CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022517
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PHD and RING finger domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 PHRF1 
Gene Synonyms/Alias
 KIAA1542 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
153PVDRTLFKCICIRAQubiquitination[1]
164IRAQFGGKILRKIPVubiquitination[1, 2]
556SRGEEGFKGCLQPRAubiquitination[1]
668VVPGPPLKPAPRRTDubiquitination[1]
768PLGPSRGKGVGSTFEubiquitination[1]
821SPLFSIKKTKQLRSEubiquitination[1]
869TISINSPKAQTVQAVubiquitination[1]
1579EEVKLAIKPFYQKREubiquitination[3]
1589YQKREVTKEEYKDILacetylation[4]
1593EVTKEEYKDILRKAVacetylation[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
  
Sequence Annotation
 ZN_FING 108 149 RING-type; degenerate.
 ZN_FING 183 233 PHD-type.
 MOD_RES 330 330 Phosphothreonine.
 MOD_RES 455 455 Phosphoserine.
 MOD_RES 864 864 Phosphoserine.
 MOD_RES 867 867 Phosphoserine.
 MOD_RES 915 915 Phosphoserine.
 MOD_RES 917 917 Phosphothreonine.
 MOD_RES 936 936 Phosphoserine.
 MOD_RES 991 991 Phosphoserine.
 MOD_RES 1032 1032 Phosphoserine (By similarity).
 MOD_RES 1034 1034 Phosphoserine (By similarity).
 MOD_RES 1127 1127 Phosphoserine (By similarity).
 MOD_RES 1128 1128 Phosphoserine.
 MOD_RES 1202 1202 Phosphoserine.
 MOD_RES 1359 1359 Phosphoserine.
 MOD_RES 1360 1360 Phosphoserine.
 MOD_RES 1371 1371 Phosphoserine.
 MOD_RES 1404 1404 Phosphothreonine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1649 AA 
Protein Sequence
MDDDSLDELV ARSPGPDGHP QVGPADPAGD FEESSVGSSG DSGDDSDSEH GDGTDGEDEG 60
ASEEEDLEDR SGSEDSEDDG ETLLEVAGTQ GKLEAAGSFN SDDDAESCPI CLNAFRDQAV 120
GTPENCAHYF CLDCIVEWSK NANSCPVDRT LFKCICIRAQ FGGKILRKIP VENTKASEEE 180
EDPTFCEVCG RSDREDRLLL CDGCDAGYHM ECLDPPLQEV PVDEWFCPEC AAPGVVLAAD 240
AGPVSEEEVS LLLADVVPTT SRLRPRAGRT RAIARTRQSE RVRATVNRNR ISTARRVQHT 300
PGRLGSSLLD EAIEAVATGL STAVYQRPLT PRTPARRKRK TRRRKKVPGR KKTPSGPSAK 360
SKSSATRSKK RQHRVKKRRG KKVKSEATTR SRIARTLGLR RPVHSSCIPS VLKPVEPSLG 420
LLRADIGAAS LSLFGDPYEL DPFDSSEELS ANPLSPLSAK RRALSRSALQ SHQPVARPVS 480
VGLSRRRLPA AVPEPDLEEE PVPDLLGSIL SGQSLLMLGS SDVIIHRDGS LSAKRAAPVS 540
FQRNSGSLSR GEEGFKGCLQ PRALPSGSPA QGPSGNRPQS TGLSCQGRSR TPARTAGAPV 600
RLDLPAAPGA VQARNLSNGS VPGFRQSHSP WFNGTNKHTL PLASAASKIS SRDSKPPCRS 660
VVPGPPLKPA PRRTDISELP RIPKIRRDDG GGRRDAAPAH GQSIEIPSAC ISRLTGREGT 720
GQPGRGTRAE SEASSRVPRE PGVHTGSSRP PAPSSHGSLA PLGPSRGKGV GSTFESFRIN 780
IPGNMAHSSQ LSSPGFCNTF RPVDDKEQRK ENPSPLFSIK KTKQLRSEVY DPSDPTGSDS 840
SAPGSSPERS GPGLLPSEIT RTISINSPKA QTVQAVRCVT SYTVESIFGT EPEPPLGPSS 900
AMSKLRGAVA AEGASDTERE EPTESQGLAA RLRRPSPPEP WDEEDGASCS TFFGSEERTV 960
TCVTVVEPEA PPSPDVLQAA THRVVELRPP SRSRSTSSSR SRKKAKRKRV SREHGRTRSG 1020
TRSESRDRSS RSASPSVGEE RPRRQRSKAK SRRSSSDRSS SRERAKRKKA KDKSREHRRG 1080
PWGHSRRTSR SRSGSPGSSS YEHYESRKKK KRRSASRPRG RECSPTSSLE RLCRHKHQRE 1140
RSHERPDRKE SVAWPRDRRK RRSRSPSSEH RAREHRRPRS REKWPQTRSH SPERKGAVRE 1200
ASPAPLAQGE PGREDLPTRL PALGEAHVSP EVATADKAPL QAPPVLEVAA ECEPDDLDLD 1260
YGDSVEAGHV FDDFSSDAVF IQLDDMSSPP SPESTDSSPE RDFPLKPALP PASLAVAAIQ 1320
REVSLMHDED PSQPPPLPEG TQEPHLLRPD AAEKAEAPSS PDVAPAGKED SPSASGRVQE 1380
AARPEEVVSQ TPLLRSRALV KRVTWNLQES ESSAPAEDRA PRAPLHRPQK PREGAWDMED 1440
VAPTGVRQVF SELPFPSHVL PEPGFPDTDP SQVYSPGLPP APAQPSSIPP CALVSQPTVQ 1500
FILQGSLPLV GCGAAQTLAP VPAALTPASE PASQATAASN SEEKTPAPRL AAEKTKKEEY 1560
MKKLHMQERA VEEVKLAIKP FYQKREVTKE EYKDILRKAV QKICHSKSGE INPVKVANLV 1620
KAYVDKYRHM RRHKKPEAGE EPPTQGAEG 1649 
Gene Ontology
 GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Compara. 
Interpro
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00628; PHD
 PF13639; zf-RING_2 
SMART
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS