PHRF1_MOUSE
ID PHRF1_MOUSE Reviewed; 1682 AA.
AC A6H619; Q505G1; Q6ZPN4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PHD and RING finger domain-containing protein 1 {ECO:0000312|MGI:MGI:2141847};
GN Name=Phrf1 {ECO:0000312|MGI:MGI:2141847}; Synonyms=Kiaa1542;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI38447.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 468-1682 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH94566.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH94566.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC98197.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1430 (ISOFORMS 1/2).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC98197.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Interacts with POLR2A (via the C-terminal domain).
CC {ECO:0000250|UniProtKB:Q63625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=A6H619-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=A6H619-2; Sequence=VSP_052978, VSP_052979;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98197.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AC108908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094566; AAH94566.1; -; mRNA.
DR EMBL; BC138446; AAI38447.1; -; mRNA.
DR EMBL; BC145719; AAI45720.1; -; mRNA.
DR EMBL; AK129387; BAC98197.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS52441.1; -. [A6H619-1]
DR RefSeq; NP_001074587.1; NM_001081118.1. [A6H619-1]
DR AlphaFoldDB; A6H619; -.
DR SMR; A6H619; -.
DR IntAct; A6H619; 1.
DR STRING; 10090.ENSMUSP00000101648; -.
DR iPTMnet; A6H619; -.
DR PhosphoSitePlus; A6H619; -.
DR EPD; A6H619; -.
DR jPOST; A6H619; -.
DR MaxQB; A6H619; -.
DR PaxDb; A6H619; -.
DR PeptideAtlas; A6H619; -.
DR PRIDE; A6H619; -.
DR ProteomicsDB; 289744; -. [A6H619-1]
DR ProteomicsDB; 289745; -. [A6H619-2]
DR Antibodypedia; 5345; 22 antibodies from 10 providers.
DR Ensembl; ENSMUST00000106027; ENSMUSP00000101648; ENSMUSG00000038611. [A6H619-1]
DR Ensembl; ENSMUST00000122143; ENSMUSP00000113195; ENSMUSG00000038611. [A6H619-2]
DR GeneID; 101471; -.
DR KEGG; mmu:101471; -.
DR UCSC; uc009kkb.1; mouse. [A6H619-1]
DR UCSC; uc009kkc.1; mouse. [A6H619-2]
DR CTD; 57661; -.
DR MGI; MGI:2141847; Phrf1.
DR VEuPathDB; HostDB:ENSMUSG00000038611; -.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR HOGENOM; CLU_003222_0_0_1; -.
DR InParanoid; A6H619; -.
DR OMA; GHIFEDF; -.
DR OrthoDB; 210024at2759; -.
DR PhylomeDB; A6H619; -.
DR TreeFam; TF332183; -.
DR BioGRID-ORCS; 101471; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Phrf1; mouse.
DR PRO; PR:A6H619; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; A6H619; protein.
DR Bgee; ENSMUSG00000038611; Expressed in manus and 212 other tissues.
DR ExpressionAtlas; A6H619; baseline and differential.
DR Genevisible; A6H619; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1682
FT /note="PHD and RING finger domain-containing protein 1"
FT /id="PRO_0000354662"
FT ZN_FING 109..150
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 185..235
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1585..1612
FT /evidence="ECO:0000255"
FT COMPBIAS 28..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..383
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1026
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63625"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052978"
FT VAR_SEQ 160..169
FT /note="AQFNGKILKK -> MFTDQYFCLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052979"
SQ SEQUENCE 1682 AA; 184081 MW; 97F5B67545D7A105 CRC64;
MDDDNLDELV AHSPGPDGPP RVGSSELASD AEESSNGQSG DSEDDTGSEQ DDDTDGEETE
GLSEEEDPED RSGSEDSEDG VEMATAAIET QGKLEASSVP NSDDDAESCP ICLNAFRDQA
VGTPETCAHY FCLDCIIEWS RNANSCPVDR TVFKCICIRA QFNGKILKKI PVENTKACEA
EEEDPTFCEV CGRSDREDRL LLCDGCDAGY HMECLDPPLQ EVPVDEWFCP ECTVPGVDPT
HDAAPVSDEE VSLLLADVVP TTSRLRPRVG RTRAIARTRQ SERVRATVNR NRISSARRVQ
HVPRYLMSSL LDETIEAVAT GLSTAVYQRP LTPRVPAKRK RKAGRRKKVL GRKKTRSRSS
VKSKSGSTRA KKRQHRVRKT KGRKLKNEVT ARSRIARTLG LRRPVRGTSM PSVYKPVDPS
LGLMRADIGA ASLSLFGDPY ELDPFDSNEE QSADPPSPLS AKRRVLSRSA LQSHQPVARP
VAMGLSRRQL PAVAPEPSVE EAPVPDLLGS ILSGQSLLMM SSADVVIHRD GSLSAKRAAP
VSLQRNSVTQ SREESRLRDN PQPGALPSES ASGGFVGDRQ PNSGLSCGNR TALCCLPARI
AQTPVRSDPS LTPRSGLSRT LSDENRPSRT HSSSPQLNGS NVRVSSASTK IVTHSSFPSK
NTASGLPQRT GPRRPDFSKL PRIPKIHRDG NKSTQDQAPA SGHIVELPST CISRLTGREG
PGQPGRGRVD SEPSSRGPQE TGSHTSGSRP PAPSSHGSLA HLGPSRGKGI GSSFESFRIN
IPGNTAHCSQ LSSPGFCNTF RPVDSKVQRK ETPFPLFSIK KPKQLKSEIY DPFDPTGSDS
SPPSSSPESL GPGLLPSEIT RTISINSPKA PAFQTVRCVT SYRVESIFGT EMEPEPQPPS
EPVSGMLELL SKGSAEGTSD LEQEGLGEIE PTEIRGSTAR TQRPPPPDPW DDEDEVSCTP
FFGSEERTVT CVTVEEPGVL PSPDAPQITT HRIVEFRASS RSRSTSSSRS RKKTKKKKKK
VAREHQRTRS STRSGSRDRT SRSVSPVAEE HTRRHRAKTK SRRSSSDRAS SQDRAKRRKD
RDDRDREHRR GSWGHGRCRR KSRSRSGSPG SSSCERHESK RRKRRHSGSR SRGSSLERDR
RHKHRERSRE RMDKQESVTR SRERRRWRSR SPSLEHRPRR PPSREKRAHS PEKKGPVREV
SPAPATQGES RQDGDHSAEP PVSEVSVLPE VVSVLPEVVV ADLNPPEVPP VLAEPVAHVP
EDLDYGESVE AGHVFEDFSN EAIFIQLDDM SSPPSPESTD SSPERDFPPN PILPPASLPQ
DSTLPTIQRE VLPIHSEDIS KPVPQALAPS DQSLLKQDTV EITTTTPSTP AVVPMTKDSP
VLSARGWEAV RPRDAVAQAP LLRSRTLVKR VTWNLQEAEH STPAALDRDP RTPLQRPQRP
QEGDWDAEDR ALIGFQQAPF SELPPPIHVL QESGLPDADP SQPPGAPRAE GLPAAGTLHS
AGGILAQVYS PNMPPPLAQP SSILPYALVS QPSVQLILQG TLPLAGCGTA QSLAPVPTMP
ATVSELAVPT TNNSEERTAT PKTAAEKTKK EEYMKKLHMQ ERAVEEVKLA IKPFYQKREV
TKEEYKDILR KAVQKICHSK SGEINPVKVA NLVKAYVDKY RHMRRHKKTE GGEEPPTQGA
ET
