O75475 (PSIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PC4 and SFRS1-interacting protein

Alternative name(s):
CLL-associated antigen KW-7
Dense fine speckles 70 kDa protein
Short name=DFS 70
Lens epithelium-derived growth factor
Transcriptional coactivator p75/p52

Gene names

Name:	PSIP1
Synonyms:	DFS70, LEDGF, PSIP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9
Subunit structure	Monomer. Interacts with IFRD1/PC4. Isoform 2 interacts with SFRS1. Isoform 1 interacts POGZ and CDCA7L. Isoform 1 interacts with lentiviral integrase and acts as a chromatin tethering factor to the chromosomal DNA. Isoform 1 interacts in particular with the human HIV-1 integrase protein (HIV-1 IN), determining its nuclear localization, its tight association with chromatin and its protection from the proteasome. Isoform 1 interacts also with HIV-2 IN. Isoform 2 does not interact with HIV-1 IN. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.20 Ref.25
Subcellular location	Nucleus. Note: Remains chromatin-associated throughout the cell cycle. Ref.9 Ref.13
Tissue specificity	Widely expressed. Expressed at high level in the thymus. Expressed in fetal and adult brain. Expressed in neurons, but not astrocytes. Markedly elevated in fetal as compared to adult brain. In the adult brain, expressed in the subventricular zone (SVZ), in hippocampus, and undetectable elsewhere. In the fetal brain, expressed in the germinal neuroepithelium and cortical plate regions. Ref.1 Ref.9
Domain	Residues 340-417 are necessary and sufficient for the interaction with HIV-1 IN (IBD domain).
Involvement in disease	A chromosomal aberration involving PSIP1 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with NUP98. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4.
Sequence similarities	Belongs to the HDGF family. Contains 1 PWWP domain.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Coiled coil
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA 5'-splice site recognition Inferred from direct assay Ref.13. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to heat Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear heterochromatin Inferred from direct assay PubMed 12796494. Source: UniProtKB nuclear periphery Inferred from direct assay PubMed 11512661. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.13. Source: UniProtKB transcriptionally active chromatin Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA polymerase II transcription coactivator activity Inferred from direct assay Ref.1Ref.13. Source: UniProtKB activating transcription factor binding Inferred from direct assay Ref.1. Source: UniProtKB chromatin binding Inferred from direct assay PubMed 20974633. Source: UniProtKB supercoiled DNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75475-1)

Also known as: p75; PSIP1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Less active than isoform 2 as transcriptional coactivator, but more abundant in cells.

Isoform 2 (identifier: O75475-2)

Also known as: p52; PSIP2;

The sequence of this isoform differs from the canonical sequence as follows:
     326-333: QQNKDEGK → HQTTCNLQ
     334-530: Missing.

Isoform 3 (identifier: O75475-3)

The sequence of this isoform differs from the canonical sequence as follows:
     326-530: QQNKDEGKKP...ISLKDSTLDN → HFAL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 530

530

PC4 and SFRS1-interacting protein

PRO_0000191708

Regions

Domain

1 – 64

64

PWWP

Coiled coil

306 – 334

29

Potential

Coiled coil

371 – 395

25

Potential

Motif

146 – 156

11

Nuclear localization signal Ref.12

Amino acid modifications

Modified residue

102

1

Phosphoserine Ref.24

Modified residue

106

1

Phosphoserine Ref.18 Ref.22 Ref.24

Modified residue

122

1

Phosphothreonine Ref.15 Ref.22

Modified residue

129

1

Phosphoserine Ref.24

Modified residue

134

1

Phosphothreonine By similarity

Modified residue

141

1

Phosphothreonine Ref.18 Ref.21 Ref.22 Ref.24

Modified residue

167

1

Phosphothreonine Ref.21

Modified residue

177

1

Phosphoserine Ref.21 Ref.24

Modified residue

206

1

Phosphoserine Ref.22 Ref.24

Modified residue

273

1

Phosphoserine Ref.18 Ref.21 Ref.22

Modified residue

275

1

Phosphoserine Ref.18 Ref.21 Ref.22 Ref.24

Modified residue

434

1

Phosphoserine Ref.18 Ref.22

Modified residue

437

1

Phosphothreonine Ref.16

Modified residue

443

1

Phosphoserine Ref.18

Modified residue

522

1

Phosphoserine Ref.18 Ref.22

Modified residue

527

1

Phosphothreonine Ref.18 Ref.22 Ref.24

Natural variations

Alternative sequence

326 – 530

205

QQNKD…STLDN → HFAL in isoform 3.

