dbPTM

ADCY9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADCY9_HUMAN
UniProt AC	O60503
Protein Name	Adenylate cyclase type 9 {ECO:0000303\|PubMed:9628827}
Gene Name	ADCY9
Organism	Homo sapiens (Human).
Sequence Length	1353
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. [PubMed: 9628827]
Protein Sequence	MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDSGGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYALFYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVSSGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKNSTKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIRMVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGSAALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSERNPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEERGRFGKAIEKDDCDETGIEEANELTKLNVSKSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASPPHQQLL -----CCCCHHHHHC	51.31	27251275
14	Phosphorylation	QQLLHHHSTEVSCDS HHHCCCCCCEEEECC	23.16	28450419
15	Phosphorylation	QLLHHHSTEVSCDSS HHCCCCCCEEEECCC	35.73	28450419
18	Phosphorylation	HHHSTEVSCDSSGDS CCCCCEEEECCCCCC	13.13	28450419
25	Phosphorylation	SCDSSGDSNSVRVKI EECCCCCCCCEEEEE	34.23	27251275
27	Phosphorylation	DSSGDSNSVRVKINP CCCCCCCCEEEEECH	18.43	28348404
35	Ubiquitination	VRVKINPKQLSSNSH EEEEECHHHHCCCCC	60.42	29967540
38	Phosphorylation	KINPKQLSSNSHPKH EECHHHHCCCCCCCC	25.61	46159713
39	Phosphorylation	INPKQLSSNSHPKHC ECHHHHCCCCCCCCC	51.44	46159719
48	Phosphorylation	SHPKHCKYSISSSCS CCCCCCCEEECCCCC	19.34	27732954
49	Phosphorylation	HPKHCKYSISSSCSS CCCCCCEEECCCCCC	11.07	23663014
51	Phosphorylation	KHCKYSISSSCSSSG CCCCEEECCCCCCCC	15.40	23663014
52	Phosphorylation	HCKYSISSSCSSSGD CCCEEECCCCCCCCC	33.42	23663014
53	Phosphorylation	CKYSISSSCSSSGDS CCEEECCCCCCCCCC	15.95	23663014
55	Phosphorylation	YSISSSCSSSGDSGG EEECCCCCCCCCCCC	29.50	23663014
56	Phosphorylation	SISSSCSSSGDSGGV EECCCCCCCCCCCCC	42.54	23663014
57	Phosphorylation	ISSSCSSSGDSGGVP ECCCCCCCCCCCCCC	30.26	23663014
60	Phosphorylation	SCSSSGDSGGVPRRV CCCCCCCCCCCCCCC	40.76	23663014
122	Phosphorylation	RFRYALFYIGFACLL HHHHHHHHHHHHHHH	10.86	141443
131	Phosphorylation	GFACLLWSIYFAVHM HHHHHHHHHHHHHHH	13.84	22210691
133	Phosphorylation	ACLLWSIYFAVHMRS HHHHHHHHHHHHHHH	4.67	141439
172	Phosphorylation	TKLYARHYAWTSLAL HHHHHHHHHHHHHHH	9.78	119501
206	N-linked_Glycosylation	SGRGDSSNLTATARP CCCCCCCCCCEECCC	45.42	UniProtKB CARBOHYD
283	Phosphorylation	ALHWELLSRGLLHGC HHHHHHHHHHHHHHH	36.61	24719451
321	Ubiquitination	GQSIMHGKDLEVEKA HHHHHCCCCHHHHHH	44.45	32015554
327	Ubiquitination	GKDLEVEKALKERMI CCCHHHHHHHHHHHH	65.28	32015554
