PHF23_MOUSE
ID PHF23_MOUSE Reviewed; 401 AA.
AC Q8BSN5; Q3TCH1; Q8BT31; Q8CDY2; Q8CIA4; Q8CIU8; Q8CIU9; Q9CWC8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PHD finger protein 23 {ECO:0000250|UniProtKB:Q9BUL5};
DE AltName: Full=PDH-containing protein JUNE-1 {ECO:0000303|Ref.1};
GN Name=Phf23 {ECO:0000250|UniProtKB:Q9BUL5};
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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen;
RA Yuan Z.Q., McCann T., Lappin T.R.J.;
RT "Identification of JUNE-1, a novel gene encoding a PHD-containing
RT protein.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Forelimb, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Acts as a negative regulator of autophagy, through promoting
CC ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that
CC promotes autophagy in response to starvation or infecting bacteria.
CC {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- SUBUNIT: Interacts with LRSAM1. {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUL5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BUL5}. Note=Mainly present in the nucleus and
CC part in the cytoplasm. {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BSN5-1; Sequence=Displayed;
CC Name=2; Synonyms=JUNE1A;
CC IsoId=Q8BSN5-2; Sequence=VSP_027965;
CC Name=3;
CC IsoId=Q8BSN5-3; Sequence=VSP_027964;
CC -!- DOMAIN: The PHD-type zinc-finger domain is required for interaction
CC with LRSAM1 and negative regulation of autophagy.
CC {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- SIMILARITY: Belongs to the PHF23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25679.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY099326; AAM44127.1; -; mRNA.
DR EMBL; AY099327; AAM44128.1; -; mRNA.
DR EMBL; AK019135; BAB31562.1; -; mRNA.
DR EMBL; AK027950; BAC25679.1; ALT_INIT; mRNA.
DR EMBL; AK029376; BAC26426.1; -; mRNA.
DR EMBL; AK031159; BAC27285.1; -; mRNA.
DR EMBL; AK170729; BAE41985.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033533; AAH33533.1; ALT_INIT; mRNA.
DR CCDS; CCDS24929.1; -. [Q8BSN5-1]
DR CCDS; CCDS70223.1; -. [Q8BSN5-2]
DR CCDS; CCDS78976.1; -. [Q8BSN5-3]
DR RefSeq; NP_001278054.1; NM_001291125.1. [Q8BSN5-2]
DR RefSeq; NP_001278055.1; NM_001291126.1. [Q8BSN5-3]
DR RefSeq; NP_001278056.1; NM_001291127.1. [Q8BSN5-3]
DR RefSeq; NP_084340.2; NM_030064.4. [Q8BSN5-1]
DR RefSeq; XP_006534565.2; XM_006534502.2. [Q8BSN5-3]
DR AlphaFoldDB; Q8BSN5; -.
DR SMR; Q8BSN5; -.
DR STRING; 10090.ENSMUSP00000018716; -.
DR iPTMnet; Q8BSN5; -.
DR PhosphoSitePlus; Q8BSN5; -.
DR EPD; Q8BSN5; -.
DR jPOST; Q8BSN5; -.
DR MaxQB; Q8BSN5; -.
DR PaxDb; Q8BSN5; -.
DR PeptideAtlas; Q8BSN5; -.
DR PRIDE; Q8BSN5; -.
DR ProteomicsDB; 287700; -. [Q8BSN5-1]
DR ProteomicsDB; 287701; -. [Q8BSN5-2]
DR ProteomicsDB; 287702; -. [Q8BSN5-3]
DR Antibodypedia; 23960; 58 antibodies from 14 providers.
DR Ensembl; ENSMUST00000018716; ENSMUSP00000018716; ENSMUSG00000018572. [Q8BSN5-1]
DR Ensembl; ENSMUST00000101526; ENSMUSP00000099064; ENSMUSG00000018572. [Q8BSN5-2]
DR Ensembl; ENSMUST00000133485; ENSMUSP00000117373; ENSMUSG00000018572. [Q8BSN5-3]
DR Ensembl; ENSMUST00000135814; ENSMUSP00000120665; ENSMUSG00000018572. [Q8BSN5-3]
DR Ensembl; ENSMUST00000153684; ENSMUSP00000121780; ENSMUSG00000018572. [Q8BSN5-3]
DR GeneID; 78246; -.
DR KEGG; mmu:78246; -.
DR UCSC; uc007jth.3; mouse. [Q8BSN5-1]
DR UCSC; uc007jti.3; mouse. [Q8BSN5-2]
DR CTD; 79142; -.
DR MGI; MGI:1925496; Phf23.
DR VEuPathDB; HostDB:ENSMUSG00000018572; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00530000063882; -.
DR HOGENOM; CLU_047981_1_0_1; -.
DR InParanoid; Q8BSN5; -.
DR OMA; SGHKKDP; -.
DR OrthoDB; 982722at2759; -.
DR PhylomeDB; Q8BSN5; -.
DR TreeFam; TF331373; -.
DR BioGRID-ORCS; 78246; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Phf23; mouse.
DR PRO; PR:Q8BSN5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BSN5; protein.
DR Bgee; ENSMUSG00000018572; Expressed in embryonic brain and 265 other tissues.
DR ExpressionAtlas; Q8BSN5; baseline and differential.
DR Genevisible; Q8BSN5; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISS:GO_Central.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; ISS:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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 SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Autophagy; Cytoplasm; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..401
FT /note="PHD finger protein 23"
FT /id="PRO_0000302831"
FT ZN_FING 337..385
FT /note="PHD-type"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027964"
FT VAR_SEQ 54..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_027965"
FT CONFLICT 9
FT /note="S -> R (in Ref. 2; BAB31562)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="L -> P (in Ref. 2; BAC27285)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="C -> Y (in Ref. 2; BAC27285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43547 MW; 831B8984C13F554F CRC64;
MLEAMAEPSP EDPPPTLKPE TQPPEKRRRT IEDFNKFCSF VLAYAGYIPP SKEESDWPAS
GSSSPLRGES AADSDGWDSA PSDLRTIQTF VKKAKSSKRR AVQSGPTQPG PPRSTFSRLQ
APDSATLLEK MKLKDSLFDL DGPKVASPLS PTSLTHTSRP PAALAPVPLS QGDLSQPRKK
DRKNRKLGPG GGAGFGVLRR PRPAPGDGEK RSRIKKSKKR KLKKADRGDR LPPPGPPRAP
PSDTDSEEEE EEEEEEDDEE EMTVGGGVPA PVLPTPPEAP RPPVTVHSEG APPTDSEGKD
VGSTETSQDG DASSSEGEMR VMDEDIMVES GDDSWDLITC YCRKPFAGRP MIECSLCGTW
IHLSCAKIKK TNVPDFFYCQ KCKELRPEAR RLGGLPKSGE P
