GPS2_HUMAN - dbPTM
GPS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPS2_HUMAN
UniProt AC Q13227
Protein Name G protein pathway suppressor 2 {ECO:0000303|PubMed:19917673, ECO:0000303|PubMed:8943324}
Gene Name GPS2 {ECO:0000312|HGNC:HGNC:4550}
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Nucleus . Mitochondrion . Cytoplasm, cytosol . Sumoylation regulates the subcellular location (PubMed:24943844). Relocates from the mitochondria to the nucleus following desumoylation, leading to mediate mitochondrial stress response (By similarity).
Protein Description Key regulator of inflammation, lipid metabolism and mitochondrion homeostasis that acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, thereby inhibiting 'Lys-63'-linked ubiquitination (By similarity). In the nucleus, can both acts as a corepressor and coactivator of transcription, depending on the context. [PubMed: 24943844 Acts as a transcription coactivator in adipocytes by promoting the recruitment of PPARG to promoters: acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, leading to stabilization of KDM4A and subsequent histone H3 'Lys-9' (H3K9) demethylation (By similarity Promotes cholesterol efflux by acting as a transcription coactivator]
Protein Sequence MPALLERPKLSNAMARALHRHIMMERERKRQEEEEVDKMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLEEKLLALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGGALSLQKQMEHANQQTGFSDSSSLRPMHPQALHPAPGLLASPQLPVQMQPAGKSGFAATSQPGPRLPFIQHSQNPRFYHK
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
45SumoylationKMMEQKMKEEQERRK
HHHHHHHHHHHHHHH
66.2024943844
66UbiquitinationRMSLEETKEQILKLE
HHCHHHHHHHHHHHH
51.4021906983
66UbiquitinationRMSLEETKEQILKLE
HHCHHHHHHHHHHHH
51.40-
71UbiquitinationETKEQILKLEEKLLA
HHHHHHHHHHHHHHH
56.3222817900
71SumoylationETKEQILKLEEKLLA
HHHHHHHHHHHHHHH
56.3224943844
71UbiquitinationETKEQILKLEEKLLA
HHHHHHHHHHHHHHH
56.32-
752-HydroxyisobutyrylationQILKLEEKLLALQEE
HHHHHHHHHHHHHHH
39.15-
75UbiquitinationQILKLEEKLLALQEE
HHHHHHHHHHHHHHH
39.1529967540
75UbiquitinationQILKLEEKLLALQEE
HHHHHHHHHHHHHHH
39.15-
83UbiquitinationLLALQEEKHQLFLQL
HHHHHHHHHHHHHHH
35.5829967540
83UbiquitinationLLALQEEKHQLFLQL
HHHHHHHHHHHHHHH
35.58-
832-HydroxyisobutyrylationLLALQEEKHQLFLQL
HHHHHHHHHHHHHHH
35.58-
91UbiquitinationHQLFLQLKKVLHEEE
HHHHHHHHHHHHHHH
28.0729967540
912-HydroxyisobutyrylationHQLFLQLKKVLHEEE
HHHHHHHHHHHHHHH
28.07-
92UbiquitinationQLFLQLKKVLHEEEK
HHHHHHHHHHHHHHH
59.63-
92UbiquitinationQLFLQLKKVLHEEEK
HHHHHHHHHHHHHHH
59.63-
119PhosphorylationTSAAYQQSLTVHTGT
HHHHHHHCCEEECCC
15.5228348404
121PhosphorylationAAYQQSLTVHTGTHL
HHHHHCCEEECCCCE
18.5828348404
124PhosphorylationQQSLTVHTGTHLLSM
HHCCEEECCCCEEEE
39.1728348404
126PhosphorylationSLTVHTGTHLLSMQG
CCEEECCCCEEEECC
15.5427251275
130PhosphorylationHTGTHLLSMQGSPGG
ECCCCEEEECCCCCC
18.5428348404
134PhosphorylationHLLSMQGSPGGHNRP
CEEEECCCCCCCCCC
11.9528348404
151UbiquitinationLMAADRAKQMFGPQV
CCHHHHHHHHHCCCE
43.09-
151UbiquitinationLMAADRAKQMFGPQV
CCHHHHHHHHHCCCE
43.0927667366
161O-linked_GlycosylationFGPQVLTTRHYVGSA
HCCCEEEECCCCCCH
15.9930379171
204PhosphorylationYGPTQPAYSPSQQLR
CCCCCCCCCHHHHCC
28.0026074081
205PhosphorylationGPTQPAYSPSQQLRA
CCCCCCCCHHHHCCC
21.8526074081
207PhosphorylationTQPAYSPSQQLRAPS
CCCCCCHHHHCCCCC
25.3126074081
251PhosphorylationLQPGGALSLQKQMEH
CCCCCHHHHHHHHHH
28.3724719451
312Asymmetric dimethylarginineATSQPGPRLPFIQHS
CCCCCCCCCCCCCCC
61.99-
312MethylationATSQPGPRLPFIQHS
CCCCCCCCCCCCCCC
61.9924129315
323MethylationIQHSQNPRFYHK---
CCCCCCCCCCCC---
52.9119917673
323Asymmetric dimethylarginineIQHSQNPRFYHK---
CCCCCCCCCCCC---
52.91-

