CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000784
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 A-kinase anchor protein 8 
Protein Synonyms/Alias
 AKAP-8; A-kinase anchor protein 95 kDa; AKAP 95 
Gene Name
 AKAP8 
Gene Synonyms/Alias
 AKAP95 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
534LNNRHIVKMLEKYLKacetylation[1]
538HIVKMLEKYLKGEDPacetylation[2]
Reference
 [1] 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]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). 
Sequence Annotation
 ZN_FING 390 414 C2H2 AKAP95-type 1.
 ZN_FING 479 504 C2H2 AKAP95-type 2.
 REGION 572 589 RII-binding (By similarity).
 MOTIF 368 377 Nuclear localization signal (Potential).
 MOD_RES 112 112 Phosphoserine.
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 328 328 Phosphoserine.
 MOD_RES 339 339 Phosphoserine.  
Keyword
 Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MDQGYGGYGA WSAGPANTQG AYGTGVASWQ GYENYNYYGA QNTSVTTGAT YSYGPASWEA 60
AKANDGGLAA GAPAMHMASY GPEPCTDNSD SLIAKINQRL DMMSKEGGRG GSGGGGEGIQ 120
DRESSFRFQP FESYDSRPCL PEHNPYRPSY SYDYEFDLGS DRNGSFGGQY SECRDPARER 180
GSLDGFMRGR GQGRFQDRSN PGTFMRSDPF VPPAASSEPL STPWNELNYV GGRGLGGPSP 240
SRPPPSLFSQ SMAPDYGVMG MQGAGGYDST MPYGCGRSQP RMRDRDRPKR RGFDRFGPDG 300
TGRKRKQFQL YEEPDTKLAR VDSEGDFSEN DDAAGDFRSG DEEFKGEDEL CDSGRQRGEK 360
EDEDEDVKKR REKQRRRDRT RDRAADRIQF ACSVCKFRSF DDEEIQKHLQ SKFHKETLRF 420
ISTKLPDKTV EFLQEYIVNR NKKIEKRRQE LMEKETAKPK PDPFKGIGQE HFFKKIEAAH 480
CLACDMLIPA QPQLLQRHLH SVDHNHNRRL AAEQFKKTSL HVAKSVLNNR HIVKMLEKYL 540
KGEDPFTSET VDPEMEGDDN LGGEDKKETP EEVAADVLAE VITAAVRAVD GEGAPAPESS 600
GEPAEDEGPT DTAEAGSDPQ AEQLLEEQVP CGTAHEKGVP KARSEAAEAG NGAETMAAEA 660
ESAQTRVAPA PAAADAEVEQ TDAESKDAVP TE 692 
Gene Ontology
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0001939; C:female pronucleus; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0016363; C:nuclear matrix; ISS:UniProtKB.
 GO:0003690; F:double-stranded DNA binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0007076; P:mitotic chromosome condensation; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR007071; AKAP95.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF04988; AKAP95 
SMART
 SM00355; ZnF_C2H2 
PROSITE
  
PRINTS