CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031991
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cDNA FLJ55380, highly similar to Protein kinase C-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
383YVENIRRKFGVFNYSubiquitination[1, 2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
  
Sequence Annotation
  
Keyword
 Kinase; Metal-binding; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1241 AA 
Protein Sequence
MVFLEEFEAR SCLAEEEIKT EQEVVEGMDI STRSKDPGSA ERTAQKRKFP SPPHSSNGHS 60
PQDTSTSPIK KKKKPGLLNS NNKEQSELRH GPFYYMKQPL TTDPVDVVPQ DGRNDFYCWV 120
CHREGQVLCC ELCPRVYHAK CLRLTSEPEG DWFCPECEKI TVAECIETQS KAMTMLTIEQ 180
LSYLLKFAIQ KMKQPGTDAF QKPVPLEQHP DYAEYIFHPM DLCTLEKNTK KKMYGCTEAF 240
LADAKWILHN CIIYNGGNHK LTQIAKVVIK ICEHEMNEIE VCPECYLAAC QKRDNWFCEP 300
CSNPHPLVWA KLKGFPFWPA KALRDKDGQV DARFFGQHDR AWVPINNCYL MFKEIPFSVK 360
KTKSIFNSAM QEMEVYVENI RRKFGVFNYS PFRTPYTPNS QYQMLLDPTN PSAGTAKIDK 420
QEKVKLNFDM TASPKILMSK PVLSGGTGRR ISLSDMPRSP MSTNSSVHTG SDVEQDAEKK 480
ATSSHFSASE ESMDFLDKST ASPASTKTGQ AGSLSGSPKP FSPQLSAPIT TKTDKTSTTG 540
SILNLNLDRS KAEMDLKELS ESVQQQSTPV PLISPKRQIR SRFQLNLDKT IESCKAQLGI 600
NEISEDVYTA VEHSDSEDSE KSDSSDSEYI SDDEQKSKNE PEDTEDKEGC QMDKEPSAVK 660
KKPKPTNPVE IKEELKSTSP ASEKADPGAV KDKASPEPEK DFSEKAKPSP HPIKDKLKGK 720
DETDSPTVHL GLDSDSESEL VIDLGEDHSG REGRKNKKEP KEPSPKQDVV GKTPPSTTVG 780
SHSPPETPVL TRSSAQTSAA GATATTSTSS TVTVTAPAPA ATGSPVKKQR PLLPKETAPA 840
VQRVVWNSSS KFQTSSQKWH MQKMQRQQQQ QQQQNQQQQP QSSQGTRYQT RQAVKAVQQK 900
EITQSPSTST ITLVTSTQSS PLVTSSGSMS TLVSSVNADL PIATASADVA ADIAKYTSKM 960
MDAIKGTMTE IYNDLSKNTT GSTIAEIRRL RIEIEKLQWL HQQELSEMKH NLELTMAEMR 1020
QSLEQERDRL IAEVKKQLEL EKQQAVDETK KKQWCANCKK EAIFYCCWNT SYCDYPCQQA 1080
HWPEHMKSCT QSATAPQQEA DAEVNTETLN KSSQGSSSST QSAPSETASA SKEKETSAEK 1140
SKESGSTLDL SGSRETPSSI LLGSNQGSVS KRCDKQPAYA PTTTDHQPHP NYPAQKYHSR 1200
SNKSSWSSSD EKRGSTRSDH NTSTSTKSLL PKESRLDTFW D 1241 
Gene Ontology
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001487; Bromodomain.
 IPR021931; DUF3544.
 IPR000313; PWWP.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR002893; Znf_MYND.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF12064; DUF3544
 PF00628; PHD
 PF00855; PWWP
 PF01753; zf-MYND 
SMART
 SM00297; BROMO
 SM00249; PHD 
PROSITE
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01360; ZF_MYND_1
 PS50865; ZF_MYND_2
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS