Details for: HNRNPU
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
-
CSI 109.98rCSI 73.1%PRS 3.68
-
CSI 108.55rCSI 87.77%PRS 3.03
-
CSI 105.07rCSI 90.98%PRS 3.46
-
CSI 98.54rCSI 94.85%PRS 3.23
-
CSI 95.66rCSI 86.39%PRS 2.72
-
CSI 88.09rCSI 67.87%PRS 2.79
-
CSI 72.58rCSI 63.83%PRS 2.25
-
CSI 71.02rCSI 81.3%PRS 6.46
-
CSI 70.91rCSI 88.99%PRS 3.92
-
CSI 68.81rCSI 56.98%PRS 3.1
-
CSI 66.03rCSI 58%PRS 3.46
-
CSI 64.74rCSI 45.2%PRS 3.26
-
CSI 62.04rCSI 59.82%PRS 1.31
-
CSI 60.13rCSI 86.73%PRS 4.3
-
CSI 59.06rCSI 44.68%PRS 4.34
-
CSI 56.48rCSI 75.47%PRS 5.93
-
CSI 56.26rCSI 64.98%PRS 2.84
-
CSI 56.16rCSI 69.85%PRS 3.31
-
CSI 55.87rCSI 58.39%PRS 3.31
-
CSI 52.86rCSI 44.31%PRS 3.73
-
CSI 51.8rCSI 88.74%PRS 4.13
-
CSI 48.42rCSI 40.14%PRS 2.9
-
CSI 46.88rCSI 71.6%PRS 3.12
-
CSI 45.37rCSI 31.54%PRS 3.63
-
CSI 44.26rCSI 54.75%PRS 2.72
-
CSI 44.23rCSI 68.34%PRS 2.91
-
CSI 42.93rCSI 50.42%PRS 3.79
-
CSI 40.21rCSI 30.21%PRS 3.18
-
CSI 39.98rCSI 39.9%PRS 2.61
-
CSI 39.96rCSI 29.96%PRS 9.4
-
CSI 39.27rCSI 34.14%PRS 3.81
-
CSI 38.79rCSI 56.19%PRS 4.55
-
CSI 37.57rCSI 43.45%PRS 2.25
-
CSI 37.32rCSI 24.87%PRS 8.79
-
CSI 37.1rCSI 51.54%PRS 3.28
-
CSI 36.93rCSI 47.36%PRS 3.58
-
CSI 35.09rCSI 52.94%PRS 3.03
-
CSI 33.97rCSI 74.39%PRS 4.33
-
CSI 33.89rCSI 35.5%PRS 2.89
-
CSI 32.82rCSI 25.94%PRS 2.15
-
CSI 32.62rCSI 63.44%PRS 3.16
-
CSI 31.94rCSI 29.47%PRS 3.13
-
CSI 31.53rCSI 24.8%PRS 3.68
-
CSI 31.14rCSI 32.62%PRS 3.34
-
CSI 30.61rCSI 82.51%PRS 4.06
-
CSI 30.59rCSI 46.79%PRS 5.07
-
CSI 30.5rCSI 18.01%PRS 4.33
-
CSI 30.03rCSI 43.29%PRS 5.05
-
CSI 29.5rCSI 42.1%PRS 3.54
-
CSI 29.05rCSI 25.45%PRS 4.18
-
CSI 28.27rCSI 53.37%PRS 3.86
-
CSI 28.2rCSI 33.85%PRS 3.1
-
CSI 27.83rCSI 24.71%PRS 3.1
-
CSI 27.4rCSI 75.28%PRS 5.22
-
CSI 27.32rCSI 65.56%PRS 5.91
-
CSI 27.1rCSI 63.18%PRS 8.48
-
CSI 27.07rCSI 77.29%PRS 5.5
-
CSI 26.14rCSI 100%PRS 5.13
-
CSI 25.63rCSI 91.08%PRS 10.25
-
CSI 25.49rCSI 71.43%PRS 4.92
-
CSI 25.02rCSI 19.4%PRS 2.95
-
CSI 25.01rCSI 55.07%PRS 4.86
-
CSI 24.85rCSI 16.74%PRS 3.76
-
CSI 24.82rCSI 31.85%PRS 3.09
-
CSI 23.5rCSI 61.06%PRS 9.74
-
CSI 23.27rCSI 22.98%PRS 13.75
