CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028029
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein partner of snf 
Protein Synonyms/Alias
  
Gene Name
 pps 
Gene Synonyms/Alias
 CG6525; Dmel_CG6525 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
269KVQRLPVKPHQVQQAacetylation[1]
401VVRQTPSKPMKPLPPacetylation[1]
511VKEIIINKNMASPKGacetylation[1]
791STPPTSAKVVRGYGRacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2016 AA 
Protein Sequence
MSSSVFTEAP SARPAAAEAD SNLVVVYSKS GISFDERAIG NIMEEKSIST ISVVRITSPT 60
PSMVDQEEDE RLEELANFME TATDSELDSD NGSQSGGDNA SEMDEHDEEN HNTGDDNNSD 120
STETEADAPR TRKRVGRKPK AIKKRKRRKP KERPQIVGLR VEQFYADNTA DMVVKNALKL 180
AGVSVYKRTA ETDALMEVIR NDHNYTPFTS PEQLKNHKRD EKMAMEMQAQ SRKIIMQAPG 240
SVKLINAKKR VQAIPLSPVQ VKVQRLPVKP HQVQQAAQLQ PKVQLIRKPI HSPLPRQKPE 300
IIANNSVNAR LRPTRAPVKV IAPPVQEYIE DDDDAQSSDS AEEENADKAY DSEEMSEESD 360
EFQESDNDRD SDMDFDMRHS NRRNPNKRKR VRKVVRQTPS KPMKPLPPPP TTPQHFPELK 420
KRKEVLEPKA PQIGQIIQMP ATKSVPAVFA LGRGLPSTSF LKIRPTHQSL PVKRPPLPTT 480
PANSNVRRMP AVQLGRIVNS PQEVKEIIIN KNMASPKGVF TNLNTLLGED NNAATKSSPV 540
PLRHRAVMSP STPRSSYNQQ MSPIVVPVPA QAHTPSKGFM PIGVDTAQSH KLPAQIVIET 600
HQSSSELAAE NDKQLDLINS IVQDELLKST LVEQPVVNAD EDIPKLVKML ESTAADLDPP 660
PVSLPTNIFP APEMQGVGNA AAADPNNIMD TANEDEITAD FLQHVVGLIE EDKQFEAEVV 720
KQVLASTEPG TLDAIVSMPT SIEPVDVPQA HTNLLPNASL TEPAQSMTSL PIACSTPSRS 780
VAASTPPTSA KVVRGYGRVI YLPPIEAPTT RAKRRAQFPS APGMAATSSS DAGNLSFGES 840
SLDASINQPL NTSSLSNDSQ PGSGPKRPNP REPSMARRST APRRSKKLDA SQNNDPDASE 900
SQEDDDDPNK LWCICRQPHN NRFMICCDLC EDWFHGTCVG VTKAMGTDME NKGIDWKCPK 960
CVKRQEERSQ PRITDMLVTR PTTQPEQRPS ETKVLTTTAE IVQVAAPSAP RRTLPVVLTV 1020
ASSPMRIPMA KPAKKFPTGA ISHQQQQQLN FIRLGPSPGK RISETLCVVC KRPASTSSVY 1080
CGEECIRKYA QSAIQAHAAT KGPLPQNAGA QSLLNNSFDA KKNKKKDLFE DVLRQADTVS 1140
KVERINVFER KSGRVITGHM APSAHQFRKW LQENPSFEVL PSGTVQSADA EKRLLKGAPE 1200
AATSTSEPAV LGVAKKPPEG PAKLSHPQNT TVQASHQLGI SSVRPLAKKD KEKTTPTVQA 1260
PTPNRIAAGK PEPVRIGIRR SLREQLLARI KEAQAAEENS GQPTTQWPTV LEVDQFVKNV 1320
ELEMFNSFGR DVGAKYKAKY RSLMFNIKDR KNRTLFEKIC AKQVEPRQLV RMTPEQLASQ 1380
ELAKWREEEN RHQLDMIKKS ELDLLACAQN YVVKTHKGEE VIATKVDVTL PEENVSEASS 1440
MADTKQTSLV SEPSTSTLER STSREKAGSS KEKRHKSHKH HHRKRSRSRS NSRGRSVDKR 1500
HRRQHNEGGE QPGSGEREHR SREKQSRERD EIVPSPLPKK RDENDQSPVP KKTAEKKTEA 1560
SAYNLVDQIL ESEKTVEQAA NLGKPKPSPK PLPTLPSSLK APEPMDNYSR YLHGLTTSSL 1620
WSGTLKMIDL ADFEIVMYPV QGNCHQLGNL MPSQMDVIGR ITRVNVWEYI KKLKKSPTKE 1680
VVIVNIFPAS PSETYKFDLF FEYLDSRQRL GVLGVDSDQI RDFYIFPLGS GDKLPPALQT 1740
AEPVPFYEEA QRPNTLLGII VRCLSKRPAD AVPSTPSVPT PVPALSSKVA KRSRSSISYP 1800
AQSSPKRKIS THSTSSKDDE FDIDAIIKAP IAKLQKTAPK VVPQPSVPND ADEPYSPGGS 1860
DDELVPSAPQ RPNDLERQVN EINKQIAAQQ MEIAGLLKVE PTGSASSSNV LAAISIPANL 1920
SKILASIKDK TNLPSSADDG DEEYNPEDDI TATSSFASKK PRSKGRLAHL SEAELLSMVP 1980
DNLAGVIPRS SRTRHQLAQS PLTPTPLPPP PPPPGV 2016 
Gene Ontology
 GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR006576; BRK_domain.
 IPR012921; SPOC_C.
 IPR003618; TFIIS_cen_dom.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF07533; BRK
 PF00628; PHD
 PF07744; SPOC
 PF07500; TFIIS_M 
SMART
 SM00592; BRK
 SM00249; PHD 
PROSITE
 PS51321; TFIIS_CENTRAL
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS