CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024453
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
768HLGPSRGKGIGSSFEacetylation[1]
810VDSKVQRKETPFPLFubiquitination[2]
820PFPLFSIKKPKQLKSacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
  
Sequence Annotation
 ZN_FING 109 150 RING-type; degenerate.
 ZN_FING 185 235 PHD-type.
 MOD_RES 332 332 Phosphothreonine (By similarity).
 MOD_RES 457 457 Phosphoserine (By similarity).
 MOD_RES 864 864 Phosphoserine (By similarity).
 MOD_RES 867 867 Phosphoserine (By similarity).
 MOD_RES 919 919 Phosphoserine (By similarity).
 MOD_RES 1000 1000 Phosphoserine (By similarity).
 MOD_RES 1043 1043 Phosphoserine.
 MOD_RES 1045 1045 Phosphoserine.
 MOD_RES 1134 1134 Phosphoserine.
 MOD_RES 1135 1135 Phosphoserine.
 MOD_RES 1201 1201 Phosphoserine (By similarity).
 MOD_RES 1368 1368 Phosphoserine (By similarity).
 MOD_RES 1379 1379 Phosphoserine (By similarity).
 MOD_RES 1412 1412 Phosphothreonine (By similarity).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1682 AA 
Protein Sequence
MDDDNLDELV AHSPGPDGPP RVGSSELASD AEESSNGQSG DSEDDTGSEQ DDDTDGEETE 60
GLSEEEDPED RSGSEDSEDG VEMATAAIET QGKLEASSVP NSDDDAESCP ICLNAFRDQA 120
VGTPETCAHY FCLDCIIEWS RNANSCPVDR TVFKCICIRA QFNGKILKKI PVENTKACEA 180
EEEDPTFCEV CGRSDREDRL LLCDGCDAGY HMECLDPPLQ EVPVDEWFCP ECTVPGVDPT 240
HDAAPVSDEE VSLLLADVVP TTSRLRPRVG RTRAIARTRQ SERVRATVNR NRISSARRVQ 300
HVPRYLMSSL LDETIEAVAT GLSTAVYQRP LTPRVPAKRK RKAGRRKKVL GRKKTRSRSS 360
VKSKSGSTRA KKRQHRVRKT KGRKLKNEVT ARSRIARTLG LRRPVRGTSM PSVYKPVDPS 420
LGLMRADIGA ASLSLFGDPY ELDPFDSNEE QSADPPSPLS AKRRVLSRSA LQSHQPVARP 480
VAMGLSRRQL PAVAPEPSVE EAPVPDLLGS ILSGQSLLMM SSADVVIHRD GSLSAKRAAP 540
VSLQRNSVTQ SREESRLRDN PQPGALPSES ASGGFVGDRQ PNSGLSCGNR TALCCLPARI 600
AQTPVRSDPS LTPRSGLSRT LSDENRPSRT HSSSPQLNGS NVRVSSASTK IVTHSSFPSK 660
NTASGLPQRT GPRRPDFSKL PRIPKIHRDG NKSTQDQAPA SGHIVELPST CISRLTGREG 720
PGQPGRGRVD SEPSSRGPQE TGSHTSGSRP PAPSSHGSLA HLGPSRGKGI GSSFESFRIN 780
IPGNTAHCSQ LSSPGFCNTF RPVDSKVQRK ETPFPLFSIK KPKQLKSEIY DPFDPTGSDS 840
SPPSSSPESL GPGLLPSEIT RTISINSPKA PAFQTVRCVT SYRVESIFGT EMEPEPQPPS 900
EPVSGMLELL SKGSAEGTSD LEQEGLGEIE PTEIRGSTAR TQRPPPPDPW DDEDEVSCTP 960
FFGSEERTVT CVTVEEPGVL PSPDAPQITT HRIVEFRASS RSRSTSSSRS RKKTKKKKKK 1020
VAREHQRTRS STRSGSRDRT SRSVSPVAEE HTRRHRAKTK SRRSSSDRAS SQDRAKRRKD 1080
RDDRDREHRR GSWGHGRCRR KSRSRSGSPG SSSCERHESK RRKRRHSGSR SRGSSLERDR 1140
RHKHRERSRE RMDKQESVTR SRERRRWRSR SPSLEHRPRR PPSREKRAHS PEKKGPVREV 1200
SPAPATQGES RQDGDHSAEP PVSEVSVLPE VVSVLPEVVV ADLNPPEVPP VLAEPVAHVP 1260
EDLDYGESVE AGHVFEDFSN EAIFIQLDDM SSPPSPESTD SSPERDFPPN PILPPASLPQ 1320
DSTLPTIQRE VLPIHSEDIS KPVPQALAPS DQSLLKQDTV EITTTTPSTP AVVPMTKDSP 1380
VLSARGWEAV RPRDAVAQAP LLRSRTLVKR VTWNLQEAEH STPAALDRDP RTPLQRPQRP 1440
QEGDWDAEDR ALIGFQQAPF SELPPPIHVL QESGLPDADP SQPPGAPRAE GLPAAGTLHS 1500
AGGILAQVYS PNMPPPLAQP SSILPYALVS QPSVQLILQG TLPLAGCGTA QSLAPVPTMP 1560
ATVSELAVPT TNNSEERTAT PKTAAEKTKK EEYMKKLHMQ ERAVEEVKLA IKPFYQKREV 1620
TKEEYKDILR KAVQKICHSK SGEINPVKVA NLVKAYVDKY RHMRRHKKTE GGEEPPTQGA 1680
ET 1682 
Gene Ontology
 GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Compara. 
Interpro
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 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
 SM00109; C1
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS