CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030617
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase type 5 
Protein Synonyms/Alias
 cDNA FLJ42701 fis, clone BRAMY3004919, highly similar to Adenylate cyclase type 5 (EC 4.6.1.1) 
Gene Name
 ADCY5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
851AGVIGARKPQYDIWGubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Lyase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 919 AA 
Protein Sequence
MAPSRFRTQL ELVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA RLHSQRENQQ 60
QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG FTSLASQCTA 120
QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC VEMGMDMIEA 180
ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA GGKAGRIHIT 240
KATLNYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA KMNRQRTNSI 300
GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD EFLGRAIDAR 360
SIDRLRSEHV RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF VQITIVPHSI 420
FMLSFYLTCS LLLTLVVFVS VIYSCVKLFP SPLQTLSRKI VRSKMNSTLV GVFTITLVFL 480
AAFVNMFTCN SRDLLGCLAQ EHNISASQVN ACHVAESAVN YSLGDEQGFC GSPWPNCNFP 540
EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLIV EVPGVTLFDN ADLLVTANAI 600
DFFNNGTSQW SLCENLRHRR MEAGTYFPSG VKEQSPEHAT KVALKVVTPI IISVFVLALY 660
LHAQQVESTA RLDFLWKLQA TEEKEEMEEL QAYNRRLLHN ILPKDVAAHF LARERRNDEL 720
YYQSCECVAV MFASIANFSE FYVELEANNE GVECLRLLNE IIADFDEIIS EDRFRQLEKI 780
KTIGSTYMAA SGLNDSTYDK VGKTHIKALA DFAMKLMDQM KYINEHSFNN FQMKIGLNIG 840
PVVAGVIGAR KPQYDIWGNT VNVASRMDST GVPDRIQVTT DMYQVLAANT YQLECRGVVK 900
VKGKGEMMTY FLNGGPPLS 919 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0004016; F:adenylate cyclase activity; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0006171; P:cAMP biosynthetic process; IEA:GOC.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro. 
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