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O75475 (PSIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence 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.21 Ref.26

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).

Post-translational modification

Citrullinated by PADI4 By similarity.

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 processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainCoiled coil
   LigandDNA-binding
   PTMCitrullination
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of integrated proviral latency

Traceable author statement. Source: Reactome

mRNA 5'-splice site recognition

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1Ref.13. Source: UniProtKB

regulation of transcription, DNA-templated

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

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

nucleus

Inferred from direct assay PubMed 12796494PubMed 12796494. Source: UniProtKB

transcriptionally active chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRNA 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

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

supercoiled DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gag-polP0458521EBI-1801773,EBI-3989067From a different organism.
SUMO1P631654EBI-1801773,EBI-80140

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530PC4 and SFRS1-interacting protein
PRO_0000191708

Regions

Domain1 – 6464PWWP
Coiled coil306 – 33429 Potential
Coiled coil371 – 39525 Potential
Motif146 – 15611Nuclear localization signal Ref.12

Amino acid modifications

Modified residue1021Phosphoserine Ref.25
Modified residue1061Phosphoserine Ref.18 Ref.23 Ref.25
Modified residue1221Phosphothreonine Ref.15 Ref.23
Modified residue1291Phosphoserine Ref.25
Modified residue1411Phosphothreonine Ref.18 Ref.22 Ref.23 Ref.25
Modified residue1671Phosphothreonine Ref.22
Modified residue1771Phosphoserine Ref.22 Ref.25
Modified residue2061Phosphoserine Ref.23 Ref.25
Modified residue2731Phosphoserine Ref.18 Ref.22 Ref.23
Modified residue2751Phosphoserine Ref.18 Ref.22 Ref.23 Ref.25
Modified residue4341Phosphoserine Ref.18 Ref.23
Modified residue4371Phosphothreonine Ref.16
Modified residue4431Phosphoserine Ref.18
Modified residue5171Citrulline By similarity
Modified residue5221Phosphoserine Ref.18
Modified residue5271Phosphothreonine Ref.18 Ref.23 Ref.25

Natural variations

Alternative sequence326 – 530205QQNKD…STLDN → HFAL in isoform 3.
VSP_044435
Alternative sequence326 – 3338QQNKDEGK → HQTTCNLQ in isoform 2.
VSP_014297
Alternative sequence334 – 530197Missing in isoform 2.
VSP_014298

Experimental info

Mutagenesis3601K → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. Ref.21
Mutagenesis3651I → A: Loss of interaction with human HIV-1 integrase; reduced interaction with POGZ and CDCA7L. Ref.21 Ref.26
Mutagenesis3661D → A or N: Loss of interaction with human HIV-1 integrase; no effect on interaction with CDCA7L. Ref.21 Ref.26
Mutagenesis3661D → A: No effect on interaction with POGZ. Ref.21 Ref.26
Mutagenesis3701V → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. Ref.21
Mutagenesis4061F → A: Loss of interaction with human HIV-1 integrase and POGZ; reduced interaction with CDCA7L. Ref.21 Ref.26
Mutagenesis4081V → A: Reduced interaction with human HIV-1 integrase; no effect on interaction with POGZ and CDCA7L. Ref.21 Ref.26
Sequence conflict153 – 1619Missing in AAH64135. Ref.7
Sequence conflict2241E → G in AAC97946. Ref.1
Sequence conflict2241E → G in AAC97945. Ref.1
Sequence conflict2721T → P in AAB52589. Ref.8
Sequence conflict4201Y → F in AAC97946. Ref.1
Sequence conflict4201Y → F in AAB52589. Ref.8

Secondary structure

................................ 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p75) (PSIP1) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 4B653D02B1D0E174

FASTA53060,103
        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 

« Hide

Isoform 2 (p52) (PSIP2) [UniParc].

Checksum: DAFEC8F815C06FCD
Show »

FASTA33337,725
Isoform 3 [UniParc].

Checksum: F35C00DDD27E9BAE
Show »

FASTA32937,268

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"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 AND THR-527, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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].
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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.
[27]"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.

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.
PIRJC7168.
RefSeqNP_001121689.1. NM_001128217.1.
NP_066967.3. NM_021144.3.
NP_150091.2. NM_033222.3.
XP_005251413.1. XM_005251356.1.
XP_005251415.1. XM_005251358.1.
UniGeneHs.658434.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z9ENMR-A347-471[»]
2B4JX-ray2.02C/D347-442[»]
2M16NMR-A1-93[»]
3F9KX-ray3.20C/G/K/O/S/W/a/e/i/m/q/u347-435[»]
3HPGX-ray3.28G/H/I/J/K/L347-435[»]
3HPHX-ray2.64E/F/G/H348-435[»]
3U88X-ray3.00C/D347-435[»]
3ZEHNMR-A3-100[»]
4FU6X-ray2.10A1-135[»]
ProteinModelPortalO75475.
SMRO75475. Positions 1-93, 348-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116339. 36 interactions.
DIPDIP-46656N.
IntActO75475. 11 interactions.
MINTMINT-4527154.
STRING9606.ENSP00000370109.

Protein family/group databases

Allergome2120. Hom s DSF70.

Proteomic databases

PaxDbO75475.
PeptideAtlasO75475.
PRIDEO75475.

Protocols and materials databases

DNASU11168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380715; ENSP00000370091; ENSG00000164985. [O75475-3]
ENST00000380716; ENSP00000370092; ENSG00000164985. [O75475-2]
ENST00000380733; ENSP00000370109; ENSG00000164985. [O75475-1]
ENST00000380738; ENSP00000370114; ENSG00000164985. [O75475-1]
ENST00000397519; ENSP00000380653; ENSG00000164985. [O75475-2]
GeneID11168.
KEGGhsa:11168.
UCSCuc003zlv.4. human. [O75475-1]
uc003zly.3. human. [O75475-3]
uc003zlz.4. human. [O75475-2]

Organism-specific databases

CTD11168.
GeneCardsGC09M015456.
HGNCHGNC:9527. PSIP1.
HPACAB013718.
HPA019697.
MIM603620. gene.
neXtProtNX_O75475.
PharmGKBPA33872.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316844.
HOVERGENHBG108300.
InParanoidO75475.
OMACPSETDM.
OrthoDBEOG7NKKMQ.
PhylomeDBO75475.
TreeFamTF105385.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressO75475.
BgeeO75475.
CleanExHS_PSIP1.
GenevestigatorO75475.

Family and domain databases

InterProIPR021567. LEDGF.
IPR000313. PWWP_dom.
IPR017859. Treacle-like_TCS.
[Graphical view]
PfamPF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSPR01503. TREACLE.
SMARTSM00293. PWWP. 1 hit.
[Graphical view]
PROSITEPS50812. PWWP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSIP1. human.
EvolutionaryTraceO75475.
GeneWikiPSIP1.
GenomeRNAi11168.
NextBio42491.
PMAP-CutDBO75475.
PROO75475.
SOURCESearch...

Entry information

Entry namePSIP1_HUMAN
AccessionPrimary (citable) accession number: O75475
Secondary accession number(s): D3DRI9 expand/collapse secondary AC list , O00256, O95368, Q6P391, Q86YB9, Q9NZI3, Q9UER6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM