CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002694
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase 
Protein Synonyms/Alias
 ATP pyrophosphate-lyase; Adenylyl cyclase 
Gene Name
 CYR1 
Gene Synonyms/Alias
 CDC35; HSR1; SRA4; YJL005W; J1401 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
616ANREQDNKTPILNKTubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. 
Sequence Annotation
 DOMAIN 676 755 Ras-associating.
 REPEAT 815 838 LRR 1.
 REPEAT 842 862 LRR 2.
 REPEAT 863 885 LRR 3.
 REPEAT 886 908 LRR 4.
 REPEAT 910 931 LRR 5.
 REPEAT 932 955 LRR 6.
 REPEAT 957 976 LRR 7.
 REPEAT 977 999 LRR 8.
 REPEAT 1001 1016 LRR 9.
 REPEAT 1017 1040 LRR 10.
 REPEAT 1042 1062 LRR 11.
 REPEAT 1063 1086 LRR 12.
 REPEAT 1088 1109 LRR 13.
 REPEAT 1110 1132 LRR 14.
 REPEAT 1134 1156 LRR 15.
 REPEAT 1188 1209 LRR 16.
 REPEAT 1210 1232 LRR 17.
 REPEAT 1233 1256 LRR 18.
 REPEAT 1258 1280 LRR 19.
 REPEAT 1285 1308 LRR 20.
 DOMAIN 1369 1625 PP2C-like.
 DOMAIN 1668 1805 Guanylate cyclase.
 METAL 1673 1673 Magnesium (By similarity).
 METAL 1716 1716 Magnesium (By similarity).
 MOD_RES 376 376 Phosphothreonine.
 MOD_RES 389 389 Phosphothreonine.
 MOD_RES 433 433 Phosphoserine.
 MOD_RES 487 487 Phosphoserine.
 MOD_RES 497 497 Phosphoserine.
 MOD_RES 562 562 Phosphoserine.  
Keyword
 ATP-binding; cAMP biosynthesis; Complete proteome; Leucine-rich repeat; Lyase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2026 AA 
Protein Sequence
MSSKPDTGSE ISGPQRQEEQ EQQIEQSSPT EANDRSIHDE VPKVKKRHEQ NSGHKSRRNS 60
AYSYYSPRSL SMTKSRESIT PNGMDDVSIS NVEHPRPTEP KIKRGPYLLK KTLSSLSMTS 120
ANSTHDDNKD HGYALNSSKT HNYTSTHNHH DGHHDHHHVQ FFPNRKPSLA ETLFKRFSGS 180
NSHDGNKSGK ESKVANLSLS TVNPAPANRK PSKDSTLSNH LADNVPSTLR RKVSSLVRGS 240
SVHDINNGIA DKQIRPKAVA QSENTLHSSD VPNSKRSHRK SFLLGSTSSS SSRRGSNVSS 300
MTNSDSASMA TSGSHVLQHN VSNVSPTTKS KDSVNSESAD HTNNKSEKVT PEYNENIPEN 360
SNSDNKREAT TPTIETPISC KPSLFRLDTN LEDVTDITKT VPPTAVNSTL NSTHGTETAS 420
PKTVIMPEGP RKSVSMADLS VAAAAPNGEF TSTSNDRSQW VAPQSWDVET KRKKTKPKGR 480
SKSRRSSIDA DELDPMSPGP PSKKDSRHHH DRKDNESMVT AGDSNSSFVD ICKENVPNDS 540
KTALDTKSVN RLKSNLAMSP PSIRYAPSNL DGDYDTSSTS SSLPSSSISS EDTSSCSDSS 600
SYTNAYMEAN REQDNKTPIL NKTKSYTKKF TSSSVNMNSP DGAQSSGLLL QDEKDDEVEC 660