-
CSI 23.19rCSI 16.29%PRS 9.41
-
CSI 22.75rCSI 36.34%PRS 3.39
-
CSI 22.69rCSI 72.8%PRS 4.75
-
CSI 22.65rCSI 65.59%PRS 3.53
-
CSI 22.52rCSI 34.59%PRS 3.59
-
CSI 22.16rCSI 22.8%PRS 5.08
-
CSI 22.11rCSI 72.38%PRS 9.76
-
CSI 21.06rCSI 50.63%PRS 4.88
-
CSI 21.03rCSI 41.93%PRS 5.32
-
CSI 20.71rCSI 21.11%PRS 4.5
-
CSI 20.46rCSI 89.8%PRS 6.1
-
CSI 20.36rCSI 31.29%PRS 4.51
-
CSI 20.3rCSI 16.95%PRS 10.24
-
CSI 20.21rCSI 48.05%PRS 4.74
-
CSI 19.87rCSI 57.49%PRS 6.87
-
CSI 19.86rCSI 100%PRS 6.2
-
CSI 19.43rCSI 20.27%PRS 3.17
-
CSI 19.24rCSI 40.93%PRS 6.15
-
CSI 19.07rCSI 25.98%PRS 2.81
-
CSI 18.11rCSI 18.34%PRS 20.56
-
CSI 17.52rCSI 13.63%PRS 4.49
-
CSI 17.41rCSI 41.89%PRS 4.89
-
CSI 17.34rCSI 14.87%PRS 9.59
-
CSI 17.28rCSI 12.9%PRS 5.24
-
CSI 17.28rCSI 45.51%PRS 6.1
-
CSI 16.98rCSI 24.85%PRS 3.28
-
CSI 16.93rCSI 57.25%PRS 5.35
-
CSI 16.64rCSI 82.04%PRS 4.23
-
CSI 16.39rCSI 35.78%PRS 6.36
-
CSI 16.22rCSI 75.93%PRS 8.86
-
CSI 15.92rCSI 21.77%PRS 3.53
-
CSI 15.73rCSI 33.48%PRS 5.06
-
CSI 15.19rCSI 70.14%PRS 7.01
-
CSI 15.18rCSI 13.09%PRS 5.18
-
CSI -35.3rCSI -28.3%PRS 5.8%
-
CSI -34.1rCSI -23.7%PRS 4.5%
-
CSI -15.0rCSI -26.3%PRS 2.5%
-
CSI -14.7rCSI -47.1%PRS 2.3%
-
CSI -14.6rCSI -60.7%PRS 9.7%
-
CSI -14.4rCSI -27.0%PRS 2.5%
-
CSI -14.3rCSI -19.2%PRS 4.2%
-
CSI -14.1rCSI -33.5%PRS 4.1%
-
CSI -12.3rCSI -40.6%PRS 2.7%
-
CSI -12.1rCSI -20.6%PRS 6.4%
-
CSI -11.0rCSI -41.5%PRS 7.0%
-
CSI -10.1rCSI -40.6%PRS 15.3%
-
CSI -8.5rCSI -19.6%PRS 2.9%
-
CSI -8.4rCSI -17.1%PRS 1.0%
-
CSI -8.0rCSI -83.1%PRS 3.1%
-
CSI -8.0rCSI -6.1%PRS 4.1%
-
CSI -7.1rCSI -40.0%PRS 0.9%
-
CSI -6.9rCSI -17.9%PRS 3.8%
-
CSI -6.5rCSI -15.4%PRS 5.6%
-
CSI -5.9rCSI -62.2%PRS 38.7%
-
CSI -5.7rCSI -27.1%PRS 1.5%
-
CSI -5.4rCSI -47.3%PRS 0.8%
-
CSI -5.4rCSI -15.3%PRS 4.3%
-
CSI -5.3rCSI -9.2%PRS 2.4%
-
CSI -4.6rCSI -77.8%PRS 16.8%
-
CSI -4.4rCSI -12.5%PRS 4.5%
-
CSI -4.3rCSI -20.6%PRS 5.4%
-
CSI -4.2rCSI -16.9%PRS 4.0%
-
CSI -4.1rCSI -16.4%PRS 3.6%
-
CSI -3.2rCSI -8.5%PRS 3.7%
-
CSI -2.9rCSI -7.6%PRS 4.5%
-
CSI -2.8rCSI -9.0%PRS 5.4%
-
CSI -2.7rCSI -13.7%PRS 24.3%
-
CSI -2.7rCSI -13.9%PRS 15.1%
