T22D2_HUMAN - dbPTM
T22D2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T22D2_HUMAN
UniProt AC O75157
Protein Name TSC22 domain family protein 2
Gene Name TSC22D2
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization
Protein Description
Protein Sequence MSKMPAKKKSCFQITSVTTAQVATSITEDTESLDDPDESRTEDVSSEIFDVSRATDYGPEEVCERSSSEETLNNVGDAETPGTVSPNLLLDGQLAAAAAAPANGGGVVSARSVSGALASTLAAAATSAPAPGAPGGPQLAGSSAGPVTAAPSQPPTTCSSRFRVIKLDHGSGEPYRRGRWTCMEYYERDSDSSVLTRSGDCIRHSSTFDQTAERDSGLGATGGSVVVVVASMQGAHGPESGTDSSLTAVSQLPPSEKMSQPTPAQPQSFSVGQPQPPPPPVGGAVAQSSAPLPPFPGAATGPQPMMAAAQPSQPQGAGPGGQTLPPTNVTLAQPAMSLPPQPGPAVGAPAAQQPQQFAYPQPQIPPGHLLPVQPSGQSEYLQQHVAGLQPPSPAQPSSTGAAASPATAATLPVGTGQNASSVGAQLMGASSQPSEAMAPRTGPAQGGQVAPCQPTGVPPATVGGVVQPCLGPAGAGQPQSVPPPQMGGSGPLSAVPGGPHAVVPGVPNVPAAVPAPSVPSVSTTSVTMPNVPAPLAQSQQLSSHTPVSRSSSIIQHVGLPLAPGTHSAPTSLPQSDLSQFQTQTQPLVGQVDDTRRKSEPLPQPPLSLIAENKPVVKPPVADSLANPLQLTPMNSLATSVFSIAIPVDGDEDRNPSTAFYQAFHLNTLKESKSLWDSASGGGVVAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELVERNSLLERENALLKSLSSNDQLSQLPTQQANPGSTSQQQAVIAQPPQPTQPPQQPNVSSA
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
45PhosphorylationESRTEDVSSEIFDVS
CCCCCCHHHHHHCHH
34.2830266825
46PhosphorylationSRTEDVSSEIFDVSR
CCCCCHHHHHHCHHH
34.2630266825
52PhosphorylationSSEIFDVSRATDYGP
HHHHHCHHHHHCCCH
20.3121815630
55PhosphorylationIFDVSRATDYGPEEV
HHCHHHHHCCCHHHH
28.7521815630
57PhosphorylationDVSRATDYGPEEVCE
CHHHHHCCCHHHHHH
30.1726552605
66PhosphorylationPEEVCERSSSEETLN
HHHHHHCCCCCCHHH
18.8730624053
67PhosphorylationEEVCERSSSEETLNN
HHHHHCCCCCCHHHC
48.2530624053
68PhosphorylationEVCERSSSEETLNNV
HHHHCCCCCCHHHCC
40.4730624053
71PhosphorylationERSSSEETLNNVGDA
HCCCCCCHHHCCCCC
30.6330624053
80PhosphorylationNNVGDAETPGTVSPN
HCCCCCCCCCCCCCC
28.8330624053
83PhosphorylationGDAETPGTVSPNLLL
CCCCCCCCCCCCEEE
21.0030624053
85PhosphorylationAETPGTVSPNLLLDG
CCCCCCCCCCEEECC
14.1230624053
112PhosphorylationGGVVSARSVSGALAS
CCEEEEEEHHHHHHH
21.9828348404
114PhosphorylationVVSARSVSGALASTL
EEEEEEHHHHHHHHH
21.4228348404
171PhosphorylationVIKLDHGSGEPYRRG
EEEECCCCCCCCCCC
36.2427732954
181PhosphorylationPYRRGRWTCMEYYER
CCCCCEEEEEEEEEC
10.70-
190PhosphorylationMEYYERDSDSSVLTR
EEEEECCCCCCEEEC
45.6828674419
192PhosphorylationYYERDSDSSVLTRSG
EEECCCCCCEEECCC
26.71-
193PhosphorylationYERDSDSSVLTRSGD
EECCCCCCEEECCCC
26.5728857561
196PhosphorylationDSDSSVLTRSGDCIR
CCCCCEEECCCCCCC
22.1927251275
198PhosphorylationDSSVLTRSGDCIRHS
CCCEEECCCCCCCCC
33.4723403867
205PhosphorylationSGDCIRHSSTFDQTA
CCCCCCCCCCCCCCC
22.6422617229
206PhosphorylationGDCIRHSSTFDQTAE
CCCCCCCCCCCCCCC
27.2823403867
207PhosphorylationDCIRHSSTFDQTAER
CCCCCCCCCCCCCCC
33.9630108239
240PhosphorylationQGAHGPESGTDSSLT
CCCCCCCCCCCCCCC
50.5627251275
242PhosphorylationAHGPESGTDSSLTAV
CCCCCCCCCCCCCCH
41.8227251275
244PhosphorylationGPESGTDSSLTAVSQ
CCCCCCCCCCCCHHC
27.3827251275
245PhosphorylationPESGTDSSLTAVSQL
CCCCCCCCCCCHHCC
32.3327251275
247PhosphorylationSGTDSSLTAVSQLPP
CCCCCCCCCHHCCCC
27.2827251275
538O-linked_GlycosylationVPAPLAQSQQLSSHT
CCCCHHHHHHHHCCC
17.81OGP
542PhosphorylationLAQSQQLSSHTPVSR
HHHHHHHHCCCCCCC
18.7426503514
543PhosphorylationAQSQQLSSHTPVSRS
HHHHHHHCCCCCCCC
39.7226503514
548O-linked_GlycosylationLSSHTPVSRSSSIIQ
HHCCCCCCCCCHHHH
27.8723301498
548PhosphorylationLSSHTPVSRSSSIIQ
HHCCCCCCCCCHHHH
27.8726503514
550O-linked_GlycosylationSHTPVSRSSSIIQHV
CCCCCCCCCHHHHHC
22.4123301498
550PhosphorylationSHTPVSRSSSIIQHV
CCCCCCCCCHHHHHC
22.4118669648
551O-linked_GlycosylationHTPVSRSSSIIQHVG
CCCCCCCCHHHHHCC
25.1723301498
551PhosphorylationHTPVSRSSSIIQHVG
CCCCCCCCHHHHHCC
25.1726699800
552PhosphorylationTPVSRSSSIIQHVGL
CCCCCCCHHHHHCCC
25.5925394399
552O-linked_GlycosylationTPVSRSSSIIQHVGL
CCCCCCCHHHHHCCC
25.5923301498
565PhosphorylationGLPLAPGTHSAPTSL
CCCCCCCCCCCCCCC
16.1726699800
567PhosphorylationPLAPGTHSAPTSLPQ
CCCCCCCCCCCCCCH
35.4629496963
570O-linked_GlycosylationPGTHSAPTSLPQSDL
CCCCCCCCCCCHHHH
42.4823301498
570PhosphorylationPGTHSAPTSLPQSDL
CCCCCCCCCCCHHHH
42.4826699800
571O-linked_GlycosylationGTHSAPTSLPQSDLS
CCCCCCCCCCHHHHH
36.6723301498
571PhosphorylationGTHSAPTSLPQSDLS
CCCCCCCCCCHHHHH
36.6726699800
575O-linked_GlycosylationAPTSLPQSDLSQFQT
CCCCCCHHHHHHCHH
38.2823301498
575PhosphorylationAPTSLPQSDLSQFQT
CCCCCCHHHHHHCHH
38.2826699800
578PhosphorylationSLPQSDLSQFQTQTQ
CCCHHHHHHCHHHCC
33.6621406692
582PhosphorylationSDLSQFQTQTQPLVG
HHHHHCHHHCCCCCC
34.5721406692
584PhosphorylationLSQFQTQTQPLVGQV
HHHCHHHCCCCCCCC
35.2321406692
594PhosphorylationLVGQVDDTRRKSEPL
CCCCCCCCCCCCCCC
28.1026074081
598PhosphorylationVDDTRRKSEPLPQPP
CCCCCCCCCCCCCCC
42.5125849741
607PhosphorylationPLPQPPLSLIAENKP
CCCCCCCCCEECCCC
24.4126074081
674 (in isoform 2)Ubiquitination-7.2821890473
689 (in isoform 2)Ubiquitination-43.8221890473
694SulfoxidationDNKIEQAMDLVKSHL
CCHHHHHHHHHHHHH
4.0121406390
698 (in isoform 1)Ubiquitination-39.1821890473
698UbiquitinationEQAMDLVKSHLMYAV
HHHHHHHHHHHHHHH
39.18-
699PhosphorylationQAMDLVKSHLMYAVR
HHHHHHHHHHHHHHH
17.8620068231
703PhosphorylationLVKSHLMYAVREEVE
HHHHHHHHHHHHHHH
14.3320068231
713UbiquitinationREEVEVLKEQIKELV
HHHHHHHHHHHHHHH
53.39-
713 (in isoform 1)Ubiquitination-53.3921890473
724PhosphorylationKELVERNSLLERENA
HHHHHHHCHHHHHHH
40.3223911959
778O-linked_GlycosylationPPQQPNVSSA-----
CCCCCCCCCC-----
27.4723301498
779O-linked_GlycosylationPQQPNVSSA------
CCCCCCCCC------
33.4423301498

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 T22D2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T22D2_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 T22D2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KEAP1_HUMANKEAP1physical
23382044
RING2_HUMANRNF2physical
27337956
WNK3_HUMANWNK3physical
27337956
OSBL1_HUMANOSBPL1Aphysical
27337956
PSA7_HUMANPSMA7physical
27337956
ZN143_HUMANZNF143physical
27337956
NRBP_HUMANNRBP1physical
27337956
FLNB_HUMANFLNBphysical
27337956
TILB_HUMANLRRC6physical
27337956
MPDZ_HUMANMPDZphysical
27337956
REV1_HUMANREV1physical
27337956
TITIN_HUMANTTNphysical
27337956
MEP50_HUMANWDR77physical
27337956
CC141_HUMANCCDC141physical
27337956
C144A_HUMANCCDC144Aphysical
27337956
TALD3_HUMANKIAA0586physical
27337956
ANM3_HUMANPRMT3physical
27337956
SNX3_HUMANSNX3physical
27337956
SPEF2_HUMANSPEF2physical
27337956
TMA7_HUMANTMA7physical
27337956
APC10_HUMANANAPC10physical
27337956
AN36A_HUMANANKRD36physical
27337956
ARID2_HUMANARID2physical
27337956
AT1B1_HUMANATP1B1physical
27337956
CLIP1_HUMANCLIP1physical
27337956
ENOPH_HUMANENOPH1physical
27337956
EPCAM_HUMANEPCAMphysical
27337956
FA8_HUMANF8physical
27337956
GPBP1_HUMANGPBP1physical
27337956
ITA2_HUMANITGA2physical
27337956
LOXH1_HUMANLOXHD1physical
27337956
LIPL_HUMANLPLphysical
27337956
MED13_HUMANMED13physical
27337956
MSH3_HUMANMSH3physical
27337956
IF2M_HUMANMTIF2physical
27337956
NGRN_HUMANNGRNphysical
27337956
PSA7L_HUMANPSMA8physical
27337956
RBL1_HUMANRBL1physical
27337956
SAP18_HUMANSAP18physical
27337956
SCEL_HUMANSCELphysical
27337956
SC31A_HUMANSEC31Aphysical
27337956
STK39_HUMANSTK39physical
27337956
UFM1_HUMANUFM1physical
27337956
ZMYM2_HUMANZMYM2physical
27337956
ZN251_HUMANZNF251physical
27337956

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 T22D2_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-598, AND MASSSPECTROMETRY.

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