TBCD4_HUMAN - dbPTM
TBCD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBCD4_HUMAN
UniProt AC O60343
Protein Name TBC1 domain family member 4
Gene Name TBC1D4
Organism Homo sapiens (Human).
Sequence Length 1298
Subcellular Localization Cytoplasm . Isoform 2 shows a cytoplasmic perinuclear localization in a myoblastic cell line in resting and insulin-stimulated cells.
Protein Description May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake..
Protein Sequence MEPPSCIQDEPFPHPLEPEPGVSAQPGPGKPSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRRRSQKPEAGGCGAPAAREVILVLSAPFLRCVPAPGAGASGGTSPSATQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKIQGEQRGPDPGEDLADLEVVVPGSPGDCLPEEADGTDTHLGLPAGASQPALTSSRVCFPERILEDSGFDEQQEFRSRCSSVTGVQRRVHEGSQKSQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPVSDQEENELVILHLRQLCEAKQKTHVHIGEGPSTISNSTIPENATSSGRFKLDILKNKAKRSLTSSLENIFSRGANRMRGRLGSVDSFERSNSLASEKDYSPGDSPPGTPPASPPSSAWQTFPEEDSDSPQFRRRAHTFSHPPSSTKRKLNLQDGRAQGVRSPLLRQSSSEQCSNLSSVRRMYKESNSSSSLPSLHTSFSAPSFTAPSFLKSFYQNSGRLSPQYENEIRQDTASESSDGEGRKRTSSTCSNESLSVGGTSVTPRRISWRQRIFLRVASPMNKSPSAMQQQDGLDRNELLPLSPLSPTMEEEPLVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLEASRDELQSRKVKLDYEEVGACQKEVLITWDKKLLNCRAKIRCDMEDIHTLLKEGVPKSRRGEIWQFLALQYRLRHRLPNKQQPPDISYKELLKQLTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIMECESFENIVEFLKNTLPDMNTSEMEKIITQVFEMDISKQLHAYEVEYHVLQDELQESSYSCEDSETLEKLERANSQLKRQNMDLLEKLQVAHTKIQALESNLENLLTRETKMKSLIRTLEQEKMAYQKTVEQLRKLLPADALVNCDLLLRDLNCNPNNKAKIGNKP
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
1Acetylation-------MEPPSCIQ
-------CCCCCCCC
60.5419413330
4 (in isoform 4)Phosphorylation-45.1625159151
4 (in isoform 5)Phosphorylation-45.1625159151
6 (in isoform 4)Phosphorylation-3.9025159151
6 (in isoform 5)Phosphorylation-3.9025159151
44PhosphorylationRLWYVGGSCLDHRTT
EEEEECCCCCCCCCH
12.9428857561
66PhosphorylationMAEIRRRSQKPEAGG
HHHHHHHCCCCCCCC
40.5217494752
68UbiquitinationEIRRRSQKPEAGGCG
HHHHHCCCCCCCCCC
46.18-
102PhosphorylationPAPGAGASGGTSPSA
ECCCCCCCCCCCCCC
36.5223401153
105PhosphorylationGAGASGGTSPSATQP
CCCCCCCCCCCCCCC
40.7821712546
106PhosphorylationAGASGGTSPSATQPN
CCCCCCCCCCCCCCC
21.8225463755
108PhosphorylationASGGTSPSATQPNPA
CCCCCCCCCCCCCCE
43.6525022875
110PhosphorylationGGTSPSATQPNPAVF
CCCCCCCCCCCCEEE
49.2325022875
133PhosphorylationISRFIHNSHDLTYFA
HHHHHHCCCCHHHEE
12.2927732954
137PhosphorylationIHNSHDLTYFAYLIK
HHCCCCHHHEEEEEC
23.7327732954
138PhosphorylationHNSHDLTYFAYLIKA
HCCCCHHHEEEEECC
8.1027732954
141PhosphorylationHDLTYFAYLIKAQPD
CCHHHEEEEECCCCC
10.0827732954
172PhosphorylationSQVPDVISSIRQLSK
HHCHHHHHHHHHHHH
21.4024719451
173PhosphorylationQVPDVISSIRQLSKA
HCHHHHHHHHHHHHH
15.6325954137
2152-HydroxyisobutyrylationGKVTVTHKKAPSSLI
EEEEEEECCCCCHHH
41.06-
220PhosphorylationTHKKAPSSLIDDCME
EECCCCCHHHHHHHH
28.4328985074
226SulfoxidationSSLIDDCMEKFSLHE
CHHHHHHHHHCCHHH
8.9121406390
228UbiquitinationLIDDCMEKFSLHEQQ
HHHHHHHHCCHHHHH
17.23-
238UbiquitinationLHEQQRLKIQGEQRG
HHHHHHHHHCCHHCC
34.86-
262PhosphorylationLEVVVPGSPGDCLPE
CEEEECCCCCCCCCC
21.4619276368
274PhosphorylationLPEEADGTDTHLGLP
CCCCCCCCCCCCCCC
37.9728387310
276PhosphorylationEEADGTDTHLGLPAG
CCCCCCCCCCCCCCC
20.8827251275
285PhosphorylationLGLPAGASQPALTSS
CCCCCCCCCCCCCCC
35.4620873877
290PhosphorylationGASQPALTSSRVCFP
CCCCCCCCCCCCCCC
27.1127251275
291PhosphorylationASQPALTSSRVCFPE
CCCCCCCCCCCCCCH
19.5927251275
292PhosphorylationSQPALTSSRVCFPER
CCCCCCCCCCCCCHH
24.4027251275
304PhosphorylationPERILEDSGFDEQQE
CHHHHHCCCCCHHHH
31.8025159151
314PhosphorylationDEQQEFRSRCSSVTG
CHHHHHHHHHHHHHC
42.8521712546
317PhosphorylationQEFRSRCSSVTGVQR
HHHHHHHHHHHCCHH
27.0821712546
318PhosphorylationEFRSRCSSVTGVQRR
HHHHHHHHHHCCHHH
27.5923401153
320PhosphorylationRSRCSSVTGVQRRVH
HHHHHHHHCCHHHHC
33.3225262027
330PhosphorylationQRRVHEGSQKSQPRR
HHHHCCCCCCCCCCC
31.3024719451
341PhosphorylationQPRRRHASAPSHVQP
CCCCCCCCCCCCCCC
34.2929255136
344PhosphorylationRRHASAPSHVQPSDS
CCCCCCCCCCCCCCC
35.6922167270
349PhosphorylationAPSHVQPSDSEKNRT
CCCCCCCCCCCCCCE
36.3623927012
351PhosphorylationSHVQPSDSEKNRTML
CCCCCCCCCCCCEEE
55.6023927012
356PhosphorylationSDSEKNRTMLFQVGR
CCCCCCCEEEEEEEE
27.85-
370PhosphorylationRFEINLISPDTKSVV
EEEEEEECCCCCCEE
21.6430266825
373PhosphorylationINLISPDTKSVVLEK
EEEECCCCCCEEEEC
28.7130266825
375PhosphorylationLISPDTKSVVLEKNF
EECCCCCCEEEECCC
21.3923312004
383AcetylationVVLEKNFKDISSCSQ
EEEECCCCCHHHCCC
64.6426051181
383UbiquitinationVVLEKNFKDISSCSQ
EEEECCCCCHHHCCC
64.64-
438PhosphorylationLTLKQAFSTAAALQS
HHHHHHHHHHHHHHH
21.8321406692
439PhosphorylationTLKQAFSTAAALQSA
HHHHHHHHHHHHHHH
17.5421406692
445PhosphorylationSTAAALQSAKTQIKL
HHHHHHHHHHHHHHH
32.3621406692
448PhosphorylationAALQSAKTQIKLCEA
HHHHHHHHHHHHHHH
34.9321406692
477AcetylationGLYPPRAKLVIQRHL
CCCCCHHHHHHHHHH
44.5619608861
485PhosphorylationLVIQRHLSSLTDNEQ
HHHHHHHHHCCCHHH
19.7128348404
486PhosphorylationVIQRHLSSLTDNEQA
HHHHHHHHCCCHHHH
41.4725884760
488PhosphorylationQRHLSSLTDNEQADI
HHHHHHCCCHHHHHH
38.4328450419
542PhosphorylationGPSTISNSTIPENAT
CCCCCCCCCCCCCCC
22.4123312004
543PhosphorylationPSTISNSTIPENATS
CCCCCCCCCCCCCCC
44.8123312004
549PhosphorylationSTIPENATSSGRFKL
CCCCCCCCCCCCCCH
34.7025159151
550PhosphorylationTIPENATSSGRFKLD
CCCCCCCCCCCCCHH
28.5226462736
551PhosphorylationIPENATSSGRFKLDI
CCCCCCCCCCCCHHH
29.6325159151
555UbiquitinationATSSGRFKLDILKNK
CCCCCCCCHHHHCHH
43.84-
560UbiquitinationRFKLDILKNKAKRSL
CCCHHHHCHHHHHHH
57.65-
566PhosphorylationLKNKAKRSLTSSLEN
HCHHHHHHHHHHHHH
34.9826846344
568PhosphorylationNKAKRSLTSSLENIF
HHHHHHHHHHHHHHH
19.9529255136
569PhosphorylationKAKRSLTSSLENIFS
HHHHHHHHHHHHHHH
37.9129255136
570PhosphorylationAKRSLTSSLENIFSR
HHHHHHHHHHHHHHH
34.1729255136
576PhosphorylationSSLENIFSRGANRMR
HHHHHHHHHCHHHHC
26.4723927012
577MethylationSLENIFSRGANRMRG
HHHHHHHHCHHHHCC
37.18-
588PhosphorylationRMRGRLGSVDSFERS
HHCCCCCCCCCCHHH
27.6119664994
591PhosphorylationGRLGSVDSFERSNSL
CCCCCCCCCHHHCCC
27.1819664994
595PhosphorylationSVDSFERSNSLASEK
CCCCCHHHCCCCCCC
24.4722115753
597PhosphorylationDSFERSNSLASEKDY
CCCHHHCCCCCCCCC
26.9322617229
600PhosphorylationERSNSLASEKDYSPG
HHHCCCCCCCCCCCC
50.9322617229
604PhosphorylationSLASEKDYSPGDSPP
CCCCCCCCCCCCCCC
28.0320873877
605PhosphorylationLASEKDYSPGDSPPG
CCCCCCCCCCCCCCC
32.3220873877
609PhosphorylationKDYSPGDSPPGTPPA
CCCCCCCCCCCCCCC
38.6226657352
613PhosphorylationPGDSPPGTPPASPPS
CCCCCCCCCCCCCCC
31.6920873877
617PhosphorylationPPGTPPASPPSSAWQ
CCCCCCCCCCCCHHC
43.0220873877
620PhosphorylationTPPASPPSSAWQTFP
CCCCCCCCCHHCCCC
35.7520873877
621PhosphorylationPPASPPSSAWQTFPE
CCCCCCCCHHCCCCC
39.0220873877
625PhosphorylationPPSSAWQTFPEEDSD
CCCCHHCCCCCCCCC
30.3820873877
631PhosphorylationQTFPEEDSDSPQFRR
CCCCCCCCCCHHHHH
43.1820873877
633PhosphorylationFPEEDSDSPQFRRRA
CCCCCCCCHHHHHHH
25.2620873877
642PhosphorylationQFRRRAHTFSHPPSS
HHHHHHHHCCCCCCC
26.3327273156
644PhosphorylationRRRAHTFSHPPSSTK
HHHHHHCCCCCCCCC
35.9227273156
648PhosphorylationHTFSHPPSSTKRKLN
