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Database: UniProt
Entry: F8WEF5_HUMAN
LinkDB: F8WEF5_HUMAN
Original site: F8WEF5_HUMAN 
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
//
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