CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036973
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 PHD finger protein 3 
Protein Synonyms/Alias
  
Gene Name
 PHF3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
190HPAASASKPSADQIRacetylation[1]
230KAAKVATKIEKELFSubiquitination[2, 3]
233KVATKIEKELFSFFRubiquitination[4]
258RSLMFNLKDPKNNILubiquitination[2, 3]
489INMPSVAKFVTKAYPubiquitination[4]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] 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]
 [4] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 861 AA 
Protein Sequence
MVGCGRCDDW FHGDCVGLSL SQAQQMGEED KEYVCVKCCA EEDKKTEILD PDTLENQATV 60
EFHSGDKTME CEKLGLSKHT TNDRTKYIDD TVKHKVKILK RESGEGRNSS DCRDNEIKKW 120
QLAPLRKMGQ PVLPRRSSEE KSEKIPKEST TVTCTGEKAS KPGTHEKQEM KKKKVEKGVL 180
NVHPAASASK PSADQIRQSV RHSLKDILMK RLTDSNLKVP EEKAAKVATK IEKELFSFFR 240
DTDAKYKNKY RSLMFNLKDP KNNILFKKVL KGEVTPDHLI RMSPEELASK ELAAWRRREN 300
RHTIEMIEKE QREVERRPIT KITHKGEIEI ESDAPMKEQE AAMEIQEPAA NKSLEKPEGS 360
EKQKEEVDSM SKDTTSQHRQ HLFDLNCKIC IGRMAPPVDD LSPKKVKVVV GVARKHSDNE 420
AESIADALSS TSNILASEFF EEEKQESPKS TFSPAPRPEM PGTVEVESTF LARLNFIWKG 480
FINMPSVAKF VTKAYPVSGS PEYLTEDLPD SIQVGGRISP QTVWDYVEKI KASGTKEICV 540
VRFTPVTEED QISYTLLFAY FSSRKRYGVA ANNMKQVKDM YLIPLGATDK IPHPLVPFDG 600
PGLELHRPNL LLGLIIRQKL KRQHSACAST SHIAETPESA PPIALPPDKK SKIEVSTEEA 660
PEEENDFFNS FTTVLHKQRN KPQQNLQEDL PTAVEPLMEV TKQEPPKPLR FLPGVLIGWE 720
NQPTTLELAN KPLPVDDILQ SLLGTTGQVY DQAQSVMEQN TVKEIPFLNE QTNSKIEKTD 780
NVEVTDGENK EIKVKVDNIS ESTDKSAEIE TSVVGSSSIS AGSLTSLSLR GKPPDVSTEA 840
FLTNLSIQSK QEETVESKEK T 861 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR012921; SPOC_C.
 IPR003618; TFIIS_cen_dom.
 IPR017890; TFS2M.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00628; PHD
 PF07744; SPOC
 PF07500; TFIIS_M 
SMART
 SM00249; PHD
 SM00510; TFS2M 
PROSITE
 PS51321; TFIIS_CENTRAL 
PRINTS