Details for: PKM

Gene ID: 5315

Symbol: PKM

Ensembl ID: ENSG00000067225

Description: pyruvate kinase M1/2

Associated with

Cells (max top 100)

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

  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 4.58
    Marker Score: 5535
  • Cell Name: glycinergic amacrine cell (CL4030028)
    Fold Change: 4.24
    Marker Score: 4005
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 3.84
    Marker Score: 10285
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 3.74
    Marker Score: 209309
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: 3.69
    Marker Score: 3610
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 3.62
    Marker Score: 9138
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 3.58
    Marker Score: 26643
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 3.47
    Marker Score: 8472
  • Cell Name: blood cell (CL0000081)
    Fold Change: 3.44
    Marker Score: 40004
  • Cell Name: GABAergic amacrine cell (CL4030027)
    Fold Change: 3.39
    Marker Score: 6886.5
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: 3.38
    Marker Score: 9653
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 3.36
    Marker Score: 6127.5
  • Cell Name: radial glial cell (CL0000681)
    Fold Change: 3.21
    Marker Score: 1184
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 3.18
    Marker Score: 110125
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 3.11
    Marker Score: 24304
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: 3.09
    Marker Score: 2438
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 3.01
    Marker Score: 4987
  • Cell Name: rod bipolar cell (CL0000751)
    Fold Change: 2.98
    Marker Score: 1557.5
  • Cell Name: mature T cell (CL0002419)
    Fold Change: 2.95
    Marker Score: 29225
  • Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
    Fold Change: 2.91
    Marker Score: 1218
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 2.91
    Marker Score: 3328
  • Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
    Fold Change: 2.91
    Marker Score: 4114
  • Cell Name: basal cell (CL0000646)
    Fold Change: 2.87
    Marker Score: 3708
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 2.84
    Marker Score: 2884
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 2.84
    Marker Score: 4024
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 2.83
    Marker Score: 5520
  • Cell Name: bronchus fibroblast of lung (CL2000093)
    Fold Change: 2.82
    Marker Score: 3876
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 2.82
    Marker Score: 10861
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 2.81
    Marker Score: 8328
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 2.8
    Marker Score: 2951.5
  • Cell Name: epithelial cell of esophagus (CL0002252)
    Fold Change: 2.8
    Marker Score: 24165
  • Cell Name: medullary thymic epithelial cell (CL0002365)
    Fold Change: 2.8
    Marker Score: 4590
  • Cell Name: fibroblast of breast (CL4006000)
    Fold Change: 2.8
    Marker Score: 1596
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 2.79
    Marker Score: 2956.5
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 2.78
    Marker Score: 4427
  • Cell Name: club cell (CL0000158)
    Fold Change: 2.78
    Marker Score: 3242
  • Cell Name: myelocyte (CL0002193)
    Fold Change: 2.75
    Marker Score: 1188
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 2.73
    Marker Score: 813
  • Cell Name: T-helper 22 cell (CL0001042)
    Fold Change: 2.72
    Marker Score: 11648
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 2.71
    Marker Score: 36402
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: 2.71
    Marker Score: 6744.5
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 2.69
    Marker Score: 643
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 2.69
    Marker Score: 17191
  • Cell Name: Mueller cell (CL0000636)
    Fold Change: 2.69
    Marker Score: 3725
  • Cell Name: platelet (CL0000233)
    Fold Change: 2.68
    Marker Score: 1215.5
  • Cell Name: B-1 B cell (CL0000819)
    Fold Change: 2.68
    Marker Score: 4668
  • Cell Name: epithelial cell of nephron (CL1000449)
    Fold Change: 2.66
    Marker Score: 5565
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: 2.65
    Marker Score: 4496
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 2.63
    Marker Score: 2812
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 2.63
    Marker Score: 89326
  • Cell Name: stem cell of epidermis (CL1000428)
    Fold Change: 2.62
    Marker Score: 887
  • Cell Name: mature alpha-beta T cell (CL0000791)
    Fold Change: 2.62
    Marker Score: 138403
  • Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
    Fold Change: 2.61
    Marker Score: 1638
  • Cell Name: lung ciliated cell (CL1000271)
    Fold Change: 2.6
    Marker Score: 1235
  • Cell Name: cell of skeletal muscle (CL0000188)
    Fold Change: 2.6
    Marker Score: 1976
  • Cell Name: chondrocyte (CL0000138)
    Fold Change: 2.59
    Marker Score: 1165.5
  • Cell Name: migratory enteric neural crest cell (CL0002607)
    Fold Change: 2.59
    Marker Score: 2434
  • Cell Name: nasal mucosa goblet cell (CL0002480)
    Fold Change: 2.58
    Marker Score: 1724
  • Cell Name: myoepithelial cell of mammary gland (CL0002324)
    Fold Change: 2.58
    Marker Score: 12652.5
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 2.57
    Marker Score: 25895
  • Cell Name: epithelial cell of stratum germinativum of esophagus (CL1000447)
    Fold Change: 2.57
    Marker Score: 621
  • Cell Name: enteroendocrine cell (CL0000164)
    Fold Change: 2.57
    Marker Score: 1332
  • Cell Name: ventricular cardiac muscle cell (CL2000046)
    Fold Change: 2.57
    Marker Score: 1066
  • Cell Name: CD1c-positive myeloid dendritic cell (CL0002399)
    Fold Change: 2.56
    Marker Score: 6639.5
  • Cell Name: fetal cardiomyocyte (CL0002495)
    Fold Change: 2.56
    Marker Score: 843
  • Cell Name: ovarian surface epithelial cell (CL2000064)
    Fold Change: 2.56
    Marker Score: 6962
  • Cell Name: epithelial cell of lung (CL0000082)
    Fold Change: 2.56
    Marker Score: 13443
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 2.56
    Marker Score: 818
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 2.55
    Marker Score: 1774
  • Cell Name: double negative T regulatory cell (CL0011024)
    Fold Change: 2.55
    Marker Score: 2468
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 2.53
    Marker Score: 33386
  • Cell Name: alveolar macrophage (CL0000583)
    Fold Change: 2.53
    Marker Score: 64724
  • Cell Name: ependymal cell (CL0000065)
    Fold Change: 2.52
    Marker Score: 879
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 2.52
    Marker Score: 1466
  • Cell Name: luminal epithelial cell of mammary gland (CL0002326)
    Fold Change: 2.51
    Marker Score: 4456
  • Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
    Fold Change: 2.51
    Marker Score: 549
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: 2.5
    Marker Score: 10240
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 2.5
    Marker Score: 5486
  • Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
    Fold Change: 2.5
    Marker Score: 1465
  • Cell Name: alternatively activated macrophage (CL0000890)
    Fold Change: 2.49
    Marker Score: 1036
  • Cell Name: neural crest cell (CL0011012)
    Fold Change: 2.48
    Marker Score: 2647
  • Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
    Fold Change: 2.47
    Marker Score: 4413
  • Cell Name: Unknown (CL0000548)
    Fold Change: 2.46
    Marker Score: 1792
  • Cell Name: mature astrocyte (CL0002627)
    Fold Change: 2.45
    Marker Score: 1611
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 2.45
    Marker Score: 10200
  • Cell Name: inhibitory interneuron (CL0000498)
    Fold Change: 2.45
    Marker Score: 11313
  • Cell Name: P/D1 enteroendocrine cell (CL0002268)
    Fold Change: 2.44
    Marker Score: 909
  • Cell Name: double-positive, alpha-beta thymocyte (CL0000809)
    Fold Change: 2.44
    Marker Score: 4774
  • Cell Name: germinal center B cell (CL0000844)
    Fold Change: 2.43
    Marker Score: 1477
  • Cell Name: choroid plexus epithelial cell (CL0000706)
    Fold Change: 2.41
    Marker Score: 2211
  • Cell Name: basal epithelial cell of prostatic duct (CL0002236)
    Fold Change: 2.41
    Marker Score: 2134
  • Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
    Fold Change: 2.4
    Marker Score: 20878
  • Cell Name: mammary gland epithelial cell (CL0002327)
    Fold Change: 2.4
    Marker Score: 853
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 2.39
    Marker Score: 1592
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 2.39
    Marker Score: 3519
  • Cell Name: interstitial cell of Cajal (CL0002088)
    Fold Change: 2.39
    Marker Score: 827
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 2.39
    Marker Score: 15530
  • Cell Name: mature gamma-delta T cell (CL0000800)
    Fold Change: 2.38
    Marker Score: 7524
  • Cell Name: Bergmann glial cell (CL0000644)
    Fold Change: 2.38
    Marker Score: 970
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 2.37
    Marker Score: 2555

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Other Information

**Key characteristics:** * PKM is a membrane-bound protein with a molecular weight of approximately 120 kDa. * It is expressed in a wide range of cell types, including neurons, epithelial cells, and blood cells. * PKM is a key regulator of energy metabolism and is involved in the regulation of glucose uptake, glycolysis, and pyruvate production. * It also plays a role in cell cycle regulation, apoptosis, and inflammation. **Pathways and functions:** * PKM is involved in the regulation of energy metabolism through its interaction with ATP. * It acts as a phosphate donor in the citric acid cycle, where it is involved in the production of ATP from pyruvate. * PKM is also involved in the regulation of cell cycle regulation and apoptosis. * It binds to the CD14 receptor, which is expressed on macrophages and dendritic cells, and facilitates the activation of the immune system. * It also binds to the MRNA of the CD14 receptor, which is expressed on monocytes and macrophages. * PKM is involved in the regulation of inflammation through its interaction with the NLRP3 inflammasome, which is a central component of the innate immune response. **Clinical significance:** * Mutations in the PKM gene have been linked to several human diseases, including diabetes, cancer, and cardiovascular disease. * PKM inhibitors are being investigated as potential therapies for these diseases. **Conclusion:** The PKM gene is a key regulator of energy metabolism and cell cycle regulation. Its mutations have been linked to several human diseases, highlighting its importance in maintaining cellular health and homeostasis.

Genular Protein ID: 655614685

Symbol: KPYM_HUMAN

Name: Pyruvate kinase PKM

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 2854097

Title: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma.

PubMed ID: 2854097

DOI: 10.1016/0378-1119(88)90515-x

PubMed ID: 2813362

Title: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase.

PubMed ID: 2813362

DOI: 10.1073/pnas.86.20.7861

PubMed ID: 2040271

Title: Isolation and characterization of the human pyruvate kinase M gene.

PubMed ID: 2040271

DOI: 10.1111/j.1432-1033.1991.tb15991.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

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: 1854723

Title: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate.

PubMed ID: 1854723

DOI: 10.1021/bi00243a010

PubMed ID: 12665801

Title: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

PubMed ID: 12665801

DOI: 10.1038/nbt810

PubMed ID: 25263439

Title: TRIM35 Interacts with pyruvate kinase isoform M2 to suppress the Warburg effect and tumorigenicity in hepatocellular carcinoma.

PubMed ID: 25263439

DOI: 10.1038/onc.2014.325

PubMed ID: 9466265

Title: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth.

PubMed ID: 9466265

DOI: 10.1046/j.1365-2958.1998.00670.x

PubMed ID: 12650930

Title: Interaction between HERC1 and M2-type pyruvate kinase.

PubMed ID: 12650930

DOI: 10.1016/s0014-5793(03)00205-9

PubMed ID: 14654843

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

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 16139798

Title: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.

PubMed ID: 16139798

DOI: 10.1016/j.bbrc.2005.08.132

PubMed ID: 15592455

Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

PubMed ID: 15592455

DOI: 10.1038/nbt1046

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17308100

Title: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death.

PubMed ID: 17308100

DOI: 10.1158/0008-5472.can-06-2870

PubMed ID: 18298799

Title: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein.

