ZNF48_MOUSE
ID ZNF48_MOUSE Reviewed; 591 AA.
AC Q3US17; Q3UFP3; Q8R0V0; Q921H7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein 48;
DE AltName: Full=Zinc finger protein 553;
GN Name=Znf48; Synonyms=Zfp48, Zfp553, Znf553;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Head, and Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and 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).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK049208; BAC33610.1; -; mRNA.
DR EMBL; AK140924; BAE24520.1; -; mRNA.
DR EMBL; AK146581; BAE27277.1; -; mRNA.
DR EMBL; AK148378; BAE28517.1; -; mRNA.
DR EMBL; BC012403; AAH12403.1; ALT_INIT; mRNA.
DR EMBL; BC026401; AAH26401.1; -; mRNA.
DR CCDS; CCDS21860.1; -.
DR RefSeq; NP_666313.1; NM_146201.1.
DR RefSeq; XP_006507802.1; XM_006507739.1.
DR AlphaFoldDB; Q3US17; -.
DR SMR; Q3US17; -.
DR BioGRID; 231466; 1.
DR STRING; 10090.ENSMUSP00000101919; -.
DR iPTMnet; Q3US17; -.
DR PhosphoSitePlus; Q3US17; -.
DR EPD; Q3US17; -.
DR jPOST; Q3US17; -.
DR MaxQB; Q3US17; -.
DR PaxDb; Q3US17; -.
DR PeptideAtlas; Q3US17; -.
DR PRIDE; Q3US17; -.
DR ProteomicsDB; 299605; -.
DR Antibodypedia; 13692; 32 antibodies from 15 providers.
DR DNASU; 233887; -.
DR Ensembl; ENSMUST00000056232; ENSMUSP00000060967; ENSMUSG00000045598.
DR Ensembl; ENSMUST00000106312; ENSMUSP00000101919; ENSMUSG00000045598.
DR GeneID; 233887; -.
DR KEGG; mmu:233887; -.
DR UCSC; uc009jur.1; mouse.
DR CTD; 233887; -.
DR MGI; MGI:2384725; Zfp553.
DR VEuPathDB; HostDB:ENSMUSG00000045598; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162332; -.
DR HOGENOM; CLU_452421_0_0_1; -.
DR InParanoid; Q3US17; -.
DR OMA; QTWDDLW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3US17; -.
DR TreeFam; TF338489; -.
DR BioGRID-ORCS; 233887; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp553; mouse.
DR PRO; PR:Q3US17; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3US17; protein.
DR Bgee; ENSMUSG00000045598; Expressed in rostral migratory stream and 270 other tissues.
DR Genevisible; Q3US17; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..591
FT /note="Zinc finger protein 48"
FT /id="PRO_0000234587"
FT ZN_FING 83..105
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 111..133
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 163..185
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 191..213
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..268
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..296
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..324
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 423..445
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..473
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MX3"
FT CONFLICT 6
FT /note="G -> E (in Ref. 1; BAE24520)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="G -> V (in Ref. 1; BAE28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> F (in Ref. 1; BAE28517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 64599 MW; EE070D2692FA4A73 CRC64;
MEASPGDEFE HSPQERDGPE IKEEEQLAPT LQVGNTSLKP DGIQCWDDLW DRREGLGKRQ
PRDPVPRILG EPRWGQGSND RAAVCGECGK SFRQMSDLVK HQRTHTGEKP YKCGVCGKGF
GDSSARIKHQ RTHTGEKAYR VRPPAPGPPK MPRSRIPAGE RPTICGECGK SFRQSSDLVK
HQRTHTGEKP YKCGICGKGF GDSSARIKHQ RTHRGDQLPR PVVPRRQPSP AAPAAPHRPK
AQDKPYICTD CGKRFVLSCS LLSHQRSHLG PKPFGCDVCG KEFARGSDLV KHLRVHTGEK
PYLCPECGKG FADSSARVKH LRTHSGQRPH ACPECNRSFS LSSTLLRHRL THVEPQDFSL
AAYPVVPLIP SPPPPPLGTS PSLTPRSPSH SSDGPFGLPG LEPEPGGPQA GEPPPPLAGD
KPHKCPECGK GFRRSSDLVK HHRVHTGEKP YLCPECGKGF ADSSARVKHL RTHQGERTRP
PPPPSTLLRP HNPPGSVPIV PQSRVQGRPS GPSQLHVCGF CGKEFPRSSD LVKHRRTHTG
EKPYKCAECG KGFGDSSARI KHQRGHLALK PFGVGDGPPR PLKEESPAGL E
