UniProt Accession

 PSIP1_HUMAN; O75475; D3DRI9; O00256; O95368; Q6P391; Q86YB9; Q9NZI3; Q9UER6 

Genbank Protein ID

 AF098483; AF098482; AF063020; AF199339; AF199339; AF432220; AL359998; AL441925; AL513423; AL441925; AL359998; AL513423; CH471071; CH471071; CH471071; BC044568; BC064135; U94319 

Genbank Nucleotide ID

 AAC97946.1; AAC97945.1; AAC25167.1; AAF25870.1; AAF25871.1; AAL99926.1; CAH71355.1; CAH71355.1; CAH71355.1; CAI13287.1; CAI13287.1; CAI13287.1; EAW58677.1; EAW58678.1; EAW58679.1; AAH44568.2; AAH64135.1; AAB52589.1 

Protein Name

 PC4 and SFRS1-interacting protein 

Protein Synonyms/Alias

 CLL-associated antigen KW-7; Dense fine speckles 70 kDa protein; DFS 70; Lens epithelium-derived growth factor; Transcriptional coactivator p75/p52 

Gene Name

 PSIP1 

Gene Synonyms/Alias

 DFS70; LEDGF; PSIP2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MTRDFKPGDLIFA	ubiquitination	[1, 2, 3, 4, 5]
34	EVPDGAVKPPTNKLP	ubiquitination	[2]
75	YGKPNKRKGFNEGLW	sumoylation	[6]
75	YGKPNKRKGFNEGLW	ubiquitination	[1, 5]
89	WEIDNNPKVKFSSQQ	ubiquitination	[1, 5]
100	SSQQAATKQSNASSD	ubiquitination	[2]
135	ASNEDVTKAVDITTP	ubiquitination	[2]
216	DIITEEDKSKKKGQE	acetylation	[7]
232	KQPKKQPKKDEEGQK	acetylation	[8]
250	KPRKEPDKKEGKKEV	sumoylation	[6]
251	PRKEPDKKEGKKEVE	sumoylation	[6]
254	EPDKKEGKKEVESKR	sumoylation	[6]
255	PDKKEGKKEVESKRK	sumoylation	[6]
360	QRIHAEIKNSLKIDN	ubiquitination	[3]
364	AEIKNSLKIDNLDVN	sumoylation	[6, 9]
364	AEIKNSLKIDNLDVN	ubiquitination	[1, 2, 3, 4, 5, 7]
392	VTMQQAQKHTEMITT	acetylation	[10]
401	TEMITTLKKIRRFKV	acetylation	[10]
407	LKKIRRFKVSQVIME	ubiquitination	[1, 4, 5]
415	VSQVIMEKSTMLYNK	ubiquitination	[1, 3, 4, 5, 7]
422	KSTMLYNKFKNMFLV	acetylation	[11]
422	KSTMLYNKFKNMFLV	ubiquitination	[1, 5]
424	TMLYNKFKNMFLVGE	ubiquitination	[1, 5]
442	VITQVLNKSLAEQRQ	ubiquitination	[3]
524	RETEISLKDSTLDN*	ubiquitination	[2]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] SUMOylation of the lens epithelium-derived growth factor/p75 attenuates its transcriptional activity on the heat shock protein 27 promoter.
 Bueno MT, Garcia-Rivera JA, Kugelman JR, Morales E, Rosas-Acosta G, Llano M.
 J Mol Biol. 2010 Jun 4;399(2):221-39. [PMID: 20382164]
 [7] 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]
 [8] 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]
 [9] Lens epithelium-derived growth factor deSumoylation by Sumo-specific protease-1 regulates its transcriptional activation of small heat shock protein and the cellular response.
 Ishihara K, Fatma N, Bhargavan B, Chhunchha B, Kubo E, Dey S, Takamura Y, Kumar A, Singh DP.
 FEBS J. 2012 Sep;279(17):3048-70. [PMID: 22748127]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 

Functional Description

 Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. 

Sequence Annotation

 DOMAIN 1 64 PWWP.
 MOTIF 146 156 Nuclear localization signal.
 MOD_RES 102 102 Phosphoserine.
 MOD_RES 106 106 Phosphoserine.
 MOD_RES 122 122 Phosphothreonine.
 MOD_RES 129 129 Phosphoserine.
 MOD_RES 134 134 Phosphothreonine (By similarity).
 MOD_RES 141 141 Phosphothreonine.
 MOD_RES 167 167 Phosphothreonine.
 MOD_RES 177 177 Phosphoserine.
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 273 273 Phosphoserine.
 MOD_RES 275 275 Phosphoserine.
 MOD_RES 434 434 Phosphoserine.
 MOD_RES 437 437 Phosphothreonine.
 MOD_RES 443 443 Phosphoserine.
 MOD_RES 522 522 Phosphoserine.
 MOD_RES 527 527 Phosphothreonine.  

Keyword

 3D-structure; Alternative splicing; Chromosomal rearrangement; Coiled coil; Complete proteome; Direct protein sequencing; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 530 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
 GO:0033613; F:activating transcription factor binding; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:UniProtKB.
 GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
 GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
 GO:0000395; P:mRNA 5'-splice site recognition; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0009408; P:response to heat; ISS:UniProtKB.
 GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR021567; LEDGF.
 IPR000313; PWWP.
 IPR017859; Treacle-like_TCS. 

Pfam

 PF11467; LEDGF
 PF00855; PWWP 

SMART

 SM00293; PWWP 

PROSITE

 PS50812; PWWP 

PRINTS

 PR01503; TREACLE.