位置:首页 > 蛋白库 > TAF1_CAEEL
TAF1_CAEEL
ID   TAF1_CAEEL              Reviewed;        1744 AA.
AC   G5EGM3;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Transcription initiation factor TFIID subunit 1 {ECO:0000250|UniProtKB:P21675};
DE   AltName: Full=TBP-associated transcription factor 1 {ECO:0000312|WormBase:W04A8.7};
GN   Name=taf-1 {ECO:0000312|WormBase:W04A8.7};
GN   ORFNames=W04A8.7 {ECO:0000312|WormBase:W04A8.7};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   NOMENCLATURE.
RX   PubMed=11963920; DOI=10.1101/gad.976402;
RA   Tora L.;
RT   "A unified nomenclature for TATA box binding protein (TBP)-associated
RT   factors (TAFs) involved in RNA polymerase II transcription.";
RL   Genes Dev. 16:673-675(2002).
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=14726532; DOI=10.1074/jbc.m310731200;
RA   Walker A.K., Shi Y., Blackwell T.K.;
RT   "An extensive requirement for transcription factor IID-specific TAF-1 in
RT   Caenorhabditis elegans embryonic transcription.";
RL   J. Biol. Chem. 279:15339-15347(2004).
CC   -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC       role in the initiation of RNA polymerase II (Pol II)-dependent
CC       transcription (By similarity). TFIID recognizes and binds promoters via
CC       its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of
CC       the pre-initiation complex (PIC) (By similarity). The TFIID complex
CC       consists of tbp-1 and TBP-associated factors (TAFs), including taf-1
CC       (By similarity). May regulate RNA polymerase II activity and thereby
CC       may control transcription initiation by RNA polymerase II
CC       (PubMed:14726532). Required for early embryonic development
CC       (PubMed:14726532). Essential for embryonic transcription of several
CC       genes (PubMed:14726532). {ECO:0000250|UniProtKB:P21675,
CC       ECO:0000269|PubMed:14726532}.
CC   -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC       composed of TATA-box-binding protein tbp-1, and a number of TBP-
CC       associated factors (TAFs). {ECO:0000250|UniProtKB:P21675}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14726532}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC       {ECO:0000269|PubMed:14726532}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic arrest
CC       at the 100-cell stage, premature cell division of E2 cells, Ea and Ep,
CC       severe loss of polymerase II large subunit ama-1 phosphorylation and
CC       reduction in the transcription of several embryonic genes.
CC       {ECO:0000269|PubMed:14726532}.
CC   -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284601; CAB04907.3; -; Genomic_DNA.
DR   RefSeq; NP_493426.2; NM_061025.4.
DR   AlphaFoldDB; G5EGM3; -.
DR   SMR; G5EGM3; -.
DR   IntAct; G5EGM3; 1.
DR   STRING; 6239.W04A8.7; -.
DR   EPD; G5EGM3; -.
DR   PaxDb; G5EGM3; -.
DR   PeptideAtlas; G5EGM3; -.
DR   EnsemblMetazoa; W04A8.7.1; W04A8.7.1; WBGene00006382.
DR   GeneID; 173257; -.
DR   KEGG; cel:CELE_W04A8.7; -.
DR   CTD; 173257; -.
DR   WormBase; W04A8.7; CE42634; WBGene00006382; taf-1.
DR   eggNOG; KOG0008; Eukaryota.
DR   GeneTree; ENSGT00940000155242; -.
DR   HOGENOM; CLU_000572_3_1_1; -.
DR   InParanoid; G5EGM3; -.
DR   OMA; DSMAMQM; -.
DR   OrthoDB; 103411at2759; -.
DR   PhylomeDB; G5EGM3; -.
DR   Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-CEL-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-CEL-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-CEL-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-CEL-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   PRO; PR:G5EGM3; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006382; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISS:WormBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISS:WormBase.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:WormBase.
DR   Gene3D; 1.20.920.10; -; 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR040240; TAF1.
DR   InterPro; IPR011177; TAF1_animal.
DR   InterPro; IPR022591; TAF1_HAT_dom.
DR   InterPro; IPR041670; Znf-CCHC_6.
DR   PANTHER; PTHR13900; PTHR13900; 2.
DR   Pfam; PF00439; Bromodomain; 2.
DR   Pfam; PF12157; DUF3591; 1.
DR   Pfam; PF15288; zf-CCHC_6; 1.
