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GLI4_HUMAN
ID   GLI4_HUMAN              Reviewed;         376 AA.
AC   P10075; Q96CK9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 193.
DE   RecName: Full=Zinc finger protein GLI4;
DE   AltName: Full=Krueppel-related zinc finger protein 4;
DE   AltName: Full=Protein HKR4;
GN   Name=GLI4; Synonyms=HKR4;
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 MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-272 AND 283-376, AND VARIANT
RP   THR-180.
RX   PubMed=2850480; DOI=10.1128/mcb.8.8.3104-3113.1988;
RA   Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T., Law M.L.,
RA   Seuanez H.N., O'Brien S.J., Vogelstein B.;
RT   "The GLI-Kruppel family of human genes.";
RL   Mol. Cell. Biol. 8:3104-3113(1988).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- INTERACTION:
CC       P10075; P28799: GRN; NbExp=3; IntAct=EBI-14061927, EBI-747754;
CC       P10075; O60333-2: KIF1B; NbExp=3; IntAct=EBI-14061927, EBI-10975473;
CC       P10075; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-14061927, EBI-5235340;
CC       P10075; O76024: WFS1; NbExp=3; IntAct=EBI-14061927, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC014165; AAH14165.1; -; mRNA.
DR   EMBL; M20678; AAA35990.1; -; Genomic_DNA.
DR   EMBL; M20679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS6398.1; -.
DR   PIR; F31201; F31201.
DR   RefSeq; NP_612474.1; NM_138465.3.
DR   AlphaFoldDB; P10075; -.
DR   SMR; P10075; -.
DR   BioGRID; 109000; 152.
DR   IntAct; P10075; 9.
DR   STRING; 9606.ENSP00000345024; -.
DR   iPTMnet; P10075; -.
DR   PhosphoSitePlus; P10075; -.
DR   BioMuta; GLI4; -.
DR   DMDM; 33302619; -.
DR   EPD; P10075; -.
DR   jPOST; P10075; -.
DR   MassIVE; P10075; -.
DR   MaxQB; P10075; -.
DR   PaxDb; P10075; -.
DR   PeptideAtlas; P10075; -.
DR   PRIDE; P10075; -.
DR   ProteomicsDB; 52562; -.
DR   Antibodypedia; 43401; 202 antibodies from 23 providers.
DR   DNASU; 2738; -.
DR   Ensembl; ENST00000340042.2; ENSP00000345024.1; ENSG00000250571.7.
DR   Ensembl; ENST00000523522.5; ENSP00000430987.1; ENSG00000250571.7.
DR   GeneID; 2738; -.
DR   KEGG; hsa:2738; -.
DR   MANE-Select; ENST00000340042.2; ENSP00000345024.1; NM_138465.4; NP_612474.1.
DR   UCSC; uc003yxx.4; human.
DR   CTD; 2738; -.
DR   DisGeNET; 2738; -.
DR   GeneCards; GLI4; -.
DR   HGNC; HGNC:4320; GLI4.
DR   HPA; ENSG00000250571; Low tissue specificity.
DR   MIM; 165280; gene.
DR   neXtProt; NX_P10075; -.
DR   OpenTargets; ENSG00000250571; -.
DR   PharmGKB; PA28723; -.
DR   VEuPathDB; HostDB:ENSG00000250571; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163360; -.
DR   HOGENOM; CLU_002678_1_0_1; -.
DR   InParanoid; P10075; -.
DR   OMA; QRIHYRE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P10075; -.
DR   TreeFam; TF337438; -.
DR   PathwayCommons; P10075; -.
DR   SignaLink; P10075; -.
DR   BioGRID-ORCS; 2738; 26 hits in 1099 CRISPR screens.
DR   ChiTaRS; GLI4; human.
DR   GenomeRNAi; 2738; -.
DR   Pharos; P10075; Tbio.
DR   PRO; PR:P10075; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P10075; protein.
DR   Bgee; ENSG00000250571; Expressed in lower esophagus mucosa and 96 other tissues.
DR   ExpressionAtlas; P10075; baseline and differential.
DR   Genevisible; P10075; HS.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..376
FT                   /note="Zinc finger protein GLI4"
FT                   /id="PRO_0000047267"
FT   ZN_FING         183..205
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         211..233
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         239..261
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         267..289
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         295..317
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         323..345
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         351..373
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         180
FT                   /note="A -> T (in dbSNP:rs1056148)"
FT                   /evidence="ECO:0000269|PubMed:2850480"
FT                   /id="VAR_052734"
FT   CONFLICT        144..146
FT                   /note="RVT -> ARD (in Ref. 2; AAA35990)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  41145 MW;  68B1A638CC0758BC CRC64;
     MAALGDIQES PSVPSPVSLS SPGTPGTQHH EPQLHLHGHQ HGSPGSSPKV LSQPSDLDLQ
     DVEEVEIGRD TFWPDSEPKP EQAPRSPGSQ APDEGAGGAL RSLLRSLPRR ARCSAGFGPE
     SSAERPAGQP PGAVPCAQPR GAWRVTLVQQ AAAGPEGAPE RAAELGVNFG RSRQGSARGA
     KPHRCEACGK SFKYNSLLLK HQRIHTGEKP YACHECGKRF RGWSGFIQHH RIHTGEKPYE
     CGQCGRAFSH SSHFTQHLRI HNGEKPYKCG ECGQAFSQSS NLVRHQRLHT GEKPYACSQC
     GKAFIWSSVL IEHQRIHTGE KPYECSDCGK AFRGRSHFFR HLRTHTGEKP FACGACGKAF
     GQSSQLIQHQ RVHYRE
 
 
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