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SP5_HUMAN
ID   SP5_HUMAN               Reviewed;         398 AA.
AC   Q6BEB4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Transcription factor Sp5;
GN   Name=SP5;
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 [MRNA].
RA   Takahashi M., Furukawa Y., Nakamura Y.;
RT   "Isolation of human Sp5 as a direct target of the b-catenin/T-cell factor 4
RT   complex and its frequent elevated expression in colon cancers.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   9AATAD MOTIF.
RX   PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA   Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT   "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT   valines and intron reservoirs.";
RL   Cell. Mol. Life Sci. 77:1793-1810(2020).
CC   -!- FUNCTION: Binds to GC boxes promoters elements. Probable
CC       transcriptional activator that has a role in the coordination of
CC       changes in transcription required to generate pattern in the developing
CC       embryo (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:31375868}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB096175; BAD34944.1; -; mRNA.
DR   CCDS; CCDS33322.1; -.
DR   RefSeq; NP_001003845.1; NM_001003845.2.
DR   AlphaFoldDB; Q6BEB4; -.
DR   SMR; Q6BEB4; -.
DR   BioGRID; 132951; 2.
DR   IntAct; Q6BEB4; 1.
DR   STRING; 9606.ENSP00000364430; -.
DR   iPTMnet; Q6BEB4; -.
DR   PhosphoSitePlus; Q6BEB4; -.
DR   BioMuta; SP5; -.
DR   DMDM; 74762296; -.
DR   jPOST; Q6BEB4; -.
DR   MassIVE; Q6BEB4; -.
DR   MaxQB; Q6BEB4; -.
DR   PaxDb; Q6BEB4; -.
DR   PeptideAtlas; Q6BEB4; -.
DR   PRIDE; Q6BEB4; -.
DR   ProteomicsDB; 66220; -.
DR   Antibodypedia; 53490; 52 antibodies from 21 providers.
DR   DNASU; 389058; -.
DR   Ensembl; ENST00000375281.4; ENSP00000364430.3; ENSG00000204335.4.
DR   GeneID; 389058; -.
DR   KEGG; hsa:389058; -.
DR   MANE-Select; ENST00000375281.4; ENSP00000364430.3; NM_001003845.3; NP_001003845.1.
DR   UCSC; uc002uge.4; human.
DR   CTD; 389058; -.
DR   DisGeNET; 389058; -.
DR   GeneCards; SP5; -.
DR   HGNC; HGNC:14529; SP5.
DR   HPA; ENSG00000204335; Tissue enhanced (cervix).
DR   MIM; 609391; gene.
DR   neXtProt; NX_Q6BEB4; -.
DR   OpenTargets; ENSG00000204335; -.
DR   PharmGKB; PA134875843; -.
DR   VEuPathDB; HostDB:ENSG00000204335; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160673; -.
DR   HOGENOM; CLU_019484_5_0_1; -.
DR   InParanoid; Q6BEB4; -.
DR   OMA; PGGCGHR; -.
DR   OrthoDB; 1085860at2759; -.
DR   PhylomeDB; Q6BEB4; -.
DR   TreeFam; TF350150; -.
DR   PathwayCommons; Q6BEB4; -.
DR   SignaLink; Q6BEB4; -.
DR   BioGRID-ORCS; 389058; 14 hits in 1096 CRISPR screens.
DR   GenomeRNAi; 389058; -.
DR   Pharos; Q6BEB4; Tdark.
DR   PRO; PR:Q6BEB4; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q6BEB4; protein.
DR   Bgee; ENSG00000204335; Expressed in endocervix and 90 other tissues.
DR   Genevisible; Q6BEB4; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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:0060349; P:bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..398
FT                   /note="Transcription factor Sp5"
FT                   /id="PRO_0000047146"
FT   ZN_FING         296..320
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         326..350
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         356..378
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          160..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           187..195
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:31375868"
FT   COMPBIAS        160..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         75
FT                   /note="A -> T (in dbSNP:rs3749036)"
FT                   /id="VAR_052713"
SQ   SEQUENCE   398 AA;  41964 MW;  BC2C27EE3ED499FA CRC64;
     MAAVAVLRND SLQAFLQDRT PSASPDLGKH SPLALLAATC SRIGQPGAAA PPDFLQVPYD
     PALGSPSRLF HPWTADMPAH SPGALPPPHP SLGLTPQKTH LQPSFGAAHE LPLTPPADPS
     YPYEFSPVKM LPSSMAALPA SCAPAYVPYA AQAALPPGYS NLLPPPPPPP PPPTCRQLSP
     NPAPDDLPWW SIPQAGAGPG ASGVPGSGLS GACAGAPHAP RFPASAAAAA AAAAALQRGL
     VLGPSDFAQY QSQIAALLQT KAPLAATARR CRRCRCPNCQ AAGGAPEAEP GKKKQHVCHV
     PGCGKVYGKT SHLKAHLRWH TGERPFVCNW LFCGKSFTRS DELQRHLRTH TGEKRFACPE
     CGKRFMRSDH LAKHVKTHQN KKLKVAEAGV KREDARDL
 
 
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