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O75475

- PSIP1_HUMAN

UniProt

O75475 - PSIP1_HUMAN

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Protein

PC4 and SFRS1-interacting protein

Gene

PSIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. activating transcription factor binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA polymerase II transcription coactivator activity Source: UniProtKB
  5. supercoiled DNA binding Source: UniProtKB

GO - Biological processi

  1. establishment of integrated proviral latency Source: Reactome
  2. mRNA 5'-splice site recognition Source: UniProtKB
  3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. response to heat Source: UniProtKB
  6. response to oxidative stress Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
  8. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PSIP1
Synonyms:DFS70, LEDGF, PSIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:9527. PSIP1.

Subcellular locationi

Nucleus 2 Publications
Note: Remains chromatin-associated throughout the cell cycle.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nuclear heterochromatin Source: UniProtKB
  3. nuclear periphery Source: UniProtKB
  4. nucleoplasm Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi360 – 3601K → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. 1 Publication
Mutagenesisi365 – 3651I → A: Loss of interaction with human HIV-1 integrase; reduced interaction with POGZ and CDCA7L. 2 Publications
Mutagenesisi366 – 3661D → A or N: Loss of interaction with human HIV-1 integrase; no effect on interaction with CDCA7L. 2 Publications
Mutagenesisi366 – 3661D → A: No effect on interaction with POGZ. 2 Publications
Mutagenesisi370 – 3701V → A: Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. 1 Publication
Mutagenesisi406 – 4061F → A: Loss of interaction with human HIV-1 integrase and POGZ; reduced interaction with CDCA7L. 2 Publications
Mutagenesisi408 – 4081V → A: Reduced interaction with human HIV-1 integrase; no effect on interaction with POGZ and CDCA7L. 2 Publications

Organism-specific databases

PharmGKBiPA33872.

Protein family/group databases

Allergomei2120. Hom s DSF70.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530PC4 and SFRS1-interacting proteinPRO_0000191708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei106 – 1061Phosphoserine3 Publications
Modified residuei122 – 1221Phosphothreonine2 Publications
Modified residuei129 – 1291Phosphoserine1 Publication
Modified residuei141 – 1411Phosphothreonine4 Publications
Modified residuei167 – 1671Phosphothreonine1 Publication
Modified residuei177 – 1771Phosphoserine2 Publications
Modified residuei206 – 2061Phosphoserine2 Publications
Modified residuei273 – 2731Phosphoserine3 Publications
Modified residuei275 – 2751Phosphoserine4 Publications
Modified residuei434 – 4341Phosphoserine2 Publications
Modified residuei437 – 4371Phosphothreonine1 Publication
Modified residuei443 – 4431Phosphoserine1 Publication
Modified residuei517 – 5171CitrullineBy similarity
Modified residuei522 – 5221Phosphoserine1 Publication
Modified residuei527 – 5271Phosphothreonine3 Publications

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

MaxQBiO75475.
PaxDbiO75475.
PeptideAtlasiO75475.
PRIDEiO75475.

Miscellaneous databases

PMAP-CutDBO75475.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiO75475.
CleanExiHS_PSIP1.
ExpressionAtlasiO75475. baseline and differential.
GenevestigatoriO75475.

Organism-specific databases

HPAiCAB013718.
HPA019697.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
gag-polP0458521EBI-1801773,EBI-3989067From a different organism.
SUMO1P631654EBI-1801773,EBI-80140

Protein-protein interaction databases

BioGridi116339. 40 interactions.
DIPiDIP-46656N.
IntActiO75475. 11 interactions.
MINTiMINT-4527154.
STRINGi9606.ENSP00000370109.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Beta strandi10 – 134Combined sources
Beta strandi21 – 255Combined sources
Beta strandi30 – 334Combined sources
Beta strandi40 – 445Combined sources
Turni45 – 473Combined sources
Beta strandi50 – 534Combined sources
Helixi55 – 573Combined sources
Beta strandi58 – 603Combined sources
Helixi61 – 688Combined sources
Helixi77 – 8610Combined sources
Helixi347 – 36216Combined sources
Helixi365 – 3673Combined sources
Helixi370 – 38112Combined sources
Helixi387 – 3915Combined sources
Helixi394 – 40310Combined sources
Helixi410 – 42516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z9ENMR-A347-471[»]
2B4JX-ray2.02C/D347-442[»]
2M16NMR-A1-93[»]
2MSRNMR-B344-426[»]
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[»]
ProteinModelPortaliO75475.
SMRiO75475. Positions 1-93, 348-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75475.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6464PWWPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili306 – 33429Sequence AnalysisAdd
BLAST
Coiled coili371 – 39525Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi146 – 15611Nuclear localization signal1 PublicationAdd
BLAST

Domaini

Residues 340-417 are necessary and sufficient for the interaction with HIV-1 IN (IBD domain).

Sequence similaritiesi

Belongs to the HDGF family.Curated
Contains 1 PWWP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG316844.
GeneTreeiENSGT00530000063013.
HOVERGENiHBG108300.
InParanoidiO75475.
OMAiCPSETDM.
OrthoDBiEOG7NKKMQ.
PhylomeDBiO75475.
TreeFamiTF105385.

Family and domain databases

InterProiIPR021567. LEDGF.
IPR000313. PWWP_dom.
IPR017859. Treacle-like_TCS.
[Graphical view]
PfamiPF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSiPR01503. TREACLE.
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
PROSITEiPS50812. PWWP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75475-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET
60 70 80 90 100
AFLGPKDIFP YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK
110 120 130 140 150
QSNASSDVEV EEKETSVSKE DTDHEEKASN EDVTKAVDIT TPKAARRGRK
160 170 180 190 200
RKAEKQVETE EAGVVTTATA SVNLKVSPKR GRPAATEVKI PKPRGRPKMV
210 220 230 240 250
KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE EDKPRKEPDK
260 270 280 290 300
KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR
310 320 330 340 350
NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS
360 370 380 390 400
RLQRIHAEIK NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL
410 420 430 440 450
KKIRRFKVSQ VIMEKSTMLY NKFKNMFLVG EGDSVITQVL NKSLAEQRQH
460 470 480 490 500
EEANKTKDQG KKGPNKKLEK EQTGSKTLNG GSDAQDGNQP QHNGESNEDS
510 520 530
KDNHEASTKK KPSSEERETE ISLKDSTLDN

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

Length:530
Mass (Da):60,103
Last modified:November 1, 1998 - v1
Checksum:i4B653D02B1D0E174
GO
Isoform 2 (identifier: O75475-2) [UniParc]FASTAAdd to Basket

Also known as: p52, PSIP2

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

Show »
Length:333
Mass (Da):37,725
Checksum:iDAFEC8F815C06FCD
GO
Isoform 3 (identifier: O75475-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:329
Mass (Da):37,268
Checksum:iF35C00DDD27E9BAE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1619Missing in AAH64135. (PubMed:15489334)Curated
Sequence conflicti224 – 2241E → G in AAC97946. (PubMed:9822615)Curated
Sequence conflicti224 – 2241E → G in AAC97945. (PubMed:9822615)Curated
Sequence conflicti272 – 2721T → P in AAB52589. (PubMed:10856157)Curated
Sequence conflicti420 – 4201Y → F in AAC97946. (PubMed:9822615)Curated
Sequence conflicti420 – 4201Y → F in AAB52589. (PubMed:10856157)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 530205QQNKD…STLDN → HFAL in isoform 3. 1 PublicationVSP_044435Add
BLAST
Alternative sequencei326 – 3338QQNKDEGK → HQTTCNLQ in isoform 2. 2 PublicationsVSP_014297
Alternative sequencei334 – 530197Missing in isoform 2. 2 PublicationsVSP_014298Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6479.1. [O75475-1]
CCDS6480.1. [O75475-2]
PIRiJC7168.
RefSeqiNP_001121689.1. NM_001128217.1. [O75475-1]
NP_066967.3. NM_021144.3. [O75475-2]
NP_150091.2. NM_033222.3. [O75475-1]
XP_005251413.1. XM_005251356.1. [O75475-2]
XP_005251415.1. XM_005251358.1. [O75475-3]
UniGeneiHs.658434.