VSP_044435

Alternative sequence

326 – 333

8

QQNKDEGK → HQTTCNLQ in isoform 2.

VSP_014297

Alternative sequence

334 – 530

197

Missing in isoform 2.

VSP_014298

Experimental info

Mutagenesis

360

1

K → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. Ref.20

Mutagenesis

365

1

I → A: Loss of interaction with human HIV-1 integrase; reduced interaction with POGZ and CDCA7L. Ref.20 Ref.25

Mutagenesis

366

1

D → A or N: Loss of interaction with human HIV-1 integrase; no effect on interaction with CDCA7L. Ref.20 Ref.25

Mutagenesis

366

1

D → A: No effect on interaction with POGZ. Ref.20 Ref.25

Mutagenesis

370

1

V → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. Ref.20

Mutagenesis

406

1

F → A: Loss of interaction with human HIV-1 integrase and POGZ; reduced interaction with CDCA7L. Ref.20 Ref.25

Mutagenesis

408

1

V → A: Reduced interaction with human HIV-1 integrase; no effect on interaction with POGZ and CDCA7L. Ref.20 Ref.25

Sequence conflict

153 – 161

9

Missing in AAH64135. Ref.7

Sequence conflict

224

1

E → G in AAC97946. Ref.1

Sequence conflict

224

1

E → G in AAC97945. Ref.1

Sequence conflict

272

1

T → P in AAB52589. Ref.8

Sequence conflict

420

1

Y → F in AAC97946. Ref.1

Sequence conflict

420

1

Y → F in AAB52589. Ref.8

Secondary structure

1

.

.

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.

.

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.

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.

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530

Helix Strand Turn

Details...

Helix

2 – 4

3

Beta strand

10 – 13

4

Beta strand

21 – 25

5

Beta strand

40 – 44

5

Turn

45 – 47

3

Beta strand

50 – 53

4

Helix

55 – 57

3

Beta strand

58 – 60

3

Helix

61 – 68

8

Helix

77 – 86

10

Helix

347 – 362

16

Helix

365 – 367

3

Helix

370 – 381

12

Helix

387 – 391

5

Helix

394 – 403

10

Helix

410 – 425

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p75) (PSIP1) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 4B653D02B1D0E174	FASTA	530	60,103
	10 20 30 40 50 60 MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP 70 80 90 100 110 120 YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK QSNASSDVEV EEKETSVSKE 130 140 150 160 170 180 DTDHEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SVNLKVSPKR 190 200 210 220 230 240 GRPAATEVKI PKPRGRPKMV KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE 250 260 270 280 290 300 EDKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR 310 320 330 340 350 360 NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS RLQRIHAEIK 370 380 390 400 410 420 NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL KKIRRFKVSQ VIMEKSTMLY 430 440 450 460 470 480 NKFKNMFLVG EGDSVITQVL NKSLAEQRQH EEANKTKDQG KKGPNKKLEK EQTGSKTLNG 490 500 510 520 530 GSDAQDGNQP QHNGESNEDS KDNHEASTKK KPSSEERETE ISLKDSTLDN
	Isoform 2 (p52) (PSIP2) [UniParc]. Checksum: DAFEC8F815C06FCD	FASTA	333	37,725
	10 20 30 40 50 60 MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP 70 80 90 100 110 120 YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK QSNASSDVEV EEKETSVSKE 130 140 150 160 170 180 DTDHEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SVNLKVSPKR 190 200 210 220 230 240 GRPAATEVKI PKPRGRPKMV KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE 250 260 270 280 290 300 EDKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR 310 320 330 NMLKGQHEKE AADRKRKQEE QMETEHQTTC NLQ
	Isoform 3 [UniParc]. Checksum: F35C00DDD27E9BAE	FASTA	329	37,268
	10 20 30 40 50 60 MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP 70 80 90 100 110 120 YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK QSNASSDVEV EEKETSVSKE 130 140 150 160 170 180 DTDHEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SVNLKVSPKR 190 200 210 220 230 240 GRPAATEVKI PKPRGRPKMV KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE 250 260 270 280 290 300 EDKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR 310 320 NMLKGQHEKE AADRKRKQEE QMETEHFAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation." Ge H., Si Y., Roeder R.G. EMBO J. 17:6723-6729(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 4-39 AND 76-89, TISSUE SPECIFICITY, INTERACTION WITH PC4. Tissue: Cervix carcinoma.
[2]	"Lens epithelium-derived growth factor: effects on growth and survival of lens epithelial cells, keratinocytes, and fibroblasts." Singh D.P., Ohguro N., Kikuchi T., Sueno T., Reddy V.N., Yuge K., Chylack L.T. Jr., Shinohara T. Biochem. Biophys. Res. Commun. 267:373-381(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lens.
[3]	"Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing." Singh D.P., Kimura A., Chylack L.T. Jr., Shinohara T. Gene 242:265-273(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[4]	"Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX." Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G. Blood 100:2123-2131(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Leukemia.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 2 AND 3). Tissue: Testis and Uterus.
[8]	"Autoantibodies to DFS 70 kd/transcription coactivator p75 in atopic dermatitis and other conditions." Ochs R.L., Muro Y., Si Y., Ge H., Chan E.K.L., Tan E.M. J. Allergy Clin. Immunol. 105:1211-1220(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 180-530 (ISOFORM 1).
[9]	"Lens epithelium-derived growth factor (LEDGF/p75) expression in fetal and adult human brain." Chylack L.T. Jr., Fu L., Mancini R., Martin-Rehrmann M.D., Saunders A.J., Konopka G., Tian D., Hedley-Whyte E.T., Folkerth R.D., Goldstein L.E. Exp. Eye Res. 79:941-948(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[10]	"Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase." Llano M., Delgado S., Vanegas M., Poeschla E.M. J. Biol. Chem. 279:55570-55577(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1).
[11]	"The interaction of LEDGF/p75 with integrase is lentiviral-specific and promotes DNA binding." Busschots K., Vercammen J., Emiliani S., Benarous R., Engelborghs Y., Christ F., Debyser Z. J. Biol. Chem. 280:17841-17847(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HIV-1 AND HIV-2 INTEGRASE (ISOFORM 1).
[12]	"Identification of the LEDGF/p75 HIV-1 integrase-interaction domain and NLS reveals NLS-independent chromatin tethering." Vanegas M., Llano M., Delgado S., Thompson D., Peretz M., Poeschla E.M. J. Cell Sci. 118:1733-1743(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1), NUCLEAR LOCALIZATION SIGNAL.
[13]	"A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2." Ge H., Si Y., Wolffe A.P. Mol. Cell 2:751-759(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SFRS1, SUBCELLULAR LOCATION.
[14]	"t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia." Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E., Micalizzi C., Panarello C. Leuk. Res. 29:467-470(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
[15]	"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 THR-122, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-437, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-141; SER-273; SER-275; SER-434; SER-443; SER-522 AND THR-527, MASS SPECTROMETRY. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[20]	"Lens epithelium-derived growth factor/p75 interacts with the transposase-derived DDE domain of PogZ." Bartholomeeusen K., Christ F., Hendrix J., Rain J.C., Emiliani S., Benarous R., Debyser Z., Gijsbers R., De Rijck J. J. Biol. Chem. 284:11467-11477(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POGZ; HIV-1 INTEGRASE AND CDCA7L, MUTAGENESIS OF LYS-360; ILE-365; ASP-366; VAL-370; PHE-406 AND VAL-408.
[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 THR-141; THR-167; SER-177; SER-273 AND SER-275, MASS SPECTROMETRY. 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-106; THR-122; THR-141; SER-206; SER-273; SER-275; SER-434; SER-522 AND THR-527, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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-102; SER-106; SER-129; THR-141; SER-177; SER-206; SER-275 AND THR-527, MASS SPECTROMETRY.
[25]	"Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75." Cherepanov P., Sun Z.-Y., Rahman S., Maertens G., Wagner G., Engelman A. Nat. Struct. Mol. Biol. 12:526-532(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 347-471, SUBUNIT, MUTAGENESIS OF ILE-365; ASP-366; PHE-406 AND VAL-408.
[26]	"Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75." Cherepanov P., Ambrosio A.L.B., Rahman S., Ellenberger T., Engelman A. Proc. Natl. Acad. Sci. U.S.A. 102:17308-17313(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 347-442 IN COMPLEX WITH HUMAN HIV-1 INTEGRASE.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF098483 mRNA. Translation: AAC97946.1.
AF098482 mRNA. Translation: AAC97945.1.
AF063020 mRNA. Translation: AAC25167.1.
AF199339 Genomic DNA. Translation: AAF25870.1.
AF199339 Genomic DNA. Translation: AAF25871.1.
AF432220 mRNA. Translation: AAL99926.1.
AL359998, AL441925, AL513423 Genomic DNA. Translation: CAH71355.1.
AL441925, AL359998, AL513423 Genomic DNA. Translation: CAI13287.1.
CH471071 Genomic DNA. Translation: EAW58677.1.
CH471071 Genomic DNA. Translation: EAW58678.1.
CH471071 Genomic DNA. Translation: EAW58679.1.
BC044568 mRNA. Translation: AAH44568.2.
BC064135 mRNA. Translation: AAH64135.1.
U94319 mRNA. Translation: AAB52589.1.

IPI

IPI00028122.
IPI00333317.

PIR

JC7168.

RefSeq

NP_001121689.1. NM_001128217.1.
NP_066967.3. NM_021144.3.
NP_150091.2. NM_033222.3.

UniGene

Hs.741408.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z9E	NMR	-	A	347-471	[»]
2B4J	X-ray	2.02	C/D	347-442	[»]
2M16	NMR	-	A	1-93	[»]
3F9K	X-ray	3.20	C/G/K/O/S/W/a/e/i/m/q/u	347-435	[»]
3HPG	X-ray	3.28	G/H/I/J/K/L	347-435	[»]
3HPH	X-ray	2.64	E/F/G/H	348-435	[»]
3U88	X-ray	3.00	C/D	347-435	[»]
4FU6	X-ray	2.10	A	1-135	[»]

ProteinModelPortal

O75475.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46656N.

IntAct

O75475. 8 interactions.

STRING

9606.ENSP00000370109.

Protein family/group databases

Allergome

2120. Hom s DSF70.

Proteomic databases

PaxDb

O75475.

PeptideAtlas

O75475.

PRIDE

O75475.

Protocols and materials databases

DNASU

11168.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380715; ENSP00000370091; ENSG00000164985.
ENST00000380716; ENSP00000370092; ENSG00000164985.
ENST00000380733; ENSP00000370109; ENSG00000164985.
ENST00000380738; ENSP00000370114; ENSG00000164985.
ENST00000397519; ENSP00000380653; ENSG00000164985.

GeneID

11168.

KEGG

hsa:11168.

UCSC

uc003zlv.4. human.
uc003zly.3. human.

Organism-specific databases

CTD

11168.

GeneCards

GC09M015456.

HGNC

HGNC:9527. PSIP1.

HPA

CAB013718.
HPA019697.

MIM

603620. gene.

neXtProt

NX_O75475.

PharmGKB

PA33872.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG316844.

HOVERGEN

HBG108300.

InParanoid

O75475.

OMA

ESKDSHE.

OrthoDB

EOG4V438N.

PhylomeDB

O75475.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

O75475.

Bgee

O75475.

CleanEx

HS_PSIP1.

Genevestigator

O75475.

GermOnline

ENSG00000164985. Homo sapiens.

Family and domain databases

InterPro

IPR021567. LEDGF.
IPR000313. PWWP.
IPR017859. Treacle-like_TCS.
[Graphical view]

Pfam

PF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]

PRINTS

PR01503. TREACLE.

SMART

SM00293. PWWP. 1 hit.
[Graphical view]

PROSITE

PS50812. PWWP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PSIP1. human.

EvolutionaryTrace

O75475.

GenomeRNAi

11168.

NextBio

42491.

PMAP-CutDB

O75475.

SOURCE

Search...

Entry information

Entry name

PSIP1_HUMAN

Accession

Primary (citable) accession number: O75475
Secondary accession number(s): D3DRI9 , O00256, O95368, Q6P391, Q86YB9, Q9NZI3, Q9UER6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.