ZN394_PANPA
ID ZN394_PANPA Reviewed; 561 AA.
AC A1YG48;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Zinc finger protein 394;
GN Name=ZNF394;
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: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; DQ977217; ABM54273.1; -; Genomic_DNA.
DR RefSeq; XP_003815772.1; XM_003815724.2.
DR AlphaFoldDB; A1YG48; -.
DR SMR; A1YG48; -.
DR STRING; 9597.XP_003815772.1; -.
DR GeneID; 100980634; -.
DR KEGG; pps:100980634; -.
DR CTD; 84124; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000240080; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="Zinc finger protein 394"
FT /id="PRO_0000285473"
FT DOMAIN 64..146
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 155..230
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 358..380
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..463
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
SQ SEQUENCE 561 AA; 64278 MW; BB7B8CB00E1BA023 CRC64;
MNSSLTAQRR GSDAELGPWV MAARSKDAAP SQRDGLLPVK VEEDSLGSWE PSYPAASPDP
ETSRLHFRQL RYQEVAGPEE ALSRLRELCR RWLRPELLSK EQILELLVLE QFLTILPEEL
QAWVREHCPE SGEEAVAVVR ALQRALDGTS SQGMVTFEDM AVSLTWEEWE RLDPARSDFC
RESAQKDSGS TVPPSLESRV ENKELIPVQQ ILEEAEPQGR LQEAFQGKRP LFSKCVSTHE
DRVEKQSGDP LPLKLENSPE AEGFNSISDV NKNGSIEGED SKNNELQNSA RCSNLVLCQH
IPKAERPTDS EEHGNKCKQS FHMVTWHVLK PHKSDSGDSF HHSSLFETQR QLHEERPYKC
GNCGKSFKQR SDLFRHQRIH TGEKPYGCQE CGKSFSQSAA LTKHQRTHTG EKPYTCLKCG
ERFRQNSHLN RHQSTHSRDK HFKCEECGET CHISNLFRHQ RLHKGERPYK CEECEKSFKQ
RSDLFKHHRI HTGEKPYGCS VCGKRFNQSA TLIKHQRIHT GEKPYKCLEC GERFRQSTHL
IRHQRIHQNK VLSAGRGGSR L
