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    PSIP1 PC4 and SFRS1 interacting protein 1 [ Homo sapiens (human) ]

    Gene ID: 11168, updated on 24-Aug-2015
    Official Symbol
    PSIP1provided by HGNC
    Official Full Name
    PC4 and SFRS1 interacting protein 1provided by HGNC
    Primary source
    HGNC:HGNC:9527
    See related
    Ensembl:ENSG00000164985; HPRD:04688; MIM:603620; Vega:OTTHUMG00000021021
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    p52; p75; PAIP; DFS70; LEDGF; PSIP2
    Orthologs
    See PSIP1 in Epigenomics, MapViewer
    Location:
    9p22.3
    Exon count:
    18
    Annotation release Status Assembly Chr Location
    107 current GRCh38.p2 (GCF_000001405.28) 9 NC_000009.12 (15464066..15511005, complement)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 9 NC_000009.11 (15464064..15511003, complement)

    Chromosome 9 - NC_000009.12Genomic Context describing neighboring genes Neighboring gene tetratricopeptide repeat domain 39B Neighboring gene ribosomal protein L7 pseudogene 33 Neighboring gene small nuclear RNA activating complex, polypeptide 3, 50kDa Neighboring gene uncharacterized LOC105369291 Neighboring gene ferritin, heavy polypeptide 1 pseudogene 12 Neighboring gene coiled-coil domain containing 171 Neighboring gene high mobility group nucleosomal binding domain 2 pseudogene 16

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    Replication interactions

    Interaction Pubs
    Knockdown of LEDGF/p75 by shRNA enhances HIV-1 replication in HIV-1-infected CD4+ T-cells and latently infected cells PubMed

    Protein interactions

    Protein Gene Interaction Pubs
    Pol gag-pol LEDGF/p75 is recruited to HIV-1 particles through its direct interaction with the IN domain of Pol PubMed
    gag-pol HIV-1 Pol is identified to have a physical interaction with PC4 and SFRS1 interacting protein 1 (PSIP1; p75/LEDGF) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses PubMed
    Rev rev Rev 35-50, Rev 75-84, LEDGF 361-370, and LEDGF 402-411 peptides can specifically prevent formation of the Rev-LEDGF/p75 complex PubMed
    rev HIV-1 Rev interacts with LEDGF/p75 to promote dissociation of HIV-1 IN-LEDGF/p75 complex PubMed
    capsid gag LEDGF/p75 is incorporated in HIV-1 particles, and fractionates with HIV-1 CA and IN viral proteins in velocity gradient purification assay PubMed
    gag HIV-1 CA mutant N74D and depletion of NUP153 and LEDGF/p75 significantly reduce HIV-1 DNA integration into gene-rich regions of chromosomes and gene bodies PubMed
    gag HIV-1 CA mutants, including Q63A/Q67A, N74D, G89V, P90A, and A92E, are less dependent on LEDGF/p75 than the wild type CA in infectivity PubMed
    integrase gag-pol LEDGF/p75 is incorporated in HIV-1 particles, and fractionates with HIV-1 CA and IN viral proteins in velocity gradient purification assay PubMed
    gag-pol LEDGF/p75 is recruited to HIV-1 particles through its direct interaction with the IN domain of Pol PubMed
    gag-pol LEDGINs are novel allosteric HIV-1 IN inhibitors, which inhibit the catalytic activity of IN, abrogate the interaction between LEDGF/p75 and IN, and enhance IN oligomerization in viral particles PubMed
    gag-pol LEDGF/p75 complexes with HIV-1 integrase and stimulates integrase strand transfer activity in vitro PubMed
    gag-pol HIV-1 IN mutant K42E reduces its ability of binding to LEDGF/p75, whereas HIV-1 IN mutants EE10/13RR and EEE6/10/13RRE abolish to bind a detectable level of LEDGF/p75 PubMed
    gag-pol Small molecules are identified to inhibit HIV-1 IN dimerization, IN/viral DNA assembly, and/or IN/LEDGF interaction PubMed
    gag-pol (E)-3-(2-chlorophenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one (NPD170) shows the antiviral activity by blocking the binding of transfected IN to endogenous LEDGF/p75 in cells PubMed
    gag-pol N-(cyclohexylmethyl)-2,3-dihydroxy-5-(piperidin-1-ylsulfonyl) benzamide (5u) inhibits the HIV-1 IN-LEDGF/p75 interaction PubMed
    gag-pol 2-(quinolin-3-yl) acetic acid derivatives inhibit the IN-LEDGF interaction in vitro and impair HIV-1 replication in infected cells. PubMed
    gag-pol Studies on integrase strand transfer activity in vitro show that LEDGF/p75 only binds HIV-1 integrase before the latter binds donor DNA, whereas donor DNA engages either free or LEDGF/p75-bound integrase PubMed
    gag-pol LEDGF/p75 interferes with HIV-1 integrase (IN) full-site product formation by competing for HIV-1 IN dimer-dimer interactions or interfering with assembled synaptic complexes that harbor a single integrated end PubMed
    gag-pol LEDGF strongly stabilizes HIV-1 integrase-LEDGF/p75 interactions and promotes IN tetramerization PubMed
    gag-pol LEDGF/p75 binds to HIV-1 integrase (IN) and tethers IN to chromatin; the N-terminal PWWP domain (residues 1-93) in LEDGF/p75, and its beta-barrel substructure (first 63 residues) are required for chromatin binding and IN tethering to chromatin PubMed
    gag-pol The N-terminal zinc binding domain (amino acids 1-52) and the central core domain (amino acids 53-212) of HIV-1 integrase are involved in the interaction with LEDGF/p75, with the core domain harboring the main determinant for interaction PubMed
    gag-pol The interaction of HIV-1 integrase with LEDGF/p75 accounts for the karyophilic properties and chromosomal targeting of integrase, which co-localizes with LEDGF/p75 in the nuclei of human cells PubMed
    gag-pol The NMR structure of the integrase-binding domain (IBD) in LEDGF/p75 reveals that residues Ile365, Asp366, or Phe406 in LEDGF/p75 mediate binding to HIV-1 integrase, and amino acids 165-173 of HIV-1 integrase are involved in the binding to LEDGF/p75 PubMed
    gag-pol A single mutation at residue Q168 of HIV-1 integrase disrupts its interaction with LEDGF/p75 and results in defective HIV-1 replication PubMed
    gag-pol HIV-1 IN K264A/K266A mutant exhibits wild-type level of LEDGF/p75 binding, whereas A128T mutant displays slightly reduced binding to the cellular cofactor PubMed
    gag-pol Enhanced nuclear accumulation of HIV-1 IN in mouse MEF cells expressing human LEDGF/p75 suggests LEDGF/p75 stably transports the viral protein to chromatin PubMed
    gag-pol Molecular modeling study demonstrates that the LEDGF/p75 integrase binding domain residues Ile365, Asp366, Phe406 and Val408 have significant contributions to the binding of LEDGF/p75 to HIV1 IN PubMed
    gag-pol Depletion of LEDGF/p75 leads to the accumulation of HIV-1 IN complex, which contains tetramers of IN exclusively in nuclear. IN Q168A mutant fails to accumulate in a nuclear low molecular weight complex PubMed
    gag-pol Mass spectrometry and Fluorescence Correlation Spectroscopy analyses show a stable complex between HIV-1 IN, viral U5 DNA, LEDGF/p75, and the integrase binding domain (amino acids 174-289) of INI1 with a 4/2/2/2 stoichiometry PubMed
    gag-pol Knockdown of HRP-2 by siRNA in LEDGF/p75-depleted cells reduces integration frequency in transcription units and shifts the integration distribution towards random PubMed
    gag-pol HRP-2 functions as a co-factor of HIV-1 IN in LEDGF/p75-depleted cells. HRP-2 overexpression rescues HIV-1 replication and restored integration in genes to wild-type levels PubMed
    gag-pol The NLS (amino acids 148-156) and AT-hook like domains (amino acids 178-197) constitute important contributions to enhance the binding of HIV-1 Integrase (IN) to DNA PubMed
    gag-pol Three peptides (354-378, 360-370, 400-413) derived from the IBD of LEDGF compete with LEDGF binding to HIV-1 IN. LEDGF-354-378 peptide shows the strongest binding competition PubMed
    gag-pol In LEDGF/p75 knock-down cells, there is an increase in ubiquitinated HIV-1 integrase, which is found exclusively in the cytoplasm of these cells, and protection of HIV-1 integrase from the proteasome requires only interaction with LEDGF/p75 PubMed
    gag-pol Using a pull-down assay, LEDGF/p75 interacts with HIV-1, HIV-2, and FIV integrases and strongly promotes the binding of HIV-1 integrase to DNA in vitro PubMed
    gag-pol HIV-1 integrase (IN) increases the binding strength of LEDGF/p75 deltaPWWP to chromatin, which requires the direct interaction of these two proteins. Integrase fails to increase chromatin binding of a LEDGF/p75 deltaPWWP/AT mutant PubMed
    gag-pol HIV-1 IN mutant K264E supports the wild-type level of concerted integration activity and the efficient integration of endogenous viral DNA in vitro in the presence of LEDGF/p75 PubMed
    gag-pol The triple mutant RRK262/3/4/EEE in HIV-1 IN still maintains wild type levels of binding with LEDGF/p75 PubMed
    gag-pol LEDGF-derived peptides inhibit HIV-1 IN binding to DNA by shifting its oligomerization equilibrium toward the tetramer. The LEDGF peptides inhibit HIV-1 replication in cell culture by eliminating viral DNA integration PubMed
    gag-pol The 146-156 amino acid stretch of LEDGF/p75 is critical for nuclear localization and a single amino acid mutation at K150A in LEDGF/p75 renders HIV-1 integrase cytoplasmic PubMed
    gag-pol Two LEDGF mutants (K401E/K402S/R405E and K401E/K402E/R405E) fail to interact with HIV-1 IN. The IN mutant (D6K/E10K/E13K) complements the interaction with the LEDGF mutant (K401E/K402E/R405E) PubMed
    gag-pol Replacing the N-terminal domain ensemble (NDE) of IN with strongly divergent chromatin-binding modules (i.e. H1 or KSHV LANA) can rescue integrase tethering and HIV-1 integration in LEDGF/p75-deficient cells PubMed
    gag-pol A serine cluster (residues 271, 273, and 275) in LEDGF/p75 is phosphorylated by protein kinase casein kinase 2 (PKCK2). S271/273/275A mutant impairs LEDGF/p75-mediate HIV-1 DNA integration without altering IN and chromatin binding PubMed
    gag-pol Alanine scan, fluorescence anisotropy studies, homology modeling and NMR demonstrate that all residues in LEDGF 361-370 contribute to IN binding and inhibition. Kinetic studies in cells show direct inhibition of viral cDNA integration by LEDGF 361-370 PubMed
    gag-pol A bi-helix motif (residues 149-186) in HIV-1 IN consists of the alpha(4) and alpha(5) helices connected by a 3 to 5-residue turn and binds to the LTR ends of virus DNA and to the IN binding domain (IBD) but not the IBD-Asp366Asn variant of LEDGF PubMed
    gag-pol HIV-1 integrase (IN) and JPO2 bind mutually exclusively to LEDGF/p75. Two LEDGF/p75 mutants (I365A and D366N) abrogate interaction between LEDGF/p75 and IN but interact with JPO2 to the same extent as wild-type LEDGF/p75 PubMed
    gag-pol HIV-1 integration in cells depleted for LEDGF/p75 is less frequent in transcription units, less frequent in genes regulated by LEDGF/p75 and more frequent in GC-rich DNA PubMed
    gag-pol Results from molecular dynamics simulations show residues Gln168, Glu170 and Thr174 in chain A of HIV-1 Integrase (IN), Thr125 and Trp131 in chain B of IN as well as Ile365, Asp366, Phe406 and Val408 in LEDGF/p75 are responsible for IN-LEDGF/p75 binding PubMed
    gag-pol HIV-1 IN mutants (V165A, A179P, and KR186,7AA) exhibit no chromatin-binding ability and fails to interact with LEDGF/p75 PubMed
    gag-pol HIV-1 Rev interacts with LEDGF/p75 to promote dissociation of HIV-1 IN-LEDGF/p75 complex PubMed
    gag-pol A domesticated transposase, pogZ, carries a DDE domain (amino acids 1117-1323) and interacts with LEDGF/p75. HIV-1 IN is efficient in displacing pogZ from LEDGF/p75 PubMed
    gag-pol Mass spectrometry analysis shows a stable complex between human LEDGF/p75 and HIV-1 IN with a stoichiometry of 2 LEDGF/p75 and 4 IN PubMed
    gag-pol The C-terminal domain of HIV-1 IN is masked in the presence of LEDGF/p75 protein in cell lysates, suggesting a structural rearrangement or oligomerization of IN PubMed
    gag-pol HIV-1 IN mutants (H171A, L172A, and EH170,1AA), located between the alpha4 and alpha5 helices of IN, severely impair the interaction with LEDGF/p75 but are still able to bind chromatin, suggesting IN-mediated LEDGF-independent chromatin targeting PubMed
    gag-pol Multiangle light scattering and small angle x-ray scattering analysis indicate full-length IN (wild-type and C56S/F139D/F185H/C280S mutant) and LEDGF/p75 (amino acids 325-530) form a tetramer complex with stoichiometry 4:4 PubMed
    gag-pol Multiangle light scattering and small angle x-ray scattering analysis indicate full-length IN (C56S/F139D/F185H/C280S) and LEDGF/p75 (amino acids 347-471) form a tetramer, where each IN dimer binds only one LEDGF/p75 PubMed
    gag-pol Analytical ultracentrifugation indicates IN (amino acids 1-212) and LEDGF/p75 (amino acids 347-471) form a complex with a molecular weight consistent with a 2:2 complex PubMed
    gag-pol Overexpression of the integrase binding domain (IBD) of LEDGF/p75 severely inhibits HIV-1 replication, while no inhibition is observed in cell lines overexpressing the interaction-deficient D366A mutant of integrase PubMed
    gag-pol A single mutation at residue A128 or H171 of HIV-1 integrase diminishes its interaction with LEDGF/p75 PubMed
    gag-pol Intensified RNA interference and dominant-negative protein approaches show that LEDGF/p75 is an essential linkage between HIV-1 integrase and chromatin PubMed
    gag-pol T-cell lines expressing a C-terminal fragment (residues 325-530) of LEDGF/p75 exhibit a reduced affinity of integrase for LEDGF/p75 and the blockage of viral replication. Both A128T and E170G IN mutations are together sufficient for viral rescue PubMed
    retropepsin gag-pol HIV-1 PR cleaves LEDGF/p75 at amino-acid positions 110-111, 159-160, 357-358, and 433-434 in HIV-1 particles PubMed

