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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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000102241-MONOMER.

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)DescriptionActionsGraphical viewLength
Mutagenesisi136Y → D: Loss of interaction with U snRNPs. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000102241.
PharmGKBiPA29540.

Polymorphism and mutation databases

BioMutaiHTATSF1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002486042 – 755HIV Tat-specific factor 1Add BLAST754

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei297N6-acetyllysineBy similarity1
Modified residuei387PhosphoserineCombined sources1
Modified residuei403PhosphoserineCombined sources1
Modified residuei407PhosphoserineCombined sources1
Modified residuei409PhosphoserineBy similarity1
Modified residuei445PhosphoserineCombined sources1
Modified residuei452PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei481PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei494PhosphoserineCombined sources1
Modified residuei498PhosphoserineCombined sources1
Modified residuei521PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
Modified residuei557PhosphoserineCombined sources1
Modified residuei561PhosphoserineCombined sources1
Modified residuei579PhosphoserineCombined sources1
Modified residuei597PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei607PhosphoserineCombined sources1
Modified residuei616PhosphoserineCombined sources1
Modified residuei624PhosphoserineCombined sources1
Modified residuei633PhosphothreonineCombined sources1
Modified residuei642PhosphoserineCombined sources1
Modified residuei676PhosphoserineCombined sources1
Modified residuei702PhosphoserineCombined sources1
Modified residuei713PhosphoserineCombined sources1
Modified residuei714PhosphoserineCombined sources1
Modified residuei721PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43719.
MaxQBiO43719.
PaxDbiO43719.
PeptideAtlasiO43719.
PRIDEiO43719.

PTM databases

iPTMnetiO43719.
PhosphoSitePlusiO43719.

Miscellaneous databases

PMAP-CutDBO43719.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000102241.
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 interactors.
DIPiDIP-42095N.
IntActiO43719. 17 interactors.
MINTiMINT-1193787.
STRINGi9606.ENSP00000218364.

Structurei

Secondary structure

1755
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi265 – 271Combined sources7
Helixi276 – 279Combined sources4
Helixi282 – 294Combined sources13
Helixi295 – 297Combined sources3
Beta strandi302 – 306Combined sources5
Beta strandi315 – 318Combined sources4
Helixi322 – 331Combined sources10
Beta strandi343 – 346Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO43719.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 218RRM 1PROSITE-ProRule annotationAdd BLAST86
Domaini264 – 349RRM 2PROSITE-ProRule annotationAdd BLAST86

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni381 – 755Mediates interaction with the P-TEFb complexAdd BLAST375

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi228 – 234Poly-Lys7
Compositional biasi423 – 754Asp/Glu-rich (acidic)Add BLAST332

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.
OrthoDBiEOG091G0O8I.
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 differs from that shown. Reason: Frameshift at positions 383, 391 and 393.Curated
The sequence BAD92540 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti125F → V in BAD92540 (Ref. 3) Curated1
Sequence conflicti587V → I in BAD92540 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027362478G → A.1 PublicationCorresponds to variant rs2071913dbSNPEnsembl.1
Natural variantiVAR_052206526N → T.Corresponds to variant rs12852634dbSNPEnsembl.1
Natural variantiVAR_052207678D → G.Corresponds to variant rs17339410dbSNPEnsembl.1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DITNMR-A256-354[»]
ProteinModelPortaliO43719.
SMRiO43719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118149. 45 interactors.
DIPiDIP-42095N.
IntActiO43719. 17 interactors.
MINTiMINT-1193787.
STRINGi9606.ENSP00000218364.

PTM databases

iPTMnetiO43719.
PhosphoSitePlusiO43719.

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.
OpenTargetsiENSG00000102241.
PharmGKBiPA29540.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1548. Eukaryota.
ENOG410YD7P. LUCA.
GeneTreeiENSGT00390000009902.
HOGENOMiHOG000049201.
HOVERGENiHBG059454.
InParanoidiO43719.
KOiK13093.
OMAiQITAEAW.
OrthoDBiEOG091G0O8I.
PhylomeDBiO43719.
TreeFamiTF313623.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000102241-MONOMER.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000102241.
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...

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: November 2, 2016
This is version 154 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.