CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030560
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase type 3 
Protein Synonyms/Alias
 cDNA FLJ37854 fis, clone BRSSN2014610, highly similar to Adenylate cyclase type 3 (EC 4.6.1.1) 
Gene Name
 ADCY3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39LGGVLGQKRWQYDVWubiquitination[1, 2, 3]
465KIEVHDQKERVYEMRubiquitination[1]
588NGFASSNKEDKSEREubiquitination[1]
591ASSNKEDKSERERWQubiquitination[2]
633MLRIGMNKGGVLAGVubiquitination[1, 4]
698GPIFVKGKGELLTFFubiquitination[4]
707ELLTFFLKGRDKLATubiquitination[4]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Lyase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 731 AA 
Protein Sequence
MGLAMVEAIS YVREKTKTGV DMRVGVHTGT VLGGVLGQKR WQYDVWSTDV TVANKMEAGG 60
IPGGSKIEER LYSCVVAPTL RLRWERVHIS QSTMDCLKGE FDVEPGDGGS RCDYLEEKGI 120
ETYLIIASKP EVKKTATQNG LNGSALPNGA PASSKSSSPA LIETKEPNGS AHSSGSTSEK 180
PEEQDAQADN PSFPNPRRRL RLQDLADRVV DASEDEHELN QLLNEALLER ESAQVVKKRN 240
TFLLSMRFMD PEMETRYSVE KEKQSGAAFS CSCVVLLCTA LVEILIDPWL MTNYVTFMVG 300
EILLLILTIC SLAAIFPRAF PKKLVAFSTW IDRTRWARNT WAMLAIFILV MANVVDMVSH 360
MVKLTLMLLV AGAVATINLY AWRPVFDEYD HKRFREHDLP MVALEQMQGF NPGLNGTDRL 420
PLVPSKYSMT VMVFLMMLSF YYFSRHVEKL ARTLFLWKIE VHDQKERVYE MRRWNEALVT 480
NMLPEHVARH FLGSKKRDEE LYSQTYDEIG VMFASLPNFA DFYTEESINN GGIECLRFLN 540
EIISDFDSLL DNPKFRVITK IKTIGSTYMA ASGVTPDVNT NGFASSNKED KSERERWQHL 600
ADLADFALAM KDTLTNINNQ SFNNFMLRIG MNKGGVLAGV IGARKPHYDI WGNTVNVASR 660
MESTGVMGNI QVVEETQVIL REYGFRFVRR GPIFVKGKGE LLTFFLKGRD KLATFPNGPS 720
VTLPHQVVDN S 731 
Gene Ontology
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
 GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro. 
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