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ZN75C_HUMAN
ID   ZN75C_HUMAN             Reviewed;         426 AA.
AC   Q92670;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Putative zinc finger protein 75C;
DE   AltName: Full=Zinc finger protein 75C pseudogene;
GN   Name=ZNF75CP; Synonyms=ZNF75C;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-422.
RC   TISSUE=Peripheral blood;
RX   PubMed=8661144; DOI=10.1006/geno.1996.0362;
RA   Villa A., Strina D., Frattini A., Faranda S., Macchi P., Finelli P.,
RA   Bozzi F., Susani L., Archidiacono N., Rocchi M., Vezzoni P.;
RT   "The ZNF75 zinc finger gene subfamily: isolation and mapping of the four
RT   members in humans and great apes.";
RL   Genomics 35:312-320(1996).
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}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AP003086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X91828; CAA62937.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92670; -.
DR   SMR; Q92670; -.
DR   iPTMnet; Q92670; -.
DR   PhosphoSitePlus; Q92670; -.
DR   BioMuta; HGNC:13148; -.
DR   DMDM; 205831223; -.
DR   jPOST; Q92670; -.
DR   MassIVE; Q92670; -.
DR   PeptideAtlas; Q92670; -.
DR   PRIDE; Q92670; -.
DR   ProteomicsDB; 75401; -.
DR   GeneCards; ZNF75CP; -.
DR   HGNC; HGNC:13148; ZNF75CP.
DR   neXtProt; NX_Q92670; -.
DR   InParanoid; Q92670; -.
DR   PhylomeDB; Q92670; -.
DR   PathwayCommons; Q92670; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   Pharos; Q92670; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q92670; protein.
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; 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; 3.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   5: Uncertain;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..426
FT                   /note="Putative zinc finger protein 75C"
FT                   /id="PRO_0000349242"
FT   DOMAIN          49..131
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          205..289
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         292..314
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         320..342
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         348..370
FT                   /note="C2H2-type 3; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         376..398
FT                   /note="C2H2-type 4; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         404..426
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CONFLICT        394
FT                   /note="Y -> H (in Ref. 2; CAA62937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408..410
FT                   /note="ICR -> LCK (in Ref. 2; CAA62937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416..417
FT                   /note="QL -> RS (in Ref. 2; CAA62937)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  49753 MW;  F88B9E97A42FA06B CRC64;
     MIMRELKADA CLNSHMGAMW ETNRSVKENS SQSKKYSTQI ECLSPGSACR HFRSFHYHEA
     TEPLEAINQL QKLCHQWLRP EIHSKKHILE MLVLEHFLTI LPKGTQNWVQ KHHPQLAKQA
     LVLVERLQRE PGGTKNEVTA HELGEEAVLL RGTTVAPGFK WKPAELEPME RILEHIQILA
     LSEHKSTKDW KMAPKLIWPE SQSLLTFEDM AVYFSEEEWQ LLGPLEKTLY NDVMQDIYET
     AISLGKQRTG KIMGIEMASS FSKEEKKLTT CKQELPKLMD LHGKGHTGEK PFKCQDCGKI
     FRVSSDLIKH QRIHTEEKLY KCQQCDRRFR WSSGLNKHFM THQGINPYRC SWYGKSISYD
     TNLQTHQRIH TGEKPFKCHE CGKIFIHKSN LIKYQRTHTG EQPYTCSICR RNFSRQLSLL
     RHQKLH
 
 
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