ZNF16_GORGO
ID ZNF16_GORGO Reviewed; 682 AA.
AC A1YF12;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger protein 16;
GN Name=ZNF16;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with INCA1; the interaction inhibits INCA1 activity
CC and induces the cell cycle process. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; DQ976502; ABM46730.1; -; Genomic_DNA.
DR RefSeq; XP_004047778.1; XM_004047730.2.
DR AlphaFoldDB; A1YF12; -.
DR SMR; A1YF12; -.
DR STRING; 9593.ENSGGOP00000001176; -.
DR PRIDE; A1YF12; -.
DR Ensembl; ENSGGOT00000001200; ENSGGOP00000001176; ENSGGOG00000001192.
DR GeneID; 101128383; -.
DR KEGG; ggo:101128383; -.
DR CTD; 7564; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163050; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; A1YF12; -.
DR OMA; EERPHLY; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000001519; Chromosome 8.
DR Bgee; ENSGGOG00000001192; Expressed in heart and 6 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator 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; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1901989; P:positive regulation of cell cycle phase transition; ISS: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; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; ISS:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS: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; 16.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 3: Inferred from homology;
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_0000285465"
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..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..210
FT /note="Necessary for transcription activation"
FT /evidence="ECO:0000250"
FT REGION 112..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..393
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 341..373
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 473..503
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT MOD_RES 487
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17020"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17020"
SQ SEQUENCE 682 AA; 76323 MW; B1830C48F9083726 CRC64;
MPSLRTRREE AEMELSAPGP SPWTPAAQAH VSDAPAVTHP GSAACGTPCC SDTELEAICP
HYQQPDCDTR TEDKEFLHKE DIHEDLESQA EISENYAGDV LQVPELGDLC DDVSERDWGV
PEGRRLPQSL SQEGDFTPAA MGLLRGPLGE KDLDCNGFDS RFSLSPNLMA CQEIPTEERP
HPYDMGGQSF QHSVDLTGHE GVPTAESPLI CNECGKTFQG NPDLIQCQIV HTGEASFMCD
DCGKTFSQNS VLKNHHRSHM SEKAYQCSEC GKAFRGHSDF SRHQSHHSSE RPYMCNECGK
AFSQNSSLKK HQKSHMSEKP YECNECGKAF RRSSNLIQHQ RIHSGEKPYV CSECGKAFRR
SSNLIKHHRT HTGEKPFECG ECGKAFSQSA HLRKHQRVHT GEKPYECNDC GKPFSRVSNL
IKHHRVHTGE KPYKCSDCGK AFSQSSSLIQ HRRIHTGEKP HVCNICGKAF SYSSVLRKHQ
IIHTGEKPYR CSVCGKAFSH SSALIQHQGV HTGDKPYACH ECGKTFGRSS NLILHQRVHT
GEKPYECTEC GKTFSQSSTL IQHQRIHNGL KPHECNQCGK AFNRSSNLIH HQKVHTGEKP
YTCVECGKGF SQSSHLIQHQ IIHTGERPYK CSECGKAFSQ RSVLIQHQRI HTGVKPYDCA
ACGKAFSQRS KLIKHQLIHT RE
