F170A_HUMAN
ID F170A_HUMAN Reviewed; 330 AA.
AC A1A519; Q66LM8; Q7Z4V2; Q8IW94;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein FAM170A;
DE AltName: Full=Zinc finger domain-containing protein;
DE AltName: Full=Zinc finger protein ZNFD;
GN Name=FAM170A; Synonyms=ZNFD;
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] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=20162441; DOI=10.1007/s11010-010-0401-1;
RA Lei C., Liu Q., Wang W., Li J., Xu F., Liu Y., Liu J., Wu S., Wang M.;
RT "Isolation and characterization of a novel zinc finger gene, ZNFD,
RT activating AP1(PMA) transcriptional activities.";
RL Mol. Cell. Biochem. 340:63-71(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Huang C.Q., Liu S., Zhai Q.T.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Guo J.H., She X.Y., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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).
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:20162441}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20162441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A1A519-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1A519-2; Sequence=VSP_032557;
CC Name=3;
CC IsoId=A1A519-3; Sequence=VSP_032556, VSP_032557;
CC Name=4;
CC IsoId=A1A519-4; Sequence=VSP_035475, VSP_035476, VSP_035477;
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis and brain and weakly
CC in prostate, spleen, pancreas and uterus.
CC {ECO:0000269|PubMed:20162441}.
CC -!- DOMAIN: The N-terminus is necessary for nuclear localization. The C-
CC terminus is necessary for transcriptional activity.
CC -!- SIMILARITY: Belongs to the FAM170 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40622.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY692447; AAU04855.1; -; mRNA.
DR EMBL; AF427126; AAP97296.1; -; mRNA.
DR EMBL; AC010409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040622; AAH40622.1; ALT_INIT; mRNA.
DR EMBL; BC128243; AAI28244.1; -; mRNA.
DR CCDS; CCDS43353.1; -. [A1A519-2]
DR CCDS; CCDS54889.1; -. [A1A519-3]
DR RefSeq; NP_001157463.1; NM_001163991.1. [A1A519-3]
DR RefSeq; NP_877438.2; NM_182761.3. [A1A519-2]
DR AlphaFoldDB; A1A519; -.
DR BioGRID; 130989; 22.
DR IntAct; A1A519; 12.
DR STRING; 9606.ENSP00000482552; -.
DR iPTMnet; A1A519; -.
DR PhosphoSitePlus; A1A519; -.
DR BioMuta; FAM170A; -.
DR MassIVE; A1A519; -.
DR PaxDb; A1A519; -.
DR PeptideAtlas; A1A519; -.
DR PRIDE; A1A519; -.
DR ProteomicsDB; 100; -. [A1A519-1]
DR ProteomicsDB; 101; -. [A1A519-2]
DR ProteomicsDB; 102; -. [A1A519-3]
DR ProteomicsDB; 103; -. [A1A519-4]
DR Antibodypedia; 50043; 62 antibodies from 11 providers.
DR DNASU; 340069; -.
DR Ensembl; ENST00000335286.10; ENSP00000334285.6; ENSG00000164334.15. [A1A519-2]
DR Ensembl; ENST00000379555.7; ENSP00000368873.3; ENSG00000164334.15. [A1A519-3]
DR Ensembl; ENST00000515256.5; ENSP00000422684.1; ENSG00000164334.15. [A1A519-1]
DR Ensembl; ENST00000613773.4; ENSP00000482552.1; ENSG00000164334.15. [A1A519-2]
DR Ensembl; ENST00000620555.4; ENSP00000483075.1; ENSG00000164334.15. [A1A519-3]
DR GeneID; 340069; -.
DR KEGG; hsa:340069; -.
DR UCSC; uc003ksm.3; human. [A1A519-1]
DR CTD; 340069; -.
DR GeneCards; FAM170A; -.
DR HGNC; HGNC:27963; FAM170A.
DR HPA; ENSG00000164334; Tissue enriched (testis).
DR MIM; 618401; gene.
DR neXtProt; NX_A1A519; -.
DR OpenTargets; ENSG00000164334; -.
DR PharmGKB; PA162387167; -.
DR VEuPathDB; HostDB:ENSG00000164334; -.
DR eggNOG; ENOG502TH7F; Eukaryota.
DR GeneTree; ENSGT00940000162220; -.
DR HOGENOM; CLU_062038_2_0_1; -.
DR InParanoid; A1A519; -.
DR OMA; MEEMTLP; -.
DR OrthoDB; 1142827at2759; -.
DR PhylomeDB; A1A519; -.
DR TreeFam; TF337124; -.
DR PathwayCommons; A1A519; -.
DR SignaLink; A1A519; -.
DR BioGRID-ORCS; 340069; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; FAM170A; human.
DR GenomeRNAi; 340069; -.
DR Pharos; A1A519; Tdark.
DR PRO; PR:A1A519; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A1A519; protein.
DR Bgee; ENSG00000164334; Expressed in left testis and 49 other tissues.
DR ExpressionAtlas; A1A519; baseline and differential.
DR Genevisible; A1A519; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Protein FAM170A"
FT /id="PRO_0000326110"
FT ZN_FING 228..252
FT /note="C2H2-type; degenerate"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66LM6"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66LM6"
FT VAR_SEQ 24..70
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032556"
FT VAR_SEQ 25..71
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035475"
FT VAR_SEQ 258..291
FT /note="HVFHLTMAQLTGNMESESTQDEQEEENGNEKEEE -> PKMSRRRKMEMRRR
FT RKRNQKQRRRRGSPQKKTLA (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035476"
FT VAR_SEQ 292..330
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035477"
FT VAR_SEQ 330
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20162441, ECO:0000303|Ref.2"
FT /id="VSP_032557"
FT VARIANT 173
FT /note="P -> S (in dbSNP:rs328694)"
FT /id="VAR_047312"
SQ SEQUENCE 330 AA; 37158 MW; DAE7F2D1E96D90AD CRC64;
MKRRQKRKHL ENEESQETAE KGGGMSKSQE DALQPGSTRV AKGWSQGVGE VTSTSEYCSC
VSSSRKLIHS GIQRIHRDSP QPQSPLAQVQ ERGETPPRSQ HVSLSSYSSY KTCVSSLCVN
KEERGMKIYY MQVQMNKGVA VSWETEETLE SLEKQPRMEE VTLSEVVRVG TPPSDVSTRN
LLSDSEPSGE EKEHEERTES DSLPGSPTVE DTPRAKTPDW LVTMENGFRC MACCRVFTTM
EALQEHVQFG IREGFSCHVF HLTMAQLTGN MESESTQDEQ EEENGNEKEE EEKPEAKEEE
GQPTEEDLGL RRSWSQCPGC VFHSPKDRNS