    Go to the HIV-1, Human Interaction Database

    • 2-LTR circle formation, organism-specific biosystem (from REACTOME)
      2-LTR circle formation, organism-specific biosystemThe formation of 2-LTR circles requires the action of the cellular non-homologous DNA end-joining pathway. Specifically the cellular Ku, XRCC4 and ligase IV proteins are needed. Evidence for this i...
    • APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystem (from REACTOME)
      APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystemRepresentatives of the apolipoprotein B mRNA editing enzyme catalytic polypeptide 3 (APOBEC3) family provide innate resistance to exogeneous and endogenous retroviruses (see Cullen 2006 for a recent ...
    • Autointegration results in viral DNA circles, organism-specific biosystem (from REACTOME)
      Autointegration results in viral DNA circles, organism-specific biosystemIn this pathway, the viral integration machinery uses a site within the viral DNA as an integration target. This results in a covalent rearrangment of the viral DNA. The resulting DNA forms are no...
    • Disease, organism-specific biosystem (from REACTOME)
      Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
    • Early Phase of HIV Life Cycle, organism-specific biosystem (from REACTOME)
      Early Phase of HIV Life Cycle, organism-specific biosystemIn the early phase of HIV lifecycle, an active virion binds and enters a target cell mainly by specific interactions of the viral envelope proteins with host cell surface receptors. The virion core...
    • HIV Infection, organism-specific biosystem (from REACTOME)
      HIV Infection, organism-specific biosystemThe global pandemic of Human Immunodeficiency Virus (HIV) infection has resulted in tens of millions of people infected by the virus and millions more affected. UNAIDS estimates around 40 million ...
    • HIV Life Cycle, organism-specific biosystem (from REACTOME)
      HIV Life Cycle, organism-specific biosystemThe life cycle of HIV-1 is divided into early and late phases, shown schematically in the figure. In the early phase, an HIV-1 virion binds to receptors and co-receptors on the human host cell surfac...
    • Host Interactions of HIV factors, organism-specific biosystem (from REACTOME)
      Host Interactions of HIV factors, organism-specific biosystemLike all viruses, HIV-1 must co-opt the host cell macromolecular transport and processing machinery. HIV-1 Vpr and Rev proteins play key roles in this co-optation. Efficient HIV-1 replication likewis...
    • Infectious disease, organism-specific biosystem (from REACTOME)
      Infectious disease, organism-specific biosystem
      Infectious disease
    • Integration of provirus, organism-specific biosystem (from REACTOME)
      Integration of provirus, organism-specific biosystemFor retroviral DNA to direct production of progeny virions it must become covalently integrated into the host cell chromosome (reviewed in Coffin et al. 1997; Hansen et al. 1998). Analyses of mutants...
    • Integration of viral DNA into host genomic DNA, organism-specific biosystem (from REACTOME)
      Integration of viral DNA into host genomic DNA, organism-specific biosystemFollowing nuclear entry, the viral preintegration complex (PIC) must select a site for integration in a host cell chromosome, and then carry out the chemical steps of the reaction. At the chromosomal...
    • Interactions of Vpr with host cellular proteins, organism-specific biosystem (from REACTOME)
      Interactions of Vpr with host cellular proteins, organism-specific biosystemVpr has been implicated in multiple processes during HIV-1 replication, including nuclear import of the pre-integration complex (PIC)(Heinzinger et al., 1994), apoptosis (Stewart et al., 1997) and in...
    • Vpr-mediated nuclear import of PICs, organism-specific biosystem (from REACTOME)
      Vpr-mediated nuclear import of PICs, organism-specific biosystemVpr appears to function in anchoring the PIC to the nuclear envelope. This anchoring likely involves interactions between Vpr and host nucleoporins.
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Clone Names

    • MGC74712

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    RNA polymerase II transcription coactivator activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    activating transcription factor binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    chromatin binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    poly(A) RNA binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    supercoiled DNA binding ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    Process Evidence Code Pubs
    establishment of integrated proviral latency TAS
    Traceable Author Statement
    more info
     
    mRNA 5'-splice site recognition IDA
    Inferred from Direct Assay
    more info
    PubMed 
    positive regulation of transcription from RNA polymerase II promoter IDA
    Inferred from Direct Assay
    more info
    PubMed 
    regulation of transcription, DNA-templated IEA
    Inferred from Electronic Annotation
    more info
     
    response to heat ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    response to oxidative stress ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    transcription, DNA-templated IEA
    Inferred from Electronic Annotation
    more info
     
