TAF1L_HUMAN
ID TAF1L_HUMAN Reviewed; 1826 AA.
AC Q8IZX4; Q0VG57;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transcription initiation factor TFIID subunit 1-like;
DE AltName: Full=TAF(II)210;
DE AltName: Full=TBP-associated factor 1-like;
DE AltName: Full=TBP-associated factor 210 kDa;
DE AltName: Full=Transcription initiation factor TFIID 210 kDa subunit;
GN Name=TAF1L;
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], FUNCTION, AND INTERACTION WITH TBP.
RC TISSUE=Testis;
RX PubMed=12217962; DOI=10.1093/hmg/11.19.2341;
RA Wang P.J., Page D.C.;
RT "Functional substitution for TAF(II)250 by a retroposed homolog that is
RT expressed in human spermatogenesis.";
RL Hum. Mol. Genet. 11:2341-2346(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1523-1654, AND SUBUNIT.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [3]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-47; GLU-171; ALA-256; VAL-371; ASN-532;
RP SER-637; PHE-750; ILE-762; ASP-794; GLN-845; CYS-1016; ASN-1038; ILE-1169;
RP LEU-1312; CYS-1356; SER-1389; VAL-1411; THR-1540; TYR-1549; ASN-1731;
RP LEU-1810 AND GLN-1824.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May act as a functional substitute for TAF1/TAFII250 during
CC male meiosis, when sex chromosomes are transcriptionally silenced.
CC {ECO:0000269|PubMed:12217962}.
CC -!- SUBUNIT: Can bind directly to TATA-box binding protein (TBP). Interacts
CC (via bromo domains) with acetylated lysine residues on the N-terminus
CC of histone H1.4, H2A, H2B, H3 and H4 (in vitro).
CC {ECO:0000269|PubMed:12217962, ECO:0000269|PubMed:22464331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific, expressed apparently in germ
CC cells.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
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DR EMBL; AF390562; AAN40840.1; -; mRNA.
DR CCDS; CCDS35003.1; -.
DR RefSeq; NP_722516.1; NM_153809.2.
DR PDB; 3HMH; X-ray; 2.05 A; A=1523-1654.
DR PDB; 5IGL; X-ray; 2.10 A; A=1523-1654.
DR PDBsum; 3HMH; -.
DR PDBsum; 5IGL; -.
DR AlphaFoldDB; Q8IZX4; -.
DR SMR; Q8IZX4; -.
DR BioGRID; 126514; 15.
DR IntAct; Q8IZX4; 6.
DR MINT; Q8IZX4; -.
DR STRING; 9606.ENSP00000418379; -.
DR BindingDB; Q8IZX4; -.
DR ChEMBL; CHEMBL3108641; -.
DR iPTMnet; Q8IZX4; -.
DR PhosphoSitePlus; Q8IZX4; -.
DR BioMuta; TAF1L; -.
DR DMDM; 57013082; -.
DR EPD; Q8IZX4; -.
DR jPOST; Q8IZX4; -.
DR MassIVE; Q8IZX4; -.
DR MaxQB; Q8IZX4; -.
DR PaxDb; Q8IZX4; -.
DR PeptideAtlas; Q8IZX4; -.
DR PRIDE; Q8IZX4; -.
DR ProteomicsDB; 71440; -.
DR Antibodypedia; 25077; 68 antibodies from 22 providers.
DR DNASU; 138474; -.
DR Ensembl; ENST00000242310.4; ENSP00000418379.1; ENSG00000122728.6.
DR GeneID; 138474; -.
DR KEGG; hsa:138474; -.
DR MANE-Select; ENST00000242310.4; ENSP00000418379.1; NM_153809.2; NP_722516.1.
DR UCSC; uc003zrg.1; human.
DR CTD; 138474; -.
DR DisGeNET; 138474; -.
DR GeneCards; TAF1L; -.
DR HGNC; HGNC:18056; TAF1L.
DR HPA; ENSG00000122728; Group enriched (retina, testis).
DR MIM; 607798; gene.
DR neXtProt; NX_Q8IZX4; -.
DR OpenTargets; ENSG00000122728; -.
DR PharmGKB; PA134947802; -.
DR VEuPathDB; HostDB:ENSG00000122728; -.
DR eggNOG; KOG0008; Eukaryota.
