ZNHI1_HUMAN
ID ZNHI1_HUMAN Reviewed; 154 AA.
AC O43257; Q6IB12;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger HIT domain-containing protein 1;
DE AltName: Full=Cyclin-G1-binding protein 1;
DE AltName: Full=Zinc finger protein subfamily 4A member 1;
DE AltName: Full=p18 Hamlet;
GN Name=ZNHIT1; Synonyms=CGBP1, ZNFN4A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y., Underwood L.J., Tanimoto H., Shigemasa K., O'Brien T.J.;
RT "Molecular cloning and characterization of cyclin G1 binding protein 1
RT (CGBP1).";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xu F., Hall F.L., Starnes V., Wu L.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP IDENTIFICATION IN THE SRCAP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15647280; DOI=10.1074/jbc.m500001200;
RA Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone
RT acetyltransferase and SRCAP complexes.";
RL J. Biol. Chem. 280:13665-13670(2005).
RN [8]
RP INTERACTION WITH MAPK11 AND MAPK14, PHOSPHORYLATION AT THR-103 BY MAPK11
RP AND MAPK14, INDUCTION BY DNA DAMAGE, FUNCTION, AND MUTAGENESIS OF THR-103.
RX PubMed=17380123; DOI=10.1038/sj.emboj.7601657;
RA Cuadrado A., Lafarga V., Cheung P.C., Dolado I., Llanos S., Cohen P.,
RA Nebreda A.R.;
RT "A new p38 MAP kinase-regulated transcriptional coactivator that stimulates
RT p53-dependent apoptosis.";
RL EMBO J. 26:2115-2126(2007).
RN [9]
RP FUNCTION, INTERACTION WITH NR1D1 AND NR1D2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=17892483; DOI=10.1111/j.1742-4658.2007.06062.x;
RA Wang J., Li Y., Zhang M., Liu Z., Wu C., Yuan H., Li Y.Y., Zhao X., Lu H.;
RT "A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with
RT orphan nuclear hormone receptor Rev-erbbeta and removes Rev-erbbeta-induced
RT inhibition of apoCIII transcription.";
RL FEBS J. 274:5370-5381(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP INTERACTION WITH RUVBL1/RUVBL2 COMPLEX.
RX PubMed=28561026; DOI=10.1038/ncomms15615;
RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL Nat. Commun. 8:15615-15615(2017).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-134.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Seems to play a role in p53-mediated apoptosis induction
CC (PubMed:17380123). Binds to NR1D2 and relieves it of its inhibitory
CC effect on the transcription of APOC3 without affecting its DNA-binding
CC activity (PubMed:17892483). {ECO:0000269|PubMed:17380123,
CC ECO:0000269|PubMed:17892483}.
CC -!- SUBUNIT: Interacts with MAPK11 and MAPK14 (PubMed:17380123). Component
CC of the chromatin-remodeling SRCAP complex composed of at least SRCAP,
CC DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1
CC (PubMed:15647280). Interacts with NR1D1 and NR2D2 (PubMed:17892483).
CC Interacts (via HIT-type zinc finger) with the RUVBL1/ RUVBL2 complex in
CC the presence of ADP (PubMed:28561026). {ECO:0000269|PubMed:15647280,
CC ECO:0000269|PubMed:17380123, ECO:0000269|PubMed:17892483,
CC ECO:0000269|PubMed:28561026}.
CC -!- INTERACTION:
CC O43257; Q9GZN1: ACTR6; NbExp=5; IntAct=EBI-347522, EBI-769329;
CC O43257; Q92870-2: APBB2; NbExp=3; IntAct=EBI-347522, EBI-21535880;
CC O43257; P41182: BCL6; NbExp=3; IntAct=EBI-347522, EBI-765407;
CC O43257; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-347522, EBI-2837444;
CC O43257; P27658: COL8A1; NbExp=3; IntAct=EBI-347522, EBI-747133;
CC O43257; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-347522, EBI-3867333;
CC O43257; O00429-3: DNM1L; NbExp=3; IntAct=EBI-347522, EBI-6896746;
CC O43257; P29692-2: EEF1D; NbExp=3; IntAct=EBI-347522, EBI-5280572;
CC O43257; Q5TD97: FHL5; NbExp=3; IntAct=EBI-347522, EBI-750641;
CC O43257; Q06787-7: FMR1; NbExp=3; IntAct=EBI-347522, EBI-25856644;
CC O43257; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-347522, EBI-5916454;
CC O43257; P0C0S5: H2AZ1; NbExp=5; IntAct=EBI-347522, EBI-1199859;
CC O43257; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-347522, EBI-2556193;
CC O43257; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-347522, EBI-12012928;
CC O43257; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-347522, EBI-10172290;
CC O43257; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-347522, EBI-10176379;
CC O43257; Q15759: MAPK11; NbExp=2; IntAct=EBI-347522, EBI-298304;
CC O43257; Q16539: MAPK14; NbExp=7; IntAct=EBI-347522, EBI-73946;
CC O43257; P45984: MAPK9; NbExp=3; IntAct=EBI-347522, EBI-713568;
CC O43257; Q99750: MDFI; NbExp=3; IntAct=EBI-347522, EBI-724076;
CC O43257; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-347522, EBI-14093244;
CC O43257; P32243-2: OTX2; NbExp=3; IntAct=EBI-347522, EBI-9087860;
CC O43257; D3DTS7: PMP22; NbExp=3; IntAct=EBI-347522, EBI-25882629;
CC O43257; Q15025: TNIP1; NbExp=3; IntAct=EBI-347522, EBI-357849;
CC O43257; Q12888: TP53BP1; NbExp=2; IntAct=EBI-347522, EBI-396540;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17892483}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in liver, but weakly in
CC skeletal muscle, ovary and small intestine.
