GRPE1_HUMAN - dbPTM
GRPE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRPE1_HUMAN
UniProt AC Q9HAV7
Protein Name GrpE protein homolog 1, mitochondrial
Gene Name GRPEL1
Organism Homo sapiens (Human).
Sequence Length 217
Subcellular Localization Mitochondrion matrix .
Protein Description Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (By similarity). Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. [PubMed: 11311562]
Protein Sequence MAAQCVRLARRSLPALALSLRPSPRLLCTATKQKNSGQNLEEDMGQSEQKADPPATEKTLLEEKVKLEEQLKETVEKYKRALADTENLRQRSQKLVEEAKLYGIQAFCKDLLEVADVLEKATQCVPKEEIKDDNPHLKNLYEGLVMTEVQIQKVFTKHGLLKLNPVGAKFDPYEHEALFHTPVEGKEPGTVALVSKVGYKLHGRTLRPALVGVVKEA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
19PhosphorylationSLPALALSLRPSPRL
HCCHHHHHCCCCCCE		19.4124719451
23PhosphorylationLALSLRPSPRLLCTA
HHHHCCCCCCEEEEE		19.0730301811
44SulfoxidationGQNLEEDMGQSEQKA
CCCHHHHHCCCHHHC		6.2728465586
47PhosphorylationLEEDMGQSEQKADPP
HHHHHCCCHHHCCCC		35.9420068231
50UbiquitinationDMGQSEQKADPPATE
HHCCCHHHCCCCCCH		51.1823503661
50AcetylationDMGQSEQKADPPATE
HHCCCHHHCCCCCCH		51.1826051181
64UbiquitinationEKTLLEEKVKLEEQL
HHHHHHHHHHHHHHH		34.9829967540
64AcetylationEKTLLEEKVKLEEQL
HHHHHHHHHHHHHHH		34.9825953088
64MalonylationEKTLLEEKVKLEEQL
HHHHHHHHHHHHHHH		34.9832601280
66AcetylationTLLEEKVKLEEQLKE
HHHHHHHHHHHHHHH		62.3423749302
66UbiquitinationTLLEEKVKLEEQLKE
HHHHHHHHHHHHHHH		62.3423503661
72UbiquitinationVKLEEQLKETVEKYK
HHHHHHHHHHHHHHH		51.5423503661
72AcetylationVKLEEQLKETVEKYK
HHHHHHHHHHHHHHH		51.5425953088
72SuccinylationVKLEEQLKETVEKYK
HHHHHHHHHHHHHHH		51.5423954790
77UbiquitinationQLKETVEKYKRALAD
HHHHHHHHHHHHHHC		52.3023503661
77AcetylationQLKETVEKYKRALAD
HHHHHHHHHHHHHHC		52.3025953088
94AcetylationNLRQRSQKLVEEAKL
HHHHHHHHHHHHHHH		56.6023749302
94MalonylationNLRQRSQKLVEEAKL
HHHHHHHHHHHHHHH		56.6032601280
94SuccinylationNLRQRSQKLVEEAKL
HHHHHHHHHHHHHHH		56.6027452117
94SuccinylationNLRQRSQKLVEEAKL
HHHHHHHHHHHHHHH		56.60-
100SuccinylationQKLVEEAKLYGIQAF
HHHHHHHHHHHHHHH		45.5923954790
100AcetylationQKLVEEAKLYGIQAF
HHHHHHHHHHHHHHH		45.5925953088
102PhosphorylationLVEEAKLYGIQAFCK
HHHHHHHHHHHHHHH		16.1028152594
120SuccinylationEVADVLEKATQCVPK
HHHHHHHHHHCCCCH		53.20-
120AcetylationEVADVLEKATQCVPK
HHHHHHHHHHCCCCH		53.2026051181
120SuccinylationEVADVLEKATQCVPK
HHHHHHHHHHCCCCH		53.20-
124GlutathionylationVLEKATQCVPKEEIK
HHHHHHCCCCHHHHC		5.0022555962
127AcetylationKATQCVPKEEIKDDN
HHHCCCCHHHHCCCC		47.8126822725
157AcetylationQIQKVFTKHGLLKLN
HHHHHHHHCCCEEEC		24.9823749302
157SuccinylationQIQKVFTKHGLLKLN
HHHHHHHHCCCEEEC		24.9827452117
162AcetylationFTKHGLLKLNPVGAK
HHHCCCEEECCCCCC		51.7925825284
169UbiquitinationKLNPVGAKFDPYEHE
EECCCCCCCCCCCCE		44.3529967540
169AcetylationKLNPVGAKFDPYEHE
EECCCCCCCCCCCCE		44.3525953088
173PhosphorylationVGAKFDPYEHEALFH
CCCCCCCCCCEECCC		31.5928152594
181PhosphorylationEHEALFHTPVEGKEP
CCEECCCCCCCCCCC		22.9928152594
186MalonylationFHTPVEGKEPGTVAL
CCCCCCCCCCCCEEE		47.4332601280
186AcetylationFHTPVEGKEPGTVAL
CCCCCCCCCCCCEEE		47.4325953088
195PhosphorylationPGTVALVSKVGYKLH
CCCEEEEEECCCEEC		23.6020068231
200AcetylationLVSKVGYKLHGRTLR
EEEECCCEECCCCCC		28.2527452117
205PhosphorylationGYKLHGRTLRPALVG
CCEECCCCCCHHHHH		31.5420068231
215AcetylationPALVGVVKEA-----
HHHHHHHCCC-----		45.5819608861
215SuccinylationPALVGVVKEA-----
HHHHHHHCCC-----		45.58-
215SuccinylationPALVGVVKEA-----
HHHHHHHCCC-----		45.58-
215UbiquitinationPALVGVVKEA-----
HHHHHHHCCC-----		45.5824816145
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GRPE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRPE1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GRPE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRPE1_HUMANGRPEL1physical
23345595
CCAR1_HUMANCCAR1physical
26186194
PALLD_HUMANPALLDphysical
26186194
GRPE2_HUMANGRPEL2physical
26186194
AHNK_HUMANAHNAKphysical
26344197
DNJA4_HUMANDNAJA4physical
26344197
DNJB1_HUMANDNAJB1physical
26344197
DNJB4_HUMANDNAJB4physical
26344197
DNJC3_HUMANDNAJC3physical
26344197
DUT_HUMANDUTphysical
26344197
HSP72_HUMANHSPA2physical
26344197
HSP74_HUMANHSPA4physical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
HSP7C_HUMANHSPA8physical
26344197
HS105_HUMANHSPH1physical
26344197
ITPA_HUMANITPAphysical
26344197
MDHM_HUMANMDH2physical
26344197
STIP1_HUMANSTIP1physical
26344197
STMN1_HUMANSTMN1physical
26344197
TIM44_HUMANTIMM44physical
26344197
PALLD_HUMANPALLDphysical
28514442
GRP75_HUMANHSPA9physical
28514442
GRPE2_HUMANGRPEL2physical
28514442
TPPP_HUMANTPPPphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRPE1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-157 AND LYS-215, AND MASSSPECTROMETRY.

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