TAB2_HUMAN - dbPTM
TAB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAB2_HUMAN
UniProt AC Q9NYJ8
Protein Name TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
Gene Name TAB2
Organism Homo sapiens (Human).
Sequence Length 693
Subcellular Localization Membrane
Peripheral membrane protein . Cytoplasm, cytosol . Following IL1 stimulation, translocation occurs from the membrane to cytosol.
Protein Description Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'-linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187'. Involved in heart development..
Protein Sequence MAQGSHQIDFQVLHDLRQKFPEVPEVVVSRCMLQNNNNLDACCAVLSQESTRYLYGEGDLNFSDDSGISGLRNHMTSLNLDLQSQNIYHHGREGSRMNGSRTLTHSISDGQLQGGQSNSELFQQEPQTAPAQVPQGFNVFGMSSSSGASNSAPHLGFHLGSKGTSSLSQQTPRFNPIMVTLAPNIQTGRNTPTSLHIHGVPPPVLNSPQGNSIYIRPYITTPGGTTRQTQQHSGWVSQFNPMNPQQVYQPSQPGPWTTCPASNPLSHTSSQQPNQQGHQTSHVYMPISSPTTSQPPTIHSSGSSQSSAHSQYNIQNISTGPRKNQIEIKLEPPQRNNSSKLRSSGPRTSSTSSSVNSQTLNRNQPTVYIAASPPNTDELMSRSQPKVYISANAATGDEQVMRNQPTLFISTNSGASAASRNMSGQVSMGPAFIHHHPPKSRAIGNNSATSPRVVVTQPNTKYTFKITVSPNKPPAVSPGVVSPTFELTNLLNHPDHYVETENIQHLTDPTLAHVDRISETRKLSMGSDDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSISQIPSLEEMQQLRSCNRQLQIDIDCLTKEIDLFQARGPHFNPSAIHNFYDNIGFVGPVPPKPKDQRSIIKTPKTQDTEDDEGAQWNCTACTFLNHPALIRCEQCEMPRHF
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
53PhosphorylationLSQESTRYLYGEGDL
CCCCCCCHHCCCCCC
12.3627642862
69PhosphorylationFSDDSGISGLRNHMT
CCCCCCCHHHHHHHH
34.9924719451
77PhosphorylationGLRNHMTSLNLDLQS
HHHHHHHHCCCCCHH
14.0028555341
84PhosphorylationSLNLDLQSQNIYHHG
HCCCCCHHCCCCCCC
32.2729978859
88PhosphorylationDLQSQNIYHHGREGS
CCHHCCCCCCCCCCC
8.7027642862
104PhosphorylationMNGSRTLTHSISDGQ
CCCCEEEEEECCCCC
16.9926074081
106PhosphorylationGSRTLTHSISDGQLQ
CCEEEEEECCCCCCC
20.6726074081
108PhosphorylationRTLTHSISDGQLQGG
EEEEEECCCCCCCCC
38.4126074081
166O-linked_GlycosylationLGSKGTSSLSQQTPR
CCCCCCCCHHCCCCC
31.7030059200
168PhosphorylationSKGTSSLSQQTPRFN
CCCCCCHHCCCCCCC
23.3827251275
171PhosphorylationTSSLSQQTPRFNPIM
CCCHHCCCCCCCCEE
14.5927251275
173MethylationSLSQQTPRFNPIMVT
CHHCCCCCCCCEEEE
47.5724129315
173Asymmetric dimethylarginineSLSQQTPRFNPIMVT
CHHCCCCCCCCEEEE
47.57-
180O-linked_GlycosylationRFNPIMVTLAPNIQT
CCCCEEEEECCCCCC
10.3830059200
207PhosphorylationVPPPVLNSPQGNSIY
CCCCCCCCCCCCEEE
17.9029523821
212PhosphorylationLNSPQGNSIYIRPYI
CCCCCCCEEEEEEEE
24.4829523821
329SumoylationRKNQIEIKLEPPQRN
CCCEEEEECCCCCCC
33.73-
329SumoylationRKNQIEIKLEPPQRN
CCCEEEEECCCCCCC
33.73-
343PhosphorylationNNSSKLRSSGPRTSS
CCCHHCCCCCCCCCC
50.5126699800
344PhosphorylationNSSKLRSSGPRTSST
CCHHCCCCCCCCCCC
46.5126699800
348PhosphorylationLRSSGPRTSSTSSSV
CCCCCCCCCCCCCCC
30.1128450419
349PhosphorylationRSSGPRTSSTSSSVN
CCCCCCCCCCCCCCC
32.6628450419
350O-linked_GlycosylationSSGPRTSSTSSSVNS
CCCCCCCCCCCCCCH
31.5330059200
350PhosphorylationSSGPRTSSTSSSVNS
CCCCCCCCCCCCCCH
31.5325394399
351PhosphorylationSGPRTSSTSSSVNSQ
CCCCCCCCCCCCCHH
32.1830576142
352PhosphorylationGPRTSSTSSSVNSQT
CCCCCCCCCCCCHHC
23.6728450419
353PhosphorylationPRTSSTSSSVNSQTL
CCCCCCCCCCCHHCC
38.0929083192
354O-linked_GlycosylationRTSSTSSSVNSQTLN
CCCCCCCCCCHHCCC
25.7030059200
354PhosphorylationRTSSTSSSVNSQTLN
CCCCCCCCCCHHCCC
25.7029083192
366PhosphorylationTLNRNQPTVYIAASP
CCCCCCCEEEEEECC
19.0425002506
368PhosphorylationNRNQPTVYIAASPPN
CCCCCEEEEEECCCC
6.3227794612
372PhosphorylationPTVYIAASPPNTDEL
CEEEEEECCCCHHHH
31.6928355574
376PhosphorylationIAASPPNTDELMSRS
EEECCCCHHHHHHCC
36.3022199227
381PhosphorylationPNTDELMSRSQPKVY
CCHHHHHHCCCCEEE
41.2130576142
388PhosphorylationSRSQPKVYISANAAT
HCCCCEEEEECCCCC
8.6928176443
390PhosphorylationSQPKVYISANAATGD
CCCEEEEECCCCCCC
9.5928176443
395PhosphorylationYISANAATGDEQVMR
EEECCCCCCCHHHHH
42.6328176443
406PhosphorylationQVMRNQPTLFISTNS
HHHHHCCEEEEECCC
25.2428176443
410PhosphorylationNQPTLFISTNSGASA
HCCEEEEECCCCCCH
17.7528176443
411PhosphorylationQPTLFISTNSGASAA
CCEEEEECCCCCCHH
28.7028176443
413PhosphorylationTLFISTNSGASAASR
EEEEECCCCCCHHHC
35.5128176443
416PhosphorylationISTNSGASAASRNMS
EECCCCCCHHHCCCC
28.0828176443
419PhosphorylationNSGASAASRNMSGQV
CCCCCHHHCCCCCCC
24.7328176443
423PhosphorylationSAASRNMSGQVSMGP
CHHHCCCCCCCCCCC
29.6222817900
427PhosphorylationRNMSGQVSMGPAFIH
CCCCCCCCCCCCCCC
15.3328555341
440PhosphorylationIHHHPPKSRAIGNNS
CCCCCCCCCCCCCCC
32.49-
441MethylationHHHPPKSRAIGNNSA
CCCCCCCCCCCCCCC
36.03115918093
447O-linked_GlycosylationSRAIGNNSATSPRVV
CCCCCCCCCCCCEEE
36.6030059200
447PhosphorylationSRAIGNNSATSPRVV
CCCCCCCCCCCCEEE
36.6021955146
449PhosphorylationAIGNNSATSPRVVVT
CCCCCCCCCCEEEEE
38.8025159151
450PhosphorylationIGNNSATSPRVVVTQ
CCCCCCCCCEEEEEC
15.4928355574
456O-linked_GlycosylationTSPRVVVTQPNTKYT
CCCEEEEECCCCEEE
27.0530059200
456PhosphorylationTSPRVVVTQPNTKYT
CCCEEEEECCCCEEE
27.05-
460O-linked_GlycosylationVVVTQPNTKYTFKIT
EEEECCCCEEEEEEE
31.9230059200
467PhosphorylationTKYTFKITVSPNKPP
CEEEEEEEECCCCCC
18.6025921289
469PhosphorylationYTFKITVSPNKPPAV
EEEEEEECCCCCCCC
17.6928464451
477PhosphorylationPNKPPAVSPGVVSPT
CCCCCCCCCCCCCCC
20.3129496963
482PhosphorylationAVSPGVVSPTFELTN
CCCCCCCCCCEEHHH
18.8029496963
484PhosphorylationSPGVVSPTFELTNLL
CCCCCCCCEEHHHHH
23.4120068231
488PhosphorylationVSPTFELTNLLNHPD
CCCCEEHHHHHCCCC
19.3420068231
497PhosphorylationLLNHPDHYVETENIQ
HHCCCCCEEECCCCC
13.8328464451
500PhosphorylationHPDHYVETENIQHLT
CCCCEEECCCCCCCC
25.0420068231
507PhosphorylationTENIQHLTDPTLAHV
CCCCCCCCCCCHHCH
37.5020068231
510PhosphorylationIQHLTDPTLAHVDRI
CCCCCCCCHHCHHHH
39.1120068231
522UbiquitinationDRISETRKLSMGSDD
HHHHHHHCCCCCCCC
52.94-
524PhosphorylationISETRKLSMGSDDAA
HHHHHCCCCCCCCHH
24.9225159151
527PhosphorylationTRKLSMGSDDAAYTQ
HHCCCCCCCCHHHHH
24.5523401153
532PhosphorylationMGSDDAAYTQALLVH
CCCCCHHHHHHHHHH
10.9123927012
533PhosphorylationGSDDAAYTQALLVHQ
CCCCHHHHHHHHHHH
11.5723927012
580PhosphorylationTRRRLKRSNSISQIP
HHHHHHHCCCHHHCC
33.0830266825
582PhosphorylationRRLKRSNSISQIPSL
HHHHHCCCHHHCCCH
25.5130266825
584PhosphorylationLKRSNSISQIPSLEE
HHHCCCHHHCCCHHH
23.1330266825
588PhosphorylationNSISQIPSLEEMQQL
CCHHHCCCHHHHHHH
50.4728450419
597PhosphorylationEEMQQLRSCNRQLQI
HHHHHHHHCCCCCEE
25.0829978859
611UbiquitinationIDIDCLTKEIDLFQA
EEHHHHHCCCCHHHH
39.46-
632PhosphorylationPSAIHNFYDNIGFVG
HHHHHHHHCCCCCCC
17.2527642862
644UbiquitinationFVGPVPPKPKDQRSI
CCCCCCCCCCCHHCC
59.64-
650PhosphorylationPKPKDQRSIIKTPKT
CCCCCHHCCCCCCCC
24.0424719451
653UbiquitinationKDQRSIIKTPKTQDT
CCHHCCCCCCCCCCC
58.04-
654PhosphorylationDQRSIIKTPKTQDTE
CHHCCCCCCCCCCCC
21.4324719451
656UbiquitinationRSIIKTPKTQDTEDD
HCCCCCCCCCCCCCC
65.14-
657PhosphorylationSIIKTPKTQDTEDDE
CCCCCCCCCCCCCCC
32.6422210691
660PhosphorylationKTPKTQDTEDDEGAQ
CCCCCCCCCCCCCCE
31.3422210691
671PhosphorylationEGAQWNCTACTFLNH
CCCEEECCCCCCCCC
22.8922210691
674PhosphorylationQWNCTACTFLNHPAL
EEECCCCCCCCCCEE
28.7922210691

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
-KUbiquitinationE3 ubiquitin ligaseRBCK1Q9BYM8
PMID:17449468

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAB2_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 TAB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CISY_HUMANCSphysical
14743216
TAB1_HUMANTAB1physical
14743216
M3K7_HUMANMAP3K7physical
14670075
TAB1_HUMANTAB1physical
14670075
TAB3_HUMANTAB3physical
14633987
TAB2_HUMANTAB2physical
14633987
TRAF6_HUMANTRAF6physical
14633987
HDAC3_HUMANHDAC3physical
12150997
HDAC1_HUMANHDAC1physical
12150997
HDAC5_HUMANHDAC5physical
12150997
TBL1X_HUMANTBL1Xphysical
12150997
NCOR1_HUMANNCOR1physical
12150997
NFKB1_HUMANNFKB1physical
12150997
M3K7_MOUSEMap3k7physical
10882101
TRAF6_HUMANTRAF6physical
10882101
TRAF2_HUMANTRAF2physical
10882101
TAB1_HUMANTAB1physical
10882101
M3K7_HUMANMAP3K7physical
10882101
TRAF6_HUMANTRAF6physical
11259596
TAB2_HUMANTAB2physical
11259596
NUMBL_HUMANNUMBLphysical
18299187
TRAF6_HUMANTRAF6physical
18180283
IRAK1_HUMANIRAK1physical
18180283
M3K7_HUMANMAP3K7physical
14633987
TRAF2_HUMANTRAF2physical
14633987
UBC_HUMANUBCphysical
19935683
M3K7_HUMANMAP3K7physical
16603398
RIPK1_HUMANRIPK1physical
16603398
IRAK1_HUMANIRAK1physical
19675569
TRAF6_HUMANTRAF6physical
19675569
TAB1_HUMANTAB1physical
21903422
TAB3_HUMANTAB3physical
21903422
M3K7_HUMANMAP3K7physical
21903422
M3K7_HUMANMAP3K7physical
18021073
TAB1_HUMANTAB1physical
18021073
TR30A_MOUSETrim30aphysical
18345001
BECN1_HUMANBECN1physical
22081109
M3K7_HUMANMAP3K7physical
22081109
TAB1_HUMANTAB1physical
19393267
ESR1_HUMANESR1physical
22249258
UBC_HUMANUBCphysical
19927120
UBC_HUMANUBCphysical
22819327
UBC_HUMANUBCphysical
15327770
TRAF6_HUMANTRAF6physical
15327770
RIPK1_HUMANRIPK1physical
15327770
HOIL1_HUMANRBCK1physical
17449468
TANK_HUMANTANKphysical
15327770
TRAF6_HUMANTRAF6physical
17720800
M3K7_MOUSEMap3k7physical
17158449
PDLI7_HUMANPDLIM7physical
16446357
TAB1_HUMANTAB1physical
17626013
NR2C2_HUMANNR2C2physical
17626013
NEMO_HUMANIKBKGphysical
17626013
IRAK1_HUMANIRAK1physical
12242293
TRAF6_HUMANTRAF6physical
12242293
TAB1_HUMANTAB1physical
12242293
M3K7_HUMANMAP3K7physical
12242293
SMAD7_HUMANSMAD7physical
17384642
M3K7_HUMANMAP3K7physical
17384642
TRAF2_HUMANTRAF2physical
17384642
EDAD_HUMANEDARADDphysical
16251197
M3K7_HUMANMAP3K7physical
20194509
NLK_HUMANNLKphysical
20194509
BECN1_HUMANBECN1physical
21976705
ATG5_HUMANATG5physical
21976705
ANDR_HUMANARphysical
16469706
TBL1R_HUMANTBL1XR1physical
16469706
MBD3_HUMANMBD3physical
16469706
SIN3A_HUMANSIN3Aphysical
16469706
A4_HUMANAPPphysical
21832049
WDR34_HUMANWDR34physical
19521662
BST2_HUMANBST2physical
23221546
IKKB_HUMANIKBKBphysical
21811235
UBC_HUMANUBCphysical
21811235
UBC_HUMANUBCphysical
23807287
TRI22_HUMANTRIM22physical
23818111
ZBT16_HUMANZBTB16physical
21988832
TGM2_HUMANTGM2physical
21988832
VIME_HUMANVIMphysical
21988832
PP2AB_HUMANPPP2CBphysical
21988832
TRAF6_HUMANTRAF6physical
21988832
1433Z_HUMANYWHAZphysical
21988832
NUMBL_HUMANNUMBLphysical
21988832
S19A3_HUMANSLC19A3physical
21988832
SIK3_HUMANSIK3physical
24061540
SIK1_HUMANSIK1physical
24061540
TRI38_HUMANTRIM38physical
24434549
IRAK1_HUMANIRAK1physical
24735611
TRAF6_HUMANTRAF6physical
24735611
PIAS3_HUMANPIAS3physical
24096733
UBC_HUMANUBCphysical
25296760
UBC_HUMANUBCphysical
19373254
UBC_HUMANUBCphysical
23986494
NEMO_HUMANIKBKGphysical
23986494
IRAK1_HUMANIRAK1physical
23986494
UBC_HUMANUBCphysical
25527291
M3K7_HUMANMAP3K7physical
25642820
RNF4_HUMANRNF4physical
26299341
M3K7_HUMANMAP3K7physical
27426733
ESR1_HUMANESR1physical
27992601
ANDR_HUMANARphysical
27992601

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614980Congenital heart defects, multiple types, 2 (CHTD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAB2_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-450, 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-372, AND MASSSPECTROMETRY.

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