PSIP1 PC4 and SRSF1 interacting protein 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PSIP1provided by HGNC
Official Full Name: PC4 and SRSF1 interacting protein 1provided by HGNC
Primary source: HGNC:HGNC:9527
See related: Ensembl:ENSG00000164985 MIM:603620; AllianceGenome:HGNC:9527
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
Summary: Enables DNA-binding transcription factor binding activity; chromatin binding activity; and transcription coactivator activity. Involved in mRNA 5'-splice site recognition and positive regulation of transcription by RNA polymerase II. Located in heterochromatin; nuclear periphery; and nucleoplasm. [provided by Alliance of Genome Resources, Oct 2024]
Expression: Ubiquitous expression in brain (RPKM 41.2), ovary (RPKM 33.4) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 9p22.3

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	9	NC_000009.12 (15464066..15510970, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	9	NC_060933.1 (15475998..15522882, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	9	NC_000009.11 (15464064..15510968, complement)

Chromosome 9 - NC_000009.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PSIP1/LEDGF reduces R-loops at transcription sites to maintain genome integrity.
Title: PSIP1/LEDGF reduces R-loops at transcription sites to maintain genome integrity.
The LncRNA MIR155HG is Upregulated by SP1 in Melanoma Cells and Drives Melanoma Progression via Modulating the MiR-485-3p/PSIP1 Axis.
Title: The LncRNA MIR155HG is Upregulated by SP1 in Melanoma Cells and Drives Melanoma Progression via Modulating the MiR-485-3p/PSIP1 Axis.
Modulation of the intrinsic chromatin binding property of HIV-1 integrase by LEDGF/p75.
Title: Modulation of the intrinsic chromatin binding property of HIV-1 integrase by LEDGF/p75.
The LEDGF/p75 Integrase Binding Domain Interactome Contributes to the Survival, Clonogenicity, and Tumorsphere Formation of Docetaxel-Resistant Prostate Cancer Cells.
Title: The LEDGF/p75 Integrase Binding Domain Interactome Contributes to the Survival, Clonogenicity, and Tumorsphere Formation of Docetaxel-Resistant Prostate Cancer Cells.
LEDGF/p75 Is Required for an Efficient DNA Damage Response.
Title: LEDGF/p75 Is Required for an Efficient DNA Damage Response.
Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R Leukemogenesis but Important for Leukemic Cell Survival.
Title: Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R Leukemogenesis but Important for Leukemic Cell Survival.
Targeted editing of the PSIP1 gene encoding LEDGF/p75 protects cells against HIV infection.
Title: Targeted editing of the PSIP1 gene encoding LEDGF/p75 protects cells against HIV infection.
LEDGF and HDGF2 colocalize with Histone H3 lysine 36 methylation 2/3 at genomic regions containing active genes.
Title: LEDGF and HDGF2 relieve the nucleosome-induced barrier to transcription in differentiated cells.
This study reports the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-A resolution.
Title: Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding.
antibodies more frequent in systemic autoimmune rheumatic disease patients than in blood donors
Title: Investigation of anti-DFS70 antibody in patients with systemic autoimmune rheumatic diseases.

Submit: New GeneRIF Correction See all GeneRIFs (107)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV-1 LAI replication requires PSIP1 (LEDGF) and TNPO3 expression as shown through CRISPR/Cas9 genome editing in primary CD4+ T cells	PubMed
HIV-1 replication, specifically reactivation, requires PSIP1 (LEDGF/p75) as shown through inhibition with LEDGINs	PubMed
HIV-1 replication requires PSIP1 (LEDGF/p75) and TPR to maintain chromatin structure amenable to integration as shown through shRNA treatment	PubMed
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	HIV-1 Integrase interacts with PSIP1 (LEDGF/p75) to determine the site of integration	PubMed
	gag-pol	PSIP1 (LEDGF/p75) L368A mutant demonstrates reduced binding to HIV-1 IN	PubMed
	gag-pol	PSIP1 (LEDGF/p75) K407D mutation increases binding to HIV-1 IN	PubMed
	gag-pol	The IN catalytic core domain has a higher binding affinity (Kd) for PSIP1 (LEDGF/p75) than the physiological binding partners, CDCA7L (JOP2), POGZ, KMT2A (MML1) and IWS1	PubMed
	gag-pol	The HIV IN interaction site on the PSIP1 (LEDGF/p75) intergrase binding domain (IBD) overlaps with that of POGZ, JPO2 and KMT2A (MLL1)	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	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	LEDGF/p75 complexes with HIV-1 integrase and stimulates integrase strand transfer activity in vitro	PubMed
	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	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 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	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

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH16596 (e-PCR)
- UniSTS:38460

D10S16 (e-PCR)
- UniSTS:155756

D9S1149 (e-PCR)
- UniSTS:83064

STS-R43279 (e-PCR)
- UniSTS:27262

G27467 (e-PCR)
- UniSTS:62598

G35007 (e-PCR)
- UniSTS:55180

SHGC-64828 (e-PCR)
- UniSTS:42662

RH102634 (e-PCR)
- UniSTS:96968

RH92265 (e-PCR)
- UniSTS:91365

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables DNA-binding transcription factor binding	IDA Inferred from Direct Assay more info	PubMed
enables RNA binding	HDA more info	PubMed
enables chromatin binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables supercoiled DNA binding	ISS Inferred from Sequence or Structural Similarity more info
enables transcription coactivator activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in mRNA 5'-splice site recognition	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in response to heat	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to oxidative stress	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in cytosol	TAS Traceable Author Statement more info
located_in euchromatin	ISS Inferred from Sequence or Structural Similarity more info
located_in heterochromatin	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear periphery	IDA Inferred from Direct Assay more info	PubMed
NOT located_in nucleolus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	TAS Traceable Author Statement more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: PC4 and SFRS1-interacting protein

Names: CLL-associated antigen KW-7; PC4 and SFRS1 interacting protein 1; dense fine speckles 70 kDa protein; lens epithelium-derived growth factor; transcriptional coactivator p52/p75

NCBI Reference Sequences (RefSeq)

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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)

NM_001128217.3 → NP_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, BI547490

Consensus CDS

CCDS6479.1

UniProtKB/Swiss-Prot

D3DRI9, O00256, O75475, O95368, Q6P391, Q86YB9, Q9NZI3, Q9UER6

Related

ENSP00000370114.4, ENST00000380738.8

Conserved Domains (3) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 525

PTZ00121; MAEBL; Provisional

pfam11467
Location:349 → 442

LEDGF; Lens epithelium-derived growth factor (LEDGF)
NM_001317898.3 → NP_001304827.1 PC4 and SFRS1-interacting protein isoform 3

Status: VALIDATED

Description

Transcript Variant: This variant (4) differs in the 5' UTR and uses an alternate splice site in the 3' terminal exon, compared to variant 1. This variant encodes isoform 3, which is shorter and has a distinct C-terminus compared to isoform 1.

Source sequence(s)

AL513423, BC044568

Consensus CDS

CCDS83348.1

UniProtKB/Swiss-Prot

O75475

Related

ENSP00000370091.1, ENST00000380715.5

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 325

PTZ00121; MAEBL; Provisional
NM_001317900.3 → NP_001304829.1 PC4 and SFRS1-interacting protein isoform 4

Status: VALIDATED

Description

Transcript Variant: This variant (5) differs in the 5' UTR and uses an alternate in-frame splice site in the coding region, compared to variant 1. This variant encodes isoform 4, which is shorter than isoform 1.

Source sequence(s)

AL513423, BC064135, BI547490

UniProtKB/Swiss-Prot

O75475

Conserved Domains (1) summary

cd05834
Location:3 → 87

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, ...
NM_021144.4 → NP_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, AL513423, BC064135, BQ186453, BX649155

Consensus CDS

CCDS6480.1

UniProtKB/Swiss-Prot

O75475

Related

ENSP00000380653.2, ENST00000397519.6

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 325

PTZ00121; MAEBL; Provisional
NM_033222.5 → NP_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

Consensus CDS

CCDS6479.1

UniProtKB/Swiss-Prot

D3DRI9, O00256, O75475, O95368, Q6P391, Q86YB9, Q9NZI3, Q9UER6

Related

ENSP00000370109.4, ENST00000380733.9

Conserved Domains (3) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 525

PTZ00121; MAEBL; Provisional

pfam11467
Location:349 → 442

LEDGF; Lens epithelium-derived growth factor (LEDGF)

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000009.12 Reference GRCh38.p14 Primary Assembly

Range

15464066..15510970 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047422702.1 → XP_047278658.1 PC4 and SFRS1-interacting protein isoform X1
XM_047422703.1 → XP_047278659.1 PC4 and SFRS1-interacting protein isoform X2

Related

ENSP00000370092.4, ENST00000380716.8
XM_024447399.2 → XP_024303167.1 PC4 and SFRS1-interacting protein isoform X1

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

cl26511
Location:89 → 344

Neuromodulin_N; Gap junction protein N-terminal region
XM_024447400.2 → XP_024303168.1 PC4 and SFRS1-interacting protein isoform X2

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 325

PTZ00121; MAEBL; Provisional
XM_024447402.2 → XP_024303170.1 PC4 and SFRS1-interacting protein isoform X4

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 325

PTZ00121; MAEBL; Provisional
XM_047422704.1 → XP_047278660.1 PC4 and SFRS1-interacting protein isoform X3
XM_024447401.2 → XP_024303169.1 PC4 and SFRS1-interacting protein isoform X3

Conserved Domains (2) summary

cd05834
Location:3 → 87

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, ...

PTZ00121
Location:89 → 330

PTZ00121; MAEBL; Provisional