CC {ECO:0000269|PubMed:17892483}.
CC -!- INDUCTION: Induced by DNA damage. {ECO:0000269|PubMed:17380123}.
CC -!- PTM: Phosphorylated on Thr by MAPK11 or MAPK14.
CC {ECO:0000269|PubMed:17380123}.
CC -!- PTM: Stres-induced ZNHIT1 is mainly regulated at the level of protein.
CC -!- SIMILARITY: Belongs to the ZNHIT1 family. {ECO:0000305}.
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DR EMBL; AF093571; AAF03558.1; -; mRNA.
DR EMBL; U61837; AAB88578.1; -; mRNA.
DR EMBL; CR456992; CAG33273.1; -; mRNA.
DR EMBL; AC004876; AAD45833.1; -; Genomic_DNA.
DR EMBL; CH471197; EAW50209.1; -; Genomic_DNA.
DR EMBL; BC017333; AAH17333.1; -; mRNA.
DR CCDS; CCDS5716.1; -.
DR RefSeq; NP_006340.1; NM_006349.2.
DR AlphaFoldDB; O43257; -.
DR BioGRID; 115730; 59.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR CORUM; O43257; -.
DR IntAct; O43257; 50.
DR MINT; O43257; -.
DR STRING; 9606.ENSP00000304593; -.
DR iPTMnet; O43257; -.
DR PhosphoSitePlus; O43257; -.
DR BioMuta; ZNHIT1; -.
DR EPD; O43257; -.
DR jPOST; O43257; -.
DR MassIVE; O43257; -.
DR MaxQB; O43257; -.
DR PaxDb; O43257; -.
DR PeptideAtlas; O43257; -.
DR PRIDE; O43257; -.
DR ProteomicsDB; 48839; -.
DR Antibodypedia; 16743; 135 antibodies from 28 providers.
DR DNASU; 10467; -.
DR Ensembl; ENST00000305105.3; ENSP00000304593.2; ENSG00000106400.12.
DR GeneID; 10467; -.
DR KEGG; hsa:10467; -.
DR MANE-Select; ENST00000305105.3; ENSP00000304593.2; NM_006349.3; NP_006340.1.
DR UCSC; uc003uye.4; human.
DR CTD; 10467; -.
DR DisGeNET; 10467; -.
DR GeneCards; ZNHIT1; -.
DR HGNC; HGNC:21688; ZNHIT1.
DR HPA; ENSG00000106400; Low tissue specificity.
DR MIM; 618617; gene.
DR neXtProt; NX_O43257; -.
DR OpenTargets; ENSG00000106400; -.
DR PharmGKB; PA134947251; -.
DR VEuPathDB; HostDB:ENSG00000106400; -.
DR eggNOG; KOG3362; Eukaryota.
DR GeneTree; ENSGT00390000018426; -.
DR HOGENOM; CLU_106918_2_1_1; -.
DR InParanoid; O43257; -.
DR OMA; PCGARYC; -.
DR OrthoDB; 1588778at2759; -.
DR PhylomeDB; O43257; -.
DR TreeFam; TF314330; -.
DR PathwayCommons; O43257; -.
DR SignaLink; O43257; -.
DR SIGNOR; O43257; -.
DR BioGRID-ORCS; 10467; 161 hits in 1089 CRISPR screens.
DR ChiTaRS; ZNHIT1; human.
DR GenomeRNAi; 10467; -.
DR Pharos; O43257; Tbio.
DR PRO; PR:O43257; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43257; protein.
DR Bgee; ENSG00000106400; Expressed in right lobe of liver and 199 other tissues.
DR Genevisible; O43257; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
DR GO; GO:1905458; P:positive regulation of lymphoid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:1900049; P:regulation of histone exchange; ISS:UniProtKB.
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 1: Evidence at protein 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_0000173546"
FT ZN_FING 117..149
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..110
FT /note="Interaction with NR1D2"
FT /evidence="ECO:0000269|PubMed:17892483"
FT COILED 23..39
FT /evidence="ECO:0000255"
FT MOTIF 38..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:17892483"
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:0000269|PubMed:17380123"
FT VARIANT 134
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs369664812)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035719"
FT MUTAGEN 103
FT /note="T->A: Impairs the p38 MAPK-mediated phosphorylation
FT of ZNHIT1."
FT /evidence="ECO:0000269|PubMed:17380123"
FT MUTAGEN 124
FT /note="S->A: No change in the in vitro MAPK14/MAPK11-
FT induced phosphorylation level of ZNHIT1."
SQ SEQUENCE 154 AA; 17536 MW; 6A45F05249DC07A6 CRC64;
MVEKKTSVRS QDPGQRRVLD RAARQRRINR QLEALENDNF QDDPHAGLPQ LGKRLPQFDD
DADTGKKKKK TRGDHFKLRF RKNFQALLEE QNLSVAEGPN YLTACAGPPS RPQRPFCAVC
GFPSPYTCVS CGARYCTVRC LGTHQETRCL KWTV
