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Protein

HIV Tat-specific factor 1

Gene

HTATSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus.8 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: GO_Central

GO - Biological processi

  • mRNA splicing, via spliceosome Source: GO_Central
  • regulation of DNA-templated transcription, elongation Source: ProtInc
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral genome replication Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
HIV Tat-specific factor 1
Short name:
Tat-SF1
Gene namesi
Name:HTATSF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:5276. HTATSF1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • U2 snRNP Source: GO_Central
  • U2-type spliceosomal complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi136 – 1361Y → D: Loss of interaction with U snRNPs. 1 Publication

Organism-specific databases

PharmGKBiPA29540.

Polymorphism and mutation databases

BioMutaiHTATSF1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 755754HIV Tat-specific factor 1PRO_0000248604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei297 – 2971N6-acetyllysineBy similarity
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei445 – 4451PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources
Modified residuei453 – 4531PhosphoserineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei498 – 4981PhosphoserineCombined sources
Modified residuei557 – 5571PhosphoserineCombined sources
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources
Modified residuei597 – 5971PhosphoserineCombined sources
Modified residuei600 – 6001PhosphoserineCombined sources
Modified residuei607 – 6071PhosphoserineCombined sources
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei624 – 6241PhosphoserineCombined sources
Modified residuei633 – 6331PhosphothreonineCombined sources
Modified residuei642 – 6421PhosphoserineCombined sources
Modified residuei676 – 6761PhosphoserineCombined sources
Modified residuei702 – 7021PhosphoserineCombined sources
Modified residuei713 – 7131PhosphoserineCombined sources
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei721 – 7211PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43719.
MaxQBiO43719.
PaxDbiO43719.
PeptideAtlasiO43719.
PRIDEiO43719.

PTM databases

iPTMnetiO43719.
PhosphoSiteiO43719.

Miscellaneous databases

PMAP-CutDBO43719.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiO43719.
CleanExiHS_HTATSF1.
ExpressionAtlasiO43719. baseline and differential.
GenevisibleiO43719. HS.

Organism-specific databases

HPAiHPA000504.

Interactioni

Subunit structurei

Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts with GTF2F2/RAP30 and POLR2A. Interacts with TCERG1/CA150. Interacts with SF3A2/SAP62 and the spliceosomal U small nuclear ribonucleoproteins (snRNPs).7 Publications

Protein-protein interaction databases

BioGridi118149. 45 interactions.
DIPiDIP-42095N.
IntActiO43719. 16 interactions.
MINTiMINT-1193787.
STRINGi9606.ENSP00000218364.

Structurei

Secondary structure

1
755
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi265 – 2717Combined sources
Helixi276 – 2794Combined sources
Helixi282 – 29413Combined sources
Helixi295 – 2973Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi315 – 3184Combined sources
Helixi322 – 33110Combined sources
Beta strandi343 – 3464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DITNMR-A256-354[»]
ProteinModelPortaliO43719.
SMRiO43719. Positions 257-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43719.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 21886RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini264 – 34986RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni381 – 755375Mediates interaction with the P-TEFb complexAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi228 – 2347Poly-Lys
Compositional biasi423 – 754332Asp/Glu-rich (acidic)Add
BLAST

