Gene HNRNPC - ENSG00000092199 | NCBI Gene ID: 3183

Details for: HNRNPC

Gene ID: 3183

Symbol: HNRNPC

Ensembl ID: ENSG00000092199

Description: heterogeneous nuclear ribonucleoprotein C

Associated with

Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mrna splicing
(R-HSA-72172)
Mrna splicing - major pathway
(R-HSA-72163)
Post-translational protein modification
(R-HSA-597592)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Rhobtb1 gtpase cycle
(R-HSA-9013422)
Rhobtb2 gtpase cycle
(R-HSA-9013418)
Rhobtb gtpase cycle
(R-HSA-9706574)
Rho gtpase cycle
(R-HSA-9012999)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of rna binding proteins
(R-HSA-4570464)
3'-utr-mediated mrna stabilization
(GO:0070935)
Actin cytoskeleton
(GO:0015629)
Catalytic step 2 spliceosome
(GO:0071013)
Chromatin
(GO:0000785)
Chromatin remodeling
(GO:0006338)
Cytosol
(GO:0005829)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Identical protein binding
(GO:0042802)
Membrane
(GO:0016020)
Mrna 3'-utr binding
(GO:0003730)
Mrna splicing, via spliceosome
(GO:0000398)
N6-methyladenosine-containing rna reader activity
(GO:1990247)
Negative regulation of telomere maintenance via telomerase
(GO:0032211)
Nucleoplasm
(GO:0005654)
Nucleosomal dna binding
(GO:0031492)
Nucleus
(GO:0005634)
Osteoblast differentiation
(GO:0001649)
Poly(u) rna binding
(GO:0008266)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Rna splicing
(GO:0008380)
Spliceosomal complex
(GO:0005681)
Telomerase holoenzyme complex
(GO:0005697)
Telomerase rna binding
(GO:0070034)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: GABAergic neuron (CL0000617)
Fold Change: 4.22
Marker Score: 17585
Cell Name: cord blood hematopoietic stem cell (CL2000095)
Fold Change: 4.18
Marker Score: 3156.5
Cell Name: erythroid progenitor cell (CL0000038)
Fold Change: 3.93
Marker Score: 4095
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 3.85
Marker Score: 130970
Cell Name: radial glial cell (CL0000681)
Fold Change: 3.82
Marker Score: 1407
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 3.74
Marker Score: 5753
Cell Name: mesodermal cell (CL0000222)
Fold Change: 3.68
Marker Score: 48484
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.58
Marker Score: 8755
Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: 3.49
Marker Score: 2975
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 3.37
Marker Score: 3594.5
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 3.34
Marker Score: 799
Cell Name: mature T cell (CL0002419)
Fold Change: 3.31
Marker Score: 32810.5
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: 3.29
Marker Score: 2577
Cell Name: erythroblast (CL0000765)
Fold Change: 3.27
Marker Score: 2043
Cell Name: chondrocyte (CL0000138)
Fold Change: 3.26
Marker Score: 1469
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 3.24
Marker Score: 3910
Cell Name: decidual natural killer cell, human (CL0002343)
Fold Change: 3.24
Marker Score: 8939
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 3.17
Marker Score: 20604.5
Cell Name: glycinergic amacrine cell (CL4030028)
Fold Change: 3.14
Marker Score: 2963
Cell Name: late pro-B cell (CL0002048)
Fold Change: 3.14
Marker Score: 3702
Cell Name: melanocyte (CL0000148)
Fold Change: 3.13
Marker Score: 1267
Cell Name: ependymal cell (CL0000065)
Fold Change: 3.12
Marker Score: 1088
Cell Name: type I NK T cell (CL0000921)
Fold Change: 3.11
Marker Score: 2442
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 3.08
Marker Score: 2331
Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
Fold Change: 3.05
Marker Score: 3293
Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
Fold Change: 3.05
Marker Score: 8556.5
Cell Name: Bergmann glial cell (CL0000644)
Fold Change: 3.03
Marker Score: 1235
Cell Name: kidney loop of Henle epithelial cell (CL1000909)
Fold Change: 3.01
Marker Score: 1885
Cell Name: cell in vitro (CL0001034)
Fold Change: 3
Marker Score: 104070
Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
Fold Change: 3
Marker Score: 4249
Cell Name: mature alpha-beta T cell (CL0000791)
Fold Change: 3
Marker Score: 158595
Cell Name: germinal center B cell (CL0000844)
Fold Change: 3
Marker Score: 1823
Cell Name: epithelial cell of urethra (CL1000296)
Fold Change: 3
Marker Score: 2360
Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
Fold Change: 2.99
Marker Score: 1245.5
Cell Name: mature gamma-delta T cell (CL0000800)
Fold Change: 2.98
Marker Score: 9418
Cell Name: podocyte (CL0000653)
Fold Change: 2.98
Marker Score: 1101
Cell Name: blood cell (CL0000081)
Fold Change: 2.97
Marker Score: 34543
Cell Name: malignant cell (CL0001064)
Fold Change: 2.97
Marker Score: 39855
Cell Name: CD4-positive helper T cell (CL0000492)
Fold Change: 2.96
Marker Score: 3215
Cell Name: naive B cell (CL0000788)
Fold Change: 2.95
Marker Score: 2633.5
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 2.93
Marker Score: 163726
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 2.92
Marker Score: 639
Cell Name: theca cell (CL0000503)
Fold Change: 2.92
Marker Score: 2091
Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
Fold Change: 2.91
Marker Score: 5197
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 2.91
Marker Score: 6383.5
Cell Name: epicardial adipocyte (CL1000309)
Fold Change: 2.9
Marker Score: 1409
Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
Fold Change: 2.9
Marker Score: 1822
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 2.88
Marker Score: 11116
Cell Name: IgG-negative class switched memory B cell (CL0002117)
Fold Change: 2.88
Marker Score: 2837
Cell Name: retinal pigment epithelial cell (CL0002586)
Fold Change: 2.87
Marker Score: 845
Cell Name: Schwann cell (CL0002573)
Fold Change: 2.86
Marker Score: 993
Cell Name: pro-B cell (CL0000826)
Fold Change: 2.86
Marker Score: 2759
Cell Name: epithelial cell of uterus (CL0002149)
Fold Change: 2.84
Marker Score: 651
Cell Name: activated CD4-positive, alpha-beta T cell, human (CL0001043)
Fold Change: 2.83
Marker Score: 1286
Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
Fold Change: 2.82
Marker Score: 2372
Cell Name: microglial cell (CL0000129)
Fold Change: 2.82
Marker Score: 5132
Cell Name: neural progenitor cell (CL0011020)
Fold Change: 2.81
Marker Score: 10878
Cell Name: basal cell (CL0000646)
Fold Change: 2.81
Marker Score: 3622
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 2.81
Marker Score: 2953
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 2.8
Marker Score: 11739
Cell Name: supporting cell (CL0000630)
Fold Change: 2.8
Marker Score: 5265
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: 2.8
Marker Score: 1628
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 2.79
Marker Score: 13714.5
Cell Name: medullary thymic epithelial cell (CL0002365)
Fold Change: 2.78
Marker Score: 4567
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 2.78
Marker Score: 3435
Cell Name: neutrophil (CL0000775)
Fold Change: 2.78
Marker Score: 1694
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 2.78
Marker Score: 793
Cell Name: kidney interstitial fibroblast (CL1000692)
Fold Change: 2.77
Marker Score: 5325
Cell Name: epithelial cell of nephron (CL1000449)
Fold Change: 2.76
Marker Score: 5754
Cell Name: B-1 B cell (CL0000819)
Fold Change: 2.75
Marker Score: 4792.5
Cell Name: memory B cell (CL0000787)
Fold Change: 2.74
Marker Score: 2073
Cell Name: granulocyte (CL0000094)
Fold Change: 2.74
Marker Score: 1226
Cell Name: renal principal cell (CL0005009)
Fold Change: 2.73
Marker Score: 2105
Cell Name: choroid plexus epithelial cell (CL0000706)
Fold Change: 2.73
Marker Score: 2504.5
Cell Name: early pro-B cell (CL0002046)
Fold Change: 2.72
Marker Score: 27608
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 2.72
Marker Score: 4626
Cell Name: mature NK T cell (CL0000814)
Fold Change: 2.72
Marker Score: 1260
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 2.72
Marker Score: 8064.5
Cell Name: stromal cell (CL0000499)
Fold Change: 2.72
Marker Score: 3184.5
Cell Name: pro-T cell (CL0000827)
Fold Change: 2.72
Marker Score: 11117.5
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 2.71
Marker Score: 48142.5
Cell Name: endothelial tip cell (CL0000704)
Fold Change: 2.71
Marker Score: 631
Cell Name: muscle precursor cell (CL0000680)
Fold Change: 2.7
Marker Score: 700
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 2.7
Marker Score: 1814
Cell Name: DN3 thymocyte (CL0000807)
Fold Change: 2.69
Marker Score: 1346
Cell Name: centroblast (CL0009112)
Fold Change: 2.69
Marker Score: 1324
Cell Name: tendon cell (CL0000388)
Fold Change: 2.68
Marker Score: 660
Cell Name: granulosa cell (CL0000501)
Fold Change: 2.68
Marker Score: 26983
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 2.68
Marker Score: 664
Cell Name: lung neuroendocrine cell (CL1000223)
Fold Change: 2.67
Marker Score: 754
Cell Name: club cell (CL0000158)
Fold Change: 2.66
Marker Score: 3102
Cell Name: secretory cell (CL0000151)
Fold Change: 2.65
Marker Score: 4835
Cell Name: promonocyte (CL0000559)
Fold Change: 2.65
Marker Score: 1706
Cell Name: hepatocyte (CL0000182)
Fold Change: 2.65
Marker Score: 1807
Cell Name: Unknown (CL0000548)
Fold Change: 2.65
Marker Score: 1928
Cell Name: rod bipolar cell (CL0000751)
Fold Change: 2.64
Marker Score: 1380.5
Cell Name: hematopoietic stem cell (CL0000037)
Fold Change: 2.64
Marker Score: 1391
Cell Name: dendritic cell (CL0000451)
Fold Change: 2.64
Marker Score: 1811
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 2.64
Marker Score: 1506
Cell Name: Sertoli cell (CL0000216)
Fold Change: 2.64
Marker Score: 15642

Hover over a box to see details here...

**Key characteristics:** * HNRNPC is a large protein (140 kDa) with a molecular weight of 140 kDa. * It is a multi-functional protein with multiple domains. * It is a key regulator of mRNA splicing and translation. * It is involved in the regulation of cell proliferation, differentiation, and apoptosis. * It is also involved in the regulation of inflammation and cancer. **Pathways and functions:** * HNRNPC is involved in the regulation of mRNA splicing and translation. It is a key factor in the formation of intron-containing pre-mRNAs, which are processed to produce mature mRNAs. * It also plays a role in the regulation of the Rhobtb1 gtpase cycle, which is involved in the production of the Rhobtb1 GTPase protein. * HNRNPC is also involved in the Rhobtb2 gtpase cycle, the Rhobtb gtpase cycle, the Rho gtpase cycle, and the Rna binding pathway. * It is involved in the regulation of cell proliferation, differentiation, and apoptosis. **Clinical significance:** HNRNPC is a key gene in human health. Mutations in HNRNPC genes have been linked to a number of diseases, including cancer, neurodegenerative diseases, and developmental disorders. * In cancer, HNRNPC mutations can lead to the activation of oncogenes and the formation of tumors. * In neurodegenerative diseases, HNRNPC mutations can lead to the accumulation of abnormal RNA species, which can disrupt normal cellular function. * HNRNPC is a promising target for the treatment of a variety of diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Heterogeneous nuclear ribonucleoproteins C1/C2

Genular Protein ID: 2539948658

Symbol: HNRPC_HUMAN

Name: Heterogeneous nuclear ribonucleoproteins C1/C2

UniProtKB Accession Codes:

P07910 D3DS19 D3DS22 P22628 Q53EX2 Q59FD3 Q5FWE8 Q86SF8 Q86U45 Q96HK7 Q96HM4 Q96IY5 Q9BTS3

Database IDs:

Citations:

PubMed ID: 2557628

Title: Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts.

PubMed ID: 2557628

DOI: 10.1073/pnas.86.24.9788

PubMed ID: 3110598

Title: Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.

PubMed ID: 3110598

DOI: 10.1128/mcb.7.5.1731-1739.1987

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: 2587210

Title: Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles.

PubMed ID: 2587210

DOI: 10.1093/nar/17.21.8441

PubMed ID: 8264621

Title: The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles.

PubMed ID: 8264621

DOI: 10.1128/mcb.14.1.518-533.1994

PubMed ID: 7567451

Title: A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction.

PubMed ID: 7567451

DOI: 10.1093/nar/23.17.3419

PubMed ID: 11687588

Title: Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.

PubMed ID: 11687588

DOI: 10.1074/jbc.m109393200

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 12564933

Title: Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2.

PubMed ID: 12564933

DOI: 10.1021/bi0268091

PubMed ID: 12509468

Title: Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner.

PubMed ID: 12509468

DOI: 10.1128/mcb.23.2.708-720.2003

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15082759

Title: SUMO modification of heterogeneous nuclear ribonucleoproteins.

PubMed ID: 15082759

DOI: 10.1128/mcb.24.9.3623-3632.2004

PubMed ID: 16010978

Title: Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells.

PubMed ID: 16010978

DOI: 10.1007/s11010-005-7644-2

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 17693683

Title: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.

PubMed ID: 17693683

DOI: 10.1074/mcp.m700120-mcp200

PubMed ID: 17289661

Title: Molecular composition of IMP1 ribonucleoprotein granules.

PubMed ID: 17289661

DOI: 10.1074/mcp.m600346-mcp200

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

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: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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

DOI: 10.1016/j.jprot.2013.11.014

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

DOI: 10.1073/pnas.1413825111

PubMed ID: 25678563

Title: Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.

PubMed ID: 25678563

DOI: 10.1093/brain/awv005

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25719671

Title: N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions.

PubMed ID: 25719671

DOI: 10.1038/nature14234

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

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: 37599448

Title: Nucleo-cytoplasmic shuttling of 14-3-3 epsilon carrying hnRNP C promotes autophagy.

PubMed ID: 37599448

DOI: 10.1080/15384047.2023.2246203

PubMed ID: 1385725

Title: 1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins.

PubMed ID: 1385725

DOI: 10.1021/bi00142a013

PubMed ID: 1380452

Title: Interaction of the RNA-binding domain of the hnRNP C proteins with RNA.

PubMed ID: 1380452

DOI: 10.1002/j.1460-2075.1992.tb05407.x

PubMed ID: 11162094

Title: An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity.

PubMed ID: 11162094

DOI: 10.1006/jmbi.2000.4331

PubMed ID: 15936032

Title: Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function.

PubMed ID: 15936032

DOI: 10.1016/j.jmb.2005.05.002

Sequence Information:

Length: 306
Mass: 33670
Checksum: 17BBC78690C69C5C
Sequence:

MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE 
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS 
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR 
GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS 
SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA 
NGEDDS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: HNRNPC

Associated with

Cells (max top 100)

Other Information

Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. PubMed ID: 2557628

Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins. PubMed ID: 3110598

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. PubMed ID: 2587210

The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles. PubMed ID: 8264621

A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction. PubMed ID: 7567451

Nuclear DNA helicase II/RNA helicase A binds to filamentous actin. PubMed ID: 11687588

Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. PubMed ID: 11991638

Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2. PubMed ID: 12564933

Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. PubMed ID: 12509468

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

SUMO modification of heterogeneous nuclear ribonucleoproteins. PubMed ID: 15082759

Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells. PubMed ID: 16010978

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Phosphoproteomic analysis of the human pituitary. PubMed ID: 16807684

Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. PubMed ID: 17693683

Molecular composition of IMP1 ribonucleoprotein granules. PubMed ID: 17289661

Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PubMed ID: 19367720

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes. PubMed ID: 25678563

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions. PubMed ID: 25719671

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Nucleo-cytoplasmic shuttling of 14-3-3 epsilon carrying hnRNP C promotes autophagy. PubMed ID: 37599448

1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins. PubMed ID: 1385725

Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. PubMed ID: 1380452

An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity. PubMed ID: 11162094

Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function. PubMed ID: 15936032