PHRF1_RAT
ID PHRF1_RAT Reviewed; 1685 AA.
AC Q63625;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=PHD and RING finger domain-containing protein 1 {ECO:0000250|UniProtKB:Q9P1Y6};
DE AltName: Full=CTD-binding SR-like protein rA9 {ECO:0000303|PubMed:8692929};
GN Name=Phrf1 {ECO:0000250|UniProtKB:Q9P1Y6};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC52658.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH POLR2A.
RC TISSUE=Hippocampus {ECO:0000312|EMBL:AAC52658.1};
RX PubMed=8692929; DOI=10.1073/pnas.93.14.6975;
RA Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M.,
RA Corden J.L.;
RT "The C-terminal domain of the largest subunit of RNA polymerase II
RT interacts with a novel set of serine/arginine-rich proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-460; SER-870;
RP SER-922 AND SER-1205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Interacts with POLR2A (via the C-terminal domain).
CC {ECO:0000269|PubMed:8692929}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q63625-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8692929};
CC IsoId=Q63625-2; Sequence=VSP_052981, VSP_052982;
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DR EMBL; U49057; AAC52658.1; -; mRNA.
DR EMBL; AC118351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T31422; T31422.
DR RefSeq; NP_620793.1; NM_139093.1.
DR RefSeq; XP_006230576.1; XM_006230514.3. [Q63625-1]
DR AlphaFoldDB; Q63625; -.
DR SMR; Q63625; -.
DR STRING; 10116.ENSRNOP00000046880; -.
DR iPTMnet; Q63625; -.
DR PhosphoSitePlus; Q63625; -.
DR PaxDb; Q63625; -.
DR PRIDE; Q63625; -.
DR Ensembl; ENSRNOT00000023376; ENSRNOP00000023376; ENSRNOG00000017299. [Q63625-2]
DR GeneID; 245925; -.
DR KEGG; rno:245925; -.
DR UCSC; RGD:708360; rat. [Q63625-1]
DR CTD; 57661; -.
DR RGD; 708360; Phrf1.
DR VEuPathDB; HostDB:ENSRNOG00000017299; -.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR HOGENOM; CLU_003222_0_0_1; -.
DR InParanoid; Q63625; -.
DR OMA; GHIFEDF; -.
DR OrthoDB; 210024at2759; -.
DR PhylomeDB; Q63625; -.
DR TreeFam; TF332183; -.
DR PRO; PR:Q63625; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017299; Expressed in thymus and 19 other tissues.
DR Genevisible; Q63625; RN.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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..1685
FT /note="PHD and RING finger domain-containing protein 1"
FT /id="PRO_0000354663"
FT ZN_FING 109..150
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 188..238
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1589..1615
FT /evidence="ECO:0000255"
FT COMPBIAS 44..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..386
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1027
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 849
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 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1002
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 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT MOD_RES 1416
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y6"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8692929"
FT /id="VSP_052981"
FT VAR_SEQ 213..244
FT /note="YHMECLDPPLQEVPVDEWFCPECAVPGVDPTH -> MRRLKRKTRPFVKCVA
FT GVIVRTGSYFVTAVML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8692929"
FT /id="VSP_052982"
FT CONFLICT 615
FT /note="T -> S (in Ref. 1; AAC52658)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="Q -> P (in Ref. 1; AAC52658)"
FT /evidence="ECO:0000305"
FT CONFLICT 855..856
FT /note="SG -> PD (in Ref. 1; AAC52658)"
FT /evidence="ECO:0000305"
FT CONFLICT 1549
FT /note="S -> G (in Ref. 1; AAC52658)"
FT /evidence="ECO:0000305"
FT CONFLICT 1592
FT /note="K -> T (in Ref. 1; AAC52658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1685 AA; 184214 MW; 54D4ACFA2FD8BAC2 CRC64;
MDDDNLDELV AHSPGPDGPP QVGSSELASD AEESSNGHSE DSEDDTGSEQ DDDTDGEETE
GLSEEEDPED RSGSEDSEDG IEVPTAAVET QRKLEASSTP NSDDDAESCP ICLNAFRDQA
VGTPETCAHY FCLDCIIEWS RNANSCPVDR TIFKCICIRA QFNGKILKKI PVENTRACED
EEAEEEDPTF CEVCGRSDRE DRLLLCDGCD AGYHMECLDP PLQEVPVDEW FCPECAVPGV
DPTHDAAPVS DEEVSLLLAD VVPTTSRLRP RVGRTRAIAR TRQSERVRAT VNRNRISSAR
RVQHVPRYLM SSLLDETIEA VATGLSTAVY QRPLTPRVPA KRKRKAGRRK KVLGRKKTRS
RSSVKSKSGG TRAKKRQHRV RRTKGRKLKN EVTARSRIAR TLGLRRPVRG TSMPSVYKPV
DPSLGLMRAD IGAASLSLFG DPYALDPFDS NGEQSADPPS PLSAKRRVLS RSALQSHQPV
ARPVAMGLAR RQLPAVAPEP SVEEAPVPDL LGSILCGQSL LMMSSADVVI HRDGSLSAKR
AAPVSLQRNS VTQSREESRL RDNLQPGALP SESVSGGLIG DRRPNSGLSC GDRTALRCLP
AQIVQTPVRS DSSVTPRSGL SGNLSDESRP KWKHSNSPRL NGSNVRVGSA STKTMTHSNF
PSKNIAPGHP QKTDPRRPDF SKLPRIPKIR RDGSNSTQDQ APASGQTVEL PSACISRLTG
REGPGQPGRG RADSEPSSRG PQETGSHTSG SRPPAPSSHG NLAPLGPSRG KGIGSSFESF
RINIPGNTAH CSQLSSPGFC NTFRPVDSKV QRKENPSPLF SIKKPKQLKS EIYDPFDPTG
SDSSPPSSSP ESLGSGLLPS EITRTISINS PKAPAFQTVR CVTSYRVESV FGTEMDPDPQ
PPGEPVSGML ELLGKGPAEG ASDLEQEGLG EIEPTEIQGS SARAQRPSPP DPWDDEDGVS
CTPFFGSEER TVTCVTVEEP SVPSPDAPQI TTHRIVEFRA SSRSRSTSSS RSRKKTKKKK
KVAREHQRTR SSTRSGSRDR TSRSVSPFTE EHTKRHRAKT KSRRSSSDRA SSQDRAKRRK
DRDREHRRGP WGHGRCWRKS RSRSGSPGSS SCERHESRRR KRRHSGSRSR GRDGSPHSSL
ERDRRHKHRE RSRERMDKKE SMTRSRERRR WRSRSPSVEH RTRRPHSREK HPHSPEKKGA
VREVSPAPAP QGEPRQDGDH STKPPVSEVS VLPEVVSVLP EVVVADLNPP EVPPVLAESV
SCVPEDLDYG DSVEAGHVFE DFSNEAIFIQ LDDMSSPPSP ESTDSSPERD FLPNPILPPA
SLPQNSTLPV TQREVLPIHS EDISKPAPQP LAPSDQCLLR QDTVETTATT LSTPGVLPMG
KDSPLLSGRG CEVVRPKDAV APAPLLRSRT LVKRVTWNLQ EAEASTPALD RDPRTPLQRP
QRPQEGDWDA EDRALIGFQQ APFSELPPPI HVLQESGLPD ADPSQPPGVP RAEGPPAVGT
LHSAGGILAQ VYSPNMPPPL AQPSSIPPYA LVNQPSVQLI LQGTLPLASC GAAQNLAPVP
TMPATASELA VPTTNNSEER TATPKTAAEK TKKEEYMKKL HMQERAVEEV KLAIKPFYQK
REVTKEEYKD ILRKAVQKIC HSKSGEINPV KVANLVKAYV DKYRHMRKHK KTEAGEEPPT
QGAET