    viral process TAS
    Traceable Author Statement
    more info
     
    Component Evidence Code Pubs
    cytosol TAS
    Traceable Author Statement
    more info
     
    nuclear heterochromatin IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nuclear periphery IDA
    Inferred from Direct Assay
    more info
    PubMed 
    NOT nucleolus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nucleoplasm IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nucleoplasm TAS
    Traceable Author Statement
    more info
     
    nucleus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    transcriptionally active chromatin ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    Preferred Names
    PC4 and SFRS1-interacting protein
    Names
    CLL-associated antigen KW-7
    DFS 70
    dense fine speckles 70 kDa protein
    lens epithelium-derived growth factor
    transcriptional coactivator p52/p75
    transcriptional coactivator p75/p52

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001128217.1NP_001121689.1  PC4 and SFRS1-interacting protein isoform 2

      See identical proteins and their annotated locations for NP_001121689.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR, 3' UTR, and 3' coding region, compared to variant 1. This results in a protein (isoform 2) with a longer, distinct C-terminus, compared to isoform 1. Variants 2 and 3 encode the same protein (isoform 2).
      Source sequence(s)
      AF063020, AF432220, AL441925, DA117094
      Consensus CDS
      CCDS6479.1
      UniProtKB/Swiss-Prot
      O75475
      Related
      ENSP00000370114, OTTHUMP00000022754, ENST00000380738, OTTHUMT00000055446
      Conserved Domains (2) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
      pfam11467
      Location:349455
      LEDGF; Lens epithelium-derived growth factor (LEDGF)
    2. NM_021144.3NP_066967.3  PC4 and SFRS1-interacting protein isoform 1

      See identical proteins and their annotated locations for NP_066967.3

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the shortest transcript and encodes isoform 1.
      Source sequence(s)
      AF098482, BC064135, BQ186453, BX649155
      Consensus CDS
      CCDS6480.1
      UniProtKB/Swiss-Prot
      O75475
      Related
      ENSP00000380653, ENST00000397519
      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
    3. NM_033222.3NP_150091.2  PC4 and SFRS1-interacting protein isoform 2

      See identical proteins and their annotated locations for NP_150091.2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR, 3' UTR, and 3' coding region, compared to variant 1. This results in a protein (isoform 2) with a longer, distinct C-terminus, compared to isoform 1. Variants 2 and 3 encode the same protein (isoform 2).
      Source sequence(s)
      AF063020, AL441925, DA117094
      Consensus CDS
      CCDS6479.1
      UniProtKB/Swiss-Prot
      O75475
      Related
      ENSP00000370109, OTTHUMP00000022753, ENST00000380733, OTTHUMT00000055445
      Conserved Domains (2) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
      pfam11467
      Location:349455
      LEDGF; Lens epithelium-derived growth factor (LEDGF)

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p2 Primary Assembly

    Genomic

    1. NC_000009.12 Reference GRCh38.p2 Primary Assembly

      Range
      15464066..15511005
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_005251358.1XP_005251415.1  

      See identical proteins and their annotated locations for XP_005251415.1

      UniProtKB/Swiss-Prot
      O75475
      Related
      ENSP00000370091, OTTHUMP00000022755, ENST00000380715, OTTHUMT00000055448
      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
    2. XM_011517697.1XP_011515999.1  

      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
    3. XM_011517699.1XP_011516001.1  

      See identical proteins and their annotated locations for XP_011516001.1

      UniProtKB/Swiss-Prot
      O75475
      Related
      ENSP00000370092, OTTHUMP00000022756, ENST00000380716, OTTHUMT00000055449
      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
    4. XM_011517698.1XP_011516000.1  

      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...
    5. XM_011517700.1XP_011516002.1  

      Conserved Domains (1) summary
      cd05834
      Location:387
      HDGF_related; The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, ...

    Alternate CHM1_1.1

    Genomic

    1. NC_018920.2 Alternate CHM1_1.1

      Range
      15464652..15511590
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)