T22D3_HUMAN - dbPTM
T22D3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T22D3_HUMAN
UniProt AC Q99576
Protein Name TSC22 domain family protein 3
Gene Name TSC22D3
Organism Homo sapiens (Human).
Sequence Length 134
Subcellular Localization Isoform 1: Cytoplasm. Nucleus. Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the cytoplasm, but in differentiating myoblasts, isoform 1 is localized to the nucleus (By similarity)..
Protein Description Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity). Isoform 1 inhibits myogenic differentiation and mediates anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG (By similarity)..
Protein Sequence MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDNSASGASVVAIDNKIEQAMDLVKNHLMYAVREEVEILKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSCLSPEEPAPESPQVPEAPGGSAV
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
5 (in isoform 4)Phosphorylation-2.5730622161
10 (in isoform 3)Phosphorylation-8.0025849741
15 (in isoform 4)Phosphorylation-8.8130622161
27 (in isoform 3)Phosphorylation-23.5823090842
33 (in isoform 3)Phosphorylation-3.8023927012
34 (in isoform 3)Phosphorylation-6.9225159151
42 (in isoform 3)Phosphorylation-20.4522167270
44 (in isoform 3)Phosphorylation-22.9122167270
46 (in isoform 3)Phosphorylation-22.2022167270
53UbiquitinationSVVAIDNKIEQAMDL
EEEEECCHHHHHHHH		43.8221906983
53 (in isoform 1)Ubiquitination-43.8221906983
62UbiquitinationEQAMDLVKNHLMYAV
HHHHHHHHHHHHHHH		46.04-
67 (in isoform 3)Phosphorylation-14.3322617229
73 (in isoform 3)Phosphorylation-4.8022617229
74 (in isoform 4)Ubiquitination-45.9721906983
77UbiquitinationREEVEILKEQIRELV
HHHHHHHHHHHHHHH		53.91-
83 (in isoform 3)Phosphorylation-4.3028270605
86UbiquitinationQIRELVEKNSQLERE
HHHHHHHHCHHHHHH		55.192190698
86 (in isoform 1)Ubiquitination-55.1921906983
98UbiquitinationERENTLLKTLASPEQ
HHHHHHHHHHCCHHH		44.60-
102PhosphorylationTLLKTLASPEQLEKF
HHHHHHCCHHHHHHH		31.8921815630
108UbiquitinationASPEQLEKFQSCLSP
CCHHHHHHHHHCCCC		58.24-
111PhosphorylationEQLEKFQSCLSPEEP
HHHHHHHHCCCCCCC		21.8425159151
114PhosphorylationEKFQSCLSPEEPAPE
HHHHHCCCCCCCCCC		34.2920068231
122PhosphorylationPEEPAPESPQVPEAP
CCCCCCCCCCCCCCC		21.4130278072
132PhosphorylationVPEAPGGSAV-----
CCCCCCCCCC-----		31.6020068231
152 (in isoform 3)Ubiquitination-21906983
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 T22D3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T22D3_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 T22D3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHF2_HUMANPLEKHF2physical
16189514
HPCL4_HUMANHPCAL4physical
16189514
RAF1_HUMANRAF1physical
12391160
FOS_HUMANFOSphysical
11397794
JUN_HUMANJUNphysical
11397794
T22D3_HUMANTSC22D3physical
11397794
NFKB1_HUMANNFKB1physical
11468175
NFKB2_HUMANNFKB2physical
11468175
HDAC1_HUMANHDAC1physical
20124407
MYOD1_HUMANMYOD1physical
20124407
HDAC2_HUMANHDAC2physical
20124407
SGK1_HUMANSGK1physical
20947508
UBC9_HUMANUBE2Iphysical
20671745
SUMO1_HUMANSUMO1physical
20671745
SGK1_HUMANSGK1physical
19380724
SCNNB_HUMANSCNN1Bphysical
19380724
NED4L_HUMANNEDD4Lphysical
19380724
RAF1_HUMANRAF1physical
19380724
P53_HUMANTP53physical
25168242
MDM2_HUMANMDM2physical
25168242
MD1L1_HUMANMAD1L1physical
25416956
CS057_HUMANC19orf57physical
25416956
T22D4_HUMANTSC22D4physical
28514442
T22D2_HUMANTSC22D2physical
28514442
T22D1_HUMANTSC22D1physical
28514442
NRBP_HUMANNRBP1physical
28514442
CEP55_HUMANCEP55physical
28514442
NUFP2_HUMANNUFIP2physical
27173435
AGAP3_HUMANAGAP3physical
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 T22D3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.

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