TADBP_HUMAN - dbPTM
TADBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TADBP_HUMAN
UniProt AC Q13148
Protein Name TAR DNA-binding protein 43
Gene Name TARDBP
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Nucleus . In patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis, it is absent from the nucleus of affected neurons but it is the primary component of cytoplasmic ubiquitin-positive inclusion bodies.
Protein Description DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR..
Protein Sequence MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQNQGNMQREPNQAFGSGNNSYSGSNSGAAIGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM
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
2Phosphorylation------MSEYIRVTE
------CCCCEEEEC
38.8219285963
4Phosphorylation----MSEYIRVTEDE
----CCCCEEEECCC
6.1619285963
8PhosphorylationMSEYIRVTEDENDEP
CCCCEEEECCCCCCC
28.0620873877
20PhosphorylationDEPIEIPSEDDGTVL
CCCCCCCCCCCCEEE
60.3625338102
25PhosphorylationIPSEDDGTVLLSTVT
CCCCCCCEEEEEEEE
18.2520873877
29PhosphorylationDDGTVLLSTVTAQFP
CCCEEEEEEEEECCC
19.3720873877
30PhosphorylationDGTVLLSTVTAQFPG
CCEEEEEEEEECCCC
23.1120873877
32PhosphorylationTVLLSTVTAQFPGAC
EEEEEEEEECCCCCC
18.1520873877
44UbiquitinationGACGLRYRNPVSQCM
CCCCCEECCHHHHHH
34.2421890473
48PhosphorylationLRYRNPVSQCMRGVR
CEECCHHHHHHHHHE
20.9421406692
73PhosphorylationAGWGNLVYVVNYPKD
CCCCCEEEEEECCCC
11.2227642862
79SumoylationVYVVNYPKDNKRKMD
EEEEECCCCCCCCCC
64.6728112733
79UbiquitinationVYVVNYPKDNKRKMD
EEEEECCCCCCCCCC
64.67-
82UbiquitinationVNYPKDNKRKMDETD
EECCCCCCCCCCCCC
64.63-
84SumoylationYPKDNKRKMDETDAS
CCCCCCCCCCCCCHH
52.92-
84UbiquitinationYPKDNKRKMDETDAS
CCCCCCCCCCCCCHH
52.92-
84SumoylationYPKDNKRKMDETDAS
CCCCCCCCCCCCCHH
52.9228112733
84 (in isoform 2)Ubiquitination-52.92-
85SulfoxidationPKDNKRKMDETDASS
CCCCCCCCCCCCHHH
6.9930846556
88PhosphorylationNKRKMDETDASSAVK
CCCCCCCCCHHHHHH
32.3819285963
91PhosphorylationKMDETDASSAVKVKR
CCCCCCHHHHHHHHH
22.9529255136
92PhosphorylationMDETDASSAVKVKRA
CCCCCHHHHHHHHHH
38.5129255136
95AcetylationTDASSAVKVKRAVQK
CCHHHHHHHHHHHHH
41.5825953088
95SumoylationTDASSAVKVKRAVQK
CCHHHHHHHHHHHHH
41.58-
95UbiquitinationTDASSAVKVKRAVQK
CCHHHHHHHHHHHHH
41.5821890473
95SumoylationTDASSAVKVKRAVQK
CCHHHHHHHHHHHHH
41.5828112733
95 (in isoform 2)Ubiquitination-41.58-
97UbiquitinationASSAVKVKRAVQKTS
HHHHHHHHHHHHHCC
28.99-
102SumoylationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.32-
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3221890473
102SumoylationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3225772364
102 (in isoform 2)Ubiquitination-43.32-
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3221890473
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3221890473
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3221890473
102AcetylationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3225953088
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.3221890473
103PhosphorylationVKRAVQKTSDLIVLG
HHHHHHHCCCEEEEC
15.4724719451
104PhosphorylationKRAVQKTSDLIVLGL
HHHHHHCCCEEEECC
37.1424719451
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.5621890473
114SumoylationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.56-
114 (in isoform 2)Ubiquitination-43.56-
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.5621890473
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.5621890473
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.5621890473
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.5621890473
115PhosphorylationVLGLPWKTTEQDLKE
EECCCCCCCHHHHHH
31.5330622161
116PhosphorylationLGLPWKTTEQDLKEY
ECCCCCCCHHHHHHH
28.1128450419
121UbiquitinationKTTEQDLKEYFSTFG
CCCHHHHHHHHHHHH
59.6721890473
121SumoylationKTTEQDLKEYFSTFG
CCCHHHHHHHHHHHH
59.67-
136AcetylationEVLMVQVKKDLKTGH
HEEEEEEECCCCCCC
24.3919824233
140AcetylationVQVKKDLKTGHSKGF
EEEECCCCCCCCCCC
63.7019824243
140UbiquitinationVQVKKDLKTGHSKGF
EEEECCCCCCCCCCC
63.7021890473
1402-HydroxyisobutyrylationVQVKKDLKTGHSKGF
EEEECCCCCCCCCCC
63.70-
145AcetylationDLKTGHSKGFGFVRF
CCCCCCCCCCCEEEE
53.2177040215
145SumoylationDLKTGHSKGFGFVRF
CCCCCCCCCCCEEEE
53.21-
145UbiquitinationDLKTGHSKGFGFVRF
CCCCCCCCCCCEEEE
53.2121890473
145SumoylationDLKTGHSKGFGFVRF
CCCCCCCCCCCEEEE
53.21-
145 (in isoform 2)Ubiquitination-53.21-
147UbiquitinationKTGHSKGFGFVRFTE
CCCCCCCCCEEEEEE
8.6821890473
153PhosphorylationGFGFVRFTEYETQVK
CCCEEEEEEEEEHHH
27.3920068231
155PhosphorylationGFVRFTEYETQVKVM
CEEEEEEEEEHHHEE
22.6328796482
155NitrationGFVRFTEYETQVKVM
CEEEEEEEEEHHHEE
22.63-
157PhosphorylationVRFTEYETQVKVMSQ
EEEEEEEEHHHEEEC
37.4528152594
160SumoylationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.54-
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5421890473
160SumoylationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.54-
160 (in isoform 2)Ubiquitination-23.54-
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5421890473
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5421890473
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5421890473
160AcetylationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5426051181
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.5421890473
162OxidationYETQVKVMSQRHMID
EEEHHHEEECCCCCC
2.0417322306
176SumoylationDGRWCDCKLPNSKQS
CCCEECCCCCCCCCC
54.45-
176UbiquitinationDGRWCDCKLPNSKQS
CCCEECCCCCCCCCC
54.4521890473
176SumoylationDGRWCDCKLPNSKQS
CCCEECCCCCCCCCC
54.45-
176 (in isoform 2)Ubiquitination-54.45-
176AcetylationDGRWCDCKLPNSKQS
CCCEECCCCCCCCCC
54.4525953088
180PhosphorylationCDCKLPNSKQSQDEP
ECCCCCCCCCCCCCC
30.0828450419
181MethylationDCKLPNSKQSQDEPL
CCCCCCCCCCCCCCH
61.68184427
181SumoylationDCKLPNSKQSQDEPL
CCCCCCCCCCCCCCH
61.68-
181UbiquitinationDCKLPNSKQSQDEPL
CCCCCCCCCCCCCCH
61.6821890473
181SumoylationDCKLPNSKQSQDEPL
CCCCCCCCCCCCCCH
61.6828112733
181 (in isoform 2)Ubiquitination-61.68-
1812-HydroxyisobutyrylationDCKLPNSKQSQDEPL
CCCCCCCCCCCCCCH
61.68-
183PhosphorylationKLPNSKQSQDEPLRS
CCCCCCCCCCCCHHH
43.2525159151
192AcetylationDEPLRSRKVFVGRCT
CCCHHHCCEEEEECC
41.0777040213
192SumoylationDEPLRSRKVFVGRCT
CCCHHHCCEEEEECC
41.07-
192UbiquitinationDEPLRSRKVFVGRCT
CCCHHHCCEEEEECC
41.0721890473
192SumoylationDEPLRSRKVFVGRCT
CCCHHHCCEEEEECC
41.07-
192 (in isoform 2)Ubiquitination-41.07-
214PhosphorylationLREFFSQYGDVMDVF
HHHHHHHHCCEEEEE
17.6927642862
224UbiquitinationVMDVFIPKPFRAFAF
EEEEECCCCEEEEEE
52.55-
242PhosphorylationADDQIAQSLCGEDLI
CCHHHHHHHHCCCEE
19.3330624053
244GlutathionylationDQIAQSLCGEDLIIK
HHHHHHHHCCCEEEE
7.3122555962
254PhosphorylationDLIIKGISVHISNAE
CEEEEEEEEEECCCC
19.1330108239
258PhosphorylationKGISVHISNAEPKHN
EEEEEEECCCCCCCC
18.3428348404
263SumoylationHISNAEPKHNSNRQL
EECCCCCCCCCCCCH
47.09-
263UbiquitinationHISNAEPKHNSNRQL
EECCCCCCCCCCCCH
47.0921890473
263SumoylationHISNAEPKHNSNRQL
EECCCCCCCCCCCCH
47.0928112733
263 (in isoform 2)Ubiquitination-47.09-
273PhosphorylationSNRQLERSGRFGGNP
CCCCHHHCCCCCCCC
25.5822115753
275MethylationRQLERSGRFGGNPGG
CCHHHCCCCCCCCCC
28.43115918217
292PhosphorylationNQGGFGNSRGGGAGL
CCCCCCCCCCCCCCC
32.4523401153
293MethylationQGGFGNSRGGGAGLG
CCCCCCCCCCCCCCC
52.3424129315
305PhosphorylationGLGNNQGSNMGGGMN
CCCCCCCCCCCCCCC
17.5522817900
307SulfoxidationGNNQGSNMGGGMNFG
CCCCCCCCCCCCCCC
5.8933144500
311SulfoxidationGSNMGGGMNFGAFSI
CCCCCCCCCCCCCCC
4.2033144500
317PhosphorylationGMNFGAFSINPAMMA
CCCCCCCCCCHHHHH
22.41-
322SulfoxidationAFSINPAMMAAAQAA
CCCCCHHHHHHHHHH
1.6633144500
323SulfoxidationFSINPAMMAAAQAAL
CCCCHHHHHHHHHHH
2.2033144500
333PhosphorylationAQAALQSSWGMMGML
HHHHHHHHHHHHHHH
18.06-
336SulfoxidationALQSSWGMMGMLASQ
HHHHHHHHHHHHHHH
1.3833144500
337SulfoxidationLQSSWGMMGMLASQQ
HHHHHHHHHHHHHHC
2.2233144500
339SulfoxidationSSWGMMGMLASQQNQ
HHHHHHHHHHHHCCC
1.2133144500
342PhosphorylationGMMGMLASQQNQSGP
HHHHHHHHHCCCCCC
28.4722817900
347PhosphorylationLASQQNQSGPSGNNQ
HHHHCCCCCCCCCCC
61.2922817900
350PhosphorylationQQNQSGPSGNNQNQG
HCCCCCCCCCCCCCC
58.6522817900