QLEHYYKDFS DLDPKRHYAI RIFNTDDTFT TLSCTPATTV EEIIPALKRK FNITAQGNFQ 720
ISLKVGKLSK ILRPTSKPIL IERKLLLLNG YRKSDPLHIM GIEDLSFVFK FLFHPVTPSH 780
FTPEQEQRIM RSEFVHVDLR NMDLTTPPII FYQHTSEIES LDVSNNANIF LPLEFIESSI 840
KLLSLRMVNI RASKFPSNIT KAYKLVSLEL QRNFIRKVPN SIMKLSNLTI LNLQCNELES 900
LPAGFVELKN LQLLDLSSNK FMHYPEVINY CTNLLQIDLS YNKIQSLPQS TKYLVKLAKM 960
NLSHNKLNFI GDLSEMTDLR TLNLRYNRIS SIKTNASNLQ NLFLTDNRIS NFEDTLPKLR 1020
ALEIQENPIT SISFKDFYPK NMTSLTLNKA QLSSIPGELL TKLSFLEKLE LNQNNLTRLP 1080
QEISKLTKLV FLSVARNKLE YIPPELSQLK SLRTLDLHSN NIRDFVDGME NLELTSLNIS 1140
SNAFGNSSLE NSFYHNMSYG SKLSKSLMFF IAADNQFDDA MWPLFNCFVN LKVLNLSYNN 1200
FSDVSHMKLE SITELYLSGN KLTTLSGDTV LKWSSLKTLM LNSNQMLSLP AELSNLSQLS 1260
VFDVGANQLK YNISNYHYDW NWRNNKELKY LNFSGNRRFE IKSFISHDID ADLSDLTVLP 1320
QLKVLGLMDV TLNTTKVPDE NVNFRLRTTA SIINGMRYGV ADTLGQRDYV SSRDVTFERF 1380
RGNDDECLLC LHDSKNQNAD YGHNISRIVR DIYDKILIRQ LERYGDETDD NIKTALRFSF 1440
LQLNKEINGM LNSVDNGADV ANLSYADLLS GACSTVIYIR GKKLFAANLG DCMAILSKNN 1500
GDYQTLTKQH LPTKREEYER IRISGGYVNN GKLDGVVDVS RAVGFFDLLP HIHASPDISV 1560
VTLTKADEML IVATHKLWEY MDVDTVCDIA RENSTDPLRA AAELKDHAMA YGCTENITIL 1620
CLALYENIQQ QNRFTLNKNS LMTRRSTFED TTLRRLQPEI SPPTGNLAMV FTDIKSSTFL 1680
WELFPNAMRT AIKTHNDIMR RQLRIYGGYE VKTEGDAFMV AFPTPTSGLT WCLSVQLKLL 1740
DAQWPEEITS VQDGCQVTDR NGNIIYQGLS VRMGIHWGCP VPELDLVTQR MDYLGPMVNK 1800
AARVQGVADG GQIAMSSDFY SEFNKIMKYH ERVVKGKESL KEVYGEEIIG EVLEREIAML 1860
ESIGWAFFDF GEHKLKGLET KELVTIAYPK ILASRHEFAS EDEQSKLINE TMLFRLRVIS 1920
NRLESIMSAL SGGFIELDSR TEGSYIKFNP KVENGIMQSI SEKDALLFFD HVITRIESSV 1980
ALLHLRQQRC SGLEICRNDK TSARSNIFNV VDELLQMVKN AKDLST 2026 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0004016; F:adenylate cyclase activity; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IGI:SGD.
 GO:0007265; P:Ras protein signal transduction; IGI:SGD. 
Interpro
 IPR001054; A/G_cyclase.
 IPR013716; Adenylate_cyclase_G-a-bd.
 IPR001611; Leu-rich_rpt.
 IPR025875; Leu-rich_rpt_4.
 IPR001932; PP2C-like.
 IPR000159; Ras-assoc. 
Pfam
 PF08509; Ad_cyc_g-alpha
 PF00211; Guanylate_cyc
 PF00560; LRR_1
 PF12799; LRR_4
 PF00481; PP2C
 PF00788; RA 
SMART
 SM00789; Ad_cyc_g-alpha
 SM00044; CYCc
 SM00332; PP2Cc
 SM00314; RA 
PROSITE
 PS50125; GUANYLATE_CYCLASE_2
 PS51450; LRR
 PS50200; RA 
PRINTS