HINFP_MOUSE
ID HINFP_MOUSE Reviewed; 503 AA.
AC Q8K1K9; E9QPQ4; Q8BWY0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histone H4 transcription factor;
DE AltName: Full=Histone nuclear factor P;
DE Short=HiNF-P;
DE AltName: Full=MBD2-interacting zinc finger protein;
DE AltName: Full=Methyl-CpG-binding protein 2-interacting zinc finger protein;
GN Name=Hinfp; Synonyms=Mizf;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-404.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [4]
RP FUNCTION.
RX PubMed=17826007; DOI=10.1016/j.gene.2007.07.027;
RA Xie R.-L., Liu L., Mitra P., Stein J.L., van Wijnen A.J., Stein G.S.;
RT "Transcriptional activation of the histone nuclear factor P (HiNF-P) gene
RT by HiNF-P and its cyclin E/CDK2 responsive co-factor p220NPAT defines a
RT novel autoregulatory loop at the G1/S phase transition.";
RL Gene 402:94-102(2007).
CC -!- FUNCTION: Transcriptional repressor that binds to the consensus
CC sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional
CC activator that promotes histone H4 gene transcription at the G1/S phase
CC transition in conjunction with NPAT. Also activates transcription of
CC the ATM and PRKDC genes. Autoregulates its expression by associating
CC with its own promoter. {ECO:0000269|PubMed:17826007}.
CC -!- SUBUNIT: Binds MBD2 and a histone deacetylase complex. Interacts with
CC NPAT (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
CC discrete nuclear foci. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination may lead to proteasome-mediated
CC degradation (By similarity). {ECO:0000250}.
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DR EMBL; AC124577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029091; AAH29091.1; -; mRNA.
DR EMBL; AK049633; BAC33849.1; -; mRNA.
DR CCDS; CCDS23102.1; -.
DR RefSeq; NP_751894.2; NM_172162.3.
DR RefSeq; XP_006509962.1; XM_006509899.2.
DR AlphaFoldDB; Q8K1K9; -.
DR SMR; Q8K1K9; -.
DR BioGRID; 221871; 14.
DR STRING; 10090.ENSMUSP00000034629; -.
DR iPTMnet; Q8K1K9; -.
DR PhosphoSitePlus; Q8K1K9; -.
DR PaxDb; Q8K1K9; -.
DR PRIDE; Q8K1K9; -.
DR ProteomicsDB; 273344; -.
DR Antibodypedia; 32617; 196 antibodies from 25 providers.
DR DNASU; 102423; -.
DR Ensembl; ENSMUST00000216508; ENSMUSP00000149879; ENSMUSG00000032119.
DR GeneID; 102423; -.
DR KEGG; mmu:102423; -.
DR UCSC; uc009pcr.2; mouse.
DR CTD; 25988; -.
DR MGI; MGI:2429620; Hinfp.
DR VEuPathDB; HostDB:ENSMUSG00000032119; -.
DR eggNOG; KOG3608; Eukaryota.
DR GeneTree; ENSGT00870000136508; -.
DR HOGENOM; CLU_026599_0_0_1; -.
DR InParanoid; Q8K1K9; -.
DR OMA; GERNCLW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8K1K9; -.
DR TreeFam; TF350923; -.
DR BioGRID-ORCS; 102423; 42 hits in 108 CRISPR screens.
DR ChiTaRS; Hinfp; mouse.
DR PRO; PR:Q8K1K9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K1K9; protein.
DR Bgee; ENSMUSG00000032119; Expressed in retinal neural layer and 220 other tissues.
DR ExpressionAtlas; Q8K1K9; baseline and differential.
DR Genevisible; Q8K1K9; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042393; F:histone 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; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..503
FT /note="Histone H4 transcription factor"
FT /id="PRO_0000047219"
FT ZN_FING 17..39
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 125..149
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 165..189
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 195..217
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 225..247
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 251..274
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..302
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..333
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..364
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 369..503
FT /note="Interaction with NPAT"
FT /evidence="ECO:0000250"
FT REGION 370..403
FT /note="Required for activation of histone H4 transcription
FT and contributes to DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 7
FT /note="V -> I (in Ref. 2; AAH29091)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="T -> S (in Ref. 2; AAH29091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 58076 MW; A2166A2522C4767B CRC64;
MSPPGKVPRK ENLGLQCEWG SCSFVCSAME EFFDHVTQHL QQHMHGSKEE EEEDPLEEEF
SCLWQECGFC SLDSSADLIR HVYFHCYHTK LKQWGLQALQ SQADLSPCIL DFQSRNVIPD
TPDHFLCLWE HCESVFDNPE WFYRHVDAHS LCCEYQAVSK DNHVVQCGWK GCTCTFKDRC
KLREHLRSHT QEKVVACPTC GGMFANNTKF LDHIRRQTSL DQQRFQCSHC SKRFATERLL
RDHMRNHVNH YKCPLCDMTC PLPSSLRNHM RFRHSEDRPY KCDCCDYSCK NLIDLRKHLD
THSKESAYRC DFENCNFSAR SLSSVKSHHR KVHEGDSEPR YKCHVCDKCF TRGNNLTVHL
RKKHQFKWPS GHPRFRYKEH EDGYMRLQLV RYESVELTQQ LLQQLQEGSD PGLALNESSL
QGIVLETVLG GPGPEEETEE EGRVVEGTAL SASQDNPSSA IHMVSQTDTQ GQRDIVYCVL
SEGPGEPPPV SETLKRDGKA RGT
