EuRBPDB

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TCGA tumor abbreviations
  • ACCAdrenocortical carcinoma
  • BLCABladder Urothelial Carcinoma
  • BRCABreast invasive carcinoma
  • CESCCervical squamous cell carcinoma and endocervical adenocarcinoma
  • CHOLCholangio carcinoma
  • COADColon adenocarcinoma
  • DLBCLymphoid Neoplasm Diffuse Large B-cell Lymphoma
  • ESCAEsophageal carcinoma
  • GBMGlioblastoma multiforme
  • HNSCHead and Neck squamous cell carcinoma
  • KICHKidney Chromophobe
  • KIRCKidney renal clear cell carcinoma
  • KIRPKidney renal papillary cell carcinoma
  • LAMLAcute Myeloid Leukemia
  • LGGBrain Lower Grade Glioma
  • LIHCLiver hepatocellular carcinoma
  • LUADLung adenocarcinoma
  • LUSCLung squamous cell carcinoma
  • MESOMesothelioma
  • OVOvarian serous cystadenocarcinoma
  • PAADPancreatic adenocarcinoma
  • PCPGPheochromocytoma and Paraganglioma
  • PRADProstate adenocarcinoma
  • READRectum adenocarcinoma
  • SARCSarcoma
  • SKCMSkin Cutaneous Melanoma
  • STADStomach adenocarcinoma
  • TGCTThyroid carcinoma
  • THCAThyroid carcinoma
  • THYMThymoma
  • UCECUterine Corpus Endometrial Carcinoma
  • UCSUterine Carcinosarcoma
  • UVMUveal Melanoma

Note: Click here to get the extension of tumor abbreviations.


  • Cancer Related Information
  • Basic Information

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
28212901The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells.J Inorg Biochem2017 MayCaruso Bavisotto Cdoi: 10.1016/j.jinorgbio.2017.02.004
12686536Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor alpha from murine macrophages.J Biol Chem2003 Jun 20Gao B-
18790094cis-acting sequences and trans-acting factors in the localization of mRNA for mitochondrial ribosomal proteins.Biochim Biophys Acta2008 DecRusso Adoi: 10.1016/j.bbagrm.2008.08.006
21642380Molecular chaperones as a common set of proteins that regulate the invasion phenotype of head and neck cancer.Clin Cancer Res2011 Jul 15Chiu CCdoi: 10.1158/1078-0432.CCR-10-2107
14634555Serum antibody response to the heat shock protein 60 of Chlamydia trachomatis in women with developing cervical cancer.Am J Obstet Gynecol2003 NovPaavonen J-
26810190The tumor promoting roles of HSP60 and HIF2α in gastric cancer cells.Tumour Biol2016 JulTong WWdoi: 10.1007/s13277-015-4783-2
26060090Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery.Cancer2015 Sep 15Campanella Cdoi: 10.1002/cncr.29499
27491302Quantitative patterns of Hsps in tubular adenoma compared with normal and tumor tissues reveal the value of Hsp10 and Hsp60 in early diagnosis of large bowel cancer.Cell Stress Chaperones2016 SepRappa Fdoi: 10.1007/s12192-016-0721-5
19369584Interaction between HSP60 and beta-catenin promotes metastasis.Carcinogenesis2009 JunTsai YPdoi: 10.1093/carcin/bgp087
19568603Expression of heat shock protein 60 kDa is upregulated in cervical cancer.Yonsei Med J2009 Jun 30Hwang YJdoi: 10.3349/ymj.2009.50.3.399
20708221Immunohistochemical expression of Hsp60 correlates with tumor progression and hormone resistance in prostate cancer.Urology2010 OctCastilla Cdoi: 10.1016/j.urology.2010.05.045
19635199[Expressions of heat shock protein (HSP) family HSP 60, 70 and 90alpha in colorectal cancer tissues and their correlations to pathohistological characteristics].Ai Zheng2009 JunZhang WL-
19132982Heat shock proteins 27, 60 and 70 as prognostic markers of prostate cancer.APMIS2008 OctGlaessgen Adoi: 10.1111/j.1600-0463.2008.01051.x.
16705742Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heatshock protein 60 as a marker for prostate malignancy.Prostate2006 Sep 1Johansson B-
25207654Heat shock protein 60 overexpression is associated with the progression and prognosis in gastric cancer.PLoS One2014 Sep 10Li XSdoi: 10.1371/journal.pone.0107507
23429486HSP60 predicts survival in advanced serous ovarian cancer.Int J Gynecol Cancer2013 MarHjerpe Edoi: 10.1097/IGC.0b013e318284308b.
24618330Antibodies against Hsp60 and Hsp65 in the sera of women with ovarian cancer.J Ovarian Res2014 Mar 11Bodzek Pdoi: 10.1186/1757-2215-7-30.
20082317Quantitative proteome analysis of multidrug resistance in human ovarian cancer cell line.J Cell Biochem2010 Mar 1Li SLdoi: 10.1002/jcb.22413.
28347227Comparative proteomics-network analysis of proteins responsible for ursolic acid-induced cytotoxicity in colorectal cancer cells.Tumour Biol2017 MarCai Qdoi: 10.1177/1010428317695015.
28591216Modification effects of genetic polymorphisms in FTO, IL-6, and HSPD1 on the associations of diabetes with breast cancer risk and survival.PLoS One2017 Jun 7Zhu RMdoi: 10.1371/journal.pone.0178850
30337218Heat shock proteins 60 and 70 are associated with long-term outcome of T1-stage high-grade urothelial tumors of the bladder treated with intravesical Bacillus Calmette-Gu??rin immunotherapy.Urol Oncol2018 DecMano Rdoi: 10.1016/j.urolonc.2018.09.007

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr2197494722Missense_MutationnovelE181Q0.08
BLCAchr2197493472Missense_MutationNAD241Y0.26
BLCAchr2197489217Missense_MutationNAL334F0.34
BLCAchr2197494722Missense_MutationnovelE181Q0.22
BLCAchr2197493329Missense_MutationNAL288F0.06
BRCAchr2197497177Missense_MutationnovelK130N0.22
BRCAchr2197493455SilentNAL246L0.31
BRCAchr2197493364Missense_MutationNAD277N0.16
BRCAchr2197489133Missense_MutationNAG362C0.11
BRCAchr2197487140Frame_Shift_DelnovelT540Kfs*30.4
BRCAchr2197498812Frame_Shift_InsNAP13Tfs*530.31
BRCAchr2197487944Missense_MutationNAM495L0.18
BRCAchr2197495344Missense_MutationNAE154K0.13
COADchr2197494746Missense_MutationnovelT173A0.28
COADchr2197494657Missense_MutationnovelK202N0.35
COADchr2197495230Intronnovel0.35
COADchr2197495230Intronnovel0.22
COADchr2197489039Missense_Mutationrs751104797R393Q0.47
COADchr2197493429Missense_MutationnovelQ255R0.37
COADchr2197497261SilentnovelA102A0.31
COADchr2197489056SilentnovelK387K0.25
COADchr2197488385Frame_Shift_DelNAG441Vfs*140.04
COADchr2197489109Missense_Mutationrs768557320R370C0.11
COADchr2197498734Missense_MutationNAL39V0.13
COADchr21974870133'UTRnovel0.33
GBMchr2197488385Missense_MutationnovelG441D0.11
GBMchr2197489217Missense_MutationnovelL334I0.57
GBMchr2197487950Nonsense_MutationnovelK493*0.11
GBMchr2197498689Missense_MutationnovelT54A0.25
HNSCchr21974869203'UTRnovel0.32
HNSCchr2197496992Intronnovel0.38
HNSCchr2197498739Missense_MutationNAR37Q0.17
HNSCchr2197489008Frame_Shift_DelnovelL404*0.3
KICHchr2197493393Missense_MutationnovelH267L0.41
KIRCchr2197497352Missense_MutationNAK72T0.27
KIRPchr2197497383Frame_Shift_DelnovelV62Dfs*30.34
LGGchr2197488447Frame_Shift_DelnovelD419Efs*350.43
LGGchr2197494196Nonsense_MutationnovelR221*0.34
LIHCchr2197489193Missense_MutationnovelL342V0.42
LIHCchr2197493349Missense_MutationnovelA282P0.29
LUADchr2197493427Missense_MutationnovelS256T0.24
LUSCchr2197487062Missense_MutationnovelG569V0.12
LUSCchr2197497197Missense_MutationNAA124P0.33
LUSCchr2197488341Missense_MutationnovelP456S0.28
LUSCchr2197494226SilentNAL211L0.12
OVchr2197498675Missense_MutationNAK58N0.29
PAADchr2197497186SilentnovelG127G0.17
PAADchr2197498735SilentnovelA38A0.03
PAADchr2197498845Missense_MutationnovelL2F0.16
PRADchr2197495230Intronnovel0.44
PRADchr2197488474SilentNAD411D0.06
PRADchr2197489109Missense_Mutationrs768557320R370C0.45
READchr2197489157Missense_MutationNAD354N0.21
READchr2197497297Nonsense_MutationNAY90*0.18
READchr2197497073Intronnovel0.07
READchr2197488371Nonsense_MutationNAR446*0.44
READchr2197497087Intronnovel0.38
SARCchr2197488422Frame_Shift_DelnovelR429Efs*260.2
SARCchr2197493399Missense_Mutationrs149003485N265S0.18
SKCMchr2197489047SilentnovelL390L0.21
SKCMchr2197487174Missense_MutationnovelA532S0.32
SKCMchr2197489009Missense_MutationNAV403G0.34
SKCMchr2197490288Missense_MutationNAV293A0.27
SKCMchr2197493401SilentnovelA264A0.41
SKCMchr2197498739Missense_MutationNAR37Q0.05
STADchr2197495230Intronnovel0.67
STADchr2197487056In_Frame_DelnovelM568_G571del0.12
STADchr2197489074SilentNAT381T0.25
STADchr2197495230Intronnovel0.71
STADchr2197495273Intronnovel0.29
STADchr2197497281Missense_MutationNAK96E0.13
STADchr2197487193SilentnovelV525V0.15
STADchr2197495294Missense_MutationnovelQ170H0.14
STADchr2197487068In_Frame_DelnovelG567_G570del0.25
STADchr2197487917Missense_MutationNAD504N0.14
STADchr2197489140Frame_Shift_DelnovelG360Efs*190.35
STADchr2197495230Intronnovel1
THCAchr2197487065Missense_Mutationrs751438836M568T0.14
THCAchr2197493489Frame_Shift_InsnovelQ235Lfs*150.05
UCECchr2197495230Intronnovel0.27
UCECchr2197488371Nonsense_MutationNAR446*0.3
UCECchr2197497183Silentrs762474761F128F0.1
UCECchr2197489109Missense_Mutationrs768557320R370C0.39
UCECchr21974868623'UTRnovel0.27
UCECchr2197488415Missense_MutationnovelA431D0.4
UCECchr2197495177Intronnovel0.57
UCECchr2197497117Intronnovel0.2
UCECchr2197497158Missense_MutationnovelP137S0.19
UCECchr21974869103'UTRnovel0.38
UCECchr2197495230Intronnovel0.58
UCECchr2197497182Missense_Mutationrs139436185E129K0.33
UCECchr2197495256Intronnovel0.33
UCECchr2197488340Missense_MutationnovelP456L0.35
UCECchr2197497099Intronnovel0.32
UCECchr2197490236Missense_MutationnovelK310N0.22
UCECchr2197497104Intronnovel0.51
UCECchr21974869663'UTRnovel0.35
UCECchr2197495230Intronnovel0.54
UCECchr2197495230Intronnovel0.48
UCECchr2197497182Missense_Mutationrs139436185E129K0.38
UCECchr21974868613'UTRnovel0.27
UCECchr2197488320Frame_Shift_DelnovelI463Lfs*30.37
UCECchr21974868703'UTRnovel0.27
UCECchr2197497013Intronnovel0.21
UCECchr2197495230Intronnovel0.82
UCECchr2197495230Intronnovel0.26
UCECchr2197489209Silentrs780050389D336D0.13
UCECchr2197497192Missense_MutationNAK125N0.33
UCECchr2197496921Intronnovel0.64
UCECchr2197494722Nonsense_MutationNAE181*0.3
UCECchr2197487122Missense_MutationNAI549S0.44
UCECchr2197489209Silentrs780050389D336D0.41
UCECchr2197497024Intronnovel0.26
UCECchr2197494197SilentnovelD220D0.33
UCECchr2197489109Missense_Mutationrs768557320R370C0.32
UCECchr2197495230Intronnovel0.3
UCECchr21974868163'UTRnovel0.29
UCSchr2197494686Frame_Shift_InsnovelV193Sfs*170.35

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
CESCAMP0.14240.012962
PAADAMP0.07070.1091
PAADDEL0.02720.2014

Survival Analysis
CancerP-value Q-value
SARC0.0051

Kaplan-Meier Survival Analysis

MESO0.027

Kaplan-Meier Survival Analysis

ACC0.0011

Kaplan-Meier Survival Analysis

HNSC0.01

Kaplan-Meier Survival Analysis

LUSC0.03

Kaplan-Meier Survival Analysis

BRCA0.05

Kaplan-Meier Survival Analysis

ESCA0.0026

Kaplan-Meier Survival Analysis

KIRP0.00032

Kaplan-Meier Survival Analysis

PAAD0.014

Kaplan-Meier Survival Analysis

KICH0.029

Kaplan-Meier Survival Analysis

UCEC0.00014

Kaplan-Meier Survival Analysis

LIHC0.00012

Kaplan-Meier Survival Analysis

THCA0.038

Kaplan-Meier Survival Analysis

LUAD0.00067

Kaplan-Meier Survival Analysis

OV0.0098

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Pathways
  • GWAS
  • PPI
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000144381 (Gene tree)
Gene ID
3329
Gene Symbol
HSPD1
Alias
GroEL|HSP60|SPG13
Full Name
heat shock protein family D (Hsp60) member 1
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
30,157 bases
Position
chr2:197,486,581-197,516,737
Accession
5261
RBP type
non-canonical RBP
Summary
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq, Jun 2010]
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & HEK2932019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & HEK2932018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & Hela2018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & MCF10A2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & U2OS2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
27453046Comprehensive Identification of RNA-Binding Domains in Human CellsRIC & Hela2016 Aug 18Castello ADOI: 10.1016/j.molcel.2016.06.029

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
19940440Potential contributions of heat shock proteins to temperature-dependent sex determination in the American alligator.Sex Dev2010Kohno Sdoi: 10.1159/000260374
12093179Binding site analysis of human HBV pol for molecular chaperonin, hsp60.Virology2002 Jun 20Park SG-
8728645Circular assemblies.Curr Opin Struct Biol1996 AprAntson AA-
16872603Chloroplast heat shock protein Cpn60 from Chlamydomonas reinhardtii exhibits a novel function as a group II intron-specific RNA-binding protein.FEBS Lett2006 Aug 7Balczun C-
15563614Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content.Plant Physiol2004 DecSjogren LL-
27158334The GroEL protein of Porphyromonas gingivalis regulates atherogenic phenomena in endothelial cells mediated by upregulating toll-like receptor 4 expression.Am J Transl Res2016 Feb 15Huang CY-
10591847Identification of salt-regulated genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 by subtractive RNA hybridization.Arch Microbiol1999 DecVinnemeier J-
15479789Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresis.J Virol2004 NovBrasier AR-
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000430176HSPD1-206754-ENSP00000393670234 (aa)-E7ESH4
ENST00000476746HSPD1-211853--- (aa)--
ENST00000439605HSPD1-207578-ENSP0000040247883 (aa)-C9JL19
ENST00000428204HSPD1-205549-ENSP0000039646094 (aa)-C9JCQ4
ENST00000440114HSPD1-208619-ENSP0000039040448 (aa)-F8WBB1
ENST00000452200HSPD1-209888-ENSP00000412717221 (aa)-E7EXB4
ENST00000426480HSPD1-204529-ENSP00000414446175 (aa)-C9JL25
ENST00000486181HSPD1-213648--- (aa)--
ENST00000491249HSPD1-214860--- (aa)--
ENST00000482167HSPD1-212491--- (aa)--
ENST00000388968HSPD1-2022455-ENSP00000373620573 (aa)-P10809
ENST00000345042HSPD1-2012299-ENSP00000340019573 (aa)-P10809
ENST00000461097HSPD1-210714--- (aa)--
ENST00000418022HSPD1-203533-ENSP0000041222758 (aa)-C9J0S9
Gene Model
Click here to download ENSG00000144381's gene model file
Pathways
Pathway IDPathway NameSource
hsa03018RNA degradationKEGG
hsa04940Type I diabetes mellitusKEGG
hsa05134LegionellosisKEGG
hsa05152TuberculosisKEGG
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000144381rs583352662197505616GMajor depression and alcohol dependence29071344[0.19-0.49] unit increase0.341EFO_0003761|EFO_0003829
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000144381's network

