ZNHI2_MOUSE
ID ZNHI2_MOUSE Reviewed; 399 AA.
AC Q9QY66; Q8C356; Q8VCQ7;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Zinc finger HIT domain-containing protein 2;
DE AltName: Full=Protein FON;
GN Name=Znhit2; Synonyms=ORF6;
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], AND TISSUE SPECIFICITY.
RX PubMed=10602999; DOI=10.1007/s003350010016;
RA Lemmens I.H., Farnebo F., Piehl F., Merregaert J., Van de Ven W.J.M.,
RA Larsson C., Kas K.;
RT "Molecular characterization of human and murine c11orf5, a new member of
RT the FAUNA gene cluster.";
RL Mamm. Genome 11:78-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 MRNA].
RC TISSUE=Liver;
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: May act as a bridging factor mediating the interaction
CC between the R2TP/Prefoldin-like (R2TP/PFDL) complex and U5 small
CC nuclear ribonucleoprotein (U5 snRNP) (By similarity). Required for the
CC interaction of R2TP complex subunit RPAP3 and prefoldin-like subunit
CC URI1 with U5 snRNP proteins EFTUD2 and PRPF8 (By similarity). May play
CC a role in regulating the composition of the U5 snRNP complex (By
CC similarity). {ECO:0000250|UniProtKB:Q9UHR6}.
CC -!- SUBUNIT: Interacts (via HIT-type zinc finger) with RUVBL2 in the
CC presence of ATP or ADP; shows a stronger interaction in the presence of
CC ADP. {ECO:0000250|UniProtKB:Q9UHR6}.
CC -!- TISSUE SPECIFICITY: Low expression in most tissues; highly expressed in
CC testis; particularly in seminiferous tubules.
CC {ECO:0000269|PubMed:10602999}.
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DR EMBL; AF119498; AAF23592.1; -; mRNA.
DR EMBL; AK086863; BAC39755.1; -; mRNA.
DR EMBL; BC019440; AAH19440.1; -; mRNA.
DR CCDS; CCDS57131.1; -.
DR RefSeq; NP_038887.2; NM_013859.2.
DR AlphaFoldDB; Q9QY66; -.
DR SMR; Q9QY66; -.
DR IntAct; Q9QY66; 2.
DR MINT; Q9QY66; -.
DR STRING; 10090.ENSMUSP00000134031; -.
DR iPTMnet; Q9QY66; -.
DR PhosphoSitePlus; Q9QY66; -.
DR EPD; Q9QY66; -.
DR MaxQB; Q9QY66; -.
DR PaxDb; Q9QY66; -.
DR PRIDE; Q9QY66; -.
DR ProteomicsDB; 275042; -.
DR Antibodypedia; 29668; 69 antibodies from 21 providers.
DR Ensembl; ENSMUST00000162726; ENSMUSP00000134031; ENSMUSG00000075227.
DR GeneID; 29805; -.
DR KEGG; mmu:29805; -.
DR UCSC; uc008ggv.1; mouse.
DR CTD; 741; -.
DR MGI; MGI:1352481; Znhit2.
DR VEuPathDB; HostDB:ENSMUSG00000075227; -.
DR eggNOG; KOG4317; Eukaryota.
DR GeneTree; ENSGT00390000017147; -.
DR HOGENOM; CLU_039057_1_0_1; -.
DR InParanoid; Q9QY66; -.
DR OMA; VPYCSLR; -.
DR OrthoDB; 1599898at2759; -.
DR PhylomeDB; Q9QY66; -.
DR TreeFam; TF324864; -.
DR BioGRID-ORCS; 29805; 26 hits in 76 CRISPR screens.
DR PRO; PR:Q9QY66; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9QY66; protein.
DR Bgee; ENSMUSG00000075227; Expressed in seminiferous tubule of testis and 236 other tissues.
DR Genevisible; Q9QY66; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR007529; Znf_HIT.
DR InterPro; IPR039646; ZNHIT2.
DR PANTHER; PTHR15555; PTHR15555; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..399
FT /note="Zinc finger HIT domain-containing protein 2"
FT /id="PRO_0000173549"
FT ZN_FING 7..41
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 70..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR6"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR6"
FT CONFLICT 89
FT /note="G -> R (in Ref. 3; AAH19440)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="AG -> RN (in Ref. 1; AAF23592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42897 MW; F4CF854C5B5FEC87 CRC64;
MEPAGLCGFC PAGEALPARY TCPRCNAPYC SLRCYRAHGA CAEDFYRDQV LRELRGRSAS
PSRLAGALRR LREQREAEDE PEEAGLGPGA RPGGLSGLWE RLTPAEKAAF ERLLSRGEAG
RLLPPWRPWW WGRGTGPRLL EELDHAANRD LAEPEPAPAR TALQSGDDAA AAEPFAEDSC
AARPLALPAR IPALASLSRS PASPLVRFQL PNVLFAYAHT LALYHGGDDD ALLSDFCATL
LDVSGALGAQ QVFGSTEEAL QAAAHVLEAG EHPPGPLGTR GAMQEVARIL LGEGPVNQKG
YTLTALGHLA QTLGRARKQA VIGGERDRLY RARKKCQFLL AWTNENEAAL TPLALDCARA
HRAHAVTAEE MATLTGELER LWGGPVPPTP RTLIEELPG
