dbPTM

AK17A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AK17A_HUMAN
UniProt AC	Q02040
Protein Name	A-kinase anchor protein 17A
Gene Name	AKAP17A
Organism	Homo sapiens (Human).
Sequence Length	695
Subcellular Localization	Nucleus speckle .
Protein Description	Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner..
Protein Sequence	MAAATIVHDTSEAVELCPAYGLYLKPITKMTISVALPQLKQPGKSISNWEVMERLKGMVQNHQFSTLRISKSTMDFIRFEGEVENKSLVKSFLACLDGKTIKLSGFSDILKVRAAEFKIDFPTRHDWDSFFRDAKDMNETLPGERPDTIHLEGLPCKWFALKESGSEKPSEDVLVKVFEKFGEIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYREYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRERLLSILLSKKPDDSHTHDELGVAHADLLQPVLDILQTVSSGCVSATTLHPLGGQPPAGAPKESPAHPEADGAPKSVNGSVAEEAPCKEVQSSCRVVPEDGSPEKRCPGGVLSCIPDNNQQPKGIPACEQNVSRKDTRSEQDKCNREPSKGRGRATGDGLADRHKRERSRARRASSREDGRPRKERRPHKKHAYKDDSPRRRSTSPDHTRSRRSHSKDRHRRERSRERRGSASRKHSRHRRRSERSRSRSPSRHRSTWNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAAATIVHDTSE ---CCCCEEEECHHH	20.85	23401153
10	Phosphorylation	AATIVHDTSEAVELC CCEEEECHHHHHHHC	17.37	23401153
11	Phosphorylation	ATIVHDTSEAVELCP CEEEECHHHHHHHCH	29.61	23401153
20	Phosphorylation	AVELCPAYGLYLKPI HHHHCHHHCEECCCC	7.88	23401153
23	Phosphorylation	LCPAYGLYLKPITKM HCHHHCEECCCCCEE	14.33	23401153
44	Acetylation	PQLKQPGKSISNWEV HHCCCCCCCCCHHHH	51.83	25953088
44	Ubiquitination	PQLKQPGKSISNWEV HHCCCCCCCCCHHHH	51.83	-
86	Ubiquitination	FEGEVENKSLVKSFL EEEEECCHHHHHHHH	31.49	-
87	Phosphorylation	EGEVENKSLVKSFLA EEEECCHHHHHHHHH	50.40	-
90	Acetylation	VENKSLVKSFLACLD ECCHHHHHHHHHHHC	40.56	26051181
91	Phosphorylation	ENKSLVKSFLACLDG CCHHHHHHHHHHHCC	20.29	-
99	Acetylation	FLACLDGKTIKLSGF HHHHHCCCEEEECCC	46.90	26051181
99	2-Hydroxyisobutyrylation	FLACLDGKTIKLSGF HHHHHCCCEEEECCC	46.90	-
99	Ubiquitination	FLACLDGKTIKLSGF HHHHHCCCEEEECCC	46.90	-
104	Phosphorylation	DGKTIKLSGFSDILK CCCEEEECCCHHHHH	32.56	23403867
107	Phosphorylation	TIKLSGFSDILKVRA EEEECCCHHHHHHEE	27.54	23403867
118	Sumoylation	KVRAAEFKIDFPTRH HHEEEEEECCCCCCC	32.63	25114211
123	Phosphorylation	EFKIDFPTRHDWDSF EEECCCCCCCCHHHH	40.40	22210691
129	Phosphorylation	PTRHDWDSFFRDAKD CCCCCHHHHHHCCHH	23.25	24719451
157	Acetylation	HLEGLPCKWFALKES EECCCCCEEEEEECC	43.33	26051181
162	Ubiquitination	PCKWFALKESGSEKP CCEEEEEECCCCCCC	46.54	-
162	Acetylation	PCKWFALKESGSEKP CCEEEEEECCCCCCC	46.54	26051181
168	Acetylation	LKESGSEKPSEDVLV EECCCCCCCCHHHHH	56.38	26051181
176	Acetylation	PSEDVLVKVFEKFGE CCHHHHHHHHHHHCC	36.73	26051181
180	Acetylation	VLVKVFEKFGEIRNV HHHHHHHHHCCCCCC	47.40	25953088
180	Ubiquitination	VLVKVFEKFGEIRNV HHHHHHHHHCCCCCC	47.40	-
218	Phosphorylation	GHLNFEAYVQYREYM CEECEEHHHHHHHHH	4.85	19053533
221	Phosphorylation	NFEAYVQYREYMGFI CEEHHHHHHHHHHHH	8.72	19053533
242	Acetylation	RGMKLMYKGEDGKAV CCCEEEEECCCCCEE	41.69	26051181
317	Acetylation	EELERERKREEKLRK HHHHHHHHHHHHHHH	60.45	19816843
324	Acetylation	KREEKLRKREQKQRD HHHHHHHHHHHHHHH	71.38	19816849
339	Acetylation	RELRRNQKKLEKLQA HHHHHHHHHHHHHHH	63.98	7975553
350	Ubiquitination	KLQAEEQKQLQEKIK HHHHHHHHHHHHHHH	57.14	-
381	Phosphorylation	RLIAELLSRAKAVKL HHHHHHHHHHHHHHH	42.70	24719451
440	Phosphorylation	ELRERLLSILLSKKP HHHHHHHHHHHCCCC	18.78	20068231
444	Phosphorylation	RLLSILLSKKPDDSH HHHHHHHCCCCCCCC	34.88	22496350
473	Phosphorylation	PVLDILQTVSSGCVS HHHHHHHHHHCCCCE	20.93	26074081
