HTSF1_HUMAN
ID HTSF1_HUMAN Reviewed; 755 AA.
AC O43719; D3DWG9; Q59G06; Q99730;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=HIV Tat-specific factor 1;
DE Short=Tat-SF1;
GN Name=HTATSF1;
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], PROTEIN SEQUENCE OF 26-45; 62-79; 155-169;
RP 199-210; 239-245 AND 410-428, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Promyelocytic leukemia;
RX PubMed=8849451; DOI=10.1126/science.274.5287.605;
RA Zhou Q., Sharp P.A.;
RT "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1
RT Tat.";
RL Science 274:605-610(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-478.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Choriocarcinoma;
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 [7]
RP INTERACTION WITH CDK9.
RX PubMed=9649438; DOI=10.1093/emboj/17.13.3681;
RA Zhou Q., Chen D., Pierstorff E., Luo K.;
RT "Transcription elongation factor P-TEFb mediates Tat activation of HIV-1
RT transcription at multiple stages.";
RL EMBO J. 17:3681-3691(1998).
RN [8]
RP FUNCTION.
RX PubMed=9765201; DOI=10.1101/gad.12.19.2992;
RA Li X.-Y., Green M.R.;
RT "The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription
RT elongation factor.";
RL Genes Dev. 12:2992-2996(1998).
RN [9]
RP INTERACTION WITH SF3A2.
RX PubMed=9710584; DOI=10.1128/mcb.18.9.5000;
RA Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.;
RT "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2
RT through an unusual RNA recognition motif.";
RL Mol. Cell. Biol. 18:5000-5009(1998).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH NCL; CCNT1; RNA POLYMERASE
RP II; SUPT5H AND CDK9.
RX PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
RA Parada C.A., Roeder R.G.;
RT "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-
RT 1 transcription.";
RL EMBO J. 18:3688-3701(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH GTF2F2; SUPT5H AND POLR2A.
RX PubMed=10454543; DOI=10.1128/mcb.19.9.5960;
RA Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
RT "Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
RL Mol. Cell. Biol. 19:5960-5968(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH CCNT1.
RX PubMed=10913173; DOI=10.1128/mcb.20.16.5897-5907.2000;
RA Fong Y.W., Zhou Q.;
RT "Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for
RT assembly of a multicomponent transcription elongation complex at the human
RT immunodeficiency virus type 1 promoter.";
RL Mol. Cell. Biol. 20:5897-5907(2000).
RN [13]
RP FUNCTION.
RX PubMed=11420046; DOI=10.1016/s1074-7613(01)00158-3;
RA Simmons A., Aluvihare V., McMichael A.;
RT "Nef triggers a transcriptional program in T cells imitating single-signal
RT T cell activation and inducing HIV virulence mediators.";
RL Immunity 14:763-777(2001).
RN [14]
RP FUNCTION, MUTAGENESIS OF TYR-136, INTERACTION WITH U SNRNPS AND CCNT1, AND
RP DOMAIN.
RX PubMed=11780068; DOI=10.1038/414929a;
RA Fong Y.W., Zhou Q.;
RT "Stimulatory effect of splicing factors on transcriptional elongation.";
RL Nature 414:929-933(2001).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TCERG1, AND
RP SUBCELLULAR LOCATION.
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 [16]
RP FUNCTION.
RX PubMed=15905670; DOI=10.1097/01.aids.0000171403.07995.92;
RA Misse D., Gajardo J., Oblet C., Religa A., Riquet N., Mathieu D., Yssel H.,
RA Veas F.;
RT "Soluble HIV-1 gp120 enhances HIV-1 replication in non-dividing CD4+ T
RT cells, mediated via cell signaling and Tat cofactor overexpression.";
RL AIDS 19:897-905(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-557; SER-561;
RP SER-579; SER-597; SER-600; SER-616; SER-624; SER-642; SER-676; SER-702;
RP SER-713 AND SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-453; SER-498;
RP SER-642; SER-713 AND SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-616; SER-624;
RP SER-642 AND SER-676, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-702; SER-713 AND
RP SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-403; SER-407;
RP SER-445; SER-498; SER-579; SER-616; SER-624; THR-633; SER-642; SER-676;
RP SER-702; SER-713; SER-714 AND SER-721, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-485; SER-579;
RP SER-597; SER-600; SER-607; SER-616; SER-642; SER-676; SER-702; SER-713;
RP SER-714 AND SER-721, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-481; SER-494;
RP SER-498; SER-521; SER-529; SER-579; SER-616; SER-624; SER-642; SER-676;
RP SER-702; SER-713; SER-714 AND SER-721, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-642 AND SER-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429 AND LYS-430, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [30]
RP STRUCTURE BY NMR OF 256-354.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM_1 domain of HIV Tat specific factor 1
RT variant.";
RL Submitted (SEP-2006) to the PDB data bank.
