dbPTM

AKP8L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AKP8L_HUMAN
UniProt AC	Q9ULX6
Protein Name	A-kinase anchor protein 8-like
Gene Name	AKAP8L
Organism	Homo sapiens (Human).
Sequence Length	646
Subcellular Localization	Nucleus . Nucleus matrix . Nucleus speckle . Nucleus, PML body . Cytoplasm . Colocalizes with PRPF40A in the nuclear matrix (PubMed:16391387). Nuclear at steady state but shuttles between the nucleus and cytoplasm (PubMed:10748171). The shuttling pro
Protein Description	Could play a role in constitutive transport element (CTE)-mediated gene expression by association with DHX9. Increases CTE-dependent nuclear unspliced mRNA export. [PubMed: 10748171]
Protein Sequence	MSYTGFVQGSETTLQSTYSDTSAQPTCDYGYGTWNSGTNRGYEGYGYGYGYGQDNTTNYGYGMATSHSWEMPSSDTNANTSASGSASADSVLSRINQRLDMVPHLETDMMQGGVYGSGGERYDSYESCDSRAVLSERDLYRSGYDYSELDPEMEMAYEGQYDAYRDQFRMRGNDTFGPRAQGWARDARSGRPMASGYGRMWEDPMGARGQCMSGASRLPSLFSQNIIPEYGMFQGMRGGGAFPGGSRFGFGFGNGMKQMRRTWKTWTTADFRTKKKKRKQGGSPDEPDSKATRTDCSDNSDSDNDEGTEGEATEGLEGTEAVEKGSRVDGEDEEGKEDGREEGKEDPEKGALTTQDENGQTKRKLQAGKKSQDKQKKRQRDRMVERIQFVCSLCKYRTFYEDEMASHLDSKFHKEHFKYVGTKLPKQTADFLQEYVTNKTKKTEELRKTVEDLDGLIHQIYRDQDLTQEIAMEHFVKKVEAAHCAACDLFIPMQFGIIQKHLKTMDHNRNRRLMMEQSKKSSLMVARSILNNKLISKKLERYLKGENPFTDSPEEEKEQEEAEGGALDEGAQGEAAGISEGAEGVPAQPPVPPEPAPGAVSPPPPPPPEEEEEGAVPLLGGALQRQIRGIPGLDVEDDEEGGGGAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	SAQPTCDYGYGTWNS CCCCCCCCCCCCCCC	17.88	11569557
31	Phosphorylation	QPTCDYGYGTWNSGT CCCCCCCCCCCCCCC	12.73	46223989
107	Phosphorylation	DMVPHLETDMMQGGV CCCCCCCCHHHCCCC	35.24	27080861
115	Phosphorylation	DMMQGGVYGSGGERY HHHCCCCCCCCCCCC	14.62	27080861
117	Phosphorylation	MQGGVYGSGGERYDS HCCCCCCCCCCCCCC	26.41	29978859
122	Phosphorylation	YGSGGERYDSYESCD CCCCCCCCCCCCCCC	12.63	27642862
124	Phosphorylation	SGGERYDSYESCDSR CCCCCCCCCCCCCCC	23.13	28796482
125	Phosphorylation	GGERYDSYESCDSRA CCCCCCCCCCCCCCH	14.68	28796482
127	Phosphorylation	ERYDSYESCDSRAVL CCCCCCCCCCCCHHH	18.26	25307156
130	Phosphorylation	DSYESCDSRAVLSER CCCCCCCCCHHHCHH	26.85	25849741
131	Methylation	SYESCDSRAVLSERD CCCCCCCCHHHCHHH	18.57	-
135	Phosphorylation	CDSRAVLSERDLYRS CCCCHHHCHHHHHHC	24.80	62169547
142	Phosphorylation	SERDLYRSGYDYSEL CHHHHHHCCCCHHHC	28.31	24043423
144	Phosphorylation	RDLYRSGYDYSELDP HHHHHCCCCHHHCCH	16.98	24043423
146	Phosphorylation	LYRSGYDYSELDPEM HHHCCCCHHHCCHHH	8.79	24043423
147	Phosphorylation	YRSGYDYSELDPEME HHCCCCHHHCCHHHH	28.87	22210691
157	Phosphorylation	DPEMEMAYEGQYDAY CHHHHHHHCCCHHHH	21.20	27642862
161	Phosphorylation	EMAYEGQYDAYRDQF HHHHCCCHHHHHHHH	17.25	22210691
