Full text data of PHF3
PHF3
(KIAA0244)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
PHD finger protein 3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
PHD finger protein 3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00170770
IPI00170770 PHD finger protein 3 ubiquitous, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00170770 PHD finger protein 3 ubiquitous, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q92576
ID PHF3_HUMAN Reviewed; 2039 AA.
AC Q92576; A3KFI8; Q14CR5; Q5CZI1; Q5T1T6; Q9NQ16; Q9UI45;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=PHD finger protein 3;
GN Name=PHF3; Synonyms=KIAA0244;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11856869;
RA Fischer U., Struss A.-K., Hemmer D., Michel A., Henn W.,
RA Steudel W.-I., Meese E.;
RT "PHF3 expression is frequently reduced in glioma.";
RL Cytogenet. Cell Genet. 94:131-136(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-299; SER-680;
RP SER-1133; SER-1178 AND SER-1642, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP STRUCTURE BY NMR OF 923-1029.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the TFIIS domain II of human PHD finger protein
RT 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92576-2; Sequence=VSP_026434;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is significantly
CC reduced or lost in glioblastomas, glioblastoma cell lines,
CC anaplastic astrocytomas, and astrocytomas.
CC -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC -!- SIMILARITY: Contains 1 TFIIS central domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13438.2; Type=Erroneous initiation;
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DR EMBL; AF091622; AAF21292.1; -; mRNA.
DR EMBL; D87685; BAA13438.2; ALT_INIT; mRNA.
DR EMBL; BX648268; CAI56715.1; -; mRNA.
DR EMBL; AL050329; CAM45842.1; -; Genomic_DNA.
DR EMBL; AL354719; CAM45842.1; JOINED; Genomic_DNA.
DR EMBL; BC113650; AAI13651.1; -; mRNA.
DR EMBL; BC113652; AAI13653.1; -; mRNA.
DR RefSeq; NP_055968.1; NM_015153.2.
DR RefSeq; XP_005248758.1; XM_005248701.1.
DR RefSeq; XP_005248759.1; XM_005248702.1.
DR UniGene; Hs.348921; -.
DR PDB; 2DME; NMR; -; A=923-1029.
DR PDBsum; 2DME; -.
DR ProteinModelPortal; Q92576; -.
DR SMR; Q92576; 723-774, 924-1029.
DR IntAct; Q92576; 3.
DR STRING; 9606.ENSP00000262043; -.
DR PhosphoSite; Q92576; -.
DR DMDM; 34098662; -.
DR PaxDb; Q92576; -.
DR PeptideAtlas; Q92576; -.
DR PRIDE; Q92576; -.
DR Ensembl; ENST00000262043; ENSP00000262043; ENSG00000118482.
DR Ensembl; ENST00000393387; ENSP00000377048; ENSG00000118482.
DR GeneID; 23469; -.
DR KEGG; hsa:23469; -.
DR UCSC; uc003pen.2; human.
DR CTD; 23469; -.
DR GeneCards; GC06P064403; -.
DR HGNC; HGNC:8921; PHF3.
DR HPA; HPA024676; -.
DR HPA; HPA025763; -.
DR MIM; 607789; gene.
DR neXtProt; NX_Q92576; -.
DR PharmGKB; PA33261; -.
DR eggNOG; NOG255142; -.
DR HOVERGEN; HBG039623; -.
DR InParanoid; Q92576; -.
DR OMA; QMPCSTV; -.
DR OrthoDB; EOG7NW685; -.
DR PhylomeDB; Q92576; -.
DR ChiTaRS; PHF3; human.
DR EvolutionaryTrace; Q92576; -.
DR GeneWiki; PHF3; -.
DR GenomeRNAi; 23469; -.
DR NextBio; 45797; -.
DR PRO; PR:Q92576; -.
DR ArrayExpress; Q92576; -.
DR Bgee; Q92576; -.
DR CleanEx; HS_PHF3; -.
DR Genevestigator; Q92576; -.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007275; P:multicellular organismal development; NAS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR017890; TFS2M.
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; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07744; SPOC; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00510; TFS2M; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 2039 PHD finger protein 3.
FT /FTId=PRO_0000059292.
FT DOMAIN 927 1046 TFIIS central.
FT ZN_FING 717 772 PHD-type.
FT COMPBIAS 1797 1865 Pro-rich.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 680 680 Phosphoserine.
FT MOD_RES 1133 1133 Phosphoserine.
FT MOD_RES 1148 1148 Phosphoserine.
FT MOD_RES 1178 1178 Phosphoserine.
FT MOD_RES 1642 1642 Phosphoserine.
FT VAR_SEQ 1 88 Missing (in isoform 2).
FT /FTId=VSP_026434.
FT VARIANT 525 525 V -> I (in dbSNP:rs34288820).
FT /FTId=VAR_051599.
FT VARIANT 1834 1834 H -> Y (in dbSNP:rs3734881).
FT /FTId=VAR_022040.
FT CONFLICT 1394 1394 E -> G (in Ref. 4; CAI56715).
FT HELIX 924 943
FT TURN 944 947
FT HELIX 952 970
FT HELIX 975 984
FT HELIX 986 989
FT STRAND 990 992
FT HELIX 996 1002
FT STRAND 1003 1005
FT HELIX 1009 1012
FT TURN 1015 1020
FT TURN 1024 1026
SQ SEQUENCE 2039 AA; 229481 MW; FDAFF00576005E9B CRC64;
MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSASQNV LEDSLKNMLS DKDPMLGSAS
NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND TIDEEELILP NRNLRDKVEE
NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS NAAPLSNTKK ASGKTVSTAK AGVKQPERSQ
VKEEVCMSLK PEYHKENRRC SRNSGQIEVV PEVSVSSSHS SVSSCLEMKD EDGLDSKHKC
NNPGEIDVPS HELNCSLLSE TCVTIGEKKN EALMECKAKP VGSPLFKFSD KEEHEQNDSI
SGKTGETVVE EMIATRKVEQ DSKETVKLSH EDDHILEDAG SSDISSDAAC TNPNKTENSL
VGLPSCVDEV TECNLELKDT MGIADKTENT LERNKIEPLG YCEDAESNRQ LESTEFNKSN
LEVVDTSTFG PESNILENAI CDVPDQNSKQ LNAIESTKIE SHETANLQDD RNSQSSSVSY
LESKSVKSKH TKPVIHSKQN MTTDAPKKIV AAKYEVIHSK TKVNVKSVKR NTDVPESQQN
FHRPVKVRKK QIDKEPKIQS CNSGVKSVKN QAHSVLKKTL QDQTLVQIFK PLTHSLSDKS
HAHPGCLKEP HHPAQTGHVS HSSQKQCHKP QQQAPAMKTN SHVKEELEHP GVEHFKEEDK
LKLKKPEKNL QPRQRRSSKS FSLDEPPLFI PDNIATIRRE GSDHSSSFES KYMWTPSKQC
GFCKKPHGNR FMVGCGRCDD WFHGDCVGLS LSQAQQMGEE DKEYVCVKCC AEEDKKTEIL
DPDTLENQAT VEFHSGDKTM ECEKLGLSKH TTNDRTKYID DTVKHKVKIL KRESGEGRNS
SDCRDNEIKK WQLAPLRKMG QPVLPRRSSE EKSEKIPKES TTVTCTGEKA SKPGTHEKQE
MKKKKVEKGV LNVHPAASAS KPSADQIRQS VRHSLKDILM KRLTDSNLKV PEEKAAKVAT
KIEKELFSFF RDTDAKYKNK YRSLMFNLKD PKNNILFKKV LKGEVTPDHL IRMSPEELAS
KELAAWRRRE NRHTIEMIEK EQREVERRPI TKITHKGEIE IESDAPMKEQ EAAMEIQEPA
ANKSLEKPEG SEKQKEEVDS MSKDTTSQHR QHLFDLNCKI CIGRMAPPVD DLSPKKVKVV