Domaini

The RRM domains mediate interaction with U snRNPs.1 Publication

Sequence similaritiesi

Belongs to the HTATSF1 family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1548. Eukaryota.
ENOG410YD7P. LUCA.
GeneTreeiENSGT00390000009902.
HOGENOMiHOG000049201.
HOVERGENiHBG059454.
InParanoidiO43719.
KOiK13093.
OMAiQITAEAW.
OrthoDBiEOG7VHSZQ.
PhylomeDBiO43719.
TreeFamiTF313623.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTNLDGND EFDEQLRMQE LYGDGKDGDT QTDAGGEPDS LGQQPTDTPY
60 70 80 90 100
EWDLDKKAWF PKITEDFIAT YQANYGFSND GASSSTANVE DVHARTAEEP
110 120 130 140 150
PQEKAPEPTD ARKKGEKRKA ESGWFHVEED RNTNVYVSGL PPDITVDEFI
160 170 180 190 200
QLMSKFGIIM RDPQTEEFKV KLYKDNQGNL KGDGLCCYLK RESVELALKL
210 220 230 240 250
LDEDEIRGYK LHVEVAKFQL KGEYDASKKK KKCKDYKKKL SMQQKQLDWR
260 270 280 290 300
PERRAGPSRM RHERVVIIKN MFHPMDFEDD PLVLNEIRED LRVECSKFGQ
310 320 330 340 350
IRKLLLFDRH PDGVASVSFR DPEEADYCIQ TLDGRWFGGR QITAQAWDGT
360 370 380 390 400
TDYQVEETSR EREERLRGWE AFLNAPEANR GLRRSDSVSA SERAGPSRAR
410 420 430 440 450
HFSEHPSTSK MNAQETATGM AFEEPIDEKK FEKTEDGGEF EEGASENNAK
460 470 480 490 500
ESSPEKEAEE GCPEKESEEG CPKRGFEGSC SQKESEEGNP VRGSEEDSPK
510 520 530 540 550
KESKKKTLKN DCEENGLAKE SEDDLNKESE EEVGPTKESE EDDSEKESDE
560 570 580 590 600
DCSEKQSEDG SEREFEENGL EKDLDEEGSE KELHENVLDK ELEENDSENS
610 620 630 640 650
EFEDDGSEKV LDEEGSEREF DEDSDEKEEE EDTYEKVFDD ESDEKEDEEY
660 670 680 690 700
ADEKGLEAAD KKAEEGDADE KLFEESDDKE DEDADGKEVE DADEKLFEDD
710 720 730 740 750
DSNEKLFDEE EDSSEKLFDD SDERGTLGGF GSVEEGPLST GSSFILSSDD

DDDDI
Length:755
Mass (Da):85,853
Last modified:June 1, 1998 - v1
Checksum:iC9CA6C89E4F2A319
GO

Sequence cautioni

The sequence AAB18823.1 differs from that shown. Reason: Frameshift at positions 383, 391 and 393. Curated
The sequence BAD92540.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251F → V in BAD92540 (Ref. 3) Curated
Sequence conflicti587 – 5871V → I in BAD92540 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti478 – 4781G → A.1 Publication
Corresponds to variant rs2071913 [ dbSNP | Ensembl ].
VAR_027362
Natural varianti526 – 5261N → T.
Corresponds to variant rs12852634 [ dbSNP | Ensembl ].
VAR_052206
Natural varianti678 – 6781D → G.
Corresponds to variant rs17339410 [ dbSNP | Ensembl ].
VAR_052207

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76992 mRNA. Translation: AAB18823.1. Frameshift.
BT006886 mRNA. Translation: AAP35532.1.
AB209303 mRNA. Translation: BAD92540.1. Different initiation.
Z97632 Genomic DNA. Translation: CAB10730.1.
CH471150 Genomic DNA. Translation: EAW88468.1.
CH471150 Genomic DNA. Translation: EAW88469.1.
BC009896 mRNA. Translation: AAH09896.1.
CCDSiCCDS14657.1.
RefSeqiNP_001156752.1. NM_001163280.1.
NP_055315.2. NM_014500.4.
XP_005262461.1. XM_005262404.3.
UniGeneiHs.204475.

Genome annotation databases

EnsembliENST00000218364; ENSP00000218364; ENSG00000102241.
ENST00000535601; ENSP00000442699; ENSG00000102241.
GeneIDi27336.
KEGGihsa:27336.
UCSCiuc004ezw.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76992 mRNA. Translation: AAB18823.1. Frameshift.
BT006886 mRNA. Translation: AAP35532.1.
AB209303 mRNA. Translation: BAD92540.1. Different initiation.
Z97632 Genomic DNA. Translation: CAB10730.1.
CH471150 Genomic DNA. Translation: EAW88468.1.
CH471150 Genomic DNA. Translation: EAW88469.1.
BC009896 mRNA. Translation: AAH09896.1.
CCDSiCCDS14657.1.
RefSeqiNP_001156752.1. NM_001163280.1.
NP_055315.2. NM_014500.4.
XP_005262461.1. XM_005262404.3.
UniGeneiHs.204475.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DITNMR-A256-354[»]
ProteinModelPortaliO43719.
SMRiO43719. Positions 257-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118149. 45 interactions.
DIPiDIP-42095N.
IntActiO43719. 16 interactions.
MINTiMINT-1193787.
STRINGi9606.ENSP00000218364.

PTM databases

iPTMnetiO43719.
PhosphoSiteiO43719.

