ID F8WEF5_HUMAN Unreviewed; 1647 AA.
AC F8WEF5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=PHD and ring finger domains 1 {ECO:0000313|Ensembl:ENSP00000388589.2};
GN Name=PHRF1 {ECO:0000313|Ensembl:ENSP00000388589.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000388589.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000388589.2, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4] {ECO:0007829|PubMed:19413330}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10] {ECO:0000313|Ensembl:ENSP00000388589.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AP006284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001273511.1; NM_001286582.1.
DR SMR; F8WEF5; -.
DR MassIVE; F8WEF5; -.
DR MaxQB; F8WEF5; -.
DR PeptideAtlas; F8WEF5; -.
DR ProteomicsDB; 31823; -.
DR Antibodypedia; 5345; 27 antibodies from 11 providers.
DR DNASU; 57661; -.
DR Ensembl; ENST00000413872.6; ENSP00000388589.2; ENSG00000070047.13.
DR GeneID; 57661; -.
DR UCSC; uc010qwd.4; human.
DR CTD; 57661; -.
DR HGNC; HGNC:24351; PHRF1.
DR VEuPathDB; HostDB:ENSG00000070047; -.
DR GeneTree; ENSGT00950000183205; -.
DR OrthoDB; 2912044at2759; -.
DR BioGRID-ORCS; 57661; 15 hits in 1193 CRISPR screens.
DR ChiTaRS; PHRF1; human.
DR GenomeRNAi; 57661; -.
DR Proteomes; UP000005640; Chromosome 11.
DR Bgee; ENSG00000070047; Expressed in sural nerve and 96 other cell types or tissues.
DR ExpressionAtlas; F8WEF5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR CDD; cd16635; mRING-HC-C3HC3D_PHRF1; 1.
DR CDD; cd15536; PHD_PHRF1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR047157; PHRF1-like.
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 PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
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; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:F8WEF5,
KW ECO:0007829|MaxQB:F8WEF5};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 107..148
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 182..232
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..350
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1013
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1084
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 178450 MW; F2089FFC6FA0265F CRC64;
MDDDSLDELV ARSPGPDGHP QVGPADPAGD FESSVGSSGD SGDDSDSEHG DGTDGEDEGA
SEEEDLEDRS GSEDSEDDGE TLLEVAGTQG KLEAAGSFNS DDDAESCPIC LNAFRDQAVG
TPENCAHYFC LDCIVEWSKN ANSCPVDRTL FKCICIRAQF GGKILRKIPV ENTKASEEEE
DPTFCEVCGR SDREDRLLLC DGCDAGYHME CLDPPLQEVP VDEWFCPECA APGVVLAADA
GPVSEEEVSL LLADVVPTTS RLRPRAGRTR AIARTRQSER VRATVNRNRI STARRVQHTP
GRLGSSLLDE AIEAVATGLS TAVYQRPLTP RTPARRKRKT RRRKKVPGRK KTPSGPSAKS
KSSATRSKKR QHRVKKRRGK KVKSEATTRS RIARTLGLRR PVHSSCIPSV LKPVEPSLGL
LRADIGAASL SLFGDPYELD PFDSEELSAN PLSPLSAKRR ALSRSALQSH QPVARPVSVG
LSRRRLPAAV PEPDLEEEPV PDLLGSILSG QSLLMLGSSD VIIHRDGSLS AKRAAPVSFQ
RNSGSLSRGE EGFKGCLQPR ALPSGSPAQG PSGNRPQSTG LSCQGRSRTP ARTAGAPVRL
DLPAAPGAVQ ARNLSNGSVP GFRQSHSPWF NGTNKHTLPL ASAASKISSR DSKPPCRSVV
PGPPLKPAPR RTDISELPRI PKIRRDDGGG RRDAAPAHGQ SIEIPSACIS RLTGREGTGQ
PGRGTRAESE ASSRVPREPG VHTGSSRPPA PSSHGSLAPL GPSRGKGVGS TFESFRINIP
GNMAHSSQLS SPGFCNTFRP VDDKEQRKEN PSPLFSIKKT KQLRSEVYDP SDPTGSDSSA
PGSSPERSGP GLLPSEITRT ISINSPKAQT VQAVRCVTSY TVESIFGTEP EPPLGPSSAM
SKLRGAVAAE GASDTEREEP TESQGLAARL RRPSPPEPWD EEDGASCSTF FGSEERTVTC
VTVVEPEAPP SPDVLQAATH RVVELRPPSR SRSTSSSRSR KKAKRKRVSR EHGRTRSGTR
SESRDRSSRS ASPSVGEERP RRQRSKAKSR RSSSDRSSSR ERAKRKKAKD KSREHRRGPW
GHSRRTSRSR SGSPGSSSYE HYESRKKKKR RSASRPRGRE CSPTSSLERL CRHKHQRERS
HERPDRKESV AWPRDRRKRR SRSPSSEHRA REHRRPRSRE KWPQTRSHSP ERKGAVREAS
PAPLAQGEPG REDLPTRLPA LGEAHVSPEV ATADKAPLQA PPVLEVAAEC EPDDLDLDYG
DSVEAGHVFD DFSSDAVFIQ LDDMSSPPSP ESTDSSPERD FPLKPALPPA SLAVAAIQRE
VSLMHDEDPS QPPPLPEGTQ EPHLLRPDAA EKAEAPSSPD VAPAGKEDSP SASGRVQEAA
RPEEVVSQTP LLRSRALVKR VTWNLQESES SAPAEDRAPR APLHRPQKPR EGAWDMEDVA
PTGVRQVFSE LPFPSHVLPE PGFPDTDPSQ VYSPGLPPAP AQPSSIPPCA LVSQPTVQFI
LQGSLPLVGC GAAQTLAPVP AALTPASEPA SQATAASNSE EKTPAPRLAA EKTKKEEYMK
KLHMQERAVE EVKLAIKPFY QKREVTKEEY KDILRKAVQK ICHSKSGEIN PVKVANLVKA
YVDKYRHMRR HKKPEAGEEP PTQGAEG
//