TAB1_HUMAN - dbPTM
TAB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAB1_HUMAN
UniProt AC Q15750
Protein Name TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
Gene Name TAB1
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization
Protein Description May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis..
Protein Sequence MAAQRRSLLQSEQQPSWTDDLPLCHLSGVGSASNRSYSADGKGTESHPPEDSWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNAEHAEADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLPPQYQKILERLKTLEREISGGAMAVVAVLLNNKLYVANVGTNRALLCKSTVDGLQVTQLNVDHTTENEDELFRLSQLGLDAGKIKQVGIICGQESTRRIGDYKVKYGYTDIDLLSAAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEIAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERARFCPRHEDMTLLVRNFGYPLGEMSQPTPSPAPAAGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGAHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVVTAP
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
7Phosphorylation-MAAQRRSLLQSEQQ
-CHHHHHHHHHCCCC
35.3023927012
11PhosphorylationQRRSLLQSEQQPSWT
HHHHHHHCCCCCCCC
37.0230266825
16PhosphorylationLQSEQQPSWTDDLPL
HHCCCCCCCCCCCCC
37.9730266825
18PhosphorylationSEQQPSWTDDLPLCH
CCCCCCCCCCCCCEE
24.7930266825
27PhosphorylationDLPLCHLSGVGSASN
CCCCEECCCCCCCCC
14.0420068231
31PhosphorylationCHLSGVGSASNRSYS
EECCCCCCCCCCCCC
26.5620068231
33PhosphorylationLSGVGSASNRSYSAD
CCCCCCCCCCCCCCC
34.1820068231
42UbiquitinationRSYSADGKGTESHPP
CCCCCCCCCCCCCCC
64.31-
46O-linked_GlycosylationADGKGTESHPPEDSW
CCCCCCCCCCCCCCC
40.9232574038
52O-linked_GlycosylationESHPPEDSWLKFRSE
CCCCCCCCCEEEECC
32.4232574038
150UbiquitinationQLPPQYQKILERLKT
HCCHHHHHHHHHHHH
44.3021890473
150UbiquitinationQLPPQYQKILERLKT
HCCHHHHHHHHHHHH
44.3021890473
157PhosphorylationKILERLKTLEREISG
HHHHHHHHHHHHHHH
38.1428122231
163PhosphorylationKTLEREISGGAMAVV
HHHHHHHHHHHHHHH
26.8228857561
179PhosphorylationVLLNNKLYVANVGTN
HHHCCEEEEEECCCC
10.1021406692
185PhosphorylationLYVANVGTNRALLCK
EEEEECCCCCEEEEE
19.7621406692
192UbiquitinationTNRALLCKSTVDGLQ
CCCEEEEECCCCCEE
49.48-
227UbiquitinationQLGLDAGKIKQVGII
HCCCCCCCCCEEEEE
48.75-
229UbiquitinationGLDAGKIKQVGIICG
CCCCCCCCEEEEEEC
42.28-
249UbiquitinationRIGDYKVKYGYTDID
CCCCEEEEECCCCHH
28.89-
259PhosphorylationYTDIDLLSAAKSKPI
CCCHHHHHHHHCCCE
33.2124719451
262UbiquitinationIDLLSAAKSKPIIAE
HHHHHHHHCCCEEEC
59.74-
264UbiquitinationLLSAAKSKPIIAEPE
HHHHHHCCCEEECCC
39.26-
339PhosphorylationDRVKRIHSDTFASGG
HHHHHHHCCCCCCCC
35.6527251275
373PhosphorylationGYPLGEMSQPTPSPA
CCCCCCCCCCCCCCC
28.8029978859
376PhosphorylationLGEMSQPTPSPAPAA
CCCCCCCCCCCCCCC
28.8529978859
378PhosphorylationEMSQPTPSPAPAAGG
CCCCCCCCCCCCCCC
35.8526055452
391O-linked_GlycosylationGGRVYPVSVPYSSAQ
CCCEEEEECCCCCCC
16.9332574038
395O-linked_GlycosylationYPVSVPYSSAQSTSK
EEEECCCCCCCCCCC
17.0932574038
396O-linked_GlycosylationPVSVPYSSAQSTSKT
EEECCCCCCCCCCCC
25.2032574038
396PhosphorylationPVSVPYSSAQSTSKT
EEECCCCCCCCCCCC
25.2028555341
399O-linked_GlycosylationVPYSSAQSTSKTSVT
