STML2_HUMAN - dbPTM
STML2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STML2_HUMAN
UniProt AC Q9UJZ1
Protein Name Stomatin-like protein 2, mitochondrial
Gene Name STOML2
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Cell membrane
Peripheral membrane protein . Mitochondrion . Mitochondrion inner membrane
Lipid-anchor . Mitochondrion intermembrane space . Membrane raft . Cytoplasm, cytoskeleton . Behaves as an integral membrane protein of the mitochondrion des
Protein Description Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation..
Protein Sequence MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTKAPVPGTPDSLSSGSSRDVQGTDASLDEELDRVKMS
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
9PhosphorylationLARAARGTGALLLRG
CHHHCCCCCCEEECH		17.4630108239
17PhosphorylationGALLLRGSLLASGRA
CCEEECHHHHHCCCC		17.4930108239
21PhosphorylationLRGSLLASGRAPRRA
ECHHHHHCCCCCCCC		28.8730108239
29PhosphorylationGRAPRRASSGLPRNT
CCCCCCCCCCCCCCE		24.1123312004
30PhosphorylationRAPRRASSGLPRNTV
CCCCCCCCCCCCCEE		43.2823312004
36PhosphorylationSSGLPRNTVVLFVPQ
CCCCCCCEEEEEEEH		17.1727174698
74MethylationIPVLDRIRYVQSLKE
HHHHHHHHHHHHHHH		26.85115917137
94UbiquitinationPEQSAVTLDNVTLQI
CCCCCEEECCEEEEE		3.4719608861
94AcetylationPEQSAVTLDNVTLQI
CCCCCEEECCEEEEE		3.4719608861
114AcetylationLRIMDPYKASYGVED
EEECCCCHHHCCCCC		35.9223236377
114UbiquitinationLRIMDPYKASYGVED
EEECCCCHHHCCCCC		35.9221890473
114UbiquitinationLRIMDPYKASYGVED
EEECCCCHHHCCCCC		35.9221890473
114AcetylationLRIMDPYKASYGVED
EEECCCCHHHCCCCC		35.92-
124PhosphorylationYGVEDPEYAVTQLAQ
CCCCCHHHHHHHHHH		16.2622817900
140AcetylationTMRSELGKLSLDKVF
HHHHHHHHHCHHHHH		47.7523236377
140AcetylationTMRSELGKLSLDKVF
HHHHHHHHHCHHHHH		47.75-
140UbiquitinationTMRSELGKLSLDKVF
HHHHHHHHHCHHHHH		47.7521890473
140UbiquitinationTMRSELGKLSLDKVF
HHHHHHHHHCHHHHH		47.7521890473
142PhosphorylationRSELGKLSLDKVFRE
HHHHHHHCHHHHHHH		37.7024719451
145AcetylationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.87-
1452-HydroxyisobutyrylationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.87-
145UbiquitinationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.87-
145SuccinylationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.8727452117
145AcetylationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.8719608861
145SuccinylationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.87-
145UbiquitinationLGKLSLDKVFRERES
HHHHCHHHHHHHHHH		48.8721890473
177UbiquitinationIRCLRYEIKDIHVPP
CEEEEEEEEECCCCH		3.44-
182AcetylationYEIKDIHVPPRVKES
EEEEECCCCHHHHHH		7.7319608861
187AcetylationIHVPPRVKESMQMQV
CCCCHHHHHHHHHHH		45.4025038526
187MalonylationIHVPPRVKESMQMQV
CCCCHHHHHHHHHHH		45.4026320211
188AcetylationHVPPRVKESMQMQVE
CCCHHHHHHHHHHHH		48.8919608861
188AcetylationHVPPRVKESMQMQVE
CCCHHHHHHHHHHHH		48.89-
190SulfoxidationPPRVKESMQMQVEAE
CHHHHHHHHHHHHHH		3.9521406390
205UbiquitinationRRKRATVLESEGTRE
HHHHHEEHHCCCCHH		5.3521890473
207UbiquitinationKRATVLESEGTRESA
HHHEEHHCCCCHHHH		36.85-
207PhosphorylationKRATVLESEGTRESA
HHHEEHHCCCCHHHH		36.85-
221AcetylationAINVAEGKKQAQILA
HHHHHHHHHHHHHHH		32.9725953088
221SuccinylationAINVAEGKKQAQILA
HHHHHHHHHHHHHHH		32.9727452117
221MalonylationAINVAEGKKQAQILA
HHHHHHHHHHHHHHH		32.9726320211
222SuccinylationINVAEGKKQAQILAS
HHHHHHHHHHHHHHH		62.8227452117
222AcetylationINVAEGKKQAQILAS
HHHHHHHHHHHHHHH		62.8226051181
2222-HydroxyisobutyrylationINVAEGKKQAQILAS
HHHHHHHHHHHHHHH		62.82-
222UbiquitinationINVAEGKKQAQILAS
HHHHHHHHHHHHHHH		62.82-
222MalonylationINVAEGKKQAQILAS
HHHHHHHHHHHHHHH		62.8226320211
229PhosphorylationKQAQILASEAEKAEQ
HHHHHHHHHHHHHHH		33.6220068231
233AcetylationILASEAEKAEQINQA
HHHHHHHHHHHHHHH		65.3619608861
233MalonylationILASEAEKAEQINQA
HHHHHHHHHHHHHHH		65.3626320211
2502-HydroxyisobutyrylationEASAVLAKAKAKAEA
HHHHHHHHHHHHHHH		46.38-
250MalonylationEASAVLAKAKAKAEA
HHHHHHHHHHHHHHH		46.3826320211
250AcetylationEASAVLAKAKAKAEA
HHHHHHHHHHHHHHH		46.3825953088
250UbiquitinationEASAVLAKAKAKAEA
HHHHHHHHHHHHHHH		46.38-
252UbiquitinationSAVLAKAKAKAEAIR
HHHHHHHHHHHHHHH		50.11-
287PhosphorylationEQYVSAFSKLAKDSN
HHHHHHHHHHHCCCC		26.8624275569
293PhosphorylationFSKLAKDSNTILLPS
HHHHHCCCCEEECCC		34.8628985074
295PhosphorylationKLAKDSNTILLPSNP
HHHCCCCEEECCCCC		19.5628985074
300PhosphorylationSNTILLPSNPGDVTS
CCEEECCCCCCHHHH		56.47-
306PhosphorylationPSNPGDVTSMVAQAM
CCCCCHHHHHHHHHH		18.82-
307PhosphorylationSNPGDVTSMVAQAMG
CCCCHHHHHHHHHHC		15.88-
308SulfoxidationNPGDVTSMVAQAMGV
CCCHHHHHHHHHHCH		1.8028465586
316PhosphorylationVAQAMGVYGALTKAP
HHHHHCHHHCHHCCC		7.3128985074
327PhosphorylationTKAPVPGTPDSLSSG
HCCCCCCCCCCCCCC		20.1829255136
330PhosphorylationPVPGTPDSLSSGSSR
CCCCCCCCCCCCCCC		31.2130266825
332PhosphorylationPGTPDSLSSGSSRDV
CCCCCCCCCCCCCCC		36.2830266825
333PhosphorylationGTPDSLSSGSSRDVQ
CCCCCCCCCCCCCCC		48.2430266825
335PhosphorylationPDSLSSGSSRDVQGT
CCCCCCCCCCCCCCC		24.9330266825
336PhosphorylationDSLSSGSSRDVQGTD
CCCCCCCCCCCCCCC		35.7030266825
342PhosphorylationSSRDVQGTDASLDEE
CCCCCCCCCCCHHHH		15.9925849741
345PhosphorylationDVQGTDASLDEELDR
CCCCCCCCHHHHHHH		38.8830266825
356PhosphorylationELDRVKMS-------
HHHHHCCC-------		31.2123898821
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
17SPhosphorylationKinasePKCZQ05513
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
17SPhosphorylation

21791414
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 STML2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RM40_HUMANMRPL40physical
26344197
PHB_HUMANPHBphysical
26344197
PHB2_HUMANPHB2physical
26344197
QCR8_HUMANUQCRQphysical
26344197
STOM_HUMANSTOMphysical
27173435
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 STML2_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-145 AND LYS-233, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASSSPECTROMETRY.

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