ZNF16_HUMAN
ID ZNF16_HUMAN Reviewed; 682 AA.
AC P17020; B3KXM4; D3DWP2; Q45SH7; Q96FG0; Q9NRA4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Zinc finger protein 16;
DE AltName: Full=Zinc finger protein KOX9;
GN Name=ZNF16; Synonyms=HZF1, KOX9;
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], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=16628192; DOI=10.1038/sj.leu.2404212;
RA Peng H., Du Z.W., Zhang J.W.;
RT "Identification and characterization of a novel zinc finger protein (HZF1)
RT gene and its function in erythroid and megakaryocytic differentiation of
RT K562 cells.";
RL Leukemia 20:1109-1116(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 461-516.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-487, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP FUNCTION.
RX PubMed=19763908; DOI=10.1007/s12033-009-9210-8;
RA Deng M.J., Li X.B., Peng H., Zhang J.W.;
RT "Identification of the trans-activation domain and the nuclear location
RT signals of human zinc finger protein HZF1 (ZNF16).";
RL Mol. Biotechnol. 44:83-89(2010).
RN [8]
RP INDUCTION.
RX PubMed=21468593; DOI=10.3892/mmr.2011.465;
RA Liu X., Jin E.Z., Zhi J.X., Li X.Q.;
RT "Identification of HZF1 as a novel target gene of the MEF2 transcription
RT factor.";
RL Mol. Med. Report. 4:465-469(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH INCA1.
RX PubMed=21874239; DOI=10.3892/mmr.2011.564;
RA Li X.B., Chen J., Deng M.J., Wang F., Du Z.W., Zhang J.W.;
RT "Zinc finger protein HZF1 promotes K562 cell proliferation by interacting
RT with and inhibiting INCA1.";
RL Mol. Med. Report. 4:1131-1137(2011).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Acts as a transcriptional activator. Promotes cell
CC proliferation by facilitating the cell cycle phase transition from the
CC S to G2/M phase. Involved in both the hemin- and phorbol myristate
CC acetate (PMA)-induced erythroid and megakaryocytic differentiation,
CC respectively. Also plays a role as an inhibitor of cell apoptosis.
CC {ECO:0000269|PubMed:16628192, ECO:0000269|PubMed:19763908,
CC ECO:0000269|PubMed:21874239}.
CC -!- SUBUNIT: Interacts with INCA1; the interaction inhibits INCA1 activity
CC and induces the cell cycle process. {ECO:0000269|PubMed:21874239}.
CC -!- INTERACTION:
CC P17020; P29972: AQP1; NbExp=3; IntAct=EBI-3921553, EBI-745213;
CC P17020; Q9NVQ4-2: FAIM; NbExp=3; IntAct=EBI-3921553, EBI-12039347;
CC P17020; Q0VD86: INCA1; NbExp=2; IntAct=EBI-3921553, EBI-6509505;
CC P17020; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-3921553, EBI-7781767;
CC P17020; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-3921553, EBI-746345;
CC P17020; Q8IZC7: ZNF101; NbExp=3; IntAct=EBI-3921553, EBI-5278328;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16628192}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16628192}.
CC -!- INDUCTION: Up-regulated by hemin during erythroid differentiation. Up-
CC regulated by phorbol myristate acetate (PMA) during megakaryocytic
CC differentiation. Up-regulated by the transcriptional activator MEF2A.
CC {ECO:0000269|PubMed:16628192, ECO:0000269|PubMed:21468593}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF75235.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAZ20773.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF244088; AAF75235.1; ALT_INIT; mRNA.
DR EMBL; DQ117529; AAZ20773.1; ALT_INIT; mRNA.
DR EMBL; AK127625; BAG54536.1; -; mRNA.
DR EMBL; CH471162; EAW82027.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82028.1; -; Genomic_DNA.
DR EMBL; BC010996; AAH10996.2; -; mRNA.
DR EMBL; X52340; CAA36566.1; -; mRNA.
DR CCDS; CCDS6437.1; -.
DR PIR; I37977; I37977.
DR RefSeq; NP_001025147.2; NM_001029976.2.
DR RefSeq; NP_008889.2; NM_006958.2.
DR RefSeq; XP_005272398.1; XM_005272341.2.
DR RefSeq; XP_011515600.1; XM_011517298.1.
DR AlphaFoldDB; P17020; -.
DR SMR; P17020; -.
DR BioGRID; 113395; 40.
DR IntAct; P17020; 38.
DR STRING; 9606.ENSP00000276816; -.
DR iPTMnet; P17020; -.
DR PhosphoSitePlus; P17020; -.
DR BioMuta; ZNF16; -.
DR DMDM; 68846743; -.
DR EPD; P17020; -.
DR jPOST; P17020; -.
DR MassIVE; P17020; -.
DR MaxQB; P17020; -.
DR PaxDb; P17020; -.
DR PeptideAtlas; P17020; -.
DR PRIDE; P17020; -.
DR ProteomicsDB; 53416; -.
DR Antibodypedia; 15018; 112 antibodies from 17 providers.
DR DNASU; 7564; -.
DR Ensembl; ENST00000276816.8; ENSP00000276816.4; ENSG00000170631.15.
DR Ensembl; ENST00000394909.7; ENSP00000378369.2; ENSG00000170631.15.
DR Ensembl; ENST00000611477.1; ENSP00000484504.1; ENSG00000170631.15.
DR GeneID; 7564; -.
DR KEGG; hsa:7564; -.
DR MANE-Select; ENST00000394909.7; ENSP00000378369.2; NM_006958.3; NP_008889.2.
DR UCSC; uc003zet.3; human.
DR CTD; 7564; -.
DR GeneCards; ZNF16; -.
DR HGNC; HGNC:12947; ZNF16.
DR HPA; ENSG00000170631; Low tissue specificity.
DR MIM; 601262; gene.
DR neXtProt; NX_P17020; -.
DR OpenTargets; ENSG00000170631; -.
DR PharmGKB; PA37530; -.
DR VEuPathDB; HostDB:ENSG00000170631; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163050; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; P17020; -.
DR OMA; EERPHLY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17020; -.
DR TreeFam; TF337005; -.
DR PathwayCommons; P17020; -.
DR SignaLink; P17020; -.
DR BioGRID-ORCS; 7564; 13 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF16; human.
DR GeneWiki; ZNF16; -.
DR GenomeRNAi; 7564; -.
DR Pharos; P17020; Tbio.
DR PRO; PR:P17020; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P17020; protein.
DR Bgee; ENSG00000170631; Expressed in oocyte and 149 other tissues.
DR ExpressionAtlas; P17020; baseline and differential.
DR Genevisible; P17020; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072707; P:cellular response to sodium dodecyl sulfate; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1901989; P:positive regulation of cell cycle phase transition; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
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; 15.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell cycle; Cell division; DNA-binding;
KW Isopeptide bond; Metal-binding; Mitogen; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..682
FT /note="Zinc finger protein 16"
FT /id="PRO_0000047338"
FT ZN_FING 209..231
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 237..259
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 265..287
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 629..651
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 657..679
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..210
FT /note="Necessary for transcription activation"
FT REGION 268..393
FT /note="Required for nuclear localization"
FT REGION 341..373
FT /note="Required for nuclear localization"
FT REGION 473..503
FT /note="Required for nuclear localization"
FT MOD_RES 487
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 105
FT /note="E -> K (in dbSNP:rs3735784)"
FT /id="VAR_024193"
FT VARIANT 227
FT /note="R -> H (in dbSNP:rs3735786)"
FT /id="VAR_024194"
SQ SEQUENCE 682 AA; 76472 MW; 3D4FA38552001430 CRC64;
MPSLRTRREE AEMELSVPGP SPWTPAAQAR VRDAPAVTHP GSAACGTPCC SDTELEAICP
HYQQPDCDTR TEDKEFLHKE DIHEDLESQA EISENYAGDV SQVPELGDLC DDVSERDWGV
PEGRRLPQSL SQEGDFTPAA MGLLRGPLGE KDLDCNGFDS RFSLSPNLMA CQEIPTEERP
HPYDMGGQSF QHSVDLTGHE GVPTAESPLI CNECGKTFQG NPDLIQRQIV HTGEASFMCD
DCGKTFSQNS VLKNRHRSHM SEKAYQCSEC GKAFRGHSDF SRHQSHHSSE RPYMCNECGK
AFSQNSSLKK HQKSHMSEKP YECNECGKAF RRSSNLIQHQ RIHSGEKPYV CSECGKAFRR
SSNLIKHHRT HTGEKPFECG ECGKAFSQSA HLRKHQRVHT GEKPYECNDC GKPFSRVSNL
IKHHRVHTGE KPYKCSDCGK AFSQSSSLIQ HRRIHTGEKP HVCNVCGKAF SYSSVLRKHQ
IIHTGEKPYR CSVCGKAFSH SSALIQHQGV HTGDKPYACH ECGKTFGRSS NLILHQRVHT
GEKPYECTEC GKTFSQSSTL IQHQRIHNGL KPHECNQCGK AFNRSSNLIH HQKVHTGEKP
YTCVECGKGF SQSSHLIQHQ IIHTGERPYK CSECGKAFSQ RSVLIQHQRI HTGVKPYDCA
ACGKAFSQRS KLIKHQLIHT RE