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. In case
CC of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and
CC gp120, acts as a cofactor required for the Tat-enhanced transcription
CC of the virus. {ECO:0000269|PubMed:10393184,
CC ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173,
CC ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:11780068,
CC ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451,
CC ECO:0000269|PubMed:9765201}.
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 TCERG1/CA150. Interacts with SF3A2/SAP62 and
CC the spliceosomal U small nuclear ribonucleoproteins (snRNPs).
CC {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10454543,
CC ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11780068,
CC ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:9649438,
CC ECO:0000269|PubMed:9710584}.
CC -!- INTERACTION:
CC O43719; O75533-1: SF3B1; NbExp=6; IntAct=EBI-720468, EBI-15565798;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15485897,
CC ECO:0000269|PubMed:8849451}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8849451}.
CC -!- DOMAIN: The RRM domains mediate interaction with U snRNPs.
CC {ECO:0000269|PubMed:11780068}.
CC -!- SIMILARITY: Belongs to the HTATSF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18823.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U76992; AAB18823.1; ALT_FRAME; mRNA.
DR EMBL; BT006886; AAP35532.1; -; mRNA.
DR EMBL; AB209303; BAD92540.1; ALT_INIT; mRNA.
DR EMBL; Z97632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471150; EAW88468.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88469.1; -; Genomic_DNA.
DR EMBL; BC009896; AAH09896.1; -; mRNA.
DR CCDS; CCDS14657.1; -.
DR RefSeq; NP_001156752.1; NM_001163280.1.
DR RefSeq; NP_055315.2; NM_014500.4.
DR RefSeq; XP_005262461.1; XM_005262404.3.
DR PDB; 2DIT; NMR; -; A=256-354.
DR PDB; 6N3D; X-ray; 1.13 A; A=260-353.
DR PDB; 6N3E; X-ray; 1.89 A; A=260-353.
DR PDB; 6N3F; X-ray; 2.10 A; A/C=260-353.
DR PDB; 6NSX; X-ray; 2.00 A; A=260-353.
DR PDB; 6Y50; EM; 4.10 A; q=1-755.
DR PDB; 6Y53; EM; 7.10 A; q=1-755.
DR PDB; 6Y5Q; EM; 7.10 A; q=1-755.
DR PDB; 7Q3L; EM; 2.30 A; q=2-755.
DR PDBsum; 2DIT; -.
DR PDBsum; 6N3D; -.
DR PDBsum; 6N3E; -.
DR PDBsum; 6N3F; -.
DR PDBsum; 6NSX; -.
DR PDBsum; 6Y50; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7Q3L; -.
DR AlphaFoldDB; O43719; -.
DR SMR; O43719; -.
DR BioGRID; 118149; 105.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; O43719; -.
DR DIP; DIP-42095N; -.
DR IntAct; O43719; 45.
DR MINT; O43719; -.
DR STRING; 9606.ENSP00000442699; -.
DR GlyGen; O43719; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43719; -.
DR MetOSite; O43719; -.
DR PhosphoSitePlus; O43719; -.
DR BioMuta; HTATSF1; -.
DR EPD; O43719; -.
DR jPOST; O43719; -.
DR MassIVE; O43719; -.
DR MaxQB; O43719; -.
DR PaxDb; O43719; -.
DR PeptideAtlas; O43719; -.
DR PRIDE; O43719; -.
DR ProteomicsDB; 49133; -.
DR Antibodypedia; 375; 284 antibodies from 34 providers.
DR DNASU; 27336; -.
DR Ensembl; ENST00000218364.5; ENSP00000218364.4; ENSG00000102241.12.
DR Ensembl; ENST00000535601.5; ENSP00000442699.1; ENSG00000102241.12.
DR GeneID; 27336; -.
DR KEGG; hsa:27336; -.
DR MANE-Select; ENST00000218364.5; ENSP00000218364.4; NM_014500.5; NP_055315.2.
DR UCSC; uc004ezw.4; human.
DR CTD; 27336; -.
DR GeneCards; HTATSF1; -.
