ZNF16_PANPA
ID ZNF16_PANPA Reviewed; 673 AA.
AC A1YG88;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Zinc finger protein 16;
GN Name=ZNF16;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
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; DQ977236; ABM54313.1; -; Genomic_DNA.
DR STRING; 9597.XP_008970964.1; -.
DR PRIDE; A1YG88; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000240080; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
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..673
FT /note="Zinc finger protein 16"
FT /id="PRO_0000285466"
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 284..306
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..418
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 424..446
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..502
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 536..558
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 564..586
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 592..614
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 620..642
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 648..670
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..42
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 177..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..364
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 464..494
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT MOD_RES 478
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 673 AA; 75377 MW; 3BEE91C5D1C36344 CRC64;
MPSLRTRREE AEMELSAPGP SPWTPAPQAR VSDAPAVTHP GSAACGTPCC SDTELEAICP
HYQQPDCDTR TEDKEFLHKE DIHEDLESQA EISENYAGDV FQVPKLGDLC DDVSERDWGV
PEGRRLPQSL SQEGDFTPAA MGLLRGPLGE KDLDCNGFDS CFSLSPNLMA CQEIPTEERP
HPYDMGGQSF QHSVDLTGHE GVPTAESPLI CNECGKTFRG NPDLIQRQIV HTGEASFMCD
DCGKTFSQNS VLKNRHXSHM SEKAFRGHSD FSRHQSHHSS ERPYTCTECG KAFSQNSSLK
KHQKSHMSEK PYECNECGKA FRRSSNLIQH QRIHSGEKPY VCSECGKAFR RSSNLIKHHR
THTGEKPFEC GECGKAFSQS AHLRKHQRVH TGEKPYECND CGKPFSRVSN LIKHHRVHTG
EKPYKCSDCG KAFSQSSSLI QHRRIHTGEK PHVCNVCGKA FSYSSVLRKH QIIHTGEKPY
RCSVCGKAFS HSSALIQHQG VHTGDKPYAC HECGKTFGRS SNLILHQRVH TGEKPYECTE
CGKTFSQSST LIQHQRIHNG LKPHECNQCG KAFNRSSNLI HHQKVHTGEK PYTCVECGKG
FSQSSHLIQH QIIHTGERPY KCSECGKAFS QRSVLIQHQR IHTGVKPYDC AACGKAFSQR
SKLIKHQLIH TRE
