Details for: HSPA1A
Gene ID: 3303
Gene Type: Protein-coding - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.
Symbol: HSPA1A
Ensembl ID: ENSG00000204389
Description: heat shock protein family A (Hsp70) member 1A
Cell Significance Landscape
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
-
CSI 56.27rCSI 41.81%PRS 16.85
-
CSI 40.39rCSI 46.24%PRS 23.34
-
CSI 37rCSI 30.06%PRS 12.06
-
CSI 36.78rCSI 28.61%PRS 16.38
-
CSI 33.92rCSI 29.37%PRS 12.66
-
CSI 32.14rCSI 38.95%PRS 15.24
-
CSI 30.87rCSI 23.2%PRS 11.77
-
CSI 30.58rCSI 30.2%PRS 43.53
-
CSI 28.72rCSI 49.14%PRS 22.99
-
CSI 27.48rCSI 20.79%PRS 15.71
-
CSI 25.72rCSI 28.95%PRS 18.16
-
CSI 25.27rCSI 36.45%PRS 15.82
-
CSI 23.73rCSI 20.46%PRS 18.51
-
CSI 23.44rCSI 40.16%PRS 15.21
-
CSI 22.96rCSI 19.16%PRS 33.54
-
CSI 22.62rCSI 26.12%PRS 10.04
-
CSI 22.19rCSI 18.37%PRS 11.36
-
CSI 21.66rCSI 22.07%PRS 16.21
-
CSI 21.46rCSI 53.77%PRS 33.92
-
CSI 21.2rCSI 25.31%PRS 19.67
-
CSI 20.78rCSI 21.28%PRS 21.22
-
CSI 19.77rCSI 31.57%PRS 12.43
-
CSI 19.59rCSI 25.13%PRS 13.13
-
CSI 19.38rCSI 13.06%PRS 13.61
-
CSI 19.35rCSI 25.35%PRS 15.91
-
CSI 19.1rCSI 15.16%PRS 19.98
-
CSI 17.87rCSI 28.5%PRS 9.81
-
CSI 17.46rCSI 16.81%PRS 11.76
-
CSI 15.74rCSI 45.54%PRS 25.38
-
CSI 14.36rCSI 12.61%PRS 12.76
-
CSI 14.32rCSI 14.07%PRS 32.56
-
CSI 13.86rCSI 18.17%PRS 49.73
-
CSI 13.81rCSI 19.9%PRS 18.35
-
CSI 13.57rCSI 18.86%PRS 11.75
-
CSI 13.56rCSI 10.72%PRS 7.84
-
CSI 13.09rCSI 46.46%PRS 18.63
-
CSI 12.99rCSI 16.67%PRS 11.09
-
CSI 12.71rCSI 17.61%PRS 16.38
-
CSI 12.57rCSI 12.54%PRS 9.75
-
CSI 12.33rCSI 64.82%PRS 21.63
-
CSI 12.16rCSI 31.25%PRS 16.75
-
CSI 12.12rCSI 22.21%PRS 48.55
-
CSI 12rCSI 14.78%PRS 36.25
-
CSI 12rCSI 12.53%PRS 34.51
-
CSI 11.74rCSI 13.62%PRS 16.85
-
CSI 11.7rCSI 11.49%PRS 17.88
-
CSI 11.59rCSI 26.41%PRS 11.92
-
CSI 11.43rCSI 38.65%PRS 19.22
-
CSI 11.34rCSI 9.5%PRS 13.63
-
CSI 11.07rCSI 9.62%PRS 14.01
-
CSI 11rCSI 16.77%PRS 10.63
-
CSI 10.72rCSI 22.24%PRS 11.36
-
CSI 10.64rCSI 15.59%PRS 53.84
-
CSI 10.62rCSI 12.44%PRS 15.46
-
CSI 10.61rCSI 19.29%PRS 44.92
-
CSI 10.55rCSI 17.09%PRS 11.63
-
CSI 10.51rCSI 15%PRS 12.82
-
CSI 10.51rCSI 12.59%PRS 19.51
-
CSI 10.46rCSI 14.23%PRS 17.43
-
CSI 10.26rCSI 13.72%PRS 15.18
-
CSI 10.23rCSI 8.96%PRS 15.09
-
CSI 10.19rCSI 24.44%PRS 20.95
-
CSI 10.06rCSI 9.09%PRS 10.04
-
CSI 10.06rCSI 45.71%PRS 39.67
-
CSI 10.02rCSI 9.33%PRS 11.44
-
CSI 9.9rCSI 17.99%PRS 9.41
-
CSI 9.88rCSI 56.22%PRS 43.89
-
CSI 9.54rCSI 14.66%PRS 16.26
-
CSI 9.52rCSI 8.8%PRS 20.7