330	Acetylation	LEVEKALKERMIHSV HHHHHHHHHHHHHHH	48.40	11789751
348	Acetylation	IIADDLMKQGDEESE HHHHHHHHCCCHHHH	59.43	11789761
348	Ubiquitination	IIADDLMKQGDEESE HHHHHHHHCCCHHHH	59.43	29967540
354	Phosphorylation	MKQGDEESENSVKRH HHCCCHHHHHHHHHH	39.78	27422710
357	Phosphorylation	GDEESENSVKRHATS CCHHHHHHHHHHCCC	25.60	23927012
359	Ubiquitination	EESENSVKRHATSSP HHHHHHHHHHCCCCC	37.98	32142685
363	Phosphorylation	NSVKRHATSSPKNRK HHHHHHCCCCCCCCC	24.50	29514088
364	Phosphorylation	SVKRHATSSPKNRKK HHHHHCCCCCCCCCC	45.48	29514088
365	Phosphorylation	VKRHATSSPKNRKKK HHHHCCCCCCCCCCC	35.22	29514088
373	Phosphorylation	PKNRKKKSSIQKAPI CCCCCCCCCCCCCCC	41.37	26699800
374	Phosphorylation	KNRKKKSSIQKAPIA CCCCCCCCCCCCCCC	37.61	24719451
377	Ubiquitination	KKKSSIQKAPIAFRP CCCCCCCCCCCCCCC	55.23	29967540
480	Ubiquitination	IEQFCQEKKEMVNMR HHHHHHHHHHHHHCC	28.31	29967540
494	Phosphorylation	RVGVHTGTVLCGILG CCCCCHHHHHHHHHC	16.09	46159731
537	Ubiquitination	HISEATAKYLDDRYE EHHHHHHHHCCCCCC	41.83	29967540
564	Ubiquitination	SVVADQLKGLKTYLI HHHHHHHCCCCHHHH	57.47	32015554
567	Ubiquitination	ADQLKGLKTYLISGQ HHHHCCCCHHHHCCC	43.74	23503661
608	Phosphorylation	SGPRGQGTASSGNVS CCCCCCCCCCCCCHH	18.58	29255136
610	Phosphorylation	PRGQGTASSGNVSDL CCCCCCCCCCCHHHH	38.32	29255136
611	Phosphorylation	RGQGTASSGNVSDLA CCCCCCCCCCHHHHH	31.74	29255136
615	Phosphorylation	TASSGNVSDLAQTVK CCCCCCHHHHHHHHH	30.79	28450419
620	Phosphorylation	NVSDLAQTVKTFDNL CHHHHHHHHHHHCCC	20.54	26852163
622	Ubiquitination	SDLAQTVKTFDNLKT HHHHHHHHHHCCCCC	47.03	21890473
622	Ubiquitination	SDLAQTVKTFDNLKT HHHHHHHHHHCCCCC	47.03	22817900
622	Ubiquitination	SDLAQTVKTFDNLKT HHHHHHHHHHCCCCC	47.03	21890473
628	Ubiquitination	VKTFDNLKTCPSCGI HHHHCCCCCCCCCCC	55.10	23503661
632	Phosphorylation	DNLKTCPSCGITFAP CCCCCCCCCCCEEEC	27.41	59152019
661	Phosphorylation	CQDEHKNSTKASGGP CCCCCCCCCCCCCCC	35.77	28450419
662	Phosphorylation	QDEHKNSTKASGGPN CCCCCCCCCCCCCCC	39.77	28450419
671	Ubiquitination	ASGGPNPKTQNGLLS CCCCCCCCCCCCCCC	70.18	29967540
678	Phosphorylation	KTQNGLLSPPQEEKL CCCCCCCCCCHHHHC	39.31	21815630
684	Ubiquitination	LSPPQEEKLTNSQTS CCCCHHHHCCCCCHH	60.91	29967540
686	Phosphorylation	PPQEEKLTNSQTSLC CCHHHHCCCCCHHHH	43.84	25850435
688	Phosphorylation	QEEKLTNSQTSLCEI HHHHCCCCCHHHHHH	29.60	29255136
690	Phosphorylation	EKLTNSQTSLCEILQ HHCCCCCHHHHHHHH	24.40	26657352
691	Phosphorylation	KLTNSQTSLCEILQE HCCCCCHHHHHHHHH	24.32	29255136
699	Ubiquitination	LCEILQEKGRWAGVS HHHHHHHCCCCCCCC	40.59	21963094
706	Phosphorylation	KGRWAGVSLDQSALL CCCCCCCCCCHHHHH	25.88	29507054
718	Ubiquitination	ALLPLRFKNIREKTD HHHCCCCCCHHHHCC	45.06	21963094
