CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000952
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase type 9 
Protein Synonyms/Alias
 ATP pyrophosphate-lyase 9; Adenylate cyclase type IX; Adenylyl cyclase 9 
Gene Name
 ADCY9 
Gene Synonyms/Alias
 KIAA0520 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
564SVVADQLKGLKTYLIubiquitination[1]
622SDLAQTVKTFDNLKTubiquitination[1, 2, 3]
699LCEILQEKGRWAGVSubiquitination[1, 4]
1218ESYRVLSKMGYDFDYubiquitination[1, 2, 3, 4, 5]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin (By similarity). 
Sequence Annotation
 DOMAIN 394 521 Guanylate cyclase 1.
 DOMAIN 1058 1198 Guanylate cyclase 2.
 METAL 399 399 Magnesium 1 (By similarity).
 METAL 399 399 Magnesium 2 (By similarity).
 METAL 400 400 Magnesium 2; via carbonyl oxygen (By
 METAL 443 443 Magnesium 1 (By similarity).
 METAL 443 443 Magnesium 2 (By similarity).
 MOD_RES 608 608 Phosphothreonine (By similarity).
 MOD_RES 610 610 Phosphoserine (By similarity).
 MOD_RES 1259 1259 Phosphoserine.
 MOD_RES 1307 1307 Phosphoserine.
 CARBOHYD 206 206 N-linked (GlcNAc...) (Potential).
 CARBOHYD 955 955 N-linked (GlcNAc...) (Potential).
 CARBOHYD 964 964 N-linked (GlcNAc...) (Potential).  
Keyword
 ATP-binding; cAMP biosynthesis; Complete proteome; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1353 AA 
Protein Sequence
MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS 60
GGVPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSVNL EEACLERCFP QTQRRFRYAL 120
FYIGFACLLW SIYFAVHMRS RLIVMVAPAL CFLLVCVGFF LFTFTKLYAR HYAWTSLALT 180
LLVFALTLAA QFQVLTPVSG RGDSSNLTAT ARPTDTCLSQ VGSFSMCIEV LFLLYTVMHL 240
PLYLSLCLGV AYSVLFETFG YHFRDEACFP SPGAGALHWE LLSRGLLHGC IHAIGVHLFV 300
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR 360
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN 420
DLFGRFDRLC EETKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK 480
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD 540
DRYEMEDGKV IERLGQSVVA DQLKGLKTYL ISGQRAKESR CSCAEALLSG FEVIDGSQVS 600
SGPRGQGTAS SGNVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGAP QNGCQDEHKN 660
STKASGGPNP KTQNGLLSPP QEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI 720
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF 780
ASPTFSSLLD VFLSTTVFLT LSTTCFLKYE AATVPPPPAA LAVFSAALLL EVLSLAVSIR 840
MVFFLEDVMA CTKRLLEWIA GWLPRHCIGA ILVSLPALAV YSHVTSEYET NIHFPVFTGS 900
AALIAVVHYC NFCQLSSWMR SSLATVVGAG PLLLLYVSLC PDSSVLTSPL DAVQNFSSER 960
NPCNSSVPRD LRRPASLIGQ EVVLVFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK 1020
IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE 1080
CYRVLNELIG DFDELLSKPD YSSIEKIKTI GATYMAASGL NTAQAQDGSH PQEHLQILFE 1140
FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT 1200
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDHRV IPQHQLSISP 1260
DIRVQVDGSI GRSPTDEIAN LVPSVQYVDK TSLGSDSSTQ AKDAHLSPKR PWKEPVKAEE 1320
RGRFGKAIEK DDCDETGIEE ANELTKLNVS KSV 1353 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0004016; F:adenylate cyclase activity; TAS:ProtInc.
 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: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: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. 
Pfam
 PF00211; Guanylate_cyc 
SMART
 SM00044; CYCc 
PROSITE
 PS00452; GUANYLATE_CYCLASE_1
 PS50125; GUANYLATE_CYCLASE_2 
PRINTS