UniProt Accession

 HTSF1_HUMAN; O43719; D3DWG9; Q59G06; Q99730 

Genbank Protein ID

 U76992; BT006886; AB209303; Z97632; CH471150; CH471150; BC009896 

Genbank Nucleotide ID

 AAB18823.1; AAP35532.1; BAD92540.1; CAB10730.1; EAW88468.1; EAW88469.1; AAH09896.1 

Protein Name

 HIV Tat-specific factor 1 

Protein Synonyms/Alias

 Tat-SF1 

Gene Name

 HTATSF1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
56	PYEWDLDKKAWFPKI	ubiquitination	[1]
57	YEWDLDKKAWFPKIT	ubiquitination	[1]
104	AEEPPQEKAPEPTDA	ubiquitination	[1, 2, 3]
169	DPQTEEFKVKLYKDN	acetylation	[3]
174	EFKVKLYKDNQGNLK	acetylation	[3]
190	DGLCCYLKRESVELA	ubiquitination	[3]
199	ESVELALKLLDEDEI	ubiquitination	[3, 4, 5, 6]
217	KLHVEVAKFQLKGEY	ubiquitination	[7, 8, 9]
221	EVAKFQLKGEYDASK	ubiquitination	[1, 2]
245	KKLSMQQKQLDWRPE	ubiquitination	[1, 3, 7, 8, 9]
297	DLRVECSKFGQIRKL	ubiquitination	[1, 3]
303	SKFGQIRKLLLFDRH	ubiquitination	[7, 9]
429	FEEPIDEKKFEKTED	ubiquitination	[2]
504	DSPKKESKKKTLKND	acetylation	[10]
505	SPKKESKKKTLKNDC	acetylation	[10]
506	PKKESKKKTLKNDCE	acetylation	[10]
661	KGLEAADKKAEEGDA	acetylation	[3]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 133 218 RRM 1.
 DOMAIN 264 349 RRM 2.
 REGION 381 755 Mediates interaction with the P-TEFb
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 387 387 Phosphoserine.
 MOD_RES 403 403 Phosphoserine.
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 445 445 Phosphoserine.
 MOD_RES 452 452 Phosphoserine.
 MOD_RES 453 453 Phosphoserine.
 MOD_RES 485 485 Phosphoserine.
 MOD_RES 498 498 Phosphoserine.
 MOD_RES 529 529 Phosphoserine (By similarity).
 MOD_RES 557 557 Phosphoserine.
 MOD_RES 561 561 Phosphoserine.
 MOD_RES 579 579 Phosphoserine.
 MOD_RES 597 597 Phosphoserine.
 MOD_RES 600 600 Phosphoserine.
 MOD_RES 607 607 Phosphoserine.
 MOD_RES 616 616 Phosphoserine.
 MOD_RES 624 624 Phosphoserine.
 MOD_RES 633 633 Phosphothreonine.
 MOD_RES 642 642 Phosphoserine.
 MOD_RES 676 676 Phosphoserine.
 MOD_RES 702 702 Phosphoserine.
 MOD_RES 713 713 Phosphoserine.
 MOD_RES 714 714 Phosphoserine.
 MOD_RES 721 721 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 755 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:HPA.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; TAS:ProtInc.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019079; P:viral genome replication; TAS:ProtInc. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS