Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  10 kDa heat shock protein, mitochondrial  

UniProtKB / Swiss-Prot ID :  CH10_HUMAN

Gene Name (Synonyms) : 
HSPE1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion matrix. 

Protein Function :  Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. 

Protein Sequence MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDK...
Predicted Secondary Structure CCCCCEEEEEECCCEEEEEEECCCEEECCCEEECCCCCCCCCEEEEEEECCCEECCCCCEEEEEECCCCE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAGQAF
---CCCCCE
20.85UniProtKB
Link-
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QAFRKFLPL
CCEEEEEEC
44.81Phosphositeplus
Link-
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETVTKGGIM
CEEECCCEE
51.29Phosphositeplus
Link-
40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSQGKVLQA
CCCCCCCEE
31.94Phosphositeplus
Link-
40N6-acetyllysineKSQGKVLQA
CCCCCCCEE
31.94Phosphositeplus
Link-
40N6-malonyllysine.KSQGKVLQA
CCCCCCCEE
31.94UniProtKB
Link-
51PhosphoserineVAVGSGSKG
EEECCCEEC
33.04HPRD
Link-
51PhosphoserineVAVGSGSKG
EEECCCEEC
33.04Phosphositeplus
Link-
54N6-malonyllysine.GSGSKGKGG
CCCEECCCC
69.07UniProtKB
Link-
56N6-acetyllysineGSKGKGGEI
CEECCCCCE
68.43HPRD
Link-
56N6-acetyllysineGSKGKGGEI
CEECCCCCE
68.43Phosphositeplus
Link-
56N6-acetyllysine; alternate.GSKGKGGEI
CEECCCCCE
68.43UniProtKB
Link-
56N6-malonyllysine; alternate.GSKGKGGEI
CEECCCCCE
68.43UniProtKB
Link-
64PhosphoserineIQPVSVKVG
EEEEEECCC
23.93HPRD
Link-
64PhosphoserineIQPVSVKVG
EEEEEECCC
23.93Phosphositeplus
Link-
70N6-acetyllysineKVGDKVLLP
CCCCEEEEC
28.93HPRD
Link-
70N6-acetyllysineKVGDKVLLP
CCCCEEEEC
28.93Phosphositeplus
Link-
70N6-acetyllysine.KVGDKVLLP
CCCCEEEEC
28.93UniProtKB
Link-
76PhosphotyrosineLLPEYGGTK
EECCCCCEE
20.93Phosphositeplus
Link-
76Phosphotyrosine.LLPEYGGTK
EECCCCCEE
20.93UniProtKB
Link-
79PhosphothreonineEYGGTKVVL
CCCCEEEEE
19.12HPRD
Link-
79PhosphothreonineEYGGTKVVL
CCCCEEEEE
19.12Phosphositeplus
Link-
86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLDDKDYFL
EECCEEEEE
54.73Phosphositeplus
Link-
86N6-acetyllysineVLDDKDYFL
EECCEEEEE
54.73HPRD
Link-
86N6-acetyllysineVLDDKDYFL
EECCEEEEE
54.73Phosphositeplus
Link-
86N6-acetyllysine.VLDDKDYFL
EECCEEEEE
54.73UniProtKB
Link-
88PhosphotyrosineDDKDYFLFR
CCEEEEEEE
14.12HPRD
Link-
88PhosphotyrosineDDKDYFLFR
CCEEEEEEE
14.12PhosphoELM
Link-
88PhosphotyrosineDDKDYFLFR
CCEEEEEEE
14.12Phosphositeplus
Link-
88Phosphotyrosine.DDKDYFLFR
CCEEEEEEE
14.12UniProtKB
Link-
99N6-acetyllysineDILGKYVD
CEEEEEEC
38.36HPRD
Link-
99N6-acetyllysineDILGKYVD
CEEEEEEC
38.36Phosphositeplus
Link-
99N6-acetyllysine.DILGKYVD
CEEEEEEC
38.36UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TLE1_HUMANphysical interactionMINT-63940MINT16169070
UN119_HUMANphysical interactionMINT-63941MINT16169070
DPYL1_HUMANphysical interactionMINT-63942MINT16169070
Q5JR01_HUMANphysical interactionMINT-63943MINT16169070
CA103_HUMANphysical interactionMINT-63945MINT16169070
DPYL1_HUMANphysical interactionEBI-728976
intact16169070
RIF1_HUMANphysical interactionEBI-728979
intact16169070
TLE1_HUMANphysical interactionEBI-728982
intact16169070
UN119_HUMANphysical interactionEBI-728985
intact16169070
APLP1_HUMANphysical interactionEBI-730195
intact16169070
ZHX1_HUMANphysical interactionEBI-730198
intact16169070
ERG28_HUMANphysical interactionEBI-728531
intact16169070
EF1A1_HUMANphysical interactionEBI-728534
intact16169070
GBP2_HUMANphysical interactionEBI-732205
intact16169070
ALDH2_HUMANyeast 2-hybridHPRD:02535HPRD12387818
CH60_HUMANin vivo
yeast 2-hybrid
HPRD:02535HPRD11050098
10205158
12387818
TLE1_HUMANyeast 2-hybridHPRD:02535HPRD16169070
DPYL1_HUMANyeast 2-hybridHPRD:02535HPRD16169070
UN119_HUMANyeast 2-hybridHPRD:02535HPRD16169070
ERG28_HUMANyeast 2-hybridHPRD:02535HPRD16169070
ZHX1_HUMANyeast 2-hybridHPRD:02535HPRD16169070
CA103_HUMANyeast 2-hybridHPRD:02535HPRD16169070
CH60_HUMANENSP00000233893STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-86 ANDLYS-99, AND MASS SPECTROMETRY.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-40; LYS-54 AND LYS-56.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures