CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008438
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase type 7 
Protein Synonyms/Alias
 ATP pyrophosphate-lyase 7; Adenylate cyclase type VII; Adenylyl cyclase 7 
Gene Name
 ADCY7 
Gene Synonyms/Alias
 KIAA0037 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
316GKFDQIAKANECMRIubiquitination[1]
324ANECMRIKILGDCYYubiquitination[1]
349THARNCVKMGLDMCQubiquitination[1]
359LDMCQAIKQVREATGubiquitination[1]
389CGVIGLRKWQYDVWSubiquitination[1]
422HITEATLKHLDKAYEacetylation[2]
422HITEATLKHLDKAYEubiquitination[1]
426ATLKHLDKAYEVEDGacetylation[2]
426ATLKHLDKAYEVEDGubiquitination[1]
443QQRDPYLKEMNIRTYubiquitination[1, 3, 4]
477PKGDAALKMRASVRMubiquitination[1]
832CLWKKKFKKEHEEFEubiquitination[1, 5]
833LWKKKFKKEHEEFETubiquitination[1, 5]
899YTECDVNKEGLECLRubiquitination[5]
929PKFSGVEKIKTIGSTubiquitination[1]
1006AGVIGARKPQYDIWGubiquitination[1, 3]
1057CRGLINVKGKGELRTubiquitination[5]
1073FVCTDTAKFQGLGLNubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 This is a membrane-bound, calcium-inhibitable adenylyl cyclase. 
Sequence Annotation
 DOMAIN 279 406 Guanylate cyclase 1.
 DOMAIN 879 1023 Guanylate cyclase 2.
 METAL 284 284 Magnesium 1 (By similarity).
 METAL 284 284 Magnesium 2 (By similarity).
 METAL 285 285 Magnesium 2; via carbonyl oxygen (By
 METAL 328 328 Magnesium 1 (By similarity).
 METAL 328 328 Magnesium 2 (By similarity).
 CARBOHYD 701 701 N-linked (GlcNAc...) (Potential).
 CARBOHYD 776 776 N-linked (GlcNAc...) (Potential).
 CARBOHYD 781 781 N-linked (GlcNAc...) (Potential).  
Keyword
 ATP-binding; cAMP biosynthesis; Complete proteome; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1080 AA 
Protein Sequence
MPAKGRYFLN EGEEGPDQDA LYEKYQLTSQ HGPLLLTLLL VAATACVALI IIAFSQGDPS 60
RHQAILGMAF LVLAVFAALS VLMYVECLLR RWLRALALLT WACLVALGYV LVFDAWTKAA 120
CAWEQVPFFL FIVFVVYTLL PFSMRGAVAV GAVSTASHLL VLGSLMGGFT TPSVRVGLQL 180
LANAVIFLCG NLTGAFHKHQ MQDASRDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH 240
ISMGMKLAII ERLKEHGDRR CMPDNNFHSL YVKRHQNVSI LYADIVGFTQ LASDCSPKEL 300
VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PTHARNCVKM GLDMCQAIKQ 360
VREATGVDIN MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS LANRMEAAGV PGRVHITEAT 420
LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY LVIDPRSQQP PPPSQHLPRP KGDAALKMRA 480
SVRMTRYLES WGAARPFAHL NHRESVSSGE THVPNGRRPK SVPQRHRRTP DRSMSPKGRS 540
EDDSYDDEML SAIEGLSSTR PCCSKSDDFY TFGSIFLEKG FEREYRLAPI PRARHDFACA 600
SLIFVCILLV HVLLMPRTAA LGVSFGLVAC VLGLVLGLCF ATKFSRCCPA RGTLCTISER 660
VETQPLLRLT LAVLTIGSLL TVAIINLPLM PFQVPELPVG NETGLLAASS KTRALCEPLP 720
YYTCSCVLGF IACSVFLRMS LEPKVVLLTV ALVAYLVLFN LSPCWQWDCC GQGLGNLTKP 780
NGTTSGTPSC SWKDLKTMTN FYLVLFYITL LTLSRQIDYY CRLDCLWKKK FKKEHEEFET 840
MENVNRLLLE NVLPAHVAAH FIGDKLNEDW YHQSYDCVCV MFASVPDFKV FYTECDVNKE 900
GLECLRLLNE IIADFDELLL KPKFSGVEKI KTIGSTYMAA AGLSVASGHE NQELERQHAH 960
IGVMVEFSIA LMSKLDGINR HSFNSFRLRV GINHGPVIAG VIGARKPQYD IWGNTVNVAS 1020
RMESTGELGK IQVTEETCTI LQGLGYSCEC RGLINVKGKG ELRTYFVCTD TAKFQGLGLN 1080 
Gene Ontology
 GO:0016021; C:integral to membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
 GO:0034199; P:activation of protein kinase A activity; TAS:Reactome.
 GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; TAS:Reactome.
 GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
 GO:0071361; P:cellular response to ethanol; IDA:UniProtKB.
 GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:UniProtKB.
 GO:0007268; P:synaptic transmission; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0006833; P:water transport; TAS:Reactome. 
Interpro
 IPR001054; A/G_cyclase.
 IPR018297; A/G_cyclase_CS.
 IPR009398; Adenylate_cyclase-like. 
Pfam
 PF06327; DUF1053
 PF00211; Guanylate_cyc 
SMART
 SM00044; CYCc 
PROSITE
 PS00452; GUANYLATE_CYCLASE_1
 PS50125; GUANYLATE_CYCLASE_2 
PRINTS