UCP2_HUMAN - dbPTM
UCP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UCP2_HUMAN
UniProt AC P55851
Protein Name Mitochondrial uncoupling protein 2
Gene Name UCP2
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat..
Protein Sequence MVGFKATDVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGESQGPVRATASAQYRGVMGTILTMVRTEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKQFYTKGSEHASIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYQSTVNAYKTIAREEGFRGLWKGTSPNVARNAIVNCAELVTYDLIKDALLKANLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSALGQYSSAGHCALTMLQKEGPRAFYKGFMPSFLRLGSWNVVMFVTYEQLKRALMAACTSREAPF
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
14PhosphorylationTDVPPTATVKFLGAG
CCCCCCCEEEECCCH
27.06-
36PhosphorylationLITFPLDTAKVRLQI
HHCCCCCCCEEEEEE
35.7424425749
54PhosphorylationSQGPVRATASAQYRG
CCCCEEEEEEEHHHH
15.5829759185
56PhosphorylationGPVRATASAQYRGVM
CCEEEEEEEHHHHCH
16.1429759185
59PhosphorylationRATASAQYRGVMGTI
EEEEEEHHHHCHHHH
14.7329759185
65PhosphorylationQYRGVMGTILTMVRT
HHHHCHHHHEEEEEC
8.5029759185
72PhosphorylationTILTMVRTEGPRSLY
HHEEEEECCCCHHHH
33.61-
77PhosphorylationVRTEGPRSLYNGLVA
EECCCCHHHHHHHHH
38.0422496350
79PhosphorylationTEGPRSLYNGLVAGL
CCCCHHHHHHHHHHH
14.3924719451
94PhosphorylationQRQMSFASVRIGLYD
HHCCCCHHHEEECHH
15.2124719451
158PhosphorylationGGGRRYQSTVNAYKT
CCCCCCHHHHHHHHH
25.95-
163PhosphorylationYQSTVNAYKTIAREE
CHHHHHHHHHHHHHH
11.94-
165PhosphorylationSTVNAYKTIAREEGF
HHHHHHHHHHHHHCC
13.75-
179PhosphorylationFRGLWKGTSPNVARN
CCCCCCCCCHHHHHH
36.97-
180PhosphorylationRGLWKGTSPNVARNA
CCCCCCCCHHHHHHH
24.12-
229PhosphorylationFGAGFCTTVIASPVD
CCCCCCEEEEECCHH
15.88-
233PhosphorylationFCTTVIASPVDVVKT
CCEEEEECCHHHHHH
17.84-

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 UCP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UCP2_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 UCP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433B_HUMANYWHABphysical
10785390
1433Z_HUMANYWHAZphysical
10785390
1433T_HUMANYWHAQphysical
10785390
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ANXA1_HUMANANXA1physical
26186194
ZG16B_HUMANZG16Bphysical
26186194
CYTS_HUMANCST4physical
26186194
CYTT_HUMANCST2physical
26186194
FILA_HUMANFLGphysical
26186194
SPB4_HUMANSERPINB4physical
26186194
AL3A1_HUMANALDH3A1physical
26186194
MUC7_HUMANMUC7physical
26186194
HUTH_HUMANHALphysical
26186194
PIGR_HUMANPIGRphysical
26186194
CRNN_HUMANCRNNphysical
26186194
MUC7_HUMANMUC7physical
28514442
CYTT_HUMANCST2physical
28514442
CYTS_HUMANCST4physical
28514442
CRNN_HUMANCRNNphysical
28514442
ZG16B_HUMANZG16Bphysical
28514442
PIGR_HUMANPIGRphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
SPB3_HUMANSERPINB3physical
28514442
FILA_HUMANFLGphysical
28514442
FBX50_HUMANNCCRP1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UCP2_HUMAN

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Related Literatures of Post-Translational Modification

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