VGVARKHSDN EAESIADALS STSNILASEF FEEEKQESPK STFSPAPRPE MPGTVEVEST
FLARLNFIWK GFINMPSVAK FVTKAYPVSG SPEYLTEDLP DSIQVGGRIS PQTVWDYVEK
IKASGTKEIC VVRFTPVTEE DQISYTLLFA YFSSRKRYGV AANNMKQVKD MYLIPLGATD
KIPHPLVPFD GPGLELHRPN LLLGLIIRQK LKRQHSACAS TSHIAETPES APPIALPPDK
KSKIEVSTEE APEEENDFFN SFTTVLHKQR NKPQQNLQED LPTAVEPLME VTKQEPPKPL
RFLPGVLIGW ENQPTTLELA NKPLPVDDIL QSLLGTTGQV YDQAQSVMEQ NTVKEIPFLN
EQTNSKIEKT DNVEVTDGEN KEIKVKVDNI SESTDKSAEI ETSVVGSSSI SAGSLTSLSL
RGKPPDVSTE AFLTNLSIQS KQEETVESKE KTLKRQLQED QENNLQDNQT SNSSPCRSNV
GKGNIDGNVS CSENLVANTA RSPQFINLKR DPRQAAGRSQ PVTTSESKDG DSCRNGEKHM
LPGLSHNKEH LTEQINVEEK LCSAEKNSCV QQSDNLKVAQ NSPSVENIQT SQAEQAKPLQ
EDILMQNIET VHPFRRGSAV ATSHFEVGNT CPSEFPSKSI TFTSRSTSPR TSTNFSPMRP
QQPNLQHLKS SPPGFPFPGP PNFPPQSMFG FPPHLPPPLL PPPGFGFAQN PMVPWPPVVH
LPGQPQRMMG PLSQASRYIG PQNFYQVKDI RRPERRHSDP WGRQDQQQLD RPFNRGKGDR
QRFYSDSHHL KRERHEKEWE QESERHRRRD RSQDKDRDRK SREEGHKDKE RARLSHGDRG
TDGKASRDSR NVDKKPDKPK SEDYEKDKER EKSKHREGEK DRDRYHKDRD HTDRTKSKR
//
ID PHF3_HUMAN Reviewed; 2039 AA.
AC Q92576; A3KFI8; Q14CR5; Q5CZI1; Q5T1T6; Q9NQ16; Q9UI45;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=PHD finger protein 3;
GN Name=PHF3; Synonyms=KIAA0244;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11856869;
RA Fischer U., Struss A.-K., Hemmer D., Michel A., Henn W.,
RA Steudel W.-I., Meese E.;
RT "PHF3 expression is frequently reduced in glioma.";
RL Cytogenet. Cell Genet. 94:131-136(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-299; SER-680;
RP SER-1133; SER-1178 AND SER-1642, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP STRUCTURE BY NMR OF 923-1029.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the TFIIS domain II of human PHD finger protein
RT 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92576-2; Sequence=VSP_026434;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is significantly
CC reduced or lost in glioblastomas, glioblastoma cell lines,
CC anaplastic astrocytomas, and astrocytomas.
CC -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC -!- SIMILARITY: Contains 1 TFIIS central domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13438.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF091622; AAF21292.1; -; mRNA.
DR EMBL; D87685; BAA13438.2; ALT_INIT; mRNA.
DR EMBL; BX648268; CAI56715.1; -; mRNA.
DR EMBL; AL050329; CAM45842.1; -; Genomic_DNA.
DR EMBL; AL354719; CAM45842.1; JOINED; Genomic_DNA.
DR EMBL; BC113650; AAI13651.1; -; mRNA.
DR EMBL; BC113652; AAI13653.1; -; mRNA.
DR RefSeq; NP_055968.1; NM_015153.2.
DR RefSeq; XP_005248758.1; XM_005248701.1.
DR RefSeq; XP_005248759.1; XM_005248702.1.
DR UniGene; Hs.348921; -.
DR PDB; 2DME; NMR; -; A=923-1029.
DR PDBsum; 2DME; -.
DR ProteinModelPortal; Q92576; -.
DR SMR; Q92576; 723-774, 924-1029.
DR IntAct; Q92576; 3.
DR STRING; 9606.ENSP00000262043; -.
DR PhosphoSite; Q92576; -.
DR DMDM; 34098662; -.
DR PaxDb; Q92576; -.
DR PeptideAtlas; Q92576; -.
DR PRIDE; Q92576; -.
DR Ensembl; ENST00000262043; ENSP00000262043; ENSG00000118482.
DR Ensembl; ENST00000393387; ENSP00000377048; ENSG00000118482.
DR GeneID; 23469; -.
DR KEGG; hsa:23469; -.
DR UCSC; uc003pen.2; human.
DR CTD; 23469; -.
DR GeneCards; GC06P064403; -.
DR HGNC; HGNC:8921; PHF3.
DR HPA; HPA024676; -.
DR HPA; HPA025763; -.
DR MIM; 607789; gene.
DR neXtProt; NX_Q92576; -.
DR PharmGKB; PA33261; -.
DR eggNOG; NOG255142; -.
DR HOVERGEN; HBG039623; -.
DR InParanoid; Q92576; -.
DR OMA; QMPCSTV; -.
DR OrthoDB; EOG7NW685; -.
DR PhylomeDB; Q92576; -.
DR ChiTaRS; PHF3; human.
DR EvolutionaryTrace; Q92576; -.
DR GeneWiki; PHF3; -.
DR GenomeRNAi; 23469; -.
DR NextBio; 45797; -.
DR PRO; PR:Q92576; -.
DR ArrayExpress; Q92576; -.
DR Bgee; Q92576; -.
DR CleanEx; HS_PHF3; -.
DR Genevestigator; Q92576; -.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007275; P:multicellular organismal development; NAS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR017890; TFS2M.
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; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07744; SPOC; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00510; TFS2M; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 2039 PHD finger protein 3.
FT /FTId=PRO_0000059292.
FT DOMAIN 927 1046 TFIIS central.
FT ZN_FING 717 772 PHD-type.
FT COMPBIAS 1797 1865 Pro-rich.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 680 680 Phosphoserine.
FT MOD_RES 1133 1133 Phosphoserine.
FT MOD_RES 1148 1148 Phosphoserine.
FT MOD_RES 1178 1178 Phosphoserine.
FT MOD_RES 1642 1642 Phosphoserine.
FT VAR_SEQ 1 88 Missing (in isoform 2).
FT /FTId=VSP_026434.
FT VARIANT 525 525 V -> I (in dbSNP:rs34288820).
FT /FTId=VAR_051599.
FT VARIANT 1834 1834 H -> Y (in dbSNP:rs3734881).
FT /FTId=VAR_022040.
FT CONFLICT 1394 1394 E -> G (in Ref. 4; CAI56715).
FT HELIX 924 943
FT TURN 944 947
FT HELIX 952 970
FT HELIX 975 984
FT HELIX 986 989
FT STRAND 990 992
FT HELIX 996 1002
FT STRAND 1003 1005
FT HELIX 1009 1012
FT TURN 1015 1020
FT TURN 1024 1026
SQ SEQUENCE 2039 AA; 229481 MW; FDAFF00576005E9B CRC64;
MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSASQNV LEDSLKNMLS DKDPMLGSAS
NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND TIDEEELILP NRNLRDKVEE
NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS NAAPLSNTKK ASGKTVSTAK AGVKQPERSQ
VKEEVCMSLK PEYHKENRRC SRNSGQIEVV PEVSVSSSHS SVSSCLEMKD EDGLDSKHKC
NNPGEIDVPS HELNCSLLSE TCVTIGEKKN EALMECKAKP VGSPLFKFSD KEEHEQNDSI
SGKTGETVVE EMIATRKVEQ DSKETVKLSH EDDHILEDAG SSDISSDAAC TNPNKTENSL
VGLPSCVDEV TECNLELKDT MGIADKTENT LERNKIEPLG YCEDAESNRQ LESTEFNKSN
LEVVDTSTFG PESNILENAI CDVPDQNSKQ LNAIESTKIE SHETANLQDD RNSQSSSVSY
LESKSVKSKH TKPVIHSKQN MTTDAPKKIV AAKYEVIHSK TKVNVKSVKR NTDVPESQQN
FHRPVKVRKK QIDKEPKIQS CNSGVKSVKN QAHSVLKKTL QDQTLVQIFK PLTHSLSDKS
HAHPGCLKEP HHPAQTGHVS HSSQKQCHKP QQQAPAMKTN SHVKEELEHP GVEHFKEEDK
LKLKKPEKNL QPRQRRSSKS FSLDEPPLFI PDNIATIRRE GSDHSSSFES KYMWTPSKQC
GFCKKPHGNR FMVGCGRCDD WFHGDCVGLS LSQAQQMGEE DKEYVCVKCC AEEDKKTEIL
DPDTLENQAT VEFHSGDKTM ECEKLGLSKH TTNDRTKYID DTVKHKVKIL KRESGEGRNS
SDCRDNEIKK WQLAPLRKMG QPVLPRRSSE EKSEKIPKES TTVTCTGEKA SKPGTHEKQE
MKKKKVEKGV LNVHPAASAS KPSADQIRQS VRHSLKDILM KRLTDSNLKV PEEKAAKVAT
KIEKELFSFF RDTDAKYKNK YRSLMFNLKD PKNNILFKKV LKGEVTPDHL IRMSPEELAS
KELAAWRRRE NRHTIEMIEK EQREVERRPI TKITHKGEIE IESDAPMKEQ EAAMEIQEPA
ANKSLEKPEG SEKQKEEVDS MSKDTTSQHR QHLFDLNCKI CIGRMAPPVD DLSPKKVKVV
VGVARKHSDN EAESIADALS STSNILASEF FEEEKQESPK STFSPAPRPE MPGTVEVEST
FLARLNFIWK GFINMPSVAK FVTKAYPVSG SPEYLTEDLP DSIQVGGRIS PQTVWDYVEK
IKASGTKEIC VVRFTPVTEE DQISYTLLFA YFSSRKRYGV AANNMKQVKD MYLIPLGATD
KIPHPLVPFD GPGLELHRPN LLLGLIIRQK LKRQHSACAS TSHIAETPES APPIALPPDK
KSKIEVSTEE APEEENDFFN SFTTVLHKQR NKPQQNLQED LPTAVEPLME VTKQEPPKPL
RFLPGVLIGW ENQPTTLELA NKPLPVDDIL QSLLGTTGQV YDQAQSVMEQ NTVKEIPFLN
EQTNSKIEKT DNVEVTDGEN KEIKVKVDNI SESTDKSAEI ETSVVGSSSI SAGSLTSLSL
RGKPPDVSTE AFLTNLSIQS KQEETVESKE KTLKRQLQED QENNLQDNQT SNSSPCRSNV
GKGNIDGNVS CSENLVANTA RSPQFINLKR DPRQAAGRSQ PVTTSESKDG DSCRNGEKHM
LPGLSHNKEH LTEQINVEEK LCSAEKNSCV QQSDNLKVAQ NSPSVENIQT SQAEQAKPLQ
EDILMQNIET VHPFRRGSAV ATSHFEVGNT CPSEFPSKSI TFTSRSTSPR TSTNFSPMRP
QQPNLQHLKS SPPGFPFPGP PNFPPQSMFG FPPHLPPPLL PPPGFGFAQN PMVPWPPVVH
LPGQPQRMMG PLSQASRYIG PQNFYQVKDI RRPERRHSDP WGRQDQQQLD RPFNRGKGDR
QRFYSDSHHL KRERHEKEWE QESERHRRRD RSQDKDRDRK SREEGHKDKE RARLSHGDRG
TDGKASRDSR NVDKKPDKPK SEDYEKDKER EKSKHREGEK DRDRYHKDRD HTDRTKSKR
//
MIM
607789
*RECORD*
*FIELD* NO
607789
*FIELD* TI
*607789 PHD FINGER PROTEIN 3; PHF3
;;KIAA0244
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid
read morecell line cDNA library, Nagase et al. (1996) cloned a partial cDNA
encoding PHF3, which they designated KIAA0244. Northern blot analysis
revealed ubiquitous low-level expression.
By immunologically screening a glioblastoma cDNA library using patient
serum, followed by 5-prime RACE, Fischer et al. (2001) cloned PHF3. The
deduced full-length protein contains 2,039 amino acids and has a PHD
finger motif, a TFIIS (601425) domain, a proline-rich region, and 2
bipartite nuclear localization signals. Northern blot analysis detected
a 7.5-kb transcript in all tissues examined. Expression was
significantly reduced or lost in glioblastomas, glioblastoma cell lines,
anaplastic astrocytomas, and astrocytomas.
MAPPING
By radiation hybrid analysis, Nagase et al. (1996) mapped the PHF3 gene
to chromosome 6. Using FISH, Fischer et al. (2001) mapped the PHF3 gene
to chromosome 6q12.
*FIELD* RF
1. Fischer, U.; Struss, A.-K.; Hemmer, D.; Michel, A.; Henn, W.; Steudel,
W.-I.; Meese, E.: PHF3 expression is frequently reduced in glioma. Cytogenet.
Cell Genet. 94: 131-136, 2001.
2. Nagase, T.; Seki, N.; Ishikawa, K.; Ohira, M.; Kawarabayasi, Y.;
Ohara, O.; Tanaka, A.; Kotani, H.; Miyajima, N.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. VI. The coding
sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis
of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329,
1996.
*FIELD* CD
Patricia A. Hartz: 5/14/2003
*FIELD* ED
mgross: 05/14/2003
*RECORD*
*FIELD* NO
607789
*FIELD* TI
*607789 PHD FINGER PROTEIN 3; PHF3
;;KIAA0244
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid
read morecell line cDNA library, Nagase et al. (1996) cloned a partial cDNA
encoding PHF3, which they designated KIAA0244. Northern blot analysis
revealed ubiquitous low-level expression.
By immunologically screening a glioblastoma cDNA library using patient
serum, followed by 5-prime RACE, Fischer et al. (2001) cloned PHF3. The
deduced full-length protein contains 2,039 amino acids and has a PHD
finger motif, a TFIIS (601425) domain, a proline-rich region, and 2
bipartite nuclear localization signals. Northern blot analysis detected
a 7.5-kb transcript in all tissues examined. Expression was
significantly reduced or lost in glioblastomas, glioblastoma cell lines,
anaplastic astrocytomas, and astrocytomas.
MAPPING
By radiation hybrid analysis, Nagase et al. (1996) mapped the PHF3 gene
to chromosome 6. Using FISH, Fischer et al. (2001) mapped the PHF3 gene
to chromosome 6q12.
*FIELD* RF
1. Fischer, U.; Struss, A.-K.; Hemmer, D.; Michel, A.; Henn, W.; Steudel,
W.-I.; Meese, E.: PHF3 expression is frequently reduced in glioma. Cytogenet.
Cell Genet. 94: 131-136, 2001.
2. Nagase, T.; Seki, N.; Ishikawa, K.; Ohira, M.; Kawarabayasi, Y.;
Ohara, O.; Tanaka, A.; Kotani, H.; Miyajima, N.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. VI. The coding
sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis
of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329,
1996.
*FIELD* CD
Patricia A. Hartz: 5/14/2003
*FIELD* ED
mgross: 05/14/2003