359SulfoxidationNNQNQGNMQREPNQA
CCCCCCCCCCCCCCC
5.2033144500
369PhosphorylationEPNQAFGSGNNSYSG
CCCCCCCCCCCCCCC
31.7122817900
375PhosphorylationGSGNNSYSGSNSGAA
CCCCCCCCCCCCCCE
35.2522817900
377PhosphorylationGNNSYSGSNSGAAIG
CCCCCCCCCCCCEEE
23.1422817900
379PhosphorylationNSYSGSNSGAAIGWG
CCCCCCCCCCEEECC
31.3518546284
387PhosphorylationGAAIGWGSASNAGSG
CCEEECCCCCCCCCC
23.2422817900
389PhosphorylationAIGWGSASNAGSGSG
EEECCCCCCCCCCCC
28.9822817900
393PhosphorylationGSASNAGSGSGFNGG
CCCCCCCCCCCCCCC
27.6322817900
395PhosphorylationASNAGSGSGFNGGFG
CCCCCCCCCCCCCCC
41.7422817900
403PhosphorylationGFNGGFGSSMDSKSS
CCCCCCCCCCCCCCC
21.8918546284
404PhosphorylationFNGGFGSSMDSKSSG
CCCCCCCCCCCCCCC
27.3018546284
405SulfoxidationNGGFGSSMDSKSSGW
CCCCCCCCCCCCCCC
7.8533144500
407PhosphorylationGFGSSMDSKSSGWGM
CCCCCCCCCCCCCCC
26.2922817900
408SumoylationFGSSMDSKSSGWGM-
CCCCCCCCCCCCCC-
44.36-
409PhosphorylationGSSMDSKSSGWGM--
CCCCCCCCCCCCC--
37.7319235466
410PhosphorylationSSMDSKSSGWGM---
CCCCCCCCCCCC---
42.1519235466
414SulfoxidationSKSSGWGM-------
CCCCCCCC-------
3.9133144500

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
2SPhosphorylationKinaseCSNK1A1P48729
GPS
4YPhosphorylationKinaseCSNK1A1P48729
GPS
25TPhosphorylationKinaseCSNK1A1P48729
GPS
88TPhosphorylationKinaseCSNK1A1P48729
GPS
91SPhosphorylationKinaseCSNK1A1P48729
GPS
92SPhosphorylationKinaseCSNK1DP48730
GPS
92SPhosphorylationKinaseCSNK1A1P48729
GPS
116TPhosphorylationKinaseCSNK1A1P48729
GPS
153TPhosphorylationKinaseMEK1Q02750
PSP
155YPhosphorylationKinaseMEK1Q02750
PSP
183SPhosphorylationKinaseCSNK1A1P48729
GPS
242SPhosphorylationKinaseCSNK1A1P48729
GPS
254SPhosphorylationKinaseCSNK1A1P48729
GPS
273SPhosphorylationKinaseCSNK1A1P48729
GPS
292SPhosphorylationKinaseCSNK1DP48730
GPS
292SPhosphorylationKinaseCSNK1A1P48729
GPS
305SPhosphorylationKinaseCSNK1A1P48729
GPS
305SPhosphorylationKinaseCSNK1DP48730
GPS
317SPhosphorylationKinaseCSNK1DP48730
GPS
333SPhosphorylationKinaseCSNK1DP48730
GPS
342SPhosphorylationKinaseCSNK1A1P48729
GPS
347SPhosphorylationKinaseCSNK1A1P48729
GPS
350SPhosphorylationKinaseCSNK1A1P48729
GPS
369SPhosphorylationKinaseCSNK1A1P48729
GPS
375SPhosphorylationKinaseCSNK1A1P48729
GPS
377SPhosphorylationKinaseCSNK1A1P48729
GPS
379SPhosphorylationKinaseCSNK2A1P68400
GPS
379SPhosphorylationKinaseCSNK1A1P48729
GPS
387SPhosphorylationKinaseCSNK1A1P48729
GPS
389SPhosphorylationKinaseCSNK1DP48730
GPS
389SPhosphorylationKinaseCSNK1A1P48729
GPS
393SPhosphorylationKinaseCSNK1DP48730
GPS
393SPhosphorylationKinaseCSNK1A1P48729
GPS
395SPhosphorylationKinaseCSNK1A1P48729
GPS
395SPhosphorylationKinaseCSNK1DP48730
GPS