CCCCCCCCCCCCEEE
34.0732574038
399PhosphorylationVPYSSAQSTSKTSVT
CCCCCCCCCCCCEEE
34.0728555341
400O-linked_GlycosylationPYSSAQSTSKTSVTL
CCCCCCCCCCCEEEE
23.3532574038
401PhosphorylationYSSAQSTSKTSVTLS
CCCCCCCCCCEEEEE
38.9028555341
401O-linked_GlycosylationYSSAQSTSKTSVTLS
CCCCCCCCCCEEEEE
38.9032574038
403O-linked_GlycosylationSAQSTSKTSVTLSLV
CCCCCCCCEEEEEEE
28.3532574038
406O-linked_GlycosylationSTSKTSVTLSLVMPS
CCCCCEEEEEEECCC
15.4732574038
423O-linked_GlycosylationQMVNGAHSASTLDEA
CEECCCCCCCCCCCC
24.3132574038
423PhosphorylationQMVNGAHSASTLDEA
CEECCCCCCCCCCCC
24.3119076070
431PhosphorylationASTLDEATPTLTNQS
CCCCCCCCCCCCCCC
18.1115590691
433PhosphorylationTLDEATPTLTNQSPT
CCCCCCCCCCCCCCE
41.6926074081
435PhosphorylationDEATPTLTNQSPTLT
CCCCCCCCCCCCEEE
33.4226074081
438PhosphorylationTPTLTNQSPTLTLQS
CCCCCCCCCEEEEEE
23.1726074081
440PhosphorylationTLTNQSPTLTLQSTN
CCCCCCCEEEEEECC
37.3126074081
442PhosphorylationTNQSPTLTLQSTNTH
CCCCCEEEEEECCCC
25.8126074081
445PhosphorylationSPTLTLQSTNTHTQS
CCEEEEEECCCCCCC
27.0826074081
446PhosphorylationPTLTLQSTNTHTQSS
CEEEEEECCCCCCCC
31.0426074081
450O-linked_GlycosylationLQSTNTHTQSSSSSS
EEECCCCCCCCCCCC
28.2732574038
452PhosphorylationSTNTHTQSSSSSSDG
ECCCCCCCCCCCCCC
33.0922216226
453PhosphorylationTNTHTQSSSSSSDGG
CCCCCCCCCCCCCCC
25.1522216226
456PhosphorylationHTQSSSSSSDGGLFR
CCCCCCCCCCCCCCC
34.1022216226
457PhosphorylationTQSSSSSSDGGLFRS
CCCCCCCCCCCCCCC
42.0722216226
469PhosphorylationFRSRPAHSLPPGEDG
CCCCCCCCCCCCCCC
44.6828857561
481PhosphorylationEDGRVEPYVDFAEFY
CCCCCCCCCCHHHHH
10.1127642862
488PhosphorylationYVDFAEFYRLWSVDH
CCCHHHHHHHHCCCC
9.0527642862
492PhosphorylationAEFYRLWSVDHGEQS
HHHHHHHCCCCCCCC
23.4328348404
499PhosphorylationSVDHGEQSVVTAP--
CCCCCCCCEEECC--
17.7928555341
502O-linked_GlycosylationHGEQSVVTAP-----
CCCCCEEECC-----
30.9332574038
502PhosphorylationHGEQSVVTAP-----
CCCCCEEECC-----
30.9329978859

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
423SPhosphorylationKinaseMAPK14Q16539
GPS
431TPhosphorylationKinaseMAPK14Q16539
GPS
438SPhosphorylationKinaseERK2P28482
PSP
438SPhosphorylationKinaseERK1P27361
PSP
438SPhosphorylationKinaseJNK1P45983
PSP
438SPhosphorylationKinaseJNK2P45984
PSP
438SPhosphorylationKinaseMAPK14Q16539
GPS
452SPhosphorylationKinaseMAP3K7O43318
GPS
452SPhosphorylationKinaseMAPK14Q16539
GPS
453SPhosphorylationKinaseMAP3K7O43318
GPS
453SPhosphorylationKinaseMAPK14Q16539
GPS
456SPhosphorylationKinaseMAP3K7O43318
GPS
456SPhosphorylationKinaseMAPK14Q16539
GPS
457SPhosphorylationKinaseMAP3K7O43318
GPS
457SPhosphorylationKinaseMAPK14Q16539
GPS
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:25714464

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAB1_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 TAB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
14743216
TAB2_HUMANTAB2physical
14670075
TAB3_HUMANTAB3physical
14670075
M3K7_HUMANMAP3K7physical
14670075
M3K7_HUMANMAP3K7physical
12975377
XIAP_HUMANXIAPphysical