PubMed ID: 18298799

DOI: 10.1111/j.1365-2443.2008.01165.x

PubMed ID: 18191611

Title: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription.

PubMed ID: 18191611

DOI: 10.1016/j.biocel.2007.11.009

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

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: 18337823

Title: The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth.

PubMed ID: 18337823

DOI: 10.1038/nature06734

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20847263

Title: Evidence for an alternative glycolytic pathway in rapidly proliferating cells.

PubMed ID: 20847263

DOI: 10.1126/science.1188015

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: 21620138

Title: Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1.

PubMed ID: 21620138

DOI: 10.1016/j.cell.2011.03.054

PubMed ID: 21483450

Title: The oxygen sensor PHD3 limits glycolysis under hypoxia via direct binding to pyruvate kinase.

PubMed ID: 21483450

DOI: 10.1038/cr.2011.66

PubMed ID: 21700219

Title: Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth.

PubMed ID: 21700219

DOI: 10.1016/j.molcel.2011.04.025

PubMed ID: 22056988

Title: Nuclear PKM2 regulates beta-catenin transactivation upon EGFR activation.

PubMed ID: 22056988

DOI: 10.1038/nature10598

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: 22901803

Title: PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis.

PubMed ID: 22901803

DOI: 10.1016/j.cell.2012.07.018

PubMed ID: 22306293

Title: Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase.

PubMed ID: 22306293

DOI: 10.1016/j.molcel.2012.01.001

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24120661

Title: Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization.

PubMed ID: 24120661

DOI: 10.1016/j.molcel.2013.09.004

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: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

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: 25944712

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

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27199445

Title: JMJD8 Regulates Angiogenic Sprouting and Cellular Metabolism by Interacting With Pyruvate Kinase M2 in Endothelial Cells.

PubMed ID: 27199445

DOI: 10.1161/atvbaha.116.307695

PubMed ID: 27573352

Title: TSC22D2 interacts with PKM2 and inhibits cell growth in colorectal cancer.

PubMed ID: 27573352

DOI: 10.3892/ijo.2016.3599

PubMed ID: 26787900

Title: SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic functions.

PubMed ID: 26787900

DOI: 10.1073/pnas.1520045113

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: 32268273

Title: TRAF4 acts as a fate checkpoint to regulate the adipogenic differentiation of MSCs by activating PKM2.

PubMed ID: 32268273

DOI: 10.1016/j.ebiom.2020.102722

PubMed ID: 15996096

Title: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis.

PubMed ID: 15996096

DOI: 10.1021/bi0474923

PubMed ID: 18337815

Title: Pyruvate kinase M2 is a phosphotyrosine-binding protein.

PubMed ID: 18337815

DOI: 10.1038/nature06667

PubMed ID: 23064226

Title: Serine is a natural ligand and allosteric activator of pyruvate kinase M2.

PubMed ID: 23064226

DOI: 10.1038/nature11540

PubMed ID: 23530218

Title: M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation.

PubMed ID: 23530218

DOI: 10.1073/pnas.1217157110

Sequence Information:

  • Length: 531
  • Mass: 57937
  • Checksum: AA94D7818ED6BBAD
  • Sequence:
  • MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET 
    LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR 
    TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 
    ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 
    FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 
    IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 
    LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS 
    FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE 
    AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P

Genular Protein ID: 3254224110

Symbol: A0A804F729_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

Sequence Information:

  • Length: 605
  • Mass: 65931
  • Checksum: DC4C65D9618A1816
  • Sequence:
  • MQWSSERGER LLTPGACSSE VPSAVPSRSG GSPGHTVFSS ERSLLVRPRS HPEPKGEHYV 
    TGSPTPENQR TSAAMSKPHS EAGTAFIQTQ QLHAAMADTF LEHMCRLDID SPPITARNTG 
    IICTIGPASR SVETLKEMIK SGMNVARLNF SHGTHEYHAE TIKNVRTATE SFASDPILYR 
    PVAVALDTKG PEIRTGLIKG SGTAEVELKK GATLKITLDN AYMEKCDENI LWLDYKNICK 
    VVEVGSKIYV DDGLISLQVK QKGADFLVTE VENGGSLGSK KGVNLPGAAV DLPAVSEKDI 
    QDLKFGVEQD VDMVFASFIR KASDVHEVRK VLGEKGKNIK IISKIENHEG VRRFDEILEA 
    SDGIMVARGD LGIEIPAEKV FLAQKMMIGR CNRAGKPVIC ATQMLESMIK KPRPTRAEGS 
    DVANAVLDGA DCIMLSGETA KGDYPLEAVR MQHLIAREAE AAMFHRKLFE ELVRASSHST 
    DLMEAMAMGS VEASYKCLAA ALIVLTESGR SAHQVARYRP RAPIIAVTRN PQTARQAHLY 
    RGIFPVLCKD PVQEAWAEDV DLRVNFAMNV GKARGFFKKG DVVIVLTGWR PGSGFTNTMR 
    VVPVP

Genular Protein ID: 782644606

Symbol: A0A804F6T5_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

Sequence Information:

  • Length: 566
  • Mass: 61594
  • Checksum: AFBF0A28554E2C10
  • Sequence:
  • MQWSSERGER LLTPGACSSE VPSAVPSRSG GTSAAMSKPH SEAGTAFIQT QQLHAAMADT 
    FLEHMCRLDI DSPPITARNT GIICTIGPAS RSVETLKEMI KSGMNVARLN FSHGTHEYHA 
    ETIKNVRTAT ESFASDPILY RPVAVALDTK GPEIRTGLIK GSGTAEVELK KGATLKITLD 
    NAYMEKCDEN ILWLDYKNIC KVVEVGSKIY VDDGLISLQV KQKGADFLVT EVENGGSLGS 
    KKGVNLPGAA VDLPAVSEKD IQDLKFGVEQ DVDMVFASFI RKASDVHEVR KVLGEKGKNI 
    KIISKIENHE GVRRFDEILE ASDGIMVARG DLGIEIPAEK VFLAQKMMIG RCNRAGKPVI 
    CATQMLESMI KKPRPTRAEG SDVANAVLDG ADCIMLSGET AKGDYPLEAV RMQHLIAREA 
    EAAMFHRKLF EELVRASSHS TDLMEAMAMG SVEASYKCLA AALIVLTESG RSAHQVARYR 
    PRAPIIAVTR NPQTARQAHL YRGIFPVLCK DPVQEAWAED VDLRVNFAMN VGKARGFFKK 
    GDVVIVLTGW RPGSGFTNTM RVVPVP

Genular Protein ID: 4055232665

Symbol: B4DNK4_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

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: 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: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

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: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

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: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

PubMed ID: 25944712

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

PubMed ID: 25944712

PubMed ID: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 457
  • Mass: 49898
  • Checksum: FC7B2566EEDC7096
  • Sequence:
  • MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVEL 
    KKGATLKITL DNAYMEKCDE NILWLDYKNI CKVVEVGSKI YVDDGLISLQ VKQKGADFLV 
    TEVENGGSLG SKKGVNLPGA AVDLPAVSEK DIQDLKFGVE QDVDMVFASF IRKASDVHEV 
    RKVLGEKGKN IKIISKIENH EGVRRFDEIL EASDGIMVAR GDLGIEIPAE KVFLAQKMMI 
    GRCNRAGKPV ICATQMLESM IKKPRPTRAE GSDVANAVLD GADCIMLSGE TAKGDYPLEA 
    VRMQHLIARE AEAAIYHLQL FEELRRLAPI TSDPTEATAV GAVEASFKCC SGAIIVLTKS 
    GRSAHQVARY RPRAPIIAVT RNPQTARQAH LYRGIFPVLC KDPVQEAWAE DVDLRVNFAM 
    NVGKARGFFK KGDVVIVLTG WRPGSGFTNT MRVVPVP

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.