DR GeneTree; ENSGT00940000155242; -.
DR HOGENOM; CLU_000572_3_0_1; -.
DR InParanoid; Q8IZX4; -.
DR OMA; RENVRKC; -.
DR OrthoDB; 103411at2759; -.
DR PhylomeDB; Q8IZX4; -.
DR TreeFam; TF313573; -.
DR PathwayCommons; Q8IZX4; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; Q8IZX4; -.
DR BioGRID-ORCS; 138474; 15 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; Q8IZX4; -.
DR GenomeRNAi; 138474; -.
DR Pharos; Q8IZX4; Tchem.
DR PRO; PR:Q8IZX4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IZX4; protein.
DR Bgee; ENSG00000122728; Expressed in sperm and 8 other tissues.
DR Genevisible; Q8IZX4; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
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; IPI:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.1100.10; -; 1.
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; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
DR InterPro; IPR041670; Znf-CCHC_6.
DR PANTHER; PTHR13900; PTHR13900; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF09247; TBP-binding; 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; SSF47055; SSF47055; 1.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bromodomain; Cell cycle; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1826
FT /note="Transcription initiation factor TFIID subunit 1-
FT like"
FT /id="PRO_0000211217"
FT DOMAIN 1416..1486
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1539..1609
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 118..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1370..1377
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1664..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 47
FT /note="G -> A (in a lung small cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041934"
FT VARIANT 171
FT /note="Q -> E (in dbSNP:rs56352331)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041935"
FT VARIANT 256
FT /note="G -> A (in dbSNP:rs55991718)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041936"
FT VARIANT 371
FT /note="M -> V (in dbSNP:rs17219559)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041937"
FT VARIANT 532
FT /note="I -> N (in dbSNP:rs56128445)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041938"
FT VARIANT 637
FT /note="P -> S (in dbSNP:rs56157814)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041939"
FT VARIANT 750
FT /note="L -> F (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041940"
FT VARIANT 762
FT /note="L -> I (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041941"
FT VARIANT 794
FT /note="E -> D (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041942"
FT VARIANT 845
FT /note="R -> Q (in dbSNP:rs34787787)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041943"
FT VARIANT 1016
FT /note="R -> C (in dbSNP:rs35905429)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041944"
FT VARIANT 1038
FT /note="K -> N (in dbSNP:rs55767137)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041945"
FT VARIANT 1169
FT /note="T -> I (in dbSNP:rs55976674)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041946"
FT VARIANT 1312
FT /note="V -> L (in dbSNP:rs55824107)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041947"
FT VARIANT 1356
FT /note="R -> C (in dbSNP:rs56107531)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041948"
FT VARIANT 1389
FT /note="P -> S (in dbSNP:rs56393725)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041949"
FT VARIANT 1411
FT /note="I -> V (in dbSNP:rs34500740)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041950"
FT VARIANT 1540
FT /note="A -> T (in dbSNP:rs55782058)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041951"
FT VARIANT 1549
FT /note="H -> Y (in a glioblastoma multiforme sample; somatic
FT mutation; dbSNP:rs1587670372)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041952"
FT VARIANT 1731
FT /note="K -> N (in dbSNP:rs34241003)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041953"
FT VARIANT 1805
FT /note="I -> V (in dbSNP:rs16918393)"
FT /id="VAR_048435"
FT VARIANT 1810
FT /note="P -> L (in dbSNP:rs56342342)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041954"
FT VARIANT 1824
FT /note="H -> Q (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041955"
FT HELIX 1523..1536
FT /evidence="ECO:0007829|PDB:3HMH"
FT TURN 1537..1540
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1545..1547
FT /evidence="ECO:0007829|PDB:3HMH"
FT TURN 1553..1555
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1557..1562
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1569..1577
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1584..1602
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1607..1625
FT /evidence="ECO:0007829|PDB:3HMH"
FT HELIX 1627..1649
FT /evidence="ECO:0007829|PDB:3HMH"
SQ SEQUENCE 1826 AA; 207302 MW; 35D780E749AC9B17 CRC64;
MRPGCDLLLR AAATVTAAIM SDSDSEEDSS GGGPFTLAGI LFGNISGAGQ LEGESVLDDE
CKKHLAGLGA LGLGSLITEL TANEELTGTG GALVNDEGWI RSTEDAVDYS DINEVAEDES
QRHQQTMGSL QPLYHSDYDE DDYDADCEDI DCKLMPPPPP PPGPMKKDKD QDAITCVSES
GEDIILPSII APSFLASEKV DFSSYSDSES EMGPQEATQA ESEDGKLTLP LAGIMQHDAT
KLLPSVTELF PEFRPGKVLR FLHLFGPGKN VPSVWRSARR KRKKHRELIQ EEQIQEVECS
VESEVSQKSL WNYDYAPPPP PEQCLADDEI TMMVPVESKF SQSTGDVDKV TDTKPRVAEW
RYGPARLWYD MLGVSEDGSG FDYGFKLRKT QHEPVIKSRM MEEFRKLEES NGTDLLADEN
FLMVTQLHWE DSIIWDGEDI KHKGTKPQGA SLAGWLPSIK TRNVMAYNVQ QGFAPTLDDD
KPWYSIFPID NEDLVYGRWE DNIIWDAQAM PRLLEPPVLA LDPNDENLIL EIPDEKEEAT
SNSPSKESKK ESSLKKSRIL LGKTGVIREE PQQNMSQPEV KDPWNLSNDE YYFPKQQGLR
GTFGGNIIQH SIPAMELWQP FFPTHMGPIK IRQFHRPPLK KYSFGALSQP GPHSVQPLLK
HIKKKAKMRE QERQASGGGE LFFMRTPQDL TGKDGDLILA EYSEENGPLM MQVGMATKIK
NYYKRKPGKD PGAPDCKYGE TVYCHTSPFL GSLHPGQLLQ ALENNLFRAP VYLHKMPETD
FLIIRTRQGY YIRELVDIFV VGQQCPLFEV PGPNSRRANM HIRDFLQVFI YRLFWKSKDR
PRRIRMEDIK KAFPSHSESS IRKRLKLCAD FKRTGMDSNW WVLKSDFRLP TEEEIRAKVS
PEQCCAYYSM IAAKQRLKDA GYGEKSFFAP EEENEEDFQM KIDDEVHAAP WNTTRAFIAA
MKGKCLLEVT GVADPTGCGE GFSYVKIPNK PTQQKDDKEP QAVKKTVTGT DADLRRLSLK
NAKQLLRKFG VPEEEIKKLS RWEVIDVVRT MSTEQAHSGE GPMSKFARGS RFSVAEHQER
YKEECQRIFD LQNKVLSSTE VLSTDTDSIS AEDSDFEEMG KNIENMLQNK KTSSQLSREW
EEQERKELRR MLLVAGSAAS GNNHRDDVTA SMTSLKSSAT GHCLKIYRTF RDEEGKEYVR
CETVRKPAVI DAYVRIRTTK DEKFIQKFAL FDEKHREEMR KERRRIQEQL RRLKRNQEKE
KLKGPPEKKP KKMKERPDLK LKCGACGAIG HMRTNKFCPL YYQTNVPPSK PVAMTEEQEE
ELEKTVIHND NEELIKVEGT KIVFGKQLIE NVHEVRRKSL VLKFPKQQLP PKKKRRVGTT
VHCDYLNIPH KSIHRRRTDP MVTLSSILES IINDMRDLPN THPFHTPVNA KVVKDYYKII
TRPMDLQTLR ENVRKCLYPS REEFREHLEL IVKNSATYNG PKHSLTQISQ SMLDLCDEKL
KEKEDKLARL EKAINPLLDD DDQVAFSFIL DNIVTQKMMA VPDSWPFHHP VNKKFVPDYY
KMIVNPVDLE TIRKNISKHK YQSRESFLDD VNLILANSVK YNGPESQYTK TAQEIVNICY
QTITEYDEHL TQLEKDICTA KEAALEEAEL ESLDPMTPGP YTSQPPDMYD TNTSLSTSRD
ASVFQDESNL SVLDISTATP EKQMCQGQGR LGEEDSDVDV EGYDDEEEDG KPKPPAPEGG
DGDLADEEEG TVQQPEASVL YEDLLISEGE DDEEDAGSDE EGDNPFSAIQ LSESGSDSDV
GYGGIRPKQP FMLQHASGEH KDGHGK