked_Glycosylation	AASSEPLSTPWNELN CCCCCCCCCCHHHCC	43.04	30620550
222	O-linked_Glycosylation	ASSEPLSTPWNELNY CCCCCCCCCHHHCCC	39.75	30620550
229	Phosphorylation	TPWNELNYVGGRGLG CCHHHCCCCCCCCCC	17.07	17360941
232	Ubiquitination	NELNYVGGRGLGGPS HHCCCCCCCCCCCCC	15.50	24816145
233	Methylation	ELNYVGGRGLGGPSP HCCCCCCCCCCCCCC	31.10	-
239	Phosphorylation	GRGLGGPSPSRPPPS CCCCCCCCCCCCCCC	38.49	26074081
241	Phosphorylation	GLGGPSPSRPPPSLF CCCCCCCCCCCCCHH	62.85	26074081
242	Methylation	LGGPSPSRPPPSLFS CCCCCCCCCCCCHHC	51.64	-
246	Phosphorylation	SPSRPPPSLFSQSMA CCCCCCCCHHCCCCC	48.06	26074081
249	Phosphorylation	RPPPSLFSQSMAPDY CCCCCHHCCCCCCCC	27.00	26074081
251	Phosphorylation	PPSLFSQSMAPDYGV CCCHHCCCCCCCCCC	18.73	26074081
260	Ubiquitination	APDYGVMGMQGAGGY CCCCCCCCCCCCCCC	11.67	24816145
277	Methylation	TMPYGCGRSQPRMRD CCCCCCCCCCCCCCC	35.87	24129315
281	Methylation	GCGRSQPRMRDRDRP CCCCCCCCCCCCCCC	25.73	-
286	Ubiquitination	QPRMRDRDRPKRRGF CCCCCCCCCCCCCCC	75.43	24816145
301	Phosphorylation	DRFGPDGTGRKRKQF CCCCCCCCCCCCCEE	40.99	46161493
306	Ubiquitination	DGTGRKRKQFQLYEE CCCCCCCCEEEEECC	59.50	24816145
311	Phosphorylation	KRKQFQLYEEPDTKL CCCEEEEECCCCCCC	13.89	21945579
316	Phosphorylation	QLYEEPDTKLARVDS EEECCCCCCCEEECC	38.38	21945579
317	Sumoylation	LYEEPDTKLARVDSE EECCCCCCCEEECCC	47.75	28112733
317	Ubiquitination	LYEEPDTKLARVDSE EECCCCCCCEEECCC	47.75	29967540
323	Phosphorylation	TKLARVDSEGDFSEN CCCEEECCCCCCCCC	40.39	29255136
328	Phosphorylation	VDSEGDFSENDDAAG ECCCCCCCCCCCCCC	39.98	19664994
339	Phosphorylation	DAAGDFRSGDEEFKG CCCCCCCCCCCCCCC	51.06	29255136
353	Phosphorylation	GEDELCDSGRQRGEK CCHHCCHHHCCCCCC	34.57	25159151
360	Ubiquitination	SGRQRGEKEDEDEDV HHCCCCCCCCCHHHH	73.60	24816145
396	Acetylation	QFACSVCKFRSFDDE HHHHHHCCCCCCCHH	41.47	26051181
399	Phosphorylation	CSVCKFRSFDDEEIQ HHHCCCCCCCHHHHH	35.84	25159151
407	Ubiquitination	FDDEEIQKHLQSKFH CCHHHHHHHHHHHHH	52.52	29967540
423	Phosphorylation	ETLRFISTKLPDKTV HHHHHHHHCCCCHHH	31.61	18551973
424	Ubiquitination	TLRFISTKLPDKTVE HHHHHHHCCCCHHHH	51.75	29967540
428	Acetylation	ISTKLPDKTVEFLQE HHHCCCCHHHHHHHH	53.16	26051181
436	Phosphorylation	TVEFLQEYIVNRNKK HHHHHHHHHHHCHHH	9.37	80839805
465	Ubiquitination	KPKPDPFKGIGQEHF CCCCCCCCCCCHHHH	55.81	29967540
474	2-Hydroxyisobutyrylation	IGQEHFFKKIEAAHC CCHHHHHHHHHHHHH	52.47	-
517	Ubiquitination	LAAEQFKKTSLHVAK HHHHHHHHHHHHHHH	44.63	29967540
524	Ubiquitination	KTSLHVAKSVLNNRH HHHHHHHHHHHCCHH	39.75	29967540
524	Acetylation	KTSLHVAKSVLNNRH HHHHHHHHHHHCCHH	39.75	25953088
534	Acetylation	LNNRHIVKMLEKYLK HCCHHHHHHHHHHHC	36.85	20167786
538	Acetylation	HIVKMLEKYLKGEDP HHHHHHHHHHCCCCC	52.50	19608861
539	Phosphorylation	IVKMLEKYLKGEDPF HHHHHHHHHCCCCCC	12.31	80839799
567	Sumoylation	NLGGEDKKETPEEVA CCCCCCCCCCHHHHH	78.22	28112733
569	Phosphorylation	GGEDKKETPEEVAAD CCCCCCCCHHHHHHH	44.90	27732954
599	Phosphorylation	EGAPAPESSGEPAED CCCCCCCCCCCCCCC	42.45	22210691
600	Phosphorylation	GAPAPESSGEPAEDE CCCCCCCCCCCCCCC	45.58	22210691