-
CSI 9.36rCSI 22.49%PRS 17.19
-
CSI 9.26rCSI 18.79%PRS 4.82
-
CSI 9.23rCSI 26.35%PRS 19.69
-
CSI 9.2rCSI 11.55%PRS 14.48
-
CSI 9.19rCSI 32.24%PRS 20.59
-
CSI 9.15rCSI 12.22%PRS 21.69
-
CSI 9.14rCSI 62.76%PRS 22.37
-
CSI 9.13rCSI 17.23%PRS 14.13
-
CSI 9.02rCSI 29.27%PRS 13.93
-
CSI 8.91rCSI 32.4%PRS 44.13
-
CSI 8.85rCSI 7.16%PRS 11.21
-
CSI 8.79rCSI 6.51%PRS 10.17
-
CSI 8.77rCSI 14.44%PRS 13.25
-
CSI 8.42rCSI 10.17%PRS 13.34
-
CSI 8.38rCSI 38.71%PRS 23.87
-
CSI 8.23rCSI 23.82%PRS 12.89
-
CSI 8.16rCSI 35.24%PRS 21.84
-
CSI 8.11rCSI 18.55%PRS 11.01
-
CSI 8.08rCSI 19.3%PRS 17.83
-
CSI 7.92rCSI 12.1%PRS 14.35
-
CSI 7.73rCSI 44.36%PRS 42.36
-
CSI 7.73rCSI 11.81%PRS 13.1
-
CSI 7.68rCSI 7.09%PRS 11.55
-
CSI 7.67rCSI 19.84%PRS 30.85
-
CSI 7.62rCSI 28.56%PRS 9.71
-
CSI 7.56rCSI 15.08%PRS 18.99
-
CSI 7.53rCSI 7.85%PRS 11.68
-
CSI 7.38rCSI 14.22%PRS 25.48
-
CSI 7.11rCSI 23.57%PRS 9.91
-
CSI 7.07rCSI 13.27%PRS 22.54
-
CSI 7.01rCSI 15.42%PRS 12.52
-
CSI -12.4rCSI -15.3%PRS 10.0%
-
CSI -12.3rCSI -12.9%PRS 12.1%
-
CSI -3.4rCSI -13.7%PRS 11.9%
-
CSI -2.9rCSI -11.4%PRS 16.3%
-
CSI -2.9rCSI -3.9%PRS 10.2%
-
CSI -2.6rCSI -3.1%PRS 6.5%
-
CSI -2.4rCSI -15.1%PRS 9.0%
-
CSI -2.1rCSI -7.9%PRS 23.7%
-
CSI -1.6rCSI -7.6%PRS 27.5%
-
CSI -1.5rCSI -8.4%PRS 34.1%
-
CSI -1.5rCSI -6.9%PRS 30.6%
-
CSI -0.2rCSI -1.0%PRS 17.1%
-
CSI 0.0rCSI 0.2%PRS 21.0%
-
CSI 0.1rCSI 0.2%PRS 7.7%
-
CSI 0.2rCSI 0.8%PRS 20.7%
-
CSI 0.2rCSI 1.2%PRS 5.7%
-
CSI 0.2rCSI 2.6%PRS 60.0%
-
CSI 0.2rCSI 1.4%PRS 16.6%
-
CSI 0.3rCSI 0.6%PRS 17.5%
-
CSI 0.3rCSI 0.4%PRS 14.0%
-
CSI 0.3rCSI 0.7%PRS 8.2%
-
CSI 0.3rCSI 1.0%PRS 20.6%
-
CSI 0.4rCSI 1.6%PRS 24.6%
-
CSI 0.4rCSI 0.8%PRS 8.3%
-
CSI 0.4rCSI 4.1%PRS 40.6%
-
CSI 0.4rCSI 0.6%PRS 6.2%
-
CSI 0.5rCSI 2.3%PRS 22.4%
-
CSI 0.5rCSI 0.7%PRS 15.6%
-
CSI 0.5rCSI 3.6%PRS 65.1%
-
CSI 0.5rCSI 0.7%PRS 12.0%
-
CSI 0.6rCSI 7.4%PRS 37.1%
-
CSI 0.6rCSI 1.1%PRS 11.5%
-
CSI 0.6rCSI 2.2%PRS 19.4%
-
CSI 0.6rCSI 1.7%PRS 22.3%
-
CSI 0.6rCSI 1.4%PRS 23.5%
-
CSI 0.7rCSI 1.0%PRS 13.1%
-
CSI 0.7rCSI 0.7%PRS 12.0%
-
CSI 0.7rCSI 2.7%PRS 20.0%
-
CSI 0.7rCSI 6.5%PRS 47.5%
-
CSI 0.7rCSI 4.3%PRS 25.5%
-
CSI 0.7rCSI 2.9%PRS 16.7%
-
CSI 0.8rCSI 1.4%PRS 9.5%
-
CSI 0.8rCSI 4.2%PRS 28.2%
-
CSI 0.8rCSI 7.1%PRS 71.3%
-
CSI 0.8rCSI 18.7%PRS 67.4%
-
CSI 0.8rCSI 1.2%PRS 16.0%
-
CSI 0.8rCSI 2.5%PRS 18.2%
-
CSI 0.8rCSI 1.9%PRS 12.9%
-
CSI 0.8rCSI 0.6%PRS 19.1%
-
CSI 0.8rCSI 1.1%PRS 7.0%
-
CSI 0.8rCSI 2.7%PRS 12.5%
-
CSI 0.9rCSI 9.5%PRS 37.1%
-
CSI 0.9rCSI 7.6%PRS 57.5%
-
CSI 0.9rCSI 1.3%PRS 10.7%
-
CSI 1.0rCSI 1.5%PRS 10.7%
-
CSI 1.0rCSI 2.7%PRS 46.2%
-
CSI 1.0rCSI 7.1%PRS 35.1%
-
CSI 1.0rCSI 6.7%PRS 29.6%
-
CSI 1.0rCSI 1.4%PRS 18.9%
-
CSI 1.0rCSI 1.1%PRS 20.3%
-
CSI 1.1rCSI 4.6%PRS 11.2%
-
CSI 1.1rCSI 9.9%PRS 34.9%
-
CSI 1.1rCSI 1.3%PRS 14.4%
-
CSI 1.2rCSI 2.7%PRS 9.4%
-
CSI 1.2rCSI 1.5%PRS 13.2%
-
CSI 1.2rCSI 2.4%PRS 26.8%
-
CSI 1.2rCSI 1.9%PRS 19.9%
-
CSI 1.2rCSI 3.3%PRS 14.7%
-
CSI 1.2rCSI 9.0%PRS 31.2%
-
CSI 1.3rCSI 3.5%PRS 10.9%
-
CSI 1.3rCSI 12.5%PRS 32.7%
-
CSI 1.3rCSI 25.8%PRS 80.8%
-
CSI 1.3rCSI 7.0%PRS 41.4%
-
CSI 1.3rCSI 30.9%PRS 20.2%
-
CSI 1.3rCSI 3.6%PRS 10.0%
-
CSI 1.3rCSI 1.0%PRS 15.4%
-
CSI 1.4rCSI 11.1%PRS 11.9%
-
CSI 1.4rCSI 8.1%PRS 17.6%
-
CSI 1.4rCSI 35.4%PRS 36.8%
-
CSI 1.4rCSI 4.6%PRS 14.3%
-
CSI 1.4rCSI 7.2%PRS 14.8%
-
CSI 1.5rCSI 6.5%PRS 33.5%
-
CSI 1.5rCSI 7.3%PRS 15.5%
-
CSI 1.5rCSI 1.7%PRS 13.5%
-
CSI 1.5rCSI 1.1%PRS 11.9%
-
CSI 1.6rCSI 1.9%PRS 11.3%
-
CSI 1.6rCSI 3.9%PRS 10.5%
-
CSI 1.6rCSI 8.0%PRS 12.8%
-
CSI 1.6rCSI 4.3%PRS 19.0%
-
CSI 1.6rCSI 3.6%PRS 15.3%
-
CSI 1.6rCSI 2.2%PRS 12.9%
-
CSI 1.7rCSI 1.8%PRS 13.4%
-
CSI 1.7rCSI 2.6%PRS 11.4%
-
CSI 1.7rCSI 9.6%PRS 36.0%
-
CSI 1.7rCSI 4.9%PRS 17.6%
-
CSI 1.7rCSI 10.7%PRS 36.7%
-
CSI 1.7rCSI 6.8%PRS 18.7%
-
CSI 1.8rCSI 3.1%PRS 6.7%
-
CSI 1.8rCSI 18.8%PRS 16.4%
-
CSI 1.8rCSI 4.6%PRS 11.6%
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: 515514565
Symbol: HS71A_HUMAN
Name: Heat shock 70 kDa protein 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 3931075
Title: Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70.
PubMed ID: 3931075
PubMed ID: 1700760
Title: Structure and expression of the three MHC-linked HSP70 genes.
PubMed ID: 1700760
DOI: 10.1007/bf00187095
PubMed ID: 14656967
Title: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.
PubMed ID: 14656967
DOI: 10.1101/gr.1736803
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
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: 2538825
Title: Human major histocompatibility complex contains genes for the major heat shock protein HSP70.
PubMed ID: 2538825
PubMed ID: 3786141
Title: In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells.
PubMed ID: 3786141
PubMed ID: 23349634
Title: A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
PubMed ID: 23349634
PubMed ID: 7935376
Title: Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo.
PubMed ID: 7935376
PubMed ID: 9499401
Title: Molecular chaperones as HSF1-specific transcriptional repressors.
PubMed ID: 9499401
DOI: 10.1101/gad.12.5.654
PubMed ID: 11274138
Title: Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.
PubMed ID: 11274138
PubMed ID: 12853476
Title: Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
PubMed ID: 12853476
DOI: 10.1093/emboj/cdg362
PubMed ID: 15963462
Title: Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.
PubMed ID: 15963462
PubMed ID: 15383005
Title: Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole.
PubMed ID: 15383005
DOI: 10.1042/bj20040690
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 17233114
Title: The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family.
PubMed ID: 17233114
PubMed ID: 16537599
Title: The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity.
PubMed ID: 16537599
PubMed ID: 17182002
Title: HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain.
PubMed ID: 17182002
PubMed ID: 17289661
Title: Molecular composition of IMP1 ribonucleoprotein granules.
PubMed ID: 17289661
PubMed ID: 17947705
Title: Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase.
PubMed ID: 17947705
PubMed ID: 18620420
Title: Role of the cochaperone Tpr2 in Hsp90 chaperoning.
PubMed ID: 18620420
DOI: 10.1021/bi800770g
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
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: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20053985
Title: Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha.
PubMed ID: 20053985
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: 21081504
Title: ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function.
PubMed ID: 21081504
PubMed ID: 22528486
Title: Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells.
PubMed ID: 22528486
PubMed ID: 22905912
Title: Resveratrol-induced changes of the human adipocyte secretion profile.
PubMed ID: 22905912
DOI: 10.1021/pr300539b
PubMed ID: 23973223
Title: The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3.
PubMed ID: 23973223
PubMed ID: 23921388
Title: Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation.
PubMed ID: 23921388
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24270810
Title: High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.
PubMed ID: 24270810
DOI: 10.1038/nature12748
PubMed ID: 24012426
Title: Hsp70 chaperone dynamics and molecular mechanism.
PubMed ID: 24012426
PubMed ID: 24613385
Title: Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1.
PubMed ID: 24613385
PubMed ID: 24318877
Title: Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.
PubMed ID: 24318877
PubMed ID: 24790089
Title: The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease.
PubMed ID: 24790089
PubMed ID: 25281747
Title: RING finger protein RNF207, a novel regulator of cardiac excitation.
PubMed ID: 25281747
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: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 27133716
Title: A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain independent manner.
PubMed ID: 27133716
PubMed ID: 26865365
Title: The human HSP70 family of chaperones: where do we stand?
PubMed ID: 26865365
PubMed ID: 27137183
Title: HSP70 regulates the function of mitotic centrosomes.
PubMed ID: 27137183
PubMed ID: 27708256
Title: ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation.
PubMed ID: 27708256
DOI: 10.1038/ncomms12882
PubMed ID: 28842558
Title: HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells.
PubMed ID: 28842558
PubMed ID: 10216320
Title: Structure of a new crystal form of human hsp70 ATPase domain.
PubMed ID: 10216320
PubMed ID: 20179333
Title: Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state.
PubMed ID: 20179333
PubMed ID: 20072699
Title: Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
PubMed ID: 20072699
PubMed ID: 20223214
Title: The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
PubMed ID: 20223214
PubMed ID: 21608060
Title: Biochemical and structural studies on the high affinity of Hsp70 for ADP.
PubMed ID: 21608060
DOI: 10.1002/pro.663
Sequence Information:
- Length: 641
- Mass: 70052
- Checksum: 78F513118C96DE66
- Sequence:
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
Genular Protein ID: 690584237
Symbol: B3KTT5_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
Sequence Information:
- Length: 476
- Mass: 51917
- Checksum: 24C7844D48228F36
- Sequence:
MAKAAAIGID LGTTYSCVGV FQHGKGERNV LIFDLGGGTF DVSILTIDDG IFEVKATAGD THLGGEDFDN RLVNHFVEEF KRKHKKDISQ NKRAVRRLRT ACERAKRTLS SSTQASLEID SLFEGIDFYT SITRARFEEL CSDLFRSTLE PVEKALRDAK LDKAQIHDLV LVGGSTRIPK VQKLLQDFFN GRDLNKSINP DEAVAYGAAV QAAILMGDKS ENVQDLLLLD VAPLSLGLET AGGVMTALIK RNSTIPTKQT QIFTTYSDNQ PGVLIQVYEG ERAMTKDNNL LGRFELSGIP PAPRGVPQIE VTFDIDANGI LNVTATDKSA GKANKITITN DKGRLSKEEI ERMVQEAEKY KAEDEVQRER VSAKNALESY AFNMKSAVED EGLKGKISEA DKKKVLDKCQ EVISWLDANT LAEKDEFEHK RKELEQVCNP IISGLYQGAG GPGPGGFGAQ GPKGGSGSGP TIEEVD