DR HGNC; HGNC:5276; HTATSF1.
DR HPA; ENSG00000102241; Low tissue specificity.
DR MIM; 300346; gene.
DR neXtProt; NX_O43719; -.
DR OpenTargets; ENSG00000102241; -.
DR PharmGKB; PA29540; -.
DR VEuPathDB; HostDB:ENSG00000102241; -.
DR eggNOG; KOG1548; Eukaryota.
DR GeneTree; ENSGT00390000009902; -.
DR HOGENOM; CLU_406872_0_0_1; -.
DR InParanoid; O43719; -.
DR OMA; CAKFGQI; -.
DR OrthoDB; 1542889at2759; -.
DR PhylomeDB; O43719; -.
DR TreeFam; TF313623; -.
DR PathwayCommons; O43719; -.
DR SignaLink; O43719; -.
DR BioGRID-ORCS; 27336; 349 hits in 714 CRISPR screens.
DR ChiTaRS; HTATSF1; human.
DR EvolutionaryTrace; O43719; -.
DR GeneWiki; HTATSF1; -.
DR GenomeRNAi; 27336; -.
DR Pharos; O43719; Tbio.
DR PRO; PR:O43719; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43719; protein.
DR Bgee; ENSG00000102241; Expressed in sural nerve and 216 other tissues.
DR ExpressionAtlas; O43719; baseline and differential.
DR Genevisible; O43719; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
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; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
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; 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 SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..755
FT /note="HIV Tat-specific factor 1"
FT /id="PRO_0000248604"
FT DOMAIN 133..218
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 264..349
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..755
FT /note="Mediates interaction with the P-TEFb complex"
FT REGION 433..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..651
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..717
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 297
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGC0"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGC0"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 478
FT /note="G -> A (in dbSNP:rs2071913)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_027362"
FT VARIANT 526
FT /note="N -> T (in dbSNP:rs12852634)"
FT /id="VAR_052206"
FT VARIANT 678
FT /note="D -> G (in dbSNP:rs17339410)"
FT /id="VAR_052207"
FT MUTAGEN 136
FT /note="Y->D: Loss of interaction with U snRNPs."
FT /evidence="ECO:0000269|PubMed:11780068"
FT CONFLICT 125
FT /note="F -> V (in Ref. 3; BAD92540)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="V -> I (in Ref. 3; BAD92540)"
FT /evidence="ECO:0000305"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:6N3D"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:6N3D"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6N3D"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:6N3D"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6N3D"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6N3D"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:6N3D"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:6N3D"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:6N3D"
SQ SEQUENCE 755 AA; 85853 MW; C9CA6C89E4F2A319 CRC64;
MSGTNLDGND EFDEQLRMQE LYGDGKDGDT QTDAGGEPDS LGQQPTDTPY EWDLDKKAWF
PKITEDFIAT YQANYGFSND GASSSTANVE DVHARTAEEP PQEKAPEPTD ARKKGEKRKA
ESGWFHVEED RNTNVYVSGL PPDITVDEFI QLMSKFGIIM RDPQTEEFKV KLYKDNQGNL
KGDGLCCYLK RESVELALKL LDEDEIRGYK LHVEVAKFQL KGEYDASKKK KKCKDYKKKL
SMQQKQLDWR PERRAGPSRM RHERVVIIKN MFHPMDFEDD PLVLNEIRED LRVECSKFGQ
IRKLLLFDRH PDGVASVSFR DPEEADYCIQ TLDGRWFGGR QITAQAWDGT TDYQVEETSR
EREERLRGWE AFLNAPEANR GLRRSDSVSA SERAGPSRAR HFSEHPSTSK MNAQETATGM
AFEEPIDEKK FEKTEDGGEF EEGASENNAK ESSPEKEAEE GCPEKESEEG CPKRGFEGSC
SQKESEEGNP VRGSEEDSPK KESKKKTLKN DCEENGLAKE SEDDLNKESE EEVGPTKESE
EDDSEKESDE DCSEKQSEDG SEREFEENGL EKDLDEEGSE KELHENVLDK ELEENDSENS
EFEDDGSEKV LDEEGSEREF DEDSDEKEEE EDTYEKVFDD ESDEKEDEEY ADEKGLEAAD
KKAEEGDADE KLFEESDDKE DEDADGKEVE DADEKLFEDD DSNEKLFDEE EDSSEKLFDD
SDERGTLGGF GSVEEGPLST GSSFILSSDD DDDDI