Polymorphism and mutation databases

BioMutaiHTATSF1.

Proteomic databases

EPDiO43719.
MaxQBiO43719.
PaxDbiO43719.
PeptideAtlasiO43719.
PRIDEiO43719.

Protocols and materials databases

DNASUi27336.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218364; ENSP00000218364; ENSG00000102241.
ENST00000535601; ENSP00000442699; ENSG00000102241.
GeneIDi27336.
KEGGihsa:27336.
UCSCiuc004ezw.4. human.

Organism-specific databases

CTDi27336.
GeneCardsiHTATSF1.
HGNCiHGNC:5276. HTATSF1.
HPAiHPA000504.
MIMi300346. gene.
neXtProtiNX_O43719.
PharmGKBiPA29540.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1548. Eukaryota.
ENOG410YD7P. LUCA.
GeneTreeiENSGT00390000009902.
HOGENOMiHOG000049201.
HOVERGENiHBG059454.
InParanoidiO43719.
KOiK13093.
OMAiQITAEAW.
OrthoDBiEOG7VHSZQ.
PhylomeDBiO43719.
TreeFamiTF313623.

Miscellaneous databases

ChiTaRSiHTATSF1. human.
EvolutionaryTraceiO43719.
GeneWikiiHTATSF1.
GenomeRNAii27336.
PMAP-CutDBO43719.
PROiO43719.
SOURCEiSearch...

Gene expression databases

BgeeiO43719.
CleanExiHS_HTATSF1.
ExpressionAtlasiO43719. baseline and differential.
GenevisibleiO43719. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat."
    Zhou Q., Sharp P.A.
    Science 274:605-610(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-45; 62-79; 155-169; 199-210; 239-245 AND 410-428, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Promyelocytic leukemia.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-478.
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Choriocarcinoma.
  7. "Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages."
    Zhou Q., Chen D., Pierstorff E., Luo K.
    EMBO J. 17:3681-3691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK9.
  8. "The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor."
    Li X.-Y., Green M.R.
    Genes Dev. 12:2992-2996(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif."
    Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.
    Mol. Cell. Biol. 18:5000-5009(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SF3A2.
  10. "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
    Parada C.A., Roeder R.G.
    EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH NCL; CCNT1; RNA POLYMERASE II; SUPT5H AND CDK9.
  11. "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."
    Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.
    Mol. Cell. Biol. 19:5960-5968(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GTF2F2; SUPT5H AND POLR2A.
  12. "Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter."
    Fong Y.W., Zhou Q.
    Mol. Cell. Biol. 20:5897-5907(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCNT1.
  13. "Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators."
    Simmons A., Aluvihare V., McMichael A.
    Immunity 14:763-777(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Stimulatory effect of splicing factors on transcriptional elongation."
    Fong Y.W., Zhou Q.
    Nature 414:929-933(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-136, INTERACTION WITH U SNRNPS AND CCNT1, DOMAIN.
  15. "FF domains of CA150 bind transcription and splicing factors through multiple weak interactions."
    Smith M.J., Kulkarni S., Pawson T.
    Mol. Cell. Biol. 24:9274-9285(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TCERG1, SUBCELLULAR LOCATION.
  16. "Soluble HIV-1 gp120 enhances HIV-1 replication in non-dividing CD4+ T cells, mediated via cell signaling and Tat cofactor overexpression."
    Misse D., Gajardo J., Oblet C., Religa A., Riquet N., Mathieu D., Yssel H., Veas F.
    AIDS 19:897-905(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-557; SER-561; SER-579; SER-597; SER-600; SER-616; SER-624; SER-642; SER-676; SER-702; SER-713 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-453; SER-498; SER-642; SER-713 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-616; SER-624; SER-642 AND SER-676, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-702; SER-713 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-403; SER-407; SER-445; SER-498; SER-579; SER-616; SER-624; THR-633; SER-642; SER-676; SER-702; SER-713; SER-714 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-485; SER-579; SER-597; SER-600; SER-607; SER-616; SER-642; SER-676; SER-702; SER-713; SER-714 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-642 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. "Solution structure of the RRM_1 domain of HIV Tat specific factor 1 variant."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 256-354.

Entry informationi

Entry nameiHTSF1_HUMAN
AccessioniPrimary (citable) accession number: O43719
Secondary accession number(s): D3DWG9, Q59G06, Q99730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.