723	Ubiquitination	RFKNIREKTDAHFVD CCCCHHHHCCCCCCH	41.68	33845483
773	Ubiquitination	SYQEEVIKNSPVKTF HCHHHHHHCCCCCCC	57.45	32142685
925	Phosphorylation	WMRSSLATVVGAGPL HHHHHHHHHHCCHHH	22.48	22210691
948	Phosphorylation	PDSSVLTSPLDAVQN CCCHHCCCHHHHHHC	21.21	22210691
955	N-linked_Glycosylation	SPLDAVQNFSSERNP CHHHHHHCCCCCCCC	31.97	UniProtKB CARBOHYD
964	N-linked_Glycosylation	SSERNPCNSSVPRDL CCCCCCCCCCCCCHH	38.28	UniProtKB CARBOHYD
1098	Ubiquitination	DFDELLSKPDYSSIE CHHHHHCCCCHHHHH	41.71	29967540
1109	Phosphorylation	SSIEKIKTIGATYMA HHHHHHHHHCHHHHH	28.28	46159725
1212	Phosphorylation	RIQVSEESYRVLSKM EEEECHHHHHHHHHC	17.75	21214269
1217	Phosphorylation	EESYRVLSKMGYDFD HHHHHHHHHCCCCCC	20.10	21214269
1218	Ubiquitination	ESYRVLSKMGYDFDY HHHHHHHHCCCCCCC	31.98	21906983
1218	Ubiquitination	ESYRVLSKMGYDFDY HHHHHHHHCCCCCCC	31.98	21890473
1218	Ubiquitination	ESYRVLSKMGYDFDY HHHHHHHHCCCCCCC	31.98	21890473
1221	Phosphorylation	RVLSKMGYDFDYRGT HHHHHCCCCCCCCCE	15.22	7362357
1225	Phosphorylation	KMGYDFDYRGTVNVK HCCCCCCCCCEEEEC	15.78	7362367
1237	Ubiquitination	NVKGKGQMKTYLYPK EECCCCEEEEEECCC	4.83	21890473
1257	Phosphorylation	VIPQHQLSISPDIRV ECCHHHCCCCCCEEE	17.91	30266825
1259	Phosphorylation	PQHQLSISPDIRVQV CHHHCCCCCCEEEEE	17.10	30266825
1269	Phosphorylation	IRVQVDGSIGRSPTD EEEEECCCCCCCCHH	19.87	26657352
1273	Phosphorylation	VDGSIGRSPTDEIAN ECCCCCCCCHHHHHH	27.26	27732954
1275	Phosphorylation	GSIGRSPTDEIANLV CCCCCCCHHHHHHHC	47.73	27251275
1295	Phosphorylation	VDKTSLGSDSSTQAK ECCCCCCCCCCHHHH	39.34	25627689
1302	Ubiquitination	SDSSTQAKDAHLSPK CCCCHHHHHCCCCCC	45.70	29967540
1307	Phosphorylation	QAKDAHLSPKRPWKE HHHHCCCCCCCCCCC	20.64	30266825
1330	Ubiquitination	RFGKAIEKDDCDETG CCCCCCCCCCCCCCC	53.40	29967540
1346	Ubiquitination	EEANELTKLNVSKSV HHHHHHHHCCCCCCC	51.17	29967540
1350	Phosphorylation	ELTKLNVSKSV---- HHHHCCCCCCC----	20.38	21712546
1352	Phosphorylation	TKLNVSKSV------ HHCCCCCCC------	26.08	23911959

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 ADCY9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ADCY9_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 ADCY9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ADCY9_HUMAN !!

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
D01697	Colforsin daropate hydrochloride (JAN); Nkh 477; Adehl (TN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ADCY9_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-354; SER-357 ANDSER-1259, AND MASS SPECTROMETRY.	18669648 [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-365, AND MASSSPECTROMETRY.	17081983 [Abstract]