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F170A_MOUSE
ID   F170A_MOUSE             Reviewed;         333 AA.
AC   Q66LM6; B2RW56; Q66LM7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein FAM170A;
DE   AltName: Full=Zinc finger domain-containing protein;
DE   AltName: Full=Zinc finger protein ZNFD;
GN   Name=Fam170a; Synonyms=Gm93, Znfd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RA   Huang C.Q., Liu S., Zhai Q.T.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213 AND SER-308, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22231842; DOI=10.1007/s11010-011-1193-7;
RA   Xu F., Wang W., Lei C., Liu Q., Qiu H., Muraleedharan V., Zhou B.,
RA   Cheng H., Huang Z., Xu W., Li B., Wang M.;
RT   "Activation of transcriptional activity of HSE by a novel mouse zinc finger
RT   protein ZNFD specifically expressed in testis.";
RL   Mol. Cell. Biochem. 363:409-417(2012).
CC   -!- FUNCTION: Acts as a nuclear transcription factor that positively
CC       regulates the expression of heat shock genes. Binds to heat shock
CC       promoter elements (HSE). {ECO:0000269|PubMed:22231842}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22231842}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=b;
CC         IsoId=Q66LM6-1; Sequence=Displayed;
CC       Name=2; Synonyms=a;
CC         IsoId=Q66LM6-2; Sequence=VSP_032558;
CC   -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:22231842}.
CC   -!- DOMAIN: The N-terminus is necessary for nuclear localization. The C-
CC       terminus is necessary for transcriptional activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAM170 family. {ECO:0000305}.
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DR   EMBL; AY692448; AAU04856.1; -; mRNA.
DR   EMBL; AY692449; AAU04857.1; -; mRNA.
DR   EMBL; BC147592; AAI47593.1; -; mRNA.
DR   EMBL; BC147595; AAI47596.1; -; mRNA.
DR   CCDS; CCDS29243.1; -. [Q66LM6-1]
DR   RefSeq; NP_001004061.1; NM_001004061.1. [Q66LM6-1]
DR   AlphaFoldDB; Q66LM6; -.
DR   BioGRID; 230401; 2.
DR   STRING; 10090.ENSMUSP00000035910; -.
DR   iPTMnet; Q66LM6; -.
DR   PhosphoSitePlus; Q66LM6; -.
DR   PaxDb; Q66LM6; -.
DR   PRIDE; Q66LM6; -.
DR   ProteomicsDB; 267678; -. [Q66LM6-1]
DR   ProteomicsDB; 267679; -. [Q66LM6-2]
DR   Antibodypedia; 50043; 62 antibodies from 11 providers.
DR   DNASU; 225497; -.
DR   Ensembl; ENSMUST00000039121; ENSMUSP00000035910; ENSMUSG00000035420. [Q66LM6-1]
DR   GeneID; 225497; -.
DR   KEGG; mmu:225497; -.
DR   UCSC; uc008ewx.1; mouse. [Q66LM6-1]
DR   CTD; 340069; -.
DR   MGI; MGI:2684939; Fam170a.
DR   VEuPathDB; HostDB:ENSMUSG00000035420; -.
DR   eggNOG; ENOG502TH7F; Eukaryota.
DR   GeneTree; ENSGT00940000162220; -.
DR   HOGENOM; CLU_062038_2_0_1; -.
DR   InParanoid; Q66LM6; -.
DR   OMA; MEEMTLP; -.
DR   OrthoDB; 1142827at2759; -.
DR   PhylomeDB; Q66LM6; -.
DR   TreeFam; TF337124; -.
DR   BioGRID-ORCS; 225497; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q66LM6; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q66LM6; protein.
DR   Bgee; ENSMUSG00000035420; Expressed in seminiferous tubule of testis and 3 other tissues.
DR   ExpressionAtlas; Q66LM6; baseline and differential.
DR   Genevisible; Q66LM6; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009566; P:fertilization; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   InterPro; IPR033376; FAM170A.
DR   InterPro; IPR040879; Spt46-like.
DR   PANTHER; PTHR33517; PTHR33517; 1.
DR   PANTHER; PTHR33517:SF3; PTHR33517:SF3; 1.
DR   Pfam; PF17734; Spt46; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..333
FT                   /note="Protein FAM170A"
FT                   /id="PRO_0000326112"
FT   ZN_FING         224..248
FT                   /note="C2H2-type; degenerate"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         213
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         19..67
FT                   /note="GISKSQEDISHPESTGVPKAQSPGVGEVSSASEYFSCVSSPQKLIHRSK ->
FT                   E (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_032558"
SQ   SEQUENCE   333 AA;  37392 MW;  145BD399D6C10F21 CRC64;
     MKRRQKRKHL EIEESKEAGI SKSQEDISHP ESTGVPKAQS PGVGEVSSAS EYFSCVSSPQ
     KLIHRSKGTW KLLQDSSKPR SPLDQVPEGE ATTAPSQQAS SSCPSYKTCV SSLCMNKEER
     GMKIYYMQVQ MKKGVAISWD TKETSESLEK QPRMEEATLP EGVWVGTPPS DVSTRNLLSD
     SEPIGEEKEH EEKPESDSPP GSPAVEERPR AKTPDWLVTM ENGFRCMACC RVFATMESLQ
     EHVQYGIREG FSCHVFHLTM AQLIGSMESE STQEEEEDHT EETEKPKEEK AEEQQPTEED
     VGMKKPWSQC PGCVFDSPKD RRRRKDHCDN SGS
 
 
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