ENY2_HUMAN - dbPTM
ENY2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENY2_HUMAN
UniProt AC Q9NPA8
Protein Name Transcription and mRNA export factor ENY2 {ECO:0000255|HAMAP-Rule:MF_03046}
Gene Name ENY2 {ECO:0000255|HAMAP-Rule:MF_03046}
Organism Homo sapiens (Human).
Sequence Length 101
Subcellular Localization Nucleus, nucleoplasm . Nucleus, nuclear pore complex .
Protein Description Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery..
Protein Sequence MVVSKMNKDAQMRAAINQKLIETGERERLKELLRAKLIECGWKDQLKAHCKEVIKEKGLEHVTVDDLVAEITPKGRALVPDSVKKELLQRIRTFLAQHASL
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
1 (in isoform 2)Acetylation-6.4022814378
4Phosphorylation----MVVSKMNKDAQ
----CCCCCCCHHHH
18.1220068231
5Acetylation---MVVSKMNKDAQM
---CCCCCCCHHHHH
34.5825953088
8AcetylationMVVSKMNKDAQMRAA
CCCCCCCHHHHHHHH
51.4425953088
8UbiquitinationMVVSKMNKDAQMRAA
CCCCCCCHHHHHHHH
51.44-
19UbiquitinationMRAAINQKLIETGER
HHHHHHHHHHHHCHH
47.1221890473
19AcetylationMRAAINQKLIETGER
HHHHHHHHHHHHCHH
47.1225953088
30UbiquitinationTGERERLKELLRAKL
HCHHHHHHHHHHHHH
53.16-
36UbiquitinationLKELLRAKLIECGWK
HHHHHHHHHHHCCCH
43.49-
36AcetylationLKELLRAKLIECGWK
HHHHHHHHHHHCCCH
43.4925953088
40S-nitrosocysteineLRAKLIECGWKDQLK
HHHHHHHCCCHHHHH
6.63-
40GlutathionylationLRAKLIECGWKDQLK
HHHHHHHCCCHHHHH
6.6322555962
40S-nitrosylationLRAKLIECGWKDQLK
HHHHHHHCCCHHHHH
6.6319483679
43UbiquitinationKLIECGWKDQLKAHC
HHHHCCCHHHHHHHH
22.38-
43AcetylationKLIECGWKDQLKAHC
HHHHCCCHHHHHHHH
22.3823954790
57UbiquitinationCKEVIKEKGLEHVTV
HHHHHHHCCCCCCCH
64.89-
72PhosphorylationDDLVAEITPKGRALV
HHHHHHCCCCCCCCC
15.51-
74UbiquitinationLVAEITPKGRALVPD
HHHHCCCCCCCCCCH
52.9921890473
74SumoylationLVAEITPKGRALVPD
HHHHCCCCCCCCCCH
52.9928112733
82PhosphorylationGRALVPDSVKKELLQ
CCCCCCHHHHHHHHH
29.7520068231
842-HydroxyisobutyrylationALVPDSVKKELLQRI
CCCCHHHHHHHHHHH
44.47-
85UbiquitinationLVPDSVKKELLQRIR
CCCHHHHHHHHHHHH
51.98-
100PhosphorylationTFLAQHASL------
HHHHHHHCC------
32.2730108239

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 ENY2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENY2_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 ENY2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GANP_HUMANMCM3APphysical
16169070
TRRAP_HUMANTRRAPphysical
18206972
KAT2A_HUMANKAT2Aphysical
18206972
TAF10_HUMANTAF10physical
18206972
UBP22_HUMANUSP22physical
18206972
AT7L3_HUMANATXN7L3physical
18206972
A4_HUMANAPPphysical
21832049
H2AX_HUMANH2AFXphysical
26344197
A7L3B_HUMANATXN7L3Bphysical
27601583
AT7L3_HUMANATXN7L3physical
27601583

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 ENY2_HUMAN

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Related Literatures of Post-Translational Modification

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