475	Phosphorylation	LDILQTVSSGCVSAT HHHHHHHHCCCCEEE	25.13	26074081
476	Phosphorylation	DILQTVSSGCVSATT HHHHHHHCCCCEEEE	31.69	26074081
480	Phosphorylation	TVSSGCVSATTLHPL HHHCCCCEEEEEECC	24.79	26074081
482	Phosphorylation	SSGCVSATTLHPLGG HCCCCEEEEEECCCC	23.53	26074081
483	Phosphorylation	SGCVSATTLHPLGGQ CCCCEEEEEECCCCC	23.84	26074081
499	Phosphorylation	PAGAPKESPAHPEAD CCCCCCCCCCCCCCC	33.25	25849741
510	Acetylation	PEADGAPKSVNGSVA CCCCCCCCCCCCCHH	67.51	26051181
511	Phosphorylation	EADGAPKSVNGSVAE CCCCCCCCCCCCHHC	21.54	23403867
515	Phosphorylation	APKSVNGSVAEEAPC CCCCCCCCHHCCCCC	16.98	23403867
523	Acetylation	VAEEAPCKEVQSSCR HHCCCCCCCCHHHCE	60.92	26051181
537	Phosphorylation	RVVPEDGSPEKRCPG EECCCCCCCCCCCCC	42.05	29255136
548	Phosphorylation	RCPGGVLSCIPDNNQ CCCCCCEECCCCCCC	13.95	18452278
572	Phosphorylation	QNVSRKDTRSEQDKC CCCCCCCCCCHHHHH	38.85	20068231
574	O-linked_Glycosylation	VSRKDTRSEQDKCNR CCCCCCCCHHHHHCC	41.52	30379171
574	Phosphorylation	VSRKDTRSEQDKCNR CCCCCCCCHHHHHCC	41.52	20068231
584	Phosphorylation	DKCNREPSKGRGRAT HHHCCCCCCCCCCCC	42.88	28985074
591	Phosphorylation	SKGRGRATGDGLADR CCCCCCCCCCCHHHH	34.15	21815630
598	Methylation	TGDGLADRHKRERSR CCCCHHHHHHHHHHH	31.45	115916701
610	Phosphorylation	RSRARRASSREDGRP HHHHHHHHHCCCCCC	28.28	30576142
611	Phosphorylation	SRARRASSREDGRPR HHHHHHHHCCCCCCC	38.41	30576142
629	Phosphorylation	RPHKKHAYKDDSPRR CCCCCCCCCCCCCCC	18.05	27174698
633	Phosphorylation	KHAYKDDSPRRRSTS CCCCCCCCCCCCCCC	30.36	19840947
638	Phosphorylation	DDSPRRRSTSPDHTR CCCCCCCCCCCCCCH	31.27	20164059
639	Phosphorylation	DSPRRRSTSPDHTRS CCCCCCCCCCCCCHH	42.33	20363803
640	Phosphorylation	SPRRRSTSPDHTRSR CCCCCCCCCCCCHHH	29.58	20164059
644	Phosphorylation	RSTSPDHTRSRRSHS CCCCCCCCHHHCHHC	37.41	30242111
649	Phosphorylation	DHTRSRRSHSKDRHR CCCHHHCHHCHHHHH	30.88	20068231
651	Phosphorylation	TRSRRSHSKDRHRRE CHHHCHHCHHHHHHH	37.18	20068231
660	Phosphorylation	DRHRRERSRERRGSA HHHHHHHHHHHHHHH	33.47	17081983
685	Phosphorylation	SERSRSRSPSRHRST HHHHHCCCCCCCCCC	28.59	20068231
687	Phosphorylation	RSRSRSPSRHRSTWN HHHCCCCCCCCCCCC	41.80	20068231

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 AK17A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AK17A_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 AK17A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC85B_HUMAN	CCDC85B	physical	16189514
NINL_HUMAN	NINL	physical	16189514
CACO2_HUMAN	CALCOCO2	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
JMJD6_HUMAN	JMJD6	physical	28514442
ACTN3_HUMAN	ACTN3	physical	28514442
KCRM_HUMAN	CKM	physical	28514442
PININ_HUMAN	PNN	physical	28514442
MYH7_HUMAN	MYH7	physical	28514442
MYH4_HUMAN	MYH4	physical	28514442
ANR17_HUMAN	ANKRD17	physical	28514442
UBE2O_HUMAN	UBE2O	physical	28514442
ANKH1_HUMAN	ANKHD1	physical	28514442
CAAP1_HUMAN	CAAP1	physical	28514442
HAUS4_HUMAN	HAUS4	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
NKAP_HUMAN	NKAP	physical	28514442
TRPM3_HUMAN	TRPM3	physical	28514442

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 AK17A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-537, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND MASSSPECTROMETRY.	19007248 [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-537 AND SER-633, ANDMASS SPECTROMETRY.	17081983 [Abstract]