DR   PIRSF; PIRSF003047; TAF1_animal; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; SSF47370; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Bromodomain; Coiled coil; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..1744
FT                   /note="Transcription initiation factor TFIID subunit 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000435363"
FT   DOMAIN          1425..1495
FT                   /note="Bromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          1547..1617
FT                   /note="Bromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1666..1702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1714..1744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1019..1080
FT                   /evidence="ECO:0000255"
FT   COILED          1161..1204
FT                   /evidence="ECO:0000255"
FT   COILED          1282..1314
FT                   /evidence="ECO:0000255"
FT   MOTIF           1379..1386
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        8..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..453
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1096
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1371..1385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1670..1695
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1744 AA;  198522 MW;  F3EBA6DE00F5937A CRC64;
     MNNTHHHTNG YRTEKPKNEE DLEDPYANLS DFYKNHPAAR NEACSSASNG GSKSVKMEPK
     VEKNEEFEEY IGDPVRLEDM EPFARPSLRD DAPLSSILHP DLDGIDPRIF FKDFNPNKTL
     RFSRLFAQNI KHTSRAEIWW ASRTFSKHQR KKEPEEPLAD DVIVGAKKLK LNIIEKVPRV
     MLADDEEERM RRPILTDAEE MAKKNEEGTV VQPWRTGPAK IWYDMMNLPM TSQAVNYGFK
     LKKSPQKVSI RSGKPLNYRT PDDLPSTSSG PAPNSAPFLD KVEVIDKSCE ASTSEDILLP
     YQVIEWENDV ILDGEEVKDQ LLEEFSNGRG CGWIPTQYTR TYEHFVYAAN NNAFEQMFDG
     KSAPINLTGP DSAILPTPGH SIFPSAPCDL DILPWETNII WDADAMPSTL EPIDFLVDFQ
     DDPLIYGMPE DRRHDEGPDH HHHHHHHRKD GQYTKKSKMI LGQVQQRQKQ EEDEQMESTM
     AQFTDNDPFN LSNDDYYVPK ATSKTLSNNS LLIQHSTPAT NIATHFFPTH PSAFRLRYWH
     RTPFTRRIVR HWQPMRFQPI QTPVKHQQRV AAMREAMRQA QGGGEVFYMR DVQDLSGKDE
     TLVMIEYSEE HPVILSQPGM ASKMKNYFKR RQANDSEPTF TFGELAFSHQ IPFLGQLQPG
     QSLQSIENML YRAPIYLHKR QNTDFLLIRS MNQWYIRPLP SIFVAGQQCP LYEVPSPNSK
     RATVFVRDFL FAFIYRLFWA SDSSPRRLKM DDVRNAFPHY AESNIRKRLK MCSTFVRQGS
     ETYWSLKPDF RLPSKEEVLS MVTPEMCCAQ YSMMAAEQRL KDAGYGEKYF FTPENDEGSE
     DEVTIEDEIK CAPWNTTRAF LASQREKCLL DQTGIADPTG CGQGFSYVRV SQKPHKDENA
     TPVPKKLVTG TNADLRKLPL KEAKQICRGY GVKEEEISAL TRWEIIDVIR TLSTQAAKAT
     KDGEIIAVSG MARFARGNTR FSSADMQEKY RKHCQRIFDQ QNQTLANTDP ISTDDDSTDA
     DSDNEELASR LESMLEANKG KKNISMSEKA KIDFETEEKE REDLKRMIHG TTNQVEKGEK
     KEEGEVTAEE KKSASQFGED VAMSASKISG ITANQQLKIY RTCKGPDGKD VTRIEIVTRP
     QLIEAYTRIR MTRDDTFIQV YAQMDEQYKE EKRKKKRRLQ DQIRRMKKNE EKAAHKVQKM
     TEKKVKPIKP PNPNLQKMRC SACHAYGHMK TNRNCPLYGK DPLTPLKEED EGSTIMTSVS
     SASLVAPDAV QVDGTKVKFN LNFAEIRKEQ NREEKLKRKL AKMAEAAVRE RQMAHLMEYG
     GGASSSGGAG GGGSGIGGST GGGITDNDDD DRFSQISGTS SFLNGPPGAI RGGNRNSSVS
     GSKRRSSMMP EEDYLQGPLK VAHRARADPK VVMSSMLTDI VNELKMISGS DAFVTPVNSK
     KVVDYYNIIK NPISLQEIKK KISEQSYLLR KDFLDDIKLM FDNSRMYNGD NNILTLTAQQ
     MLQLAGKRMI EREQKFIGLE KQINPLLDTN DLIGFSYLLG EIVQKMKNIP KSALFHTRVD
     PKKIPAYYLK ISDPMDLSIM EQKSKSQEYK SIDEFLKDAE KIYTNSVVFN GAESVYSLKA
     KEMFEMAEML VKDQMDTLGE LERNINPSAI NDAAAAQRGL AMDSDDHMDE MEDHPTEEEE
     EDDDDEIMDD DMDIDATGYS YDHDDNVAVG QIFNDLAMSD SDEDERAEDV KRPANGDDNL
     LDSF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024