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 GPS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
45KSumoylation

24943844
45KSumoylation

24943844
71KSumoylation

24943844
71KSumoylation

24943844
71KSumoylation

24943844
312RMethylation

-
323RMethylation

-
323RMethylation

-
323RMethylation

-
323Rubiquitylation

-

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 GPS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CS057_HUMANC19orf57physical
16189514
M3KCL_HUMANMAP3K7CLphysical
16189514
CCNA1_HUMANCCNA1physical
15159402
NCOR1_HUMANNCOR1physical
11931768
TBL1X_HUMANTBL1Xphysical
11931768
HDAC3_HUMANHDAC3physical
11931768
EP300_HUMANEP300physical
10846067
GOGA2_HUMANGOLGA2physical
16169070
CHD3_HUMANCHD3physical
16169070
SETB1_HUMANSETDB1physical
16169070
P53_HUMANTP53physical
11486030
NR0B2_HUMANNR0B2physical
17895379
NR0B2_RATNr0b2physical
17895379
HDAC1_HUMANHDAC1physical
17895379
HDAC3_HUMANHDAC3physical
17895379
NR5A2_HUMANNR5A2physical
17895379
HNF4A_HUMANHNF4Aphysical
17895379
NR1H4_HUMANNR1H4physical
17895379
MSH4_HUMANMSH4physical
16122992
MSH5_HUMANMSH5physical
16122992
TBL1X_HUMANTBL1Xphysical
24943844
NCOR2_HUMANNCOR2physical
24943844
HDAC3_HUMANHDAC3physical
24943844
K1H1_HUMANKRT31physical
25416956
RBP1_HUMANRALBP1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
TFP11_HUMANTFIP11physical
25416956
SESD1_HUMANSESTD1physical
25416956
TBL1R_HUMANTBL1XR1physical
26186194
TBL1X_HUMANTBL1Xphysical
26186194
NCOR1_HUMANNCOR1physical
26186194
NCOR2_HUMANNCOR2physical
26186194
LIPA1_HUMANPPFIA1physical
26186194
LIPA3_HUMANPPFIA3physical
26186194
MK03_HUMANMAPK3physical
26186194
ARMC8_HUMANARMC8physical
26186194
MKLN1_HUMANMKLN1physical
26186194
MAEA_HUMANMAEAphysical
26186194
DCTN4_HUMANDCTN4physical
26186194
RMD5A_HUMANRMND5Aphysical
26186194
RBP10_HUMANRANBP10physical
26186194
ANR11_HUMANANKRD11physical
26186194
CYH3_HUMANCYTH3physical
26186194
GID4_HUMANGID4physical
26186194
ARP10_HUMANACTR10physical
26186194
DAPK3_HUMANDAPK3physical
26186194
TRI68_HUMANTRIM68physical
26186194
GID8_HUMANGID8physical
26186194
FOXK2_HUMANFOXK2physical
26186194
FOXK1_HUMANFOXK1physical
26186194
CREB1_HUMANCREB1physical
26186194
DCTN6_HUMANDCTN6physical
26186194
DCTN3_HUMANDCTN3physical
26186194
YPEL5_HUMANYPEL5physical
26186194
HDAC3_HUMANHDAC3physical
26186194
TBL1X_HUMANTBL1Xphysical
26070566
GPA1_YEASTGPA1genetic
8943324
GBB_YEASTSTE4genetic
8943324
MK08_HUMANMAPK8genetic
8943324
ANR11_HUMANANKRD11physical
28514442
NCOR2_HUMANNCOR2physical
28514442
LIPA3_HUMANPPFIA3physical
28514442
TBL1X_HUMANTBL1Xphysical
28514442
DAPK3_HUMANDAPK3physical
28514442
NCOR1_HUMANNCOR1physical
28514442
LIPA1_HUMANPPFIA1physical
28514442
TBL1R_HUMANTBL1XR1physical
28514442
HDAC3_HUMANHDAC3physical
28514442
CYH3_HUMANCYTH3physical
28514442
DCTN6_HUMANDCTN6physical
28514442
TRI68_HUMANTRIM68physical
28514442
FOXK1_HUMANFOXK1physical
28514442
GID4_HUMANGID4physical
28514442
FOXK2_HUMANFOXK2physical
28514442
ARP10_HUMANACTR10physical
28514442
MK03_HUMANMAPK3physical
28514442
ARMC8_HUMANARMC8physical
28514442
DCTN4_HUMANDCTN4physical
28514442
DCTN3_HUMANDCTN3physical
28514442
MKLN1_HUMANMKLN1physical
28514442
CREB1_HUMANCREB1physical
28514442
GID8_HUMANGID8physical
28514442
ACTY_HUMANACTR1Bphysical
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 GPS2_HUMAN

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Related Literatures of Post-Translational Modification

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