Genome annotation databases

EnsembliENST00000380715; ENSP00000370091; ENSG00000164985. [O75475-3]
ENST00000380716; ENSP00000370092; ENSG00000164985. [O75475-2]
ENST00000380733; ENSP00000370109; ENSG00000164985. [O75475-1]
ENST00000380738; ENSP00000370114; ENSG00000164985. [O75475-1]
ENST00000397519; ENSP00000380653; ENSG00000164985. [O75475-2]
GeneIDi11168.
KEGGihsa:11168.
UCSCiuc003zlv.4. human. [O75475-1]
uc003zly.3. human. [O75475-3]
uc003zlz.4. human. [O75475-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6479.1. [O75475-1 ]
CCDS6480.1. [O75475-2 ]
PIRi JC7168.
RefSeqi NP_001121689.1. NM_001128217.1. [O75475-1 ]
NP_066967.3. NM_021144.3. [O75475-2 ]
NP_150091.2. NM_033222.3. [O75475-1 ]
XP_005251413.1. XM_005251356.1. [O75475-2 ]
XP_005251415.1. XM_005251358.1. [O75475-3 ]
UniGenei Hs.658434.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
2MSR NMR - B 344-426 [» ]
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 [» ]
3ZEH NMR - A 3-100 [» ]
4FU6 X-ray 2.10 A 1-135 [» ]
ProteinModelPortali O75475.
SMRi O75475. Positions 1-93, 348-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116339. 40 interactions.
DIPi DIP-46656N.
IntActi O75475. 11 interactions.
MINTi MINT-4527154.
STRINGi 9606.ENSP00000370109.

Protein family/group databases

Allergomei 2120. Hom s DSF70.

Proteomic databases

MaxQBi O75475.
PaxDbi O75475.
PeptideAtlasi O75475.
PRIDEi O75475.

Protocols and materials databases

DNASUi 11168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380715 ; ENSP00000370091 ; ENSG00000164985 . [O75475-3 ]
ENST00000380716 ; ENSP00000370092 ; ENSG00000164985 . [O75475-2 ]
ENST00000380733 ; ENSP00000370109 ; ENSG00000164985 . [O75475-1 ]
ENST00000380738 ; ENSP00000370114 ; ENSG00000164985 . [O75475-1 ]
ENST00000397519 ; ENSP00000380653 ; ENSG00000164985 . [O75475-2 ]
GeneIDi 11168.
KEGGi hsa:11168.
UCSCi uc003zlv.4. human. [O75475-1 ]
uc003zly.3. human. [O75475-3 ]
uc003zlz.4. human. [O75475-2 ]

Organism-specific databases

CTDi 11168.
GeneCardsi GC09M015456.
HGNCi HGNC:9527. PSIP1.
HPAi CAB013718.
HPA019697.
MIMi 603620. gene.
neXtProti NX_O75475.
PharmGKBi PA33872.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316844.
GeneTreei ENSGT00530000063013.
HOVERGENi HBG108300.
InParanoidi O75475.
OMAi CPSETDM.
OrthoDBi EOG7NKKMQ.
PhylomeDBi O75475.
TreeFami TF105385.

Enzyme and pathway databases

Reactomei REACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Miscellaneous databases

ChiTaRSi PSIP1. human.
EvolutionaryTracei O75475.
GeneWikii PSIP1.
GenomeRNAii 11168.
NextBioi 42491.
PMAP-CutDB O75475.
PROi O75475.
SOURCEi Search...

Gene expression databases

Bgeei O75475.
CleanExi HS_PSIP1.
ExpressionAtlasi O75475. baseline and differential.
Genevestigatori O75475.

Family and domain databases

InterProi IPR021567. LEDGF.
IPR000313. PWWP_dom.
IPR017859. Treacle-like_TCS.
[Graphical view ]
Pfami PF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view ]
PRINTSi PR01503. TREACLE.
SMARTi SM00293. PWWP. 1 hit.
[Graphical view ]
PROSITEi PS50812. PWWP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiPSIP1_HUMAN
AccessioniPrimary (citable) accession number: O75475
Secondary accession number(s): D3DRI9
, O00256, O95368, Q6P391, Q86YB9, Q9NZI3, Q9UER6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 137 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3