ZNHI1_MOUSE
ID ZNHI1_MOUSE Reviewed; 154 AA.
AC Q8R331; Q9CZS6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Zinc finger HIT domain-containing protein 1;
GN Name=Znhit1;
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=Embryo;
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].
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: Seems to play a role in p53-mediated apoptosis induction (By
CC similarity). Binds to NR1D2 and relieves it of its inhibitory effect on
CC the transcription of APOC3 without affecting its DNA-binding activity
CC (By similarity). {ECO:0000250|UniProtKB:O43257}.
CC -!- SUBUNIT: Interacts with MAPK11 and MAPK14 (By similarity). Component of
CC the chromatin-remodeling SRCAP complex composed of at least SRCAP,
CC DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1 (By
CC similarity). Interacts with NR1D1 and NR2D2 (By similarity). Interacts
CC (via HIT-type zinc finger) with the RUVBL1/RUVBL2 complex in the
CC presence of ADP (By similarity). {ECO:0000250|UniProtKB:O43257}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43257}.
CC -!- PTM: Phosphorylated on Thr by MAPK11 or MAPK14.
CC {ECO:0000250|UniProtKB:O43257}.
CC -!- SIMILARITY: Belongs to the ZNHIT1 family. {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; AK012199; BAB28094.1; -; mRNA.
DR EMBL; AK080799; BAC38025.1; -; mRNA.
DR EMBL; BC026751; AAH26751.1; -; mRNA.
DR CCDS; CCDS80438.1; -.
DR RefSeq; NP_001297676.1; NM_001310747.1.
DR RefSeq; NP_081594.1; NM_027318.4.
DR AlphaFoldDB; Q8R331; -.
DR ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR STRING; 10090.ENSMUSP00000115929; -.
DR iPTMnet; Q8R331; -.
DR PhosphoSitePlus; Q8R331; -.
DR EPD; Q8R331; -.
DR MaxQB; Q8R331; -.
DR PaxDb; Q8R331; -.
DR PRIDE; Q8R331; -.
DR ProteomicsDB; 275101; -.
DR Antibodypedia; 16743; 135 antibodies from 28 providers.
DR Ensembl; ENSMUST00000085941; ENSMUSP00000083103; ENSMUSG00000059518.
DR GeneID; 70103; -.
DR KEGG; mmu:70103; -.
DR UCSC; uc009abh.1; mouse.
DR CTD; 10467; -.
DR MGI; MGI:1917353; Znhit1.
DR VEuPathDB; HostDB:ENSMUSG00000059518; -.
DR eggNOG; KOG3362; Eukaryota.
DR GeneTree; ENSGT00390000018426; -.
DR HOGENOM; CLU_106918_2_1_1; -.
DR InParanoid; Q8R331; -.
DR OMA; PCGARYC; -.
DR PhylomeDB; Q8R331; -.
DR TreeFam; TF314330; -.
DR BioGRID-ORCS; 70103; 20 hits in 60 CRISPR screens.
DR ChiTaRS; Znhit1; mouse.
DR PRO; PR:Q8R331; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R331; protein.
DR Bgee; ENSMUSG00000059518; Expressed in seminiferous tubule of testis and 261 other tissues.
DR ExpressionAtlas; Q8R331; baseline and differential.
DR Genevisible; Q8R331; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:UniProtKB.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:1905458; P:positive regulation of lymphoid progenitor cell differentiation; IMP:UniProtKB.
DR GO; GO:0031063; P:regulation of histone deacetylation; IDA:MGI.
DR GO; GO:1900049; P:regulation of histone exchange; IMP:UniProtKB.
DR GO; GO:0042129; P:regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR039723; Vps71/ZNHIT1.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR13093; PTHR13093; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..154
FT /note="Zinc finger HIT domain-containing protein 1"
FT /id="PRO_0000173547"
FT ZN_FING 117..149
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..110
FT /note="Interaction with NR1D2"
FT /evidence="ECO:0000250|UniProtKB:O43257"
FT COILED 23..39
FT /evidence="ECO:0000255"
FT MOTIF 38..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O43257"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 103
FT /note="Phosphothreonine; by MAPK11 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:O43257"
FT CONFLICT 1..7
FT /note="MVEKKPA -> MQTARQ (in Ref. 1; BAB28094/BAC38025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17504 MW; DE56C728392F803C CRC64;
MVEKKPAVRS QDPGQRRVLD RAARQRRINR QLEALENDNF QDDPHAGLPQ LGKRLPQFDD
DADTGKKKKK TRGDHFKLRF RKNFQALLEE QNLSASEGPN YLTACAGPPS RPQRPFCAVC
GFPSPYTCVS CGARYCTVRC LGTHQETRCL KWTV
