T22D4_HUMAN - dbPTM
T22D4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T22D4_HUMAN
UniProt AC Q9Y3Q8
Protein Name TSC22 domain family protein 4
Gene Name TSC22D4
Organism Homo sapiens (Human).
Sequence Length 395
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor..
Protein Sequence MSGGKKKSSFQITSVTTDYEGPGSPGASDPPTPQPPTGPPPRLPNGEPSPDPGGKGTPRNGSPPPGAPSSRFRVVKLPHGLGEPYRRGRWTCVDVYERDLEPHSFGGLLEGIRGASGGAGGRSLDSRLELASLGLGAPTPPSGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLVVPSKAKAEKPPLSASSPQQRPPEPETGESAGTSRAATPLPSLRVEAEAGGSGARTPPLSRRKAVDMRLRMELGAPEEMGQVPPLDSRPSSPALYFTHDASLVHKSPDPFGAVAAQKFSLAHSMLAISGHLDSDDDSGSGSLVGIDNKIEQAMDLVKSHLMFAVREEVEVLKEQIRELAERNAALEQENGLLRALASPEQLAQLPSSGVPRLGPPAPNGPSV
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
19PhosphorylationITSVTTDYEGPGSPG
EEEEEECCCCCCCCC
22.2427080861
24PhosphorylationTDYEGPGSPGASDPP
ECCCCCCCCCCCCCC
24.2426503514
28PhosphorylationGPGSPGASDPPTPQP
CCCCCCCCCCCCCCC
57.4727080861
37PhosphorylationPPTPQPPTGPPPRLP
CCCCCCCCCCCCCCC
69.8424719451
49PhosphorylationRLPNGEPSPDPGGKG
CCCCCCCCCCCCCCC
37.3223401153
57PhosphorylationPDPGGKGTPRNGSPP
CCCCCCCCCCCCCCC
23.6629255136
62PhosphorylationKGTPRNGSPPPGAPS
CCCCCCCCCCCCCCC
37.4729255136
69PhosphorylationSPPPGAPSSRFRVVK
CCCCCCCCCCEEEEE
33.3423403867
70PhosphorylationPPPGAPSSRFRVVKL
CCCCCCCCCEEEEEC
34.0923403867
104PhosphorylationERDLEPHSFGGLLEG
ECCCCCCCCHHHHHH
35.9825850435
116PhosphorylationLEGIRGASGGAGGRS
HHHHHCCCCCCCCCC
40.3523403867
123PhosphorylationSGGAGGRSLDSRLEL
CCCCCCCCHHHHHHH
39.5423401153
126PhosphorylationAGGRSLDSRLELASL
CCCCCHHHHHHHHHC
44.0223403867
132PhosphorylationDSRLELASLGLGAPT
HHHHHHHHCCCCCCC
35.2820068231
139PhosphorylationSLGLGAPTPPSGLSQ
HCCCCCCCCCCCCCC
47.5021712546
142PhosphorylationLGAPTPPSGLSQGPT
CCCCCCCCCCCCCCC
54.2728450419
145PhosphorylationPTPPSGLSQGPTSWL
CCCCCCCCCCCCCCC
36.2928450419
149PhosphorylationSGLSQGPTSWLRPPP
CCCCCCCCCCCCCCC
39.0828450419
150PhosphorylationGLSQGPTSWLRPPPT
CCCCCCCCCCCCCCC
27.5228450419
157PhosphorylationSWLRPPPTSPGPQAR
CCCCCCCCCCCCCCC
54.0122115753
158PhosphorylationWLRPPPTSPGPQARS
CCCCCCCCCCCCCCC
33.3621712546
165PhosphorylationSPGPQARSFTGGLGQ
CCCCCCCCCCCCCCC
30.1229255136
167PhosphorylationGPQARSFTGGLGQLV
CCCCCCCCCCCCCEE
31.4225463755
177PhosphorylationLGQLVVPSKAKAEKP
CCCEECCCCCCCCCC
33.3723927012
180AcetylationLVVPSKAKAEKPPLS
EECCCCCCCCCCCCC
61.907493427
187PhosphorylationKAEKPPLSASSPQQR
CCCCCCCCCCCCCCC
31.7029255136
189PhosphorylationEKPPLSASSPQQRPP
CCCCCCCCCCCCCCC
38.8929255136
190PhosphorylationKPPLSASSPQQRPPE
CCCCCCCCCCCCCCC
26.8429255136
200PhosphorylationQRPPEPETGESAGTS
CCCCCCCCCCCCCCC
57.8923403867
203PhosphorylationPEPETGESAGTSRAA
CCCCCCCCCCCCCCC
33.0929255136
206PhosphorylationETGESAGTSRAATPL
CCCCCCCCCCCCCCC
18.1129255136
207PhosphorylationTGESAGTSRAATPLP
CCCCCCCCCCCCCCC
21.0029255136
211PhosphorylationAGTSRAATPLPSLRV
CCCCCCCCCCCCCEE
25.1129255136
215PhosphorylationRAATPLPSLRVEAEA
CCCCCCCCCEEEEEC
36.1721082442
225PhosphorylationVEAEAGGSGARTPPL
EEEECCCCCCCCCCC
28.5025159151
229PhosphorylationAGGSGARTPPLSRRK
CCCCCCCCCCCCHHH
28.8223927012
233PhosphorylationGARTPPLSRRKAVDM
CCCCCCCCHHHHHHH
35.4923927012
260PhosphorylationGQVPPLDSRPSSPAL
CCCCCCCCCCCCCCE
54.4929255136
263PhosphorylationPPLDSRPSSPALYFT
CCCCCCCCCCCEEEE
48.0929255136
264PhosphorylationPLDSRPSSPALYFTH
CCCCCCCCCCEEEEC
19.5129255136
268PhosphorylationRPSSPALYFTHDASL
CCCCCCEEEECCHHH
14.4529255136
270PhosphorylationSSPALYFTHDASLVH
CCCCEEEECCHHHCC
12.8029255136
274PhosphorylationLYFTHDASLVHKSPD
EEEECCHHHCCCCCC
36.6629255136
279PhosphorylationDASLVHKSPDPFGAV
CHHHCCCCCCCCHHH
21.4719664994
292PhosphorylationAVAAQKFSLAHSMLA
HHHHHHHHHHHHHHH
31.5129514088
296PhosphorylationQKFSLAHSMLAISGH
HHHHHHHHHHHHHCC
15.1929514088
301PhosphorylationAHSMLAISGHLDSDD
HHHHHHHHCCCCCCC
17.9829514088
306PhosphorylationAISGHLDSDDDSGSG
HHHCCCCCCCCCCCC
49.6628464451
310PhosphorylationHLDSDDDSGSGSLVG
CCCCCCCCCCCCEEE
41.6829514088
312PhosphorylationDSDDDSGSGSLVGID
CCCCCCCCCCEEEEC
29.2129514088
314PhosphorylationDDDSGSGSLVGIDNK
CCCCCCCCEEEECHH
22.9129514088
345UbiquitinationREEVEVLKEQIRELA
HHHHHHHHHHHHHHH
53.39-
370PhosphorylationGLLRALASPEQLAQL
CHHHHHCCHHHHHCC
29.8029255136
394PhosphorylationPPAPNGPSV------
CCCCCCCCC------
41.6925159151

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 T22D4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T22D4_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 T22D4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FRMD6_HUMANFRMD6physical
16189514
ENKD1_HUMANENKD1physical
16189514
CCD42_HUMANCCDC42physical
16189514
LNX1_HUMANLNX1physical
16189514
UBCP1_HUMANUBLCP1physical
16189514
K1C40_HUMANKRT40physical
25416956
NRBP2_HUMANNRBP2physical
25416956
SMG8_HUMANSMG8physical
26186194
STK39_HUMANSTK39physical
26186194
P4HA1_HUMANP4HA1physical
26186194
T22D2_HUMANTSC22D2physical
26186194
T22D1_HUMANTSC22D1physical
26186194
T22D3_HUMANTSC22D3physical
26186194
CRTAP_HUMANCRTAPphysical
26186194
MD2L1_HUMANMAD2L1physical
26186194
ELOC_HUMANTCEB1physical
26186194
NRBP2_HUMANNRBP2physical
26186194
P3H1_HUMANP3H1physical
26186194
NRBP_HUMANNRBP1physical
26186194
IF172_HUMANIFT172physical
26186194
LRWD1_HUMANLRWD1physical
26186194
CUL1_HUMANCUL1physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
RHOA_HUMANRHOAphysical
26186194
PDPR_HUMANPDPRphysical
26186194
WNK3_HUMANWNK3physical
26186194
WNK1_HUMANWNK1physical
26186194
WNK2_HUMANWNK2physical
26186194
P4HA2_HUMANP4HA2physical
26186194
CPVL_HUMANCPVLphysical
26186194
TTL_HUMANTTLphysical
26186194
FBW1B_HUMANFBXW11physical
26186194
FBW1A_HUMANBTRCphysical
26186194
TBL1R_HUMANTBL1XR1physical
26186194
TBL1X_HUMANTBL1Xphysical
26186194
KEAP1_HUMANKEAP1physical
26186194
MD2BP_HUMANMAD2L1BPphysical
26186194
KPCD2_HUMANPRKD2physical
26186194
T22D1_HUMANTSC22D1physical
28514442
T22D2_HUMANTSC22D2physical
28514442
TTL_HUMANTTLphysical
28514442
NRBP_HUMANNRBP1physical
28514442
WNK2_HUMANWNK2physical
28514442
WNK3_HUMANWNK3physical
28514442
MD2BP_HUMANMAD2L1BPphysical
28514442
FBW1B_HUMANFBXW11physical
28514442
FBW1A_HUMANBTRCphysical
28514442
NRBP2_HUMANNRBP2physical
28514442
STK39_HUMANSTK39physical
28514442
RHOA_HUMANRHOAphysical
28514442
MD2L1_HUMANMAD2L1physical
28514442
WNK1_HUMANWNK1physical
28514442
KPCD2_HUMANPRKD2physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
TBL1X_HUMANTBL1Xphysical
28514442
PDPR_HUMANPDPRphysical
28514442
GDS1_HUMANRAP1GDS1physical
28514442
P4HA1_HUMANP4HA1physical
28514442
CUL1_HUMANCUL1physical
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 T22D4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211; SER-225;THR-229; SER-233; SER-279 AND SER-370, AND MASS SPECTROMETRY.
"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-62; SER-165; THR-211 ANDSER-279, AND MASS SPECTROMETRY.

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