CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001482
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PHD finger protein 14 
Protein Synonyms/Alias
  
Gene Name
 PHF14 
Gene Synonyms/Alias
 KIAA0783 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
307EDSLILEKSQNWSSQubiquitination[1, 2, 3]
396PNQDGIFKETDAGRWubiquitination[2]
435LTEMNYSKYGAKECSacetylation[4, 5]
435LTEMNYSKYGAKECSubiquitination[1, 3, 6]
439NYSKYGAKECSFCEDubiquitination[2]
527MSLQEREKQLSPEAQubiquitination[5]
582AIRKLMRKAELMGISubiquitination[2]
641QENMAEQKNIKDKLEubiquitination[1, 3]
674ELQNLNGKLRSEGQGubiquitination[5]
693LGRITGQKLNIPAILubiquitination[5, 6]
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] 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]
 [3] 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]
 [4] 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]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] 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
Functional Description
  
Sequence Annotation
 ZN_FING 319 380 PHD-type 1.
 ZN_FING 725 779 PHD-type 2.
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 84 84 Phosphoserine.
 MOD_RES 91 91 Phosphoserine.
 MOD_RES 196 196 Phosphoserine.
 MOD_RES 208 208 Phosphoserine.
 MOD_RES 287 287 Phosphothreonine.
 MOD_RES 290 290 Phosphoserine.
 MOD_RES 294 294 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 530 530 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 888 AA 
Protein Sequence
MDRSSKRRQV KPLAASLLEA LDYDSSDDSD FKVGDASDSE GSGNGSEDAS KDSGEGSCSD 60
SEENILEEEL NEDIKVKEEQ LKNSAEEEVL SSEKQLIKME KKEEEENGER PRKKKEKEKE 120
KEKEKEKEKE REKEKEKATV SENVAASAAA TTPATSPPAV NTSPSVPTTT TATEEQVSEP 180
KKWNLRRNRP LLDFVSMEEL NDMDDYDSED DNDWRPTVVK RKGRSASQKE GSDGDNEDDE 240
DEGSGSDEDE NDEGNDEDHS SPASEGGCKK KKSKVLSRNS ADDEELTNDS LTLSQSKSNE 300
DSLILEKSQN WSSQKMDHIL ICCVCLGDNS EDADEIIQCD NCGITVHEGC YGVDGESDSI 360
MSSASENSTE PWFCDACKCG VSPSCELCPN QDGIFKETDA GRWVHIVCAL YVPGVAFGDI 420
DKLRPVTLTE MNYSKYGAKE CSFCEDPRFA RTGVCISCDA GMCRAYFHVT CAQKEGLLSE 480
AAAEEDIADP FFAYCKQHAD RLDRKWKRKN YLALQSYCKM SLQEREKQLS PEAQARINAR 540
LQQYRAKAEL ARSTRPQAWV PREKLPRPLT SSASAIRKLM RKAELMGIST DIFPVDNSDT 600
SSSVDGRRKH KQPALTADFV NYYFERNMRM IQIQENMAEQ KNIKDKLENE QEKLHVEYNK 660
LCESLEELQN LNGKLRSEGQ GIWALLGRIT GQKLNIPAIL RAPKERKPSK KEGGTQKTST 720
LPAVLYSCGI CKKNHDQHLL LLCDTCKLHY HLGCLDPPLT RMPRKTKNSY WQCSECDQAG 780
SSDMEADMAM ETLPDGTKRS RRQIKEPVKF VPQDVPPEPK KIPIRNTRTR GRKRSFVPEE 840
EKHEERVPRE RRQRQSVLQK KPKAEDLRTE CATCKGTGDN ENLVRYPS 888 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00628; PHD 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS