Details for: TFRC

Gene ID: 7037

Symbol: TFRC

Ensembl ID: ENSG00000072274

Description: transferrin receptor

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: early promyelocyte (CL0002154)
    Fold Change: 3.8
    Marker Score: 3045
  • Cell Name: alveolar macrophage (CL0000583)
    Fold Change: 2.36
    Marker Score: 60405
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 2.24
    Marker Score: 1337
  • Cell Name: syncytiotrophoblast cell (CL0000525)
    Fold Change: 2.04
    Marker Score: 1679
  • Cell Name: proerythroblast (CL0000547)
    Fold Change: 1.92
    Marker Score: 1305
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 1.76
    Marker Score: 2013
  • Cell Name: myoepithelial cell of mammary gland (CL0002324)
    Fold Change: 1.69
    Marker Score: 8281
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 1.68
    Marker Score: 6610
  • Cell Name: OFF retinal ganglion cell (CL4023033)
    Fold Change: 1.55
    Marker Score: 648
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 1.55
    Marker Score: 1651
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 1.55
    Marker Score: 2277
  • Cell Name: myeloid leukocyte (CL0000766)
    Fold Change: 1.49
    Marker Score: 1804
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 1.49
    Marker Score: 1583
  • Cell Name: elicited macrophage (CL0000861)
    Fold Change: 1.49
    Marker Score: 9060
  • Cell Name: mural cell (CL0008034)
    Fold Change: 1.46
    Marker Score: 166988
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 1.45
    Marker Score: 1601
  • Cell Name: megakaryocyte progenitor cell (CL0000553)
    Fold Change: 1.42
    Marker Score: 398
  • Cell Name: glandular epithelial cell (CL0000150)
    Fold Change: 1.41
    Marker Score: 3467
  • Cell Name: colon epithelial cell (CL0011108)
    Fold Change: 1.35
    Marker Score: 4235
  • Cell Name: hematopoietic multipotent progenitor cell (CL0000837)
    Fold Change: 1.34
    Marker Score: 655
  • Cell Name: late promyelocyte (CL0002151)
    Fold Change: 1.34
    Marker Score: 336
  • Cell Name: intestinal crypt stem cell (CL0002250)
    Fold Change: 1.33
    Marker Score: 501
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 1.33
    Marker Score: 330
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 1.32
    Marker Score: 1391
  • Cell Name: pneumocyte (CL0000322)
    Fold Change: 1.3
    Marker Score: 2082
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 1.28
    Marker Score: 1550
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 1.28
    Marker Score: 1716.5
  • Cell Name: choroid plexus epithelial cell (CL0000706)
    Fold Change: 1.27
    Marker Score: 1164
  • Cell Name: basal cell (CL0000646)
    Fold Change: 1.27
    Marker Score: 1633
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 1.26
    Marker Score: 1254.5
  • Cell Name: ON retinal ganglion cell (CL4023032)
    Fold Change: 1.25
    Marker Score: 342
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 1.23
    Marker Score: 7821
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: 1.21
    Marker Score: 637
  • Cell Name: non-classical monocyte (CL0000875)
    Fold Change: 1.19
    Marker Score: 2864
  • Cell Name: A2 amacrine cell (CL0004219)
    Fold Change: 1.18
    Marker Score: 375
  • Cell Name: macrophage (CL0000235)
    Fold Change: 1.15
    Marker Score: 1279
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: 1.15
    Marker Score: 1770
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: 1.13
    Marker Score: 41717
  • Cell Name: enterocyte (CL0000584)
    Fold Change: 1.12
    Marker Score: 5373
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: 1.11
    Marker Score: 4596
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 1.1
    Marker Score: 2412
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 1.09
    Marker Score: 638
  • Cell Name: germ cell (CL0000586)
    Fold Change: 1.08
    Marker Score: 1895
  • Cell Name: immature innate lymphoid cell (CL0001082)
    Fold Change: 1.08
    Marker Score: 2205
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 1.04
    Marker Score: 16337.5
  • Cell Name: ependymal cell (CL0000065)
    Fold Change: 1.04
    Marker Score: 364
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: 1.04
    Marker Score: 8955.5
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 1.04
    Marker Score: 1179
  • Cell Name: myelocyte (CL0002193)
    Fold Change: 1.03
    Marker Score: 446
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 1.03
    Marker Score: 2758
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.03
    Marker Score: 63285
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 1.02
    Marker Score: 597
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.02
    Marker Score: 34647.5
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.01
    Marker Score: 9626.5
  • Cell Name: cortical thymic epithelial cell (CL0002364)
    Fold Change: 1.01
    Marker Score: 3739.5
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 1.01
    Marker Score: 7853
  • Cell Name: lung microvascular endothelial cell (CL2000016)
    Fold Change: 1
    Marker Score: 213
  • Cell Name: erythroblast (CL0000765)
    Fold Change: 1
    Marker Score: 625
  • Cell Name: type II pneumocyte (CL0002063)
    Fold Change: 1
    Marker Score: 6492
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71635.5
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 0.99
    Marker Score: 47861
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 0.99
    Marker Score: 595
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.99
    Marker Score: 34231
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 0.98
    Marker Score: 21017.5
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30381
  • Cell Name: mucous neck cell (CL0000651)
    Fold Change: 0.98
    Marker Score: 2218
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: 0.97
    Marker Score: 9132
  • Cell Name: stem cell (CL0000034)
    Fold Change: 0.96
    Marker Score: 2280
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.96
    Marker Score: 4016
  • Cell Name: primitive red blood cell (CL0002355)
    Fold Change: 0.95
    Marker Score: 709
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 0.94
    Marker Score: 9753.5
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.94
    Marker Score: 2144
  • Cell Name: dendritic cell (CL0000451)
    Fold Change: 0.94
    Marker Score: 645
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.94
    Marker Score: 2390
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 0.94
    Marker Score: 1493
  • Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
    Fold Change: 0.93
    Marker Score: 204.5
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 0.93
    Marker Score: 3058
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 0.93
    Marker Score: 9367
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.93
    Marker Score: 477
  • Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
    Fold Change: 0.92
    Marker Score: 433
  • Cell Name: alternatively activated macrophage (CL0000890)
    Fold Change: 0.91
    Marker Score: 380
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.91
    Marker Score: 5182
  • Cell Name: vip GABAergic cortical interneuron (CL4023016)
    Fold Change: 0.9
    Marker Score: 34195.5
  • Cell Name: mesenchymal lymphangioblast (CL0005021)
    Fold Change: 0.9
    Marker Score: 201
  • Cell Name: precursor cell (CL0011115)
    Fold Change: 0.9
    Marker Score: 218
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.9
    Marker Score: 2689
  • Cell Name: common dendritic progenitor (CL0001029)
    Fold Change: 0.89
    Marker Score: 308
  • Cell Name: ovarian surface epithelial cell (CL2000064)
    Fold Change: 0.88
    Marker Score: 2407
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 0.88
    Marker Score: 1248
  • Cell Name: endothelial tip cell (CL0000704)
    Fold Change: 0.88
    Marker Score: 205
  • Cell Name: basal epithelial cell of prostatic duct (CL0002236)
    Fold Change: 0.87
    Marker Score: 776
  • Cell Name: erythroid progenitor cell, mammalian (CL0001066)
    Fold Change: 0.87
    Marker Score: 280
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5290
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 0.87
    Marker Score: 1445
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 0.87
    Marker Score: 389
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 0.87
    Marker Score: 8784
  • Cell Name: epicardial adipocyte (CL1000309)
    Fold Change: 0.87
    Marker Score: 420
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 0.86
    Marker Score: 206
  • Cell Name: peritubular capillary endothelial cell (CL1001033)
    Fold Change: 0.86
    Marker Score: 199
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.85
    Marker Score: 307

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Other Information

**Key Characteristics** 1. **Structure**: TFRC is a transmembrane glycoprotein composed of two subunits: a light chain (LT) and a heavy chain (HT). The LT subunit is responsible for binding transferrin, while the HT subunit interacts with the cytoplasmic domain of the transferrin receptor. 2. **Function**: TFRC mediates the uptake of iron from transferrin through a clathrin-coated endocytic pathway. It also regulates iron ion homeostasis, cell growth, and differentiation. 3. **Expression**: TFRC is widely expressed in various cell types, including hematopoietic cells, endothelial cells, placental cells, and certain types of cancer cells. **Pathways and Functions** 1. **Iron Uptake and Transport**: TFRC mediates the uptake of iron from transferrin through a clathrin-coated endocytic pathway. This process involves the binding of transferrin to the LT subunit of TFRC, followed by the endocytosis of the transferrin-TFRC complex. 2. **Cell Growth and Differentiation**: TFRC regulates cell growth and differentiation by controlling the availability of iron. Iron is essential for the synthesis of proteins, DNA, and other biomolecules necessary for cell growth and differentiation. 3. **Apoptosis Regulation**: TFRC can regulate apoptosis (programmed cell death) by controlling the availability of iron. Iron is necessary for the activation of caspases, which are enzymes involved in the apoptosis pathway. 4. **Signaling Pathways**: TFRC can interact with various signaling pathways, including the Rho GTPase cycle, the Rac GTPase cycle, and the NF-κB signaling pathway. These interactions can regulate cell growth, differentiation, and survival. **Clinical Significance** 1. **Iron Deficiency Anemia**: TFRC dysregulation has been implicated in iron deficiency anemia, a condition characterized by a decrease in red blood cell production. 2. **Anemia of Chronic Disease**: TFRC dysregulation has also been implicated in anemia of chronic disease, a condition characterized by a decrease in iron availability due to chronic inflammation. 3. **Cancer**: TFRC dysregulation has been implicated in certain types of cancer, including leukemia and lymphoma. TFRC can promote cell growth and survival by controlling the availability of iron. 4. **Neurological Disorders**: TFRC dysregulation has been implicated in certain neurological disorders, including Parkinson's disease and Alzheimer's disease. TFRC can regulate iron homeostasis in the brain, which is essential for neuronal function and survival. In conclusion, the TFRC gene plays a crucial role in iron homeostasis, cell growth, and differentiation. Its dysregulation has been implicated in several diseases, including iron deficiency anemia, anemia of chronic disease, and certain types of cancer. Further research is needed to fully understand the mechanisms by which TFRC regulates iron homeostasis and its role in various diseases.

Genular Protein ID: 3134889831

Symbol: TFR1_HUMAN

Name: Transferrin receptor protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 6090955

Title: Primary structure of human transferrin receptor deduced from the mRNA sequence.

PubMed ID: 6090955

DOI: 10.1038/311675b0

PubMed ID: 6094009

Title: The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence.

PubMed ID: 6094009

DOI: 10.1016/0092-8674(84)90004-7

PubMed ID: 9358047

Title: Exon/intron structure of the human transferrin receptor gene.

PubMed ID: 9358047

DOI: 10.1016/s0378-1119(97)00356-9

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: 2229063

Title: Serum transferrin receptor is a truncated form of tissue receptor.

PubMed ID: 2229063

DOI: 10.1016/s0021-9258(17)30627-0

PubMed ID: 1871153

Title: Characterization of transferrin receptor released by K562 erythroleukemia cells.

PubMed ID: 1871153

DOI: 10.3181/00379727-197-43276

PubMed ID: 7864799

Title: Identification of a novel form of the alpha 3 integrin subunit: covalent association with transferrin receptor.

PubMed ID: 7864799

DOI: 10.1042/bj3060129

PubMed ID: 1380674

Title: Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size.

PubMed ID: 1380674

DOI: 10.1038/358764a0

PubMed ID: 3568132

Title: Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site.

PubMed ID: 3568132

DOI: 10.1016/0092-8674(87)90295-9

PubMed ID: 3582362

Title: Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site.

PubMed ID: 3582362

DOI: 10.1002/j.1460-2075.1987.tb04758.x

PubMed ID: 2507316

Title: Intermolecular disulfide bonds are not required for the expression of the dimeric state and functional activity of the transferrin receptor.

PubMed ID: 2507316

DOI: 10.1002/j.1460-2075.1989.tb08347.x

PubMed ID: 2327986

Title: A point mutation in the cytoplasmic domain of the transferrin receptor inhibits endocytosis.

PubMed ID: 2327986

DOI: 10.1042/bj2670031

PubMed ID: 2298808

Title: Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization.

PubMed ID: 2298808

DOI: 10.1083/jcb.110.2.283

PubMed ID: 1421756

Title: Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.

PubMed ID: 1421756

DOI: 10.1093/glycob/2.4.345

PubMed ID: 1421757

Title: Identification of the O-linked glycosylation site of the human transferrin receptor.

PubMed ID: 1421757

DOI: 10.1093/glycob/2.4.355

PubMed ID: 8408022

Title: YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis.

PubMed ID: 8408022

DOI: 10.1016/s0021-9258(20)80596-1

PubMed ID: 7780197

Title: The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.

PubMed ID: 7780197

DOI: 10.1093/glycob/5.2.227

PubMed ID: 8631371

Title: Functional analysis of human/chicken transferrin receptor chimeras indicates that the carboxy-terminal region is important for ligand binding.

PubMed ID: 8631371

DOI: 10.1111/j.1432-1033.1996.0009u.x

PubMed ID: 10377239

Title: A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin.

PubMed ID: 10377239

DOI: 10.1042/bj3410011

PubMed ID: 11800564

Title: Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites.

PubMed ID: 11800564

DOI: 10.1006/jmbi.2001.5048

PubMed ID: 16325581

Title: TTP specifically regulates the internalization of the transferrin receptor.

PubMed ID: 16325581

DOI: 10.1016/j.cell.2005.10.021

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 15592455

Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

PubMed ID: 15592455

DOI: 10.1038/nbt1046

PubMed ID: 17081065

Title: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

PubMed ID: 17081065

DOI: 10.1021/pr060363j

PubMed ID: 17287727

Title: Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses.

PubMed ID: 17287727

DOI: 10.1038/nature05539

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18268337

Title: Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses.

PubMed ID: 18268337

DOI: 10.1073/pnas.0709254105

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19349973

Title: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.

PubMed ID: 19349973

DOI: 10.1038/nbt.1532

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: 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: 26214738

Title: Regulation of mitochondrial morphology and function by stearoylation of TFR1.

PubMed ID: 26214738

DOI: 10.1038/nature14601

PubMed ID: 25944712

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

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 9782058

Title: Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy.

PubMed ID: 9782058

DOI: 10.1016/s0969-2126(98)00124-5

PubMed ID: 10531064

Title: Crystal structure of the ectodomain of human transferrin receptor.

PubMed ID: 10531064

DOI: 10.1126/science.286.5440.779

PubMed ID: 11702220

Title: Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach.

PubMed ID: 11702220

DOI: 10.1007/s004390100599

PubMed ID: 26642240

Title: A missense mutation in TFRC, encoding transferrin receptor 1, causes combined immunodeficiency.

PubMed ID: 26642240

DOI: 10.1038/ng.3465

Sequence Information:

  • Length: 760
  • Mass: 84871
  • Checksum: C886F14000D90154
  • Sequence:
  • MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK 
    RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR 
    RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK 
    VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK 
    KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 
    AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD 
    STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG 
    VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT 
    YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA 
    AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 
    LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF 
    GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK 
    QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF

Genular Protein ID: 604985350

Symbol: Q7Z3E0_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 13
  • Mass: 1468
  • Checksum: 8FE0E6255E80CDC5
  • Sequence:
  • MDQARSAFSN LDL

Genular Protein ID: 1454524531

Symbol: G3V0E5_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: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 25944712

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

PubMed ID: 25944712

Sequence Information:

  • Length: 679
  • Mass: 75964
  • Checksum: 00830FDA9668C11B
  • Sequence:
  • MIGYLGYCKG VEPKTECERL AGTESPVREE PGEDFPAARR LYWDDLKRKL SEKLDSTDFT 
    GTIKLLNENS YVPREAGSQK DENLALYVEN QFREFKLSKV WRDQHFVKIQ VKDSAQNSVI 
    IVDKNGRLVY LVENPGGYVA YSKAATVTGK LVHANFGTKK DFEDLYTPVN GSIVIVRAGK 
    ITFAEKVANA ESLNAIGVLI YMDQTKFPIV NAELSFFGHA HLGTGDPYTP GFPSFNHTQF 
    PPSRSSGLPN IPVQTISRAA AEKLFGNMEG DCPSDWKTDS TCRMVTSESK NVKLTVSNVL 
    KEIKILNIFG VIKGFVEPDH YVVVGAQRDA WGPGAAKSGV GTALLLKLAQ MFSDMVLKDG 
    FQPSRSIIFA SWSAGDFGSV GATEWLEGYL SSLHLKAFTY INLDKAVLGT SNFKVSASPL 
    LYTLIEKTMQ NVKHPVTGQF LYQDSNWASK VEKLTLDNAA FPFLAYSGIP AVSFCFCEDT 
    DYPYLGTTMD TYKELIERIP ELNKVARAAA EVAGQFVIKL THDVELNLDY ERYNSQLLSF 
    VRDLNQYRAD IKEMGLSLQW LYSARGDFFR ATSRLTTDFG NAEKTDRFVM KKLNDRVMRV 
    EYHFLSPYVS PKESPFRHVF WGSGSHTLPA LLENLKLRKQ NNGAFNETLF RNQLALATWT 
    IQGAANALSG DVWDIDNEF

Genular Protein ID: 1748059015

Symbol: A8K6Q8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 760
  • Mass: 84873
  • Checksum: 3DAEE97671E394D4
  • Sequence:
  • MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK 
    RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR 
    RLYWDDLKRK LSEKLDSTDF TSTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK 
    VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATATG KLVHANFGTK 
    KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 
    AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD 
    STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG 
    VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT 
    YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA 
    AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 
    LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF 
    GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK 
    QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF

Genular Protein ID: 937746282

Symbol: A0A8V8TM46_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

Sequence Information:

  • Length: 478
  • Mass: 53436
  • Checksum: 223C6210920B6596
  • Sequence:
  • MDQTKFPIVN AELSFFGHAH LGTGDPYTPG FPSFNHTQFP PSRSSGLPNI PVQTISRAAA 
    EKLFGNMEGD CPSDWKTDST CRMVTSESKN VKLTVSNVLK EIKILNIFGV IKGFVEPDHY 
    VVVGAQRDAW GPGAAKSGVG TALLLKLAQM FSDMVLKDGF QPSRSIIFAS WSAGDFGSVG 
    ATEWLEGYLS SLHLKAFTYI NLDKAVLGTS NFKVSASPLL YTLIEKTMQN VKHPVTGQFL 
    YQDSNWASKV EKLTLDNAAF PFLAYSGIPA VSFCFCEDTD YPYLGTTMDT YKELIERIPE 
    LNKVARAAAE VAGQFVIKLT HDVELNLDYE RYNSQLLSFV RDLNQYRADI KEMGLSLQWL 
    YSARGDFFRA TSRLTTDFGN AEKTDRFVMK KLNDRVMRVE YHFLSPYVSP KESPFRHVFW 
    GSGSHTLPAL LENLKLRKQN NGAFNETLFR NQLALATWTI QGAANALSGD VWDIDNEF

Genular Protein ID: 662021783

Symbol: B7Z2I6_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 478
  • Mass: 53484
  • Checksum: D23C6217E3CC79EB
  • Sequence:
  • MDQTKFPIVN AELSFFGHAH LGTGDPYTPG FPSFNHTQFP PSRSSGLPNI PVQTISRAAA 
    EKLFGNMEGD CPSDWKTDST CRMVTSESKN VKLTVSNVLK EIKILNIFGV IKGFVEPDHY 
    VVVGAQRDAW GPGAAKSGVG TALLLKLAQM FSDMVLKDGF QPSRSIIFAS WSAGDFGSVG 
    ATEWLEGYLS SLHLKAFTYI NLDKAVLGTS NFKVSASPLL YTLIEKTMQN VKHPFTGQFL 
    YQDSNWASKV EKLTLDNAAF PFLAYSGIPA VSFCFCEDTD YPYLGTTMDT YKELIERIPE 
    LNKVARAAAE VAGQFVIKLT HDVELNLDYE RYNSQLLSFV RDLNQYRADI KEMGLSLQWL 
    YSARGDFFRA TSRLTTDFGN AEKTDRFVMK KLNDRVMRVE YHFLSPYVSP KESPFRHVFW 
    GSGSHTLPAL LENLKLRKQN NGAFNETLFR NQLALATWTI QGAANALSGD VWDIDNEF

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.