MIEAP_HUMAN - dbPTM
MIEAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIEAP_HUMAN
UniProt AC Q8TC71
Protein Name Mitochondria-eating protein
Gene Name SPATA18
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization Cytoplasm . Mitochondrion outer membrane . Localizes to the cytoplasm under normal conditions (PubMed:21264228). Relocalizes to mitochondrion outer membrane following cellular stress. Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer membr
Protein Description Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix..
Protein Sequence MAENLKRLVSNETLRTLQEKLDFWLKEYNTNTCDQNLNHCLELIEQVAKVQGQLFGILTAAAQEGGRNDGVETIKSRLLPWLEASFTAASLGKSVDSKVPSLQDTFDRERHKDPSPRDRDMQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEPWSLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQGRSSRSRSPSPAPRSRSCSRSRSASPSTAVKVRRPSPNRSKLSNVARKAALLSRFSDSYSQARLDAQCLLRRCIDKAETVQRIIYIATVEAFHVAKMAFRHFKIHVRKSLTPSYVGSNDFENAVLDYVICHLDLYDSQSSVNDVIRAMNVNPKISFPPVVDFCLLSDFIQEICCIAFAMQALEPPLDIAYGADGEVFNDCKYRRSYDSDFTAPLVLYHVWPALMENDCVIMKGEAVTRRGAFWNSVRSVSRCRSRSLSPICPRSQIGLNTMSRSRSPSPIRCGLPRF
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
10PhosphorylationENLKRLVSNETLRTL
HHHHHHHCHHHHHHH		33.2730622161
20AcetylationTLRTLQEKLDFWLKE
HHHHHHHHHHHHHHH		40.1625038526
85PhosphorylationLLPWLEASFTAASLG
HHHHHHHHHHHHHCC		17.4730622161
87PhosphorylationPWLEASFTAASLGKS
HHHHHHHHHHHCCCC		20.8630622161
90PhosphorylationEASFTAASLGKSVDS
HHHHHHHHCCCCCCC		34.8830622161
94PhosphorylationTAASLGKSVDSKVPS
HHHHCCCCCCCCCCC		29.3825693802
97PhosphorylationSLGKSVDSKVPSLQD
HCCCCCCCCCCCHHH		33.1430622161
101PhosphorylationSVDSKVPSLQDTFDR
CCCCCCCCHHHHHCH		41.4727966365
105PhosphorylationKVPSLQDTFDRERHK
CCCCHHHHHCHHHCC		17.9330622161
133 (in isoform 2)Phosphorylation-38.8930622161
133PhosphorylationSNLNSTRSQCNQVQD
HHHHHHHHHHHHHHH		38.8930622161
144 (in isoform 2)Phosphorylation-59.5525693802
145PhosphorylationVQDDLVETEKNLEES
HHHHHHHHHHHHHHH		44.7928787133
156PhosphorylationLEESKNRSAISLLAA
HHHHCCHHHHHHHHH		39.0730622161
159PhosphorylationSKNRSAISLLAAEEE
HCCHHHHHHHHHHHH		19.6330622161
171UbiquitinationEEEINQLKKQLKSLQ
HHHHHHHHHHHHHHH		28.80-
198PhosphorylationRSSENRRSEPWSLEE
HCCCCCCCCCCCHHH		44.7823403867
202PhosphorylationNRRSEPWSLEERKRE
CCCCCCCCHHHHHHH		36.3023403867
213PhosphorylationRKREQWNSLKQNADQ
HHHHHHHHHHHCHHH		33.7024719451
223PhosphorylationQNADQQDTEAMSDYK
HCHHHHHHHHHHHHH		22.7029978859
227PhosphorylationQQDTEAMSDYKKQLR
HHHHHHHHHHHHHHH		44.8530622161
229PhosphorylationDTEAMSDYKKQLRNL
HHHHHHHHHHHHHHH		16.8729978859
244PhosphorylationKEEIAVLSAEKSALQ
HHHHHHHHHHHHHHC		27.9925693802
254PhosphorylationKSALQGRSSRSRSPS
HHHHCCCCCCCCCCC		36.6130631047
255PhosphorylationSALQGRSSRSRSPSP
HHHCCCCCCCCCCCC		32.6830631047
257PhosphorylationLQGRSSRSRSPSPAP
HCCCCCCCCCCCCCC		38.7726699800
259PhosphorylationGRSSRSRSPSPAPRS
CCCCCCCCCCCCCCC		30.8626699800
261PhosphorylationSSRSRSPSPAPRSRS
CCCCCCCCCCCCCCC		34.6326699800
266PhosphorylationSPSPAPRSRSCSRSR
CCCCCCCCCCCCCCC		27.7323532336
268PhosphorylationSPAPRSRSCSRSRSA
CCCCCCCCCCCCCCC		20.0730622161
270PhosphorylationAPRSRSCSRSRSASP
CCCCCCCCCCCCCCC		34.2430622161
272PhosphorylationRSRSCSRSRSASPST
CCCCCCCCCCCCCCC		17.8130622161
274PhosphorylationRSCSRSRSASPSTAV
CCCCCCCCCCCCCCE		34.0526657352
276PhosphorylationCSRSRSASPSTAVKV
CCCCCCCCCCCCEEE		22.1925849741
278PhosphorylationRSRSASPSTAVKVRR
CCCCCCCCCCEEECC		26.8823403867
279PhosphorylationSRSASPSTAVKVRRP
CCCCCCCCCEEECCC		38.5623403867
287PhosphorylationAVKVRRPSPNRSKLS
CEEECCCCCCHHHHH		32.7526699800
496PhosphorylationRRGAFWNSVRSVSRC
CCCHHHHHHHHHHHH		14.9828857561
499PhosphorylationAFWNSVRSVSRCRSR
HHHHHHHHHHHHHCC		23.4530622161
501PhosphorylationWNSVRSVSRCRSRSL
HHHHHHHHHHHCCCC		27.2330622161
505PhosphorylationRSVSRCRSRSLSPIC
HHHHHHHCCCCCCCC		29.8226657352
507PhosphorylationVSRCRSRSLSPICPR
HHHHHCCCCCCCCCH		34.1523927012
509PhosphorylationRCRSRSLSPICPRSQ
HHHCCCCCCCCCHHH		17.2923927012
515PhosphorylationLSPICPRSQIGLNTM
CCCCCCHHHHCCCCC		15.9930622161
521PhosphorylationRSQIGLNTMSRSRSP
HHHHCCCCCCCCCCC		22.9030622161
523PhosphorylationQIGLNTMSRSRSPSP
HHCCCCCCCCCCCCC		25.6830622161
525PhosphorylationGLNTMSRSRSPSPIR
CCCCCCCCCCCCCCC		29.7820363803
527PhosphorylationNTMSRSRSPSPIRCG
CCCCCCCCCCCCCCC		30.8620363803
529PhosphorylationMSRSRSPSPIRCGLP
CCCCCCCCCCCCCCC		33.9220363803
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 MIEAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIEAP_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 MIEAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MIEAP_HUMAN !!
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 MIEAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525 AND SER-527, ANDMASS SPECTROMETRY.

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