403SPhosphorylationKinaseCSNK1A1P48729
GPS
403SPhosphorylationKinaseCSNK1DP48730
GPS
404SPhosphorylationKinaseCSNK1DP48730
GPS
404SPhosphorylationKinaseCSNK1A1P48729
GPS
407SPhosphorylationKinaseCSNK1A1P48729
GPS
409SPhosphorylationKinaseCSNK1A1P48729
GPS
409SPhosphorylationKinaseCSNK1DP48730
GPS
409SPhosphorylationKinaseCSNK2A1P68400
GPS
409SPhosphorylationKinaseCSNK1EP49674
GPS
410SPhosphorylationKinaseCSNK1DP48730
GPS
410SPhosphorylationKinaseCSNK1EP49674
GPS
410SPhosphorylationKinaseCSNK2A1P68400
GPS
410SPhosphorylationKinaseCSNK1A1P48729
GPS
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:23258539

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TADBP_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 TADBP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
16169070
ZHX1_HUMANZHX1physical
16169070
HDAC6_HUMANHDAC6physical
19910924
THP2_YEASTTHP2genetic
21508314
MFT1_YEASTMFT1genetic
21508314
TEX1_YEASTTEX1genetic
21508314
THO2_YEASTTHO2genetic
21508314
RPB2_YEASTRPB2genetic
21508314
FUS_HUMANFUSphysical
20720006
PABP2_HUMANPABPN1physical
20720006
TERA_HUMANVCPphysical
19237541
SQSTM_HUMANSQSTM1physical
22674379
SQSTM_HUMANSQSTM1physical
18584184
ARG28_HUMANARHGEF28physical
22941224
HSP74_HUMANHSPA4physical
20804554
HS90A_HUMANHSP90AA1physical
20804554
NACC1_HUMANNACC1physical
23022214
A4_HUMANAPPphysical
21832049
U2AF2_HUMANU2AF2physical
22939629
PRKN_MOUSEPark2physical
23258539
HDAC6_MOUSEHdac6physical
23258539
HNRH1_HUMANHNRNPH1physical
20020773
PABP1_HUMANPABPC1physical
20020773
TADBP_HUMANTARDBPphysical
20020773
DDX21_HUMANDDX21physical
20020773
MSI2H_HUMANMSI2physical
20020773
XRCC6_HUMANXRCC6physical
20020773
ZCCHV_HUMANZC3HAV1physical
20020773
PRC2C_HUMANPRRC2Cphysical
20020773
IF4G1_HUMANEIF4G1physical
20020773
TOP1_HUMANTOP1physical
20020773
LARP4_HUMANLARP4physical
20020773
RS11_HUMANRPS11physical
20020773
MATR3_HUMANMATR3physical
20020773
YTDC2_HUMANYTHDC2physical
20020773
DCD_HUMANDCDphysical
20020773
ROAA_HUMANHNRNPABphysical
20020773
HS105_HUMANHSPH1physical
20020773
HNRL2_HUMANHNRNPUL2physical
20020773
LA_HUMANSSBphysical
20020773
DIM1_HUMANDIMT1physical
20020773
RL5_HUMANRPL5physical
20020773
MSI1H_HUMANMSI1physical
20020773
1433S_HUMANSFNphysical
20020773
STAU1_HUMANSTAU1physical
20020773
XRCC5_HUMANXRCC5physical
20020773
H1X_HUMANH1FXphysical
20020773
DHX57_HUMANDHX57physical
20020773
RS7_HUMANRPS7physical
20020773
FUBP3_HUMANFUBP3physical
20020773
GNL3_HUMANGNL3physical
20020773
HNRPR_HUMANHNRNPRphysical
20020773
RRBP1_HUMANRRBP1physical
20020773
SRPK1_HUMANSRPK1physical
20020773
SRSF6_HUMANSRSF6physical
20020773
TIF1B_HUMANTRIM28physical
20020773
DDX50_HUMANDDX50physical
20020773
PRC2A_HUMANPRRC2Aphysical
20020773
NUFP2_HUMANNUFIP2physical
20020773
PKP1_HUMANPKP1physical
20020773
PAIRB_HUMANSERBP1physical
20020773
LYRIC_HUMANMTDHphysical
20020773
SRRT_HUMANSRRTphysical
20020773
U520_HUMANSNRNP200physical
20020773
ZFR_HUMANZFRphysical
20020773
RS23_HUMANRPS23physical
20020773
RL17_HUMANRPL17physical
20020773
RL28_HUMANRPL28physical
20020773
RL9_HUMANRPL9physical
20020773
NKRF_HUMANNKRFphysical
20020773
NXF1_HUMANNXF1physical
20020773
NOP56_HUMANNOP56physical
20020773
PCBP1_HUMANPCBP1physical
20020773
LC7L2_HUMANLUC7L2physical
20020773
RALY_HUMANRALYphysical
20020773
FBRL_HUMANFBLphysical
20020773
YTHD2_HUMANYTHDF2physical
20020773
RT29_HUMANDAP3physical
20020773
ATX2L_HUMANATXN2Lphysical
20020773
CDC5L_HUMANCDC5Lphysical
20020773
DSC1_HUMANDSC1physical
20020773
RPOM_HUMANPOLRMTphysical
20020773
DSRAD_HUMANADARphysical
20020773
GRSF1_HUMANGRSF1physical
20020773
NCBP1_HUMANNCBP1physical
20020773
NOP58_HUMANNOP58physical
20020773
TSR1_HUMANTSR1physical
20020773
NOP2_HUMANNOP2physical
20020773
TRM1L_HUMANTRMT1Lphysical
20020773
UBP10_HUMANUSP10physical
20020773
RT27_HUMANMRPS27physical
20020773
RM12_HUMANMRPL12physical
20020773
RM22_HUMANMRPL22physical
20020773
RM44_HUMANMRPL44physical
20020773
RS17_HUMANRPS17physical
20020773
XRN1_HUMANXRN1physical
20020773
RL18A_HUMANRPL18Aphysical
20020773
ASPH_HUMANASPHphysical
20020773
BAG2_HUMANBAG2physical
20020773
C1QBP_HUMANC1QBPphysical
20020773
CELF1_HUMANCELF1physical
20020773
ELAV2_HUMANELAVL2physical
20020773
EIF3I_HUMANEIF3Iphysical
20020773
IF4G3_HUMANEIF4G3physical
20020773
RACK1_HUMANGNB2L1physical
20020773
IMA1_HUMANKPNA2physical
20020773
MAP4_HUMANMAP4physical
20020773
MBB1A_HUMANMYBBP1Aphysical
20020773
PYM1_HUMANWIBGphysical
20020773
FA98A_HUMANFAM98Aphysical
20020773
LSM12_HUMANLSM12physical
20020773
PATL1_HUMANPATL1physical
20020773
RFC4_HUMANRFC4physical
20020773
RBM39_HUMANRBM39physical
20020773
RUVB2_HUMANRUVBL2physical
20020773
PURB_HUMANPURBphysical
20020773
TERA_HUMANVCPphysical
20020773
SR140_HUMANU2SURPphysical
20020773
PRPF3_HUMANPRPF3physical
20020773
BCLF1_HUMANBCLAF1physical
20020773
ZC11A_HUMANZC3H11Aphysical
20020773
ZN346_HUMANZNF346physical
20020773
RT34_HUMANMRPS34physical
20020773
RM48_HUMANMRPL48physical
20020773
RS24_HUMANRPS24physical
20020773
XRN2_HUMANXRN2physical
20020773
RL13A_HUMANRPL13Aphysical
20020773
RL21_HUMANRPL21physical
20020773
ATPA_HUMANATP5A1physical
20020773
SCMC3_HUMANSLC25A23physical
20020773
CDK4_HUMANCDK4physical
20020773
CPSF1_HUMANCPSF1physical
20020773
DNJB6_HUMANDNAJB6physical
20020773
IF2G_HUMANEIF2S3physical
20020773
EIF3A_HUMANEIF3Aphysical
20020773
EIF3H_HUMANEIF3Hphysical
20020773
QPCTL_HUMANQPCTLphysical
20020773
NACAM_HUMANNACAphysical
20020773
NACA_HUMANNACAphysical
20020773
AHNK_HUMANAHNAKphysical
20020773
NOP14_HUMANNOP14physical
20020773
NOP16_HUMANNOP16physical
20020773
PWP2_HUMANPWP2physical
20020773
RNF10_HUMANRNF10physical
20020773
SRBD1_HUMANSRBD1physical
20020773
SK2L2_HUMANSKIV2L2physical
20020773
PURA_HUMANPURAphysical
20020773
SNUT1_HUMANSART1physical
20020773
DDX17_HUMANDDX17physical
20020773
HNRL1_HUMANHNRNPUL1physical
20020773
DHX30_HUMANDHX30physical
20020773
DHX36_HUMANDHX36physical
20020773
RENT1_HUMANUPF1physical
20020773
IF2B2_HUMANIGF2BP2physical
20020773
RS2_HUMANRPS2physical
20020773
ROA3_HUMANHNRNPA3physical
20020773
PTBP1_HUMANPTBP1physical
20020773
RS6_HUMANRPS6physical
20020773
RL6_HUMANRPL6physical
20020773
RL26_HUMANRPL26physical
20020773
H13_HUMANHIST1H1Dphysical
20020773
PABP4_HUMANPABPC4physical
20020773
RS20_HUMANRPS20physical
20020773
NPM_HUMANNPM1physical
20020773
RL4_HUMANRPL4physical
20020773
HSP74_HUMANHSPA4physical
20020773
RS14_HUMANRPS14physical
20020773
HNRPM_HUMANHNRNPMphysical
20020773
DESP_HUMANDSPphysical
20020773
LARP1_HUMANLARP1physical
20020773
RL8_HUMANRPL8physical
20020773
FUBP2_HUMANKHSRPphysical
20020773
RS18_HUMANRPS18physical
20020773
RS3A_HUMANRPS3Aphysical
20020773
G3BP1_HUMANG3BP1physical
20020773
GRP78_HUMANHSPA5physical
20020773
ROA0_HUMANHNRNPA0physical
20020773
RS16_HUMANRPS16physical
20020773
HNRPC_HUMANHNRNPCphysical
20020773
RLA0_HUMANRPLP0physical
20020773
EIF3B_HUMANEIF3Bphysical
20020773
RL7_HUMANRPL7physical
20020773
RL12_HUMANRPL12physical
20020773
DDX3X_HUMANDDX3Xphysical
20020773
SRSF7_HUMANSRSF7physical
20020773
ADT2_HUMANSLC25A5physical
20020773
RS9_HUMANRPS9physical
20020773
RSSA_HUMANRPSAphysical
20020773
ILF3_HUMANILF3physical
20020773
DDX5_HUMANDDX5physical
20020773
F120A_HUMANFAM120Aphysical
20020773
RL14_HUMANRPL14physical
20020773
RL11_HUMANRPL11physical
20020773
EIF3C_HUMANEIF3Cphysical
20020773
DDX6_HUMANDDX6physical
20020773
SND1_HUMANSND1physical
20020773
HSP7C_HUMANHSPA8physical
20020773
MOV10_HUMANMOV10physical
20020773
RL3_HUMANRPL3physical
20020773
YBOX3_HUMANYBX3physical
20020773
DHX9_HUMANDHX9physical
20020773
RL7A_HUMANRPL7Aphysical
20020773
ROA1_HUMANHNRNPA1physical
20020773
ELAV1_HUMANELAVL1physical
20020773
TBA1B_HUMANTUBA1Bphysical
20020773
RS3_HUMANRPS3physical
20020773
NUCL_HUMANNCLphysical
20020773
ILF2_HUMANILF2physical
20020773
RL19_HUMANRPL19physical
20020773
RL10A_HUMANRPL10Aphysical
20020773
RL23_HUMANRPL23physical
20020773
G3BP2_HUMANG3BP2physical
20020773
RT22_HUMANMRPS22physical
20020773
RL15_HUMANRPL15physical
20020773
RL32_HUMANRPL32physical
20020773
LRC15_HUMANLRRC15physical
20020773
GGYF2_HUMANGIGYF2physical
20020773
HNRPU_HUMANHNRNPUphysical
20020773
ROA2_HUMANHNRNPA2B1physical
20020773
HNRPQ_HUMANSYNCRIPphysical
20020773
RS4X_HUMANRPS4Xphysical
20020773
RL31_HUMANRPL31physical
20020773
EF2_HUMANEEF2physical
20020773
RBMX_HUMANRBMXphysical
20020773
RL10_HUMANRPL10physical
20020773
HNRDL_HUMANHNRNPDLphysical
20020773
CAPR1_HUMANCAPRIN1physical
20020773
RL13_HUMANRPL13physical
20020773
RS25_HUMANRPS25physical
20020773
RL23A_HUMANRPL23Aphysical
20020773
PLAK_HUMANJUPphysical
20020773
TBB5_HUMANTUBBphysical
20020773
PCBP2_HUMANPCBP2physical
20020773
RL35_HUMANRPL35physical
20020773
RU2A_HUMANSNRPA1physical
20020773
RL22_HUMANRPL22physical
20020773
PRP19_HUMANPRPF19physical
20020773
MYH9_HUMANMYH9physical
20020773
SERA_HUMANPHGDHphysical
20020773
EF1G_HUMANEEF1Gphysical
20020773
AGO2_HUMANAGO2physical
20020773
CCAR2_HUMANCCAR2physical
20020773
SDA1_HUMANSDAD1physical
20020773
TPIS_HUMANTPI1physical
20020773
LSM6_HUMANLSM6physical
24825905
MED6_HUMANMED6physical
24825905
RACK1_HUMANGNB2L1physical
24825905
RBM45_HUMANRBM45physical
24825905
RING2_HUMANRNF2physical
24825905
UB2E3_HUMANUBE2E3physical
24825905
UBP8_HUMANUSP8physical
24825905
STAU1_HUMANSTAU1physical
23125841
TADBP_HUMANTARDBPphysical
19465477
ZFN2B_HUMANZFAND2Bphysical
25416956
SEI1_YEASTFLD1genetic
23104007
RM39_YEASTMRPL39genetic
23104007
MSN2_YEASTMSN2genetic
23104007
NHX1_YEASTNHX1genetic
23104007
RL16B_YEASTRPL16Bgenetic
23104007
IF4F1_YEASTTIF4631genetic
23104007
CCE1_YEASTCCE1genetic
23104007
DBR1_YEASTDBR1genetic
23104007
DOM34_YEASTDOM34genetic
23104007
PBP1_YEASTPBP1genetic
23104007
RL16A_YEASTRPL16Agenetic
23104007
SET3_YEASTSET3genetic
23104007
SIW14_YEASTSIW14genetic
23104007
OCA6_YEASTOCA6genetic
23104007
HS104_YEASTHSP104genetic
25062688
ATX2_HUMANATXN2physical
26344197
FLNB_HUMANFLNBphysical
26344197
GMFB_HUMANGMFBphysical
26344197
KIF4B_HUMANKIF4Bphysical
26344197
TYW4_HUMANLCMT2physical
26344197
PDCD6_HUMANPDCD6physical
26344197
PDIA3_HUMANPDIA3physical
26344197
CUL2_HUMANCUL2physical
26751167
VHL_HUMANVHLphysical
26751167
NCF2_HUMANNCF2physical
28514442
NCAM1_HUMANNCAM1physical
28514442
EPHA2_HUMANEPHA2physical
28514442
SIS1_YEASTSIS1genetic
28531192
DNJB1_HUMANDNAJB1genetic
28531192

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612069Amyotrophic lateral sclerosis 10 (ALS10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TADBP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-92, AND MASSSPECTROMETRY.

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