9878061
MK14_HUMANMAPK14physical
11847341
ZMY11_HUMANZMYND11physical
9663660
TAB3_HUMANTAB3physical
21903422
M3K7_HUMANMAP3K7physical
21903422
MO4L1_HUMANMORF4L1physical
21903422
MO4L2_HUMANMORF4L2physical
21903422
TAB2_HUMANTAB2physical
21903422
MTG2_HUMANMTG2physical
21900206
PHAR3_HUMANPHACTR3physical
21900206
TLS1_HUMANC9orf78physical
21900206
CAR11_HUMANCARD11physical
21900206
PDC6I_HUMANPDCD6IPphysical
21900206
CASP6_HUMANCASP6physical
21900206
PP1R7_HUMANPPP1R7physical
21900206
GIT1_HUMANGIT1physical
21900206
XPO7_HUMANXPO7physical
21900206
MK14_HUMANMAPK14physical
21900206
NXPH3_HUMANNXPH3physical
21900206
NPA1P_HUMANURB1physical
21900206
PHC2_HUMANPHC2physical
21900206
RPC4_HUMANPOLR3Dphysical
21900206
RL10_HUMANRPL10physical
21900206
ACAP3_HUMANACAP3physical
21900206
KAIN_HUMANSERPINA4physical
21900206
KCRB_HUMANCKBphysical
21900206
COF1_HUMANCFL1physical
21900206
DREB_HUMANDBN1physical
21900206
MICA1_HUMANMICAL1physical
21900206
KIFC2_HUMANKIFC2physical
21900206
MON1A_HUMANMON1Aphysical
21900206
AMPL_HUMANLAP3physical
21900206
ASGL1_HUMANASRGL1physical
21900206
RBX1_HUMANRBX1physical
21900206
MAPK5_HUMANMAPKAPK5physical
21900206
PDIP2_HUMANPOLDIP2physical
21900206
FADD_HUMANFADDphysical
21900206
LCMT1_HUMANLCMT1physical
21900206
PTPM1_HUMANPTPMT1physical
21900206
SYEP_HUMANEPRSphysical
21900206
WDCP_HUMANC2orf44physical
21900206
HNRPR_HUMANHNRNPRphysical
21900206
ARAP1_HUMANARAP1physical
21900206
RLA1_HUMANRPLP1physical
21900206
U1SBP_HUMANSNRNP35physical
21900206
TSSC4_HUMANTSSC4physical
21900206
TP4AP_HUMANTRPC4APphysical
21900206
KAP0_HUMANPRKAR1Aphysical
21900206
IKKB_HUMANIKBKBphysical
18316610
BST2_HUMANBST2physical
23221546
M3K7_HUMANMAP3K7physical
16260783
TRIP6_HUMANTRIP6physical
21988832
FL2D_HUMANWTAPphysical
21988832
PP2AB_HUMANPPP2CBphysical
21988832
2AAA_HUMANPPP2R1Aphysical
21988832
TAB2_HUMANTAB2physical
21988832
MDM2_HUMANMDM2physical
23934659
M3K7_HUMANMAP3K7physical
23934659
XIAP_HUMANXIAPphysical
11865055
BIRC1_HUMANNAIPphysical
11865055
BIRC7_HUMANBIRC7physical
11865055
TAB2_HUMANTAB2physical
19675569
TAB2_HUMANTAB2physical
25260751
ITCH_HUMANITCHphysical
25714464
UBP18_HUMANUSP18physical
26240016
M3K7_HUMANMAP3K7physical
27880917
TAB2_HUMANTAB2physical
27880917
TAB3_HUMANTAB3physical
27880917

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 TAB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, 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-7, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
"The Yersinia enterocolitica effector YopP inhibits host cellsignalling by inactivating the protein kinase TAK1 in the IL-1signalling pathway.";
Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K.,Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K.,Kracht M.;
EMBO Rep. 7:838-844(2006).
Cited for: UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438,AND DEUBIQUITINATION BY YOPP.

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