ZSC12_GORGO
ID ZSC12_GORGO Reviewed; 604 AA.
AC A1YEP8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 12;
DE AltName: Full=Zinc finger protein 96;
GN Name=ZSCAN12; Synonyms=ZNF96;
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: 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; DQ976435; ABM46616.1; -; Genomic_DNA.
DR AlphaFoldDB; A1YEP8; -.
DR SMR; A1YEP8; -.
DR STRING; 9593.ENSGGOP00000020304; -.
DR PRIDE; A1YEP8; -.
DR Ensembl; ENSGGOT00000034595; ENSGGOP00000020304; ENSGGOG00000026544.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163105; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; A1YEP8; -.
DR OMA; QCEPQAG; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000026544; Expressed in heart and 6 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..604
FT /note="Zinc finger and SCAN domain-containing protein 12"
FT /id="PRO_0000285482"
FT DOMAIN 46..128
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 274..296
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..324
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..463
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..578
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 201..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43309"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43309"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43309"
SQ SEQUENCE 604 AA; 70176 MW; 3377BA01CDEC4406 CRC64;
MASTWAIQAH MDQNEPLEVK IEEEKYTTRQ DWDLRKNNTH SREVFRQYFR QFCYQETSGP
REALSRLREL CHQWLRPETH TKEQILELLV LEQFLTILPE ELQAWVQEQH PESGEEVVTV
LEDLERELDE PGEQVSVHTG EQEMFLQEMV PLRKEGEPSM SLQSMKAQPK YESPELESQQ
EQVLDVETGN EYGNLKQEVS EEMEPHGNTS SKFENDMSKS ARCGETREPE EITEEPSACS
REDKQPTCDE NGVSLTENSD HTEHQRICPG EESYGCDDCG KAFSQHSYLI EHQRIHTGDR
PYKCEECGKA FRGRTVLIRH KIIHTGEKPY KCNECGKAFG RWSALNQHQR LHTGEKHYHC
NDCGKAFSQK AGLFHHIKIH TRDKPYQCTQ CNKSFSRRSI LTQHQGVHTG AKPYECNECG
KAFVYNSSLV SHQEIHHKEK CYQCKECGKS FSQSGLIQHQ RIHTGEKPYK CDVCEKAFIQ
RTSLTEHQRI HTGERPYKCD KCGKAFTQRS VLTEHQRIHT GERPYKCDEC GNAFRGITSL
IQHQRIHTGE KPYQCDECGK AFRQRKKTSY KEILLKNHSE PQAGVNLLLS SLIPEWQSCF
RKDL