-
CSI -2.6rCSI -4.0%PRS 8.0%
-
CSI -2.5rCSI -3.4%PRS 3.5%
-
CSI -2.4rCSI -32.9%PRS 35.7%
-
CSI -2.4rCSI -15.4%PRS 8.7%
-
CSI -2.4rCSI -5.3%PRS 8.0%
-
CSI -2.3rCSI -5.7%PRS 3.3%
-
CSI -2.3rCSI -1.6%PRS 4.2%
-
CSI -2.1rCSI -3.7%PRS 4.4%
-
CSI -1.9rCSI -11.8%PRS 16.4%
-
CSI -1.9rCSI -5.6%PRS 5.5%
-
CSI -1.8rCSI -3.5%PRS 9.2%
-
CSI -1.6rCSI -6.0%PRS 5.3%
-
CSI -1.5rCSI -2.0%PRS 4.1%
-
CSI -1.5rCSI -3.3%PRS 2.0%
-
CSI -1.4rCSI -2.5%PRS 4.1%
-
CSI -1.3rCSI -6.6%PRS 19.4%
-
CSI -0.8rCSI -1.8%PRS 4.5%
-
CSI -0.8rCSI -10.4%PRS 27.1%
-
CSI -0.8rCSI -11.0%PRS 34.1%
-
CSI -0.8rCSI -1.5%PRS 2.3%
-
CSI -0.7rCSI -4.3%PRS 2.6%
-
CSI -0.6rCSI -1.8%PRS 13.4%
-
CSI -0.5rCSI -3.5%PRS 5.8%
-
CSI -0.4rCSI -2.2%PRS 16.5%
-
CSI -0.4rCSI -1.9%PRS 6.7%
-
CSI -0.3rCSI -2.7%PRS 29.9%
-
CSI -0.2rCSI -1.2%PRS 15.5%
-
CSI -0.1rCSI -0.3%PRS 5.0%
-
CSI 0.0rCSI 0.1%PRS 14.6%
-
CSI 0.1rCSI 0.5%PRS 17.2%
-
CSI 0.2rCSI 0.8%PRS 1.0%
-
CSI 0.2rCSI 6.1%PRS 40.8%
-
CSI 0.3rCSI 1.0%PRS 3.9%
-
CSI 0.3rCSI 1.5%PRS 7.8%
-
CSI 0.3rCSI 1.9%PRS 18.5%
-
CSI 0.4rCSI 3.1%PRS 22.3%
-
CSI 0.4rCSI 0.7%PRS 1.9%
-
CSI 0.4rCSI 9.4%PRS 23.5%
-
CSI 0.5rCSI 3.1%PRS 24.7%
-
CSI 0.6rCSI 0.8%PRS 4.8%
-
CSI 0.6rCSI 1.5%PRS 5.8%
-
CSI 0.6rCSI 1.9%PRS 2.0%
-
CSI 0.6rCSI 4.0%PRS 6.5%
-
CSI 0.6rCSI 3.3%PRS 7.7%
-
CSI 0.7rCSI 5.7%PRS 0.3%
-
CSI 0.7rCSI 3.9%PRS 4.8%
-
CSI 0.7rCSI 1.7%PRS 3.0%
-
CSI 0.7rCSI 7.3%PRS 13.0%
-
CSI 0.7rCSI 6.6%PRS 20.5%
-
CSI 0.7rCSI 5.9%PRS 14.6%
-
CSI 0.8rCSI 2.4%PRS 2.2%
-
CSI 0.8rCSI 1.9%PRS 1.9%
-
CSI 0.8rCSI 3.0%PRS 3.4%
-
CSI 0.8rCSI 3.6%PRS 3.1%
-
CSI 0.8rCSI 8.3%PRS 9.6%
-
CSI 0.9rCSI 17.9%PRS 28.6%
-
CSI 0.9rCSI 7.5%PRS 6.4%
-
CSI 0.9rCSI 13.1%PRS 39.5%
-
CSI 0.9rCSI 9.7%PRS 5.5%
-
CSI 0.9rCSI 6.3%PRS 6.3%
-
CSI 0.9rCSI 3.6%PRS 2.0%
-
CSI 1.0rCSI 10.4%PRS 22.7%
-
CSI 1.0rCSI 5.2%PRS 8.3%
-
CSI 1.0rCSI 3.8%PRS 6.8%
-
CSI 1.0rCSI 3.7%PRS 1.7%
-
CSI 1.0rCSI 0.9%PRS 4.9%
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 914217558
Symbol: HNRPU_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 1628625
Title: Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box.
PubMed ID: 1628625
PubMed ID: 7509195
Title: hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells.
PubMed ID: 7509195
PubMed ID: 16710414
Title: The DNA sequence and biological annotation of human chromosome 1.
PubMed ID: 16710414
DOI: 10.1038/nature04727
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 7993898
Title: Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins.
PubMed ID: 7993898
DOI: 10.1021/bi00253a007
PubMed ID: 1324173
Title: Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements.
PubMed ID: 1324173
PubMed ID: 8068679
Title: Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity.
PubMed ID: 8068679
DOI: 10.1021/bi00200a024
PubMed ID: 8174554
Title: Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro.
PubMed ID: 8174554
PubMed ID: 7753047
Title: Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein.
PubMed ID: 7753047
PubMed ID: 9204873
Title: The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A) is directly bound to chromosomal DNA in vivo: a chemical cross-linking study.
PubMed ID: 9204873
DOI: 10.1021/bi970480f
PubMed ID: 9105675
Title: The class III POU factor Brn-4 interacts with other class III POU factors and the heterogeneous nuclear ribonucleoprotein U.
PubMed ID: 9105675
PubMed ID: 9405365
Title: The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown.
PubMed ID: 9405365
PubMed ID: 9353307
Title: The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U.
PubMed ID: 9353307
PubMed ID: 10490622
Title: hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation.
PubMed ID: 10490622
PubMed ID: 10671544
Title: Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3 occurs at a noncanonical cleavage site.
PubMed ID: 10671544
PubMed ID: 11003645
Title: SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA.
PubMed ID: 11003645
PubMed ID: 11909954
Title: Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes.
PubMed ID: 11909954
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 14608463
Title: Scaffold attachment factor A (SAF-A) is concentrated in inactive X chromosome territories through its RGG domain.
PubMed ID: 14608463
PubMed ID: 14654843
Title: Proteomic characterization of the human centrosome by protein correlation profiling.
PubMed ID: 14654843
DOI: 10.1038/nature02166
PubMed ID: 15563465
Title: A stable proteinaceous structure in the territory of inactive X chromosomes.
PubMed ID: 15563465
PubMed ID: 15592455
Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.
PubMed ID: 15592455
DOI: 10.1038/nbt1046
PubMed ID: 15711563
Title: Actin and hnRNP U cooperate for productive transcription by RNA polymerase II.
PubMed ID: 15711563
DOI: 10.1038/nsmb904
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16916646
Title: Inhibition of HIV-1 gene expression by a fragment of hnRNP U.
PubMed ID: 16916646
PubMed ID: 17487921
Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.
PubMed ID: 17487921
PubMed ID: 17174306
Title: hnRNP-U enhances the expression of specific genes by stabilizing mRNA.
PubMed ID: 17174306
PubMed ID: 18082603
Title: Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation.
PubMed ID: 18082603
PubMed ID: 17289661
Title: Molecular composition of IMP1 ribonucleoprotein granules.
PubMed ID: 17289661
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19617346
Title: Physical and functional interaction between heterochromatin protein 1alpha and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U.
PubMed ID: 19617346
PubMed ID: 19808671
Title: Identification of a heterogeneous nuclear ribonucleoprotein-recognition region in the HIV Rev protein.
PubMed ID: 19808671
PubMed ID: 19029303
Title: Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.
PubMed ID: 19029303
DOI: 10.1261/rna.1175909
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20858735
Title: Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways.
PubMed ID: 20858735
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21242313
Title: The nuclear scaffold protein SAF-A is required for kinetochore-microtubule attachment and contributes to the targeting of Aurora-A to mitotic spindles.
PubMed ID: 21242313
DOI: 10.1242/jcs.063347
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22325991
Title: Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation.