164	Phosphorylation	YEGQYDAYRDQFRMR HCCCHHHHHHHHHHC	16.30	22210691
171	Methylation	YRDQFRMRGNDTFGP HHHHHHHCCCCCCCC	36.18	-
175	Phosphorylation	FRMRGNDTFGPRAQG HHHCCCCCCCCCHHC	34.20	22210691
179	Methylation	GNDTFGPRAQGWARD CCCCCCCCHHCHHCC	39.66	-
185	Methylation	PRAQGWARDARSGRP CCHHCHHCCCCCCCC	31.45	-
188	Methylation	QGWARDARSGRPMAS HCHHCCCCCCCCCCC	43.89	-
191	Methylation	ARDARSGRPMASGYG HCCCCCCCCCCCCCC	21.04	-
196	Acetylation	SGRPMASGYGRMWED CCCCCCCCCCCCCCC	21.26	19608861
196	Ubiquitination	SGRPMASGYGRMWED CCCCCCCCCCCCCCC	21.26	21890473
197	Phosphorylation	GRPMASGYGRMWEDP CCCCCCCCCCCCCCC	10.08	68853877
199	Methylation	PMASGYGRMWEDPMG CCCCCCCCCCCCCCC	20.68	-
203	Ubiquitination	GYGRMWEDPMGARGQ CCCCCCCCCCCCCCC	23.99	21890473
208	Asymmetric dimethylarginine	WEDPMGARGQCMSGA CCCCCCCCCCCCCHH	29.95	-
208	Methylation	WEDPMGARGQCMSGA CCCCCCCCCCCCCHH	29.95	24129315
217	Dimethylation	QCMSGASRLPSLFSQ CCCCHHHHCHHHHHC	50.51	-
217	Methylation	QCMSGASRLPSLFSQ CCCCHHHHCHHHHHC	50.51	24129315
222	Phosphorylation	ASRLPSLFSQNIIPE HHHCHHHHHCCCCCC	9.18	33259812
223	Ubiquitination	SRLPSLFSQNIIPEY HHCHHHHHCCCCCCC	27.84	21890473
229	Ubiquitination	FSQNIIPEYGMFQGM HHCCCCCCCCCCCCC	44.29	24816145
230	Ubiquitination	SQNIIPEYGMFQGMR HCCCCCCCCCCCCCC	14.45	21890473
237	Dimethylation	YGMFQGMRGGGAFPG CCCCCCCCCCCCCCC	47.64	-
237	Methylation	YGMFQGMRGGGAFPG CCCCCCCCCCCCCCC	47.64	24129315
247	Dimethylation	GAFPGGSRFGFGFGN CCCCCCCCCCCCCCC	38.69	-
247	Methylation	GAFPGGSRFGFGFGN CCCCCCCCCCCCCCC	38.69	24129315
256	Ubiquitination	GFGFGNGMKQMRRTW CCCCCCCHHHHHHHH	2.94	24816145
257	Ubiquitination	FGFGNGMKQMRRTWK CCCCCCHHHHHHHHH	42.20	21890473
257	Ubiquitination	FGFGNGMKQMRRTWK CCCCCCHHHHHHHHH	42.20	21890473
257	Acetylation	FGFGNGMKQMRRTWK CCCCCCHHHHHHHHH	42.20	19608861
257	Ubiquitination	FGFGNGMKQMRRTWK CCCCCCHHHHHHHHH	42.20	21890473
264	Ubiquitination	KQMRRTWKTWTTADF HHHHHHHHHCCHHHH	33.31	21890473
264	Ubiquitination	KQMRRTWKTWTTADF HHHHHHHHHCCHHHH	33.31	21890473
264	Acetylation	KQMRRTWKTWTTADF HHHHHHHHHCCHHHH	33.31	25953088
264	Ubiquitination	KQMRRTWKTWTTADF HHHHHHHHHCCHHHH	33.31	21890473
265	Phosphorylation	QMRRTWKTWTTADFR HHHHHHHHCCHHHHH	21.43	28555341
267	Phosphorylation	RRTWKTWTTADFRTK HHHHHHCCHHHHHHH	19.82	23917254
268	Phosphorylation	RTWKTWTTADFRTKK HHHHHCCHHHHHHHH	18.78	30821383
272	Methylation	TWTTADFRTKKKKRK HCCHHHHHHHHHHHH	46.30	-
283	Phosphorylation	KKRKQGGSPDEPDSK HHHHCCCCCCCCCCC	35.68	29255136
288	Ubiquitination	GGSPDEPDSKATRTD CCCCCCCCCCCCCCC	61.80	24816145
289	Phosphorylation	GSPDEPDSKATRTDC CCCCCCCCCCCCCCC	34.60	28985074