610	Phosphorylation	PAEDEGPTDTAEAGS CCCCCCCCCHHHCCC	57.76	30576142
612	Phosphorylation	EDEGPTDTAEAGSDP CCCCCCCHHHCCCCH	28.95	30576142
617	Phosphorylation	TDTAEAGSDPQAEQL CCHHHCCCCHHHHHH	53.84	30576142
637	Acetylation	PCGTAHEKGVPKARS CCCCCCCCCCCHHHH	56.17	26051181
644	Phosphorylation	KGVPKARSEAAEAGN CCCCHHHHHHHHHCC	36.13	28985074
655	Phosphorylation	EAGNGAETMAAEAES HHCCCHHHHHHHHHH	16.15	27251275
656	Sulfoxidation	AGNGAETMAAEAESA HCCCHHHHHHHHHHH	2.21	21406390
662	Phosphorylation	TMAAEAESAQTRVAP HHHHHHHHHCCCCCC	32.50	27251275
665	Phosphorylation	AEAESAQTRVAPAPA HHHHHHCCCCCCCCH	27.16	21406692
681	Phosphorylation	ADAEVEQTDAESKDA HCCHHCCCCHHHCCC	24.54	29255136
685	Phosphorylation	VEQTDAESKDAVPTE HCCCCHHHCCCCCCC	37.24	29255136
686	Acetylation	EQTDAESKDAVPTE- CCCCHHHCCCCCCC-	41.01	26051181

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
51	Y	Phosphorylation	Kinase	LYN	P07948	PSP
51	Y	Phosphorylation	Kinase	SRC	P12931	PSP
53	Y	Phosphorylation	Kinase	LYN	P07948	PSP
53	Y	Phosphorylation	Kinase	SRC	P12931	PSP
80	Y	Phosphorylation	Kinase	SRC	P12931	PSP
80	Y	Phosphorylation	Kinase	LYN	P07948	PSP
146	Y	Phosphorylation	Kinase	LYN	P07948	PSP
146	Y	Phosphorylation	Kinase	SRC	P12931	PSP
150	Y	Phosphorylation	Kinase	SRC	P12931	PSP
150	Y	Phosphorylation	Kinase	LYN	P07948	PSP
152	Y	Phosphorylation	Kinase	LYN	P07948	PSP
152	Y	Phosphorylation	Kinase	SRC	P12931	PSP
154	Y	Phosphorylation	Kinase	LYN	P07948	PSP
154	Y	Phosphorylation	Kinase	SRC	P12931	PSP
170	Y	Phosphorylation	Kinase	SRC	P12931	PSP
170	Y	Phosphorylation	Kinase	LYN	P07948	PSP
311	Y	Phosphorylation	Kinase	LYN	P07948	PSP
311	Y	Phosphorylation	Kinase	SRC	P12931	PSP
436	Y	Phosphorylation	Kinase	LYN	P07948	PSP
436	Y	Phosphorylation	Kinase	SRC	P12931	PSP
539	Y	Phosphorylation	Kinase	SRC	P12931	PSP
539	Y	Phosphorylation	Kinase	LYN	P07948	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AKAP8_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 AKAP8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM2_HUMAN	MCM2	physical	12740381
CCND3_HUMAN	CCND3	physical	14641107
CCND1_HUMAN	CCND1	physical	14641107
CCND2_HUMAN	CCND2	physical	14641107
KAP2_HUMAN	PRKAR2A	physical	9473338
AMY1_HUMAN	AMY1A	physical	12414807
DDX5_HUMAN	DDX5	physical	11279182
EF1B_HUMAN	EEF1B2	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
TBB4B_HUMAN	TUBB4B	physical	26344197

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 AKAP8_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-538, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-323 AND SER-328, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, ANDMASS SPECTROMETRY.	19413330 [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-323; SER-328 ANDSER-339, AND MASS SPECTROMETRY.	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-328, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 ANDSER-339, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASSSPECTROMETRY.	15302935 [Abstract]