HTSF1_MOUSE
ID HTSF1_MOUSE Reviewed; 757 AA.
AC Q8BGC0; B1AVC7; Q1WWK0; Q9CT41; Q9DAU3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=HIV Tat-specific factor 1 homolog;
GN Name=Htatsf1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP INTERACTION WITH TCERG1.
RX PubMed=15485897; DOI=10.1128/mcb.24.21.9274-9285.2004;
RA Smith M.J., Kulkarni S., Pawson T.;
RT "FF domains of CA150 bind transcription and splicing factors through
RT multiple weak interactions.";
RL Mol. Cell. Biol. 24:9274-9285(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-621; SER-705 AND
RP SER-724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; SER-441; SER-613;
RP SER-621; SER-645; SER-705 AND SER-724, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Functions as a general transcription factor playing a role in
CC the process of transcriptional elongation. May mediate the reciprocal
CC stimulatory effect of splicing on transcriptional elongation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin. Interacts with GTF2F2/RAP30
CC and POLR2A. Interacts with SF3A2/SAP62 and the spliceosomal U small
CC nuclear ribonucleoproteins (snRNPs) (By similarity). Interacts with
CC TCERG1/CA150. {ECO:0000250, ECO:0000269|PubMed:15485897}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGC0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGC0-2; Sequence=VSP_020332, VSP_020333;
CC -!- DOMAIN: The RRM domains mediate interaction with U snRNPs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HTATSF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI14589.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI14590.1; Type=Erroneous initiation; Evidence={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; AK005527; BAB24100.1; -; mRNA.
DR EMBL; AK011234; BAB27483.1; -; mRNA.
DR EMBL; AK049495; BAC33777.1; -; mRNA.
DR EMBL; AL672263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037711; AAH37711.1; -; mRNA.
DR EMBL; BC114588; AAI14589.1; ALT_INIT; mRNA.
DR EMBL; BC114589; AAI14590.1; ALT_INIT; mRNA.
DR CCDS; CCDS40983.1; -. [Q8BGC0-1]
DR RefSeq; NP_082518.1; NM_028242.2. [Q8BGC0-1]
DR RefSeq; NP_083647.1; NM_029371.1. [Q8BGC0-1]
DR AlphaFoldDB; Q8BGC0; -.
DR BioGRID; 215380; 68.
DR DIP; DIP-46367N; -.
DR IntAct; Q8BGC0; 2.
DR STRING; 10090.ENSMUSP00000086027; -.
DR iPTMnet; Q8BGC0; -.
DR PhosphoSitePlus; Q8BGC0; -.
DR EPD; Q8BGC0; -.
DR jPOST; Q8BGC0; -.
DR MaxQB; Q8BGC0; -.
DR PaxDb; Q8BGC0; -.
DR PeptideAtlas; Q8BGC0; -.
DR PRIDE; Q8BGC0; -.
DR ProteomicsDB; 273284; -. [Q8BGC0-1]
DR ProteomicsDB; 273285; -. [Q8BGC0-2]
DR Antibodypedia; 375; 284 antibodies from 34 providers.
DR DNASU; 72459; -.
DR Ensembl; ENSMUST00000088652; ENSMUSP00000086027; ENSMUSG00000067873. [Q8BGC0-1]
DR Ensembl; ENSMUST00000114751; ENSMUSP00000110399; ENSMUSG00000067873. [Q8BGC0-2]
DR GeneID; 72459; -.
DR KEGG; mmu:72459; -.
DR UCSC; uc009tgv.2; mouse. [Q8BGC0-2]
DR UCSC; uc009tgw.2; mouse. [Q8BGC0-1]
DR CTD; 27336; -.
DR MGI; MGI:1919709; Htatsf1.
DR VEuPathDB; HostDB:ENSMUSG00000067873; -.
DR eggNOG; KOG1548; Eukaryota.
DR GeneTree; ENSGT00390000009902; -.
DR HOGENOM; CLU_026945_4_0_1; -.
DR InParanoid; Q8BGC0; -.
DR OMA; CAKFGQI; -.
DR OrthoDB; 1542889at2759; -.
DR PhylomeDB; Q8BGC0; -.
DR TreeFam; TF313623; -.
DR BioGRID-ORCS; 72459; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Htatsf1; mouse.
DR PRO; PR:Q8BGC0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BGC0; protein.
DR Bgee; ENSMUSG00000067873; Expressed in pituitary gland and 259 other tissues.
DR Genevisible; Q8BGC0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd12281; RRM1_TatSF1_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034393; TatSF1-like.
DR InterPro; IPR034392; TatSF1-like_RRM1.
DR PANTHER; PTHR15608; PTHR15608; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT CHAIN 2..757
FT /note="HIV Tat-specific factor 1 homolog"
FT /id="PRO_0000248605"
FT DOMAIN 134..219
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 265..350
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..757
FT /note="Mediates interaction with the P-TEFb complex"
FT /evidence="ECO:0000250"
FT REGION 383..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..691
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT VAR_SEQ 192..195
FT /note="KESV -> VFSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020332"
FT VAR_SEQ 196..757
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020333"
SQ SEQUENCE 757 AA; 86240 MW; AC84BE3125EC253E CRC64;
MSGNNLSGND EFDEQLRMQE LYGGDPKEGD TQNEPSGEAH SLGQPPDDTP YEWDLDKKAW
FPKITEDFIA TYQANYGFSS DGASSSTANV QDANTKAVEE PPQKEVPETP DSKRKGEKRK
AESGWFHVEE DRNTNVYVSG LPPDITVDEF IQLMSKFGII MRDPQTEEFK VKLYKDDQGN
LKGDGLCCYL KKESVELALK LLDEDEIRGY KLHVEVAKFQ LKGEYDASKK KKKCKDYKKK
LSLQQKQLDW RPERRAGPNR LRHERVVILK NMFHPMDFED DPLVLNEIRE DLRVECSKFG
QIRKLLLFDR HPDGVASVSF REPEEADHCI QTLDGRWFGG RQITAQAWDG TTDYQVEETS
REREERLRGW EAFLNAPEAS RGLRRMDSIA GSERPGPSRM RHFSEHPSMS NMKAQEATTG
MAFEETIDEN KFEKAEEGGE SEGDASEKDA KEGGSDGDHP EREGGEGCSK KENEEGCPER
ALEPEEGNPQ TEAQENGPER EARKKSKMDY EKNGFSKESE DNDLGKESEG EDSLKKESED
DDSEEESEED SSEKQSQDGS DKEIEENGVK KDVDQDVSDK EFPEDVEKES EENETDKSEF
DEGSERVLDE EGSEREFEED SDEKEEEGDD DEEEVVYERV FDDDSDDIEE EEEADEKECE
DADDKEEDND IDEKLFDDSD EKEDEEDTDG KKDDDASDKV FEDNSNEKLF DEEEGPNEKL
FDDSDERGTV GNVKEDGSQS TDSSFALSSS DDDDDEV