290	Ubiquitination	SPDEPDSKATRTDCS CCCCCCCCCCCCCCC	62.24	21906983
292	Phosphorylation	DEPDSKATRTDCSDN CCCCCCCCCCCCCCC	37.53	25137130
294	Phosphorylation	PDSKATRTDCSDNSD CCCCCCCCCCCCCCC	36.68	21712546
297	Phosphorylation	KATRTDCSDNSDSDN CCCCCCCCCCCCCCC	42.51	22617229
300	Phosphorylation	RTDCSDNSDSDNDEG CCCCCCCCCCCCCCC	43.41	22617229
302	Phosphorylation	DCSDNSDSDNDEGTE CCCCCCCCCCCCCCC	37.83	26055452
308	Phosphorylation	DSDNDEGTEGEATEG CCCCCCCCCCCHHCC	38.48	25022875
309	Ubiquitination	SDNDEGTEGEATEGL CCCCCCCCCCHHCCC	66.93	24816145
313	Phosphorylation	EGTEGEATEGLEGTE CCCCCCHHCCCCCCH	26.70	30576142
315	Ubiquitination	TEGEATEGLEGTEAV CCCCHHCCCCCCHHH	25.36	24816145
319	Phosphorylation	ATEGLEGTEAVEKGS HHCCCCCCHHHHCCC	16.05	26552605
326	Phosphorylation	TEAVEKGSRVDGEDE CHHHHCCCCCCCCCC	39.95	25849741
336	Ubiquitination	DGEDEEGKEDGREEG CCCCCCCCCCCCCCC	56.78	24816145
349	Ubiquitination	EGKEDPEKGALTTQD CCCCCCCCCCCCCCC	55.67	24816145
350	Ubiquitination	GKEDPEKGALTTQDE CCCCCCCCCCCCCCC	24.94	29967540
353	Ubiquitination	DPEKGALTTQDENGQ CCCCCCCCCCCCCCH	23.13	29967540
357	Ubiquitination	GALTTQDENGQTKRK CCCCCCCCCCHHHHH	54.14	29967540
362	Ubiquitination	QDENGQTKRKLQAGK CCCCCHHHHHHHHCC	39.38	21906983
365	Ubiquitination	NGQTKRKLQAGKKSQ CCHHHHHHHHCCCCH	4.98	29967540
370	Ubiquitination	RKLQAGKKSQDKQKK HHHHHCCCCHHHHHH	53.05	24816145
378	Ubiquitination	SQDKQKKRQRDRMVE CHHHHHHHHHHHHHH	43.75	29967540
387	Ubiquitination	RDRMVERIQFVCSLC HHHHHHHHHHHHHHH	2.06	21890473
395	Acetylation	QFVCSLCKYRTFYED HHHHHHHCCCHHCHH	42.96	26051181
397	Methylation	VCSLCKYRTFYEDEM HHHHHCCCHHCHHHH	12.12	-
411	Acetylation	MASHLDSKFHKEHFK HHHHHCHHHHHHHHH	51.67	25953088
411	Ubiquitination	MASHLDSKFHKEHFK HHHHHCHHHHHHHHH	51.67	29967540
414	Ubiquitination	HLDSKFHKEHFKYVG HHCHHHHHHHHHHCC	56.89	21890473
416	Ubiquitination	DSKFHKEHFKYVGTK CHHHHHHHHHHCCCC	29.33	32015554
418	Ubiquitination	KFHKEHFKYVGTKLP HHHHHHHHHCCCCCC	40.72	29967540
423	Acetylation	HFKYVGTKLPKQTAD HHHHCCCCCCHHHHH	57.79	26051181
423	Ubiquitination	HFKYVGTKLPKQTAD HHHHCCCCCCHHHHH	57.79	29967540
426	Ubiquitination	YVGTKLPKQTADFLQ HCCCCCCHHHHHHHH	71.38	29967540
435	Phosphorylation	TADFLQEYVTNKTKK HHHHHHHHHHCCCCC	10.30	80495613
439	Acetylation	LQEYVTNKTKKTEEL HHHHHHCCCCCHHHH	52.97	25953088
439	Ubiquitination	LQEYVTNKTKKTEEL HHHHHHCCCCCHHHH	52.97	29967540
442	Ubiquitination	YVTNKTKKTEELRKT HHHCCCCCHHHHHHH	67.41	29967540
448	Ubiquitination	KKTEELRKTVEDLDG CCHHHHHHHHHHHHH	70.33	21890473
448	Ubiquitination	KKTEELRKTVEDLDG CCHHHHHHHHHHHHH	70.33	21890473
