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O75475

- PSIP1_HUMAN

UniProt

O75475 - PSIP1_HUMAN

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. RNA polymerase II transcription coactivator activity Source: UniProtKB
    6. 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

    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

    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

    ArrayExpressiO75475.
    BgeeiO75475.
    CleanExiHS_PSIP1.
    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. 39 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 – 43
    Beta strandi10 – 134
    Beta strandi21 – 255
    Beta strandi30 – 334
    Beta strandi40 – 445
    Turni45 – 473
    Beta strandi50 – 534
    Helixi55 – 573
    Beta strandi58 – 603
    Helixi61 – 688
    Helixi77 – 8610
    Helixi347 – 36216
    Helixi365 – 3673
    Helixi370 – 38112
    Helixi387 – 3915
    Helixi394 – 40310
    Helixi410 – 42516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    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.
    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

    MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET    50
    AFLGPKDIFP YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK 100
    QSNASSDVEV EEKETSVSKE DTDHEEKASN EDVTKAVDIT TPKAARRGRK 150
    RKAEKQVETE EAGVVTTATA SVNLKVSPKR GRPAATEVKI PKPRGRPKMV 200
    KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE EDKPRKEPDK 250
    KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR 300
    NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS 350
    RLQRIHAEIK NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL 400
    KKIRRFKVSQ VIMEKSTMLY NKFKNMFLVG EGDSVITQVL NKSLAEQRQH 450
    EEANKTKDQG KKGPNKKLEK EQTGSKTLNG GSDAQDGNQP QHNGESNEDS 500
    KDNHEASTKK KPSSEERETE ISLKDSTLDN 530

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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. 39 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.
    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

    ArrayExpressi O75475.
    Bgeei O75475.
    CleanExi HS_PSIP1.
    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

    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: October 1, 2014
    This is version 135 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