SODM_HUMAN - dbPTM
SODM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SODM_HUMAN
UniProt AC P04179
Protein Name Superoxide dismutase [Mn], mitochondrial
Gene Name SOD2
Organism Homo sapiens (Human).
Sequence Length 222
Subcellular Localization Mitochondrion matrix.
Protein Description Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems..
Protein Sequence MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
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
3Phosphorylation-----MLSRAVCGTS
-----CCCCCCCCCH		19.5222210691
19PhosphorylationQLAPVLGYLGSRQKH
HHHHHHHHHCCCCCC		14.5622210691
22AcetylationPVLGYLGSRQKHSLP
HHHHHHCCCCCCCCC		29.01-
53AcetylationIMQLHHSKHHAAYVN
HHHHHHCHHHHCHHC		34.7466699259
58Nitrated tyrosineHSKHHAAYVNNLNVT
HCHHHHCHHCCCCCC		12.42-
58NitrationHSKHHAAYVNNLNVT
HCHHHHCHHCCCCCC		12.4210334867
58NitrationHSKHHAAYVNNLNVT
HCHHHHCHHCCCCCC		12.4210334867
58PhosphorylationHSKHHAAYVNNLNVT
HCHHHHCHHCCCCCC		12.4228857561
68AcetylationNLNVTEEKYQEALAK
CCCCCHHHHHHHHHC		46.1019608861
68MalonylationNLNVTEEKYQEALAK
CCCCCHHHHHHHHHC		46.1026320211
68SuccinylationNLNVTEEKYQEALAK
CCCCCHHHHHHHHHC		46.1027452117
68SuccinylationNLNVTEEKYQEALAK
CCCCCHHHHHHHHHC		46.10-
69Nitrated tyrosineLNVTEEKYQEALAKG
CCCCHHHHHHHHHCC		18.18-
69NitrationLNVTEEKYQEALAKG
CCCCHHHHHHHHHCC		18.18-
75AcetylationKYQEALAKGDVTAQI
HHHHHHHCCCCHHEE		57.4025038526
75MalonylationKYQEALAKGDVTAQI
HHHHHHHCCCCHHEE		57.4032601280
75SuccinylationKYQEALAKGDVTAQI
HHHHHHHCCCCHHEE		57.40-
75SuccinylationKYQEALAKGDVTAQI
HHHHHHHCCCCHHEE		57.40-
76AcetylationYQEALAKGDVTAQIA
HHHHHHCCCCHHEEE		29.07-
79PhosphorylationALAKGDVTAQIALQP
HHHCCCCHHEEEEEE		19.9928857561
84UbiquitinationDVTAQIALQPALKFN
CCHHEEEEEEHHHCC		7.19-
84AcetylationDVTAQIALQPALKFN
CCHHEEEEEEHHHCC		7.19-
91UbiquitinationLQPALKFNGGGHINH
EEEHHHCCCCCCCCC		46.7621890473
91AcetylationLQPALKFNGGGHINH
EEEHHHCCCCCCCCC		46.7619608861
91UbiquitinationLQPALKFNGGGHINH
EEEHHHCCCCCCCCC		46.7619608861
106PhosphorylationSIFWTNLSPNGGGEP
EEEEECCCCCCCCCC		20.56-
114AcetylationPNGGGEPKGELLEAI
CCCCCCCCHHHHHHH		61.79-
122UbiquitinationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.62-
122AcetylationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.6223236377
122SuccinylationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.62-
122SuccinylationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.6227452117
122MalonylationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.6226320211
1222-HydroxyisobutyrylationGELLEAIKRDFGSFD
HHHHHHHHHHHCCHH		53.62-
127PhosphorylationAIKRDFGSFDKFKEK
HHHHHHCCHHHHHHH		30.2028857561
130MalonylationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.2226320211
130UbiquitinationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.2221890473
130MethylationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.2214496159
130SuccinylationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.22-
130AcetylationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.2219608861
130SuccinylationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.22-
130UbiquitinationRDFGSFDKFKEKLTA
HHHCCHHHHHHHHHH		57.2221890473
132AcetylationFGSFDKFKEKLTAAS
HCCHHHHHHHHHHCE		60.7325038526
132MalonylationFGSFDKFKEKLTAAS
HCCHHHHHHHHHHCE		60.7326320211
200PhosphorylationYKNVRPDYLKAIWNV
CCCCCHHHHHHHHHH		16.8828152594
202AcetylationNVRPDYLKAIWNVIN
CCCHHHHHHHHHHHC		31.4325038526
217NitrationWENVTERYMACKK--
CCCHHHHHHHCCC--		5.26-
217Nitrated tyrosineWENVTERYMACKK--
CCCHHHHHHHCCC--		5.26-
221AcetylationTERYMACKK------
HHHHHHCCC------		52.566568103
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
79TPhosphorylationKinaseMAPK11Q15759
GPS
106SPhosphorylationKinaseCDK1P06493
PSP
106SPhosphorylationKinaseCDK4P11802
PSP
106SPhosphorylationKinaseMAPK11Q15759
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
122KAcetylation

-
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 SODM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP36_HUMANUSP36physical
21268071
A4_HUMANAPPphysical
21832049
VAPA_HUMANVAPAphysical
22939629
SSDH_HUMANALDH5A1physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
SOSB1_HUMANNABP2physical
22939629
TBL2_HUMANTBL2physical
22939629
STX7_HUMANSTX7physical
22939629
SODM_HUMANSOD2physical
21988832
UBR2_HUMANUBR2physical
26186194
GABT_HUMANABATphysical
26344197
ACON_HUMANACO2physical
26344197
AL1B1_HUMANALDH1B1physical
26344197
ALDH2_HUMANALDH2physical
26344197
AL4A1_HUMANALDH4A1physical
26344197
CATA_HUMANCATphysical
26344197
ENOB_HUMANENO3physical
26344197
FUMH_HUMANFHphysical
26344197
GPX4_HUMANGPX4physical
26344197
CH10_HUMANHSPE1physical
26344197
MDHC_HUMANMDH1physical
26344197
PEBP1_HUMANPEBP1physical
26344197
PEPD_HUMANPEPDphysical
26344197
PRDX5_HUMANPRDX5physical
26344197
TPIS_HUMANTPI1physical
26344197
UCHL3_HUMANUCHL3physical
26344197
UBR2_HUMANUBR2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612634Microvascular complications of diabetes 6 (MVCD6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SODM_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-68 AND LYS-130, AND MASSSPECTROMETRY.
Nitration
ReferencePubMed
"Detection of sequence-specific tyrosine nitration of manganese SODand SERCA in cardiovascular disease and aging.";
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H.,Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.;
Am. J. Physiol. 290:H2220-H2227(2006).
Cited for: NITRATION AT TYR-58.

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