458	Ubiquitination	EDLDGLIHQIYRDQD HHHHHHHHHHHCCCC	17.02	24816145
472	Ubiquitination	DLTQEIAMEHFVKKV CHHHHHHHHHHHHHH	5.16	32015554
477	2-Hydroxyisobutyrylation	IAMEHFVKKVEAAHC HHHHHHHHHHHHHHH	50.59	-
477	Ubiquitination	IAMEHFVKKVEAAHC HHHHHHHHHHHHHHH	50.59	32015554
483	Ubiquitination	VKKVEAAHCAACDLF HHHHHHHHHHHCCHH	14.59	29967540
485	Ubiquitination	KVEAAHCAACDLFIP HHHHHHHHHCCHHHH	10.97	24816145
500	Acetylation	MQFGIIQKHLKTMDH HHHHHHHHHHHHCCC	40.26	26051181
503	2-Hydroxyisobutyrylation	GIIQKHLKTMDHNRN HHHHHHHHHCCCHHH	41.33	-
503	Ubiquitination	GIIQKHLKTMDHNRN HHHHHHHHHCCCHHH	41.33	29967540
504	Phosphorylation	IIQKHLKTMDHNRNR HHHHHHHHCCCHHHH	33.90	50588765
519	Ubiquitination	RLMMEQSKKSSLMVA HHHHHHHHHHHHHHH	57.26	24816145
520	Acetylation	LMMEQSKKSSLMVAR HHHHHHHHHHHHHHH	50.99	6570347
533	Acetylation	ARSILNNKLISKKLE HHHHHCCHHHHHHHH	46.23	23236377
533	Ubiquitination	ARSILNNKLISKKLE HHHHHCCHHHHHHHH	46.23	32015554
537	Acetylation	LNNKLISKKLERYLK HCCHHHHHHHHHHHC	55.15	26051181
538	Acetylation	NNKLISKKLERYLKG CCHHHHHHHHHHHCC	49.11	26051181
544	Sumoylation	KKLERYLKGENPFTD HHHHHHHCCCCCCCC	56.07	-
544	Sumoylation	KKLERYLKGENPFTD HHHHHHHCCCCCCCC	56.07	-
544	Ubiquitination	KKLERYLKGENPFTD HHHHHHHCCCCCCCC	56.07	21906983
550	Phosphorylation	LKGENPFTDSPEEEK HCCCCCCCCCHHHHH	36.50	29255136
552	Phosphorylation	GENPFTDSPEEEKEQ CCCCCCCCHHHHHHH	31.02	29255136
601	Phosphorylation	EPAPGAVSPPPPPPP CCCCCCCCCCCCCCC	31.02	26074081

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF43	Q68DV7	PMID:18313049

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AKP8L_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 AKP8L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LBR_HUMAN	LBR	physical	11034899
EMD_HUMAN	EMD	physical	11034899
LAP2A_HUMAN	TMPO	physical	11034899
LAP2B_HUMAN	TMPO	physical	11034899
LAP2A_HUMAN	TMPO	physical	12538639
LAP2B_HUMAN	TMPO	physical	12538639
CDC6_HUMAN	CDC6	physical	12538639
RNF43_HUMAN	RNF43	physical	18313049

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 AKP8L_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-257, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 THR-292; SER-297; SER-300AND THR-308, AND MASS SPECTROMETRY.	19369195 [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-552, AND MASSSPECTROMETRY.	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 THR-292; THR-294; SER-297;SER-300; SER-302 AND THR-308, 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-283, AND MASSSPECTROMETRY.	18691976 [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-283, AND MASSSPECTROMETRY.	15302935 [Abstract]