* RBP PPI network refers to all genes directly bind to RBP
Orthologs identified by RBPome
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000144381HSPD110098.643ENSMUSG00000025980Hspd110098.592Mus_musculus
ENSG00000144381HSPD19259.709YLR259CHSP609456.852Saccharomyces_cerevisiae
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0001530lipopolysaccharide binding17164250.IDAFunction
GO:0002039p53 binding18086682.IPIFunction
GO:0002368B cell cytokine production16148103.IDAProcess
GO:0002755MyD88-dependent toll-like receptor signaling pathway16148103.IDAProcess
GO:0002842positive regulation of T cell mediated immune response to tumor cell10663613.IDAProcess
GO:0003688DNA replication origin binding-ISSFunction
GO:0003697single-stranded DNA binding-ISSFunction
GO:0003723RNA binding22658674.HDAFunction
GO:0003725double-stranded RNA binding21266579.IDAFunction
GO:0005515protein binding15846844.17823127.18086682.21516116.21988832.23349634.23840630.24286120.25416956.25910212.26871637.29568061.30021884.IPIFunction
GO:0005524ATP binding-IEAFunction
GO:0005615extracellular space18229457.IDAComponent
GO:0005737cytoplasm21328542.IDAComponent
GO:0005739mitochondrion21873635.IBAComponent
GO:0005739mitochondrion17823127.18086682.21245038.IDAComponent
GO:0005743mitochondrial inner membrane-ISSComponent
GO:0005759mitochondrial matrix19393246.24746669.IDAComponent
GO:0005759mitochondrial matrix17823127.TASComponent
GO:0005769early endosome11807771.IDAComponent
GO:0005829cytosol21873635.IBAComponent
GO:0005829cytosol17823127.18086682.IDAComponent
GO:0005886plasma membrane11027668.IDAComponent
GO:0005905clathrin-coated pit11807771.IDAComponent
GO:0006357regulation of transcription by RNA polymerase II-TASProcess
GO:0006458'de novo' protein folding21873635.IBAProcess
GO:0006458'de novo' protein folding-ISSProcess
GO:0006919activation of cysteine-type endopeptidase activity involved in apoptotic process17823127.IDAProcess
GO:0006986response to unfolded protein11050098.IDAProcess
GO:0007005mitochondrion organization21873635.IBAProcess
GO:0008035high-density lipoprotein particle binding11027668.IDAFunction
GO:0008637apoptotic mitochondrial changes21873635.IBAProcess
GO:0009409response to cold-ISSProcess
GO:0009986cell surface9243807.10663613.11807771.IDAComponent
GO:0016020membrane19946888.HDAComponent
GO:0016032viral process-IEAProcess
GO:0016887ATPase activity-ISSFunction
GO:0019899enzyme binding20507888.IPIFunction
GO:0030135coated vesicle11807771.IDAComponent
GO:0030141secretory granule-ISSComponent
GO:0031625ubiquitin protein ligase binding19725078.21753002.IPIFunction
GO:0032727positive regulation of interferon-alpha production17164250.IDAProcess
GO:0032729positive regulation of interferon-gamma production17164250.IDAProcess
GO:0032729positive regulation of interferon-gamma production-ISSProcess
GO:0032733positive regulation of interleukin-10 production16148103.IDAProcess
GO:0032735positive regulation of interleukin-12 production17164250.IDAProcess
GO:0032755positive regulation of interleukin-6 production16148103.IDAProcess
GO:0032991protein-containing complex21328542.23349634.IDAComponent
GO:0034185apolipoprotein binding11027668.IPIFunction
GO:0034186apolipoprotein A-I binding11027668.IPIFunction
GO:0042026protein refolding11050098.IDAProcess
GO:0042100B cell proliferation16148103.IDAProcess
GO:0042110T cell activation21873635.IBAProcess
GO:0042110T cell activation15371451.17164250.18256040.IDAProcess
GO:0042113B cell activation16148103.IDAProcess
GO:0043032positive regulation of macrophage activation17164250.IDAProcess
GO:0043065positive regulation of apoptotic process17823127.IMPProcess
GO:0043066negative regulation of apoptotic process17823127.18086682.IMPProcess
GO:0044406adhesion of symbiont to host20633027.IDAProcess
GO:0045041protein import into mitochondrial intermembrane space21873635.IBAProcess
GO:0046696lipopolysaccharide receptor complex17164250.IDAComponent
GO:0048291isotype switching to IgG isotypes16148103.IDAProcess
GO:0050821protein stabilization18086682.IMPProcess
GO:0050821protein stabilization-ISSProcess
GO:0050870positive regulation of T cell activation16148103.17164250.IDAProcess
GO:0050870positive regulation of T cell activation-ISSProcess
GO:0051082unfolded protein binding21873635.IBAFunction
GO:0051082unfolded protein binding11050098.ICFunction
GO:0051082unfolded protein binding-ISSFunction
GO:0051087chaperone binding10205158.IPIFunction
GO:0051131chaperone-mediated protein complex assembly-ISSProcess
GO:0051604protein maturation-ISSProcess
GO:0051702interaction with symbiont20507888.IMPProcess
GO:0070062extracellular exosome19056867.20458337.HDAComponent
GO:0070062extracellular exosome21276792.IDAComponent
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