PubMed ID: 22325991
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23811339
Title: H19 inhibits RNA polymerase II-mediated transcription by disrupting the hnRNP U-actin complex.
PubMed ID: 23811339
PubMed ID: 23640942
Title: Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains.
PubMed ID: 23640942
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25911097
Title: Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression.
PubMed ID: 25911097
PubMed ID: 25616961
Title: ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1.
PubMed ID: 25616961
DOI: 10.1093/hmg/ddv020
PubMed ID: 25986610
Title: Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is required for mitosis.
PubMed ID: 25986610
DOI: 10.1128/mcb.01312-14
PubMed ID: 26244333
Title: Xist exon 7 contributes to the stable localization of Xist RNA on the inactive X-chromosome.
PubMed ID: 26244333
PubMed ID: 26030138
Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.
PubMed ID: 26030138
PubMed ID: 28622508
Title: SAF-A regulates interphase chromosome structure through oligomerization with chromatin-associated RNAs.
PubMed ID: 28622508
PubMed ID: 28190768
Title: Serine ADP-ribosylation depends on HPF1.
PubMed ID: 28190768
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 23708187
Title: Targeted resequencing in epileptic encephalopathies identifies de novo mutations in CHD2 and SYNGAP1.
PubMed ID: 23708187
DOI: 10.1038/ng.2646
PubMed ID: 25356899
Title: De novo mutations in moderate or severe intellectual disability.
PubMed ID: 25356899
Sequence Information:
- Length: 825
- Mass: 90584
- Checksum: 5D4EC4188436831F
- Sequence:
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR PAMEPGNGSL DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD GDQMELGEEN GAAGAADSGP MEEEEAASED ENGDDQGFQE GEDELGDEEE GAGDENGHGE QQPQPPATQQ QQPQQQRGAA KEAAGKSSGP TSLFAVTVAP PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG DKKRGVKRPR EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY TKDIDIHEVR IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF DENDVITCFA NFESDEVELS YAKNGQDLGV AFKISKEVLA GRPLFPHVLC HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP LEDRVRGPKG PEEKKDCEVV MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA GFKKQMADTG KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD EITYVELQKE EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF NRGGGHRGRG GFNMRGGNFR GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG NYNQNFRGRG NNRGYKNQSQ GYNQWQQGQF WGQKPWSQHY HQGYY
Genular Protein ID: 2637126500
Symbol: Q96BA7_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
Sequence Information:
- Length: 722
- Mass: 79716
- Checksum: A35C0DA46EAE6FD2
- Sequence:
MELGEENGAA GAADSGPMEE EEAASEDENG DDQGFQEGED ELGDEEEGAG DENGHGEQQP QPPATQQQQP QQQRGAAKEA AGKSSGPTSL FAVTVAPPGA RQGQQQAGGK KKAEGGGGGG RPGAPAAGDG KTEQKGGDKK RGVKRPREDH GRGYFEYIEE NKYSRAKSPQ PPVEEEDEHF DDTVVCLDTY NCDLHFKISR DRLSASSLTM ESFAFLWAGG RASYGVSKGK VCFEMKVTEK IPVRHLYTKD IDIHEVRIGW SLTTSGMLLG EEEFSYGYSL KGIKTCNCET EDYGEKFDEN DVITCFANFE SDEVELSYAK NGQDLGVAFK ISKEVLAGRP LFPHVLCHNC AVEFNFGQKE KPYFPIPEEY TFIQNVPLED RVRGPKGPEE KKDCEVVMMI GLPGAGKTTW VTKHAAENPG KYNILGTNTI MDKMMVAGFK KQMADTGKLN TLLQRAPQCL GKFIEIAARK KRNFILDQTN VSAAAQRRKM CLFAGFQRKA VVVCPKDEDY KQRTQKKAEV EGKDLPEHAV LKMKGNFTLP EVAECFDEIT YVELQKEEAQ KLLEQYKEES KKALPPEKKQ NTGSKKSNKN KSGKNQFNRG GGHRGRGGFN MRGGNFRGGA PGNRGGYNRR GNMPQRGGGG GGSGGIGYPY PRAPVFPGRG SYSNRGNYNR GGMPNRGNYN QNFRGRGNNR GYKNQSQGYN QWQQGQFWGQ KPWSQHYHQG YY