ADCY6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ADCY6_HUMAN
• UniProt AC: O43306
• Protein Name: Adenylate cyclase type 6
• Gene Name: ADCY6
• Organism: Homo sapiens (Human).
• Sequence Length: 1168
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Cell projection, cilium .
• Protein Description: Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors. [PubMed: 17916776]
• Protein Sequence: MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGPPRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWRRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLWCPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTNVIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSCGSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLTPADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLAMIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS

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
2	Phosphorylation	------MSWFSGLLV ------CCCCCCCCC	48.40	27470641
5	Phosphorylation	---MSWFSGLLVPKV ---CCCCCCCCCCCC	23.44	27251275
16	Ubiquitination	VPKVDERKTAWGERN CCCCCCCCCHHCCCC	40.31	29967540
40	Phosphorylation	TRAGGFCTPRYMSCL CCCCCCCCHHHHHHC	14.45	22817900
45	Phosphorylation	FCTPRYMSCLRDAEP CCCHHHHHHCCCCCC	10.89	28270605
54	Phosphorylation	LRDAEPPSPTPAGPP CCCCCCCCCCCCCCC	52.71	29255136
56	Phosphorylation	DAEPPSPTPAGPPRC CCCCCCCCCCCCCCC	30.06	30266825
80	Ubiquitination	RGGPGKGKELGLRAV CCCCCCCHHHHCCEE	53.93	-
129	Ubiquitination	LVQVFQSKQFRSAKL HHHHHHHHHHHHHHH	42.55	22817900
129 (in isoform 2)	Ubiquitination	-	42.55	21890473
129 (in isoform 1)	Ubiquitination	-	42.55	21890473
207	Phosphorylation	RHSFRQDSMWVVSYV CCCCCCCCHHHHHHH	13.25	68730037
212	Phosphorylation	QDSMWVVSYVVLGIL CCCHHHHHHHHHHHH	11.55	68730043
477	Phosphorylation	NMRVGIHSGRVHCGV CEEEEECCCCEEEEE	26.78	-
556	Phosphorylation	TFLILGASQKRKEEK HHHHHCCCHHHHHHH	34.14	-
568	Ubiquitination	EEKAMLAKLQRTRAN HHHHHHHHHHHHHHH	40.99	29967540
572	Phosphorylation	MLAKLQRTRANSMEG HHHHHHHHHHHHCCC	22.60	22617229
576	Phosphorylation	LQRTRANSMEGLMPR HHHHHHHHCCCCCCC	19.75	29255136
607	Phosphorylation	RQMGIDDSSKDNRGT HHCCCCCCCCCCCCC	35.22	46159647
608	Phosphorylation	QMGIDDSSKDNRGTQ HCCCCCCCCCCCCCC	51.53	46159653
614	Phosphorylation	SSKDNRGTQDALNPE CCCCCCCCCCCCCCH	21.75	28270605
636	Phosphorylation	SRAIDARSIDQLRKD HHHHCCCCHHHHHHH	32.03	24825855
662	Phosphorylation	EDLEKKYSRKVDPRF HHHHHHHHCCCCHHH	34.21	-
732	Phosphorylation	PKALQRLSRSIVRSR HHHHHHHHHHHHHHC	26.60	28985074
734	Phosphorylation	ALQRLSRSIVRSRAH HHHHHHHHHHHHCHH	23.27	28985074
793	N-linked_Glycosylation	ACHLQQLNYSLGLDA HHHHHHHCCCCCCCC	21.73	UniProtKB CARBOHYD
833	Ubiquitination	ASSVFLHISSIGKLA HHHHHHHHHHHHHHH	3.62	23503661
881 (in isoform 2)	Ubiquitination	-	5.98	-
919	Phosphorylation	HAQQVESTARLDFLW HHHHHHHHHHHHHHH	11.42	-
934	Ubiquitination	KLQATGEKEEMEELQ HHHCCCCHHHHHHHH	61.39	29901268
1000	Ubiquitination	VELEANNEGVECLRL EEHHHCCCHHHHHHH	65.51	22817900
1049	Ubiquitination	GLNASTYDQVGRSHI CCCCCCCCCCCHHHH	36.46	23503661
1051	Ubiquitination	NASTYDQVGRSHITA CCCCCCCCCHHHHHH	6.68	23503661
1053	Ubiquitination	STYDQVGRSHITALA CCCCCCCHHHHHHHH	26.63	23503661
1077	Phosphorylation	MKHINEHSFNNFQMK HHHHCCCCCCCHHHC	24.40	28270605
1101	Ubiquitination	AGVIGARKPQYDIWG HHHHCCCCCCCCCCC	35.62	22817900
1101 (in isoform 2)	Ubiquitination	-	35.62	-
1104	Phosphorylation	IGARKPQYDIWGNTV HCCCCCCCCCCCCEE	20.23	25954137
1110	Phosphorylation	QYDIWGNTVNVSSRM CCCCCCCEEECHHHC	14.98	25954137
1115	Phosphorylation	GNTVNVSSRMDSTGV CCEEECHHHCCCCCC	27.60	25954137
1150	Ubiquitination	LECRGVVKVKGKGEM EEEEEEEEEECCCEE	35.50	23503661
1152	Ubiquitination	CRGVVKVKGKGEMTT EEEEEEEECCCEEEE	49.54	23503661
1154	Ubiquitination	GVVKVKGKGEMTTYF EEEEEECCCEEEEEE	46.08	23503661

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ADCY6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
556	S	Phosphorylation	Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity.	-
662	S	Phosphorylation	Phosphorylation by PKA at Ser-662 inhibits the GNAS-mediated increase in catalytic activity.	-
662	S	Phosphorylation	Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity.	-
919	T	Phosphorylation	Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ADCY6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACHA7_HUMAN	CHRNA7	physical	12748066
GBB1_MOUSE	Gnb1	physical	17110384

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616287: Lethal congenital contracture syndrome 8 (LCCS8)
• Kegg Drug
• D01697: Colforsin daropate hydrochloride (JAN); Nkh 477; Adehl (TN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-576, AND MASSSPECTROMETRY.
PubMed: 18669648

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-576, AND MASSSPECTROMETRY.
PubMed: 18088087

"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-54, AND MASSSPECTROMETRY.
PubMed: 15302935