HHCCCCCCCCCCEEC
55.9023401153
649PhosphorylationTFSHPPSSTKRKLNL
HCCCCCCCCCCEECC
43.6625159151
650PhosphorylationFSHPPSSTKRKLNLQ
CCCCCCCCCCEECCC
38.9225159151
666PhosphorylationGRAQGVRSPLLRQSS
CCCCCCCCHHHHCCC
19.9329255136
666 (in isoform 2)Phosphorylation-19.9325849741
672PhosphorylationRSPLLRQSSSEQCSN
CCHHHHCCCHHHHCC
29.4218669648
672 (in isoform 2)Phosphorylation-29.4223927012
673PhosphorylationSPLLRQSSSEQCSNL
CHHHHCCCHHHHCCH
29.5618669648
673 (in isoform 2)Phosphorylation-29.5623927012
674 (in isoform 2)Phosphorylation-36.6123927012
678PhosphorylationQSSSEQCSNLSSVRR
CCCHHHHCCHHHHHH
40.2618669648
678 (in isoform 2)Phosphorylation-40.2618669648
681PhosphorylationSEQCSNLSSVRRMYK
HHHHCCHHHHHHHHH
30.9124719451
686 (in isoform 2)Phosphorylation-3.8229116813
687 (in isoform 2)Phosphorylation-15.1429116813
688 (in isoform 2)Phosphorylation-45.3725849741
689 (in isoform 2)Phosphorylation-37.3525849741
691 (in isoform 2)Phosphorylation-47.1825849741
701PhosphorylationSSLPSLHTSFSAPSF
CCCCCCCCCCCCCCC
36.4421712546
702PhosphorylationSLPSLHTSFSAPSFT
CCCCCCCCCCCCCCC
13.3730576142
704PhosphorylationPSLHTSFSAPSFTAP
CCCCCCCCCCCCCCH
38.7522817900
707PhosphorylationHTSFSAPSFTAPSFL
CCCCCCCCCCCHHHH
34.6430576142
709PhosphorylationSFSAPSFTAPSFLKS
CCCCCCCCCHHHHHH
41.8330576142
712PhosphorylationAPSFTAPSFLKSFYQ
CCCCCCHHHHHHHHH
40.5224719451
716PhosphorylationTAPSFLKSFYQNSGR
CCHHHHHHHHHHCCC
31.1926437602
716 (in isoform 3)Phosphorylation-31.1926437602
721 (in isoform 3)Phosphorylation-15.1222673903
725PhosphorylationYQNSGRLSPQYENEI
HHHCCCCCHHHHHHH
14.4826437602
725 (in isoform 3)Phosphorylation-14.4826437602
749PhosphorylationDGEGRKRTSSTCSNE
CCCCCCCCCCCCCCC
30.0223927012
750PhosphorylationGEGRKRTSSTCSNES
CCCCCCCCCCCCCCC
27.9023927012
751PhosphorylationEGRKRTSSTCSNESL
CCCCCCCCCCCCCCC
32.5923927012
752PhosphorylationGRKRTSSTCSNESLS
CCCCCCCCCCCCCCC
21.5223927012
754PhosphorylationKRTSSTCSNESLSVG
CCCCCCCCCCCCCCC
43.6625159151
757PhosphorylationSSTCSNESLSVGGTS
CCCCCCCCCCCCCEE
30.1423927012
759PhosphorylationTCSNESLSVGGTSVT
CCCCCCCCCCCEECC
28.1723927012
763PhosphorylationESLSVGGTSVTPRRI
CCCCCCCEECCCCCC
17.6923927012
764PhosphorylationSLSVGGTSVTPRRIS
CCCCCCEECCCCCCC
27.5423927012
766PhosphorylationSVGGTSVTPRRISWR
CCCCEECCCCCCCHH
15.7323927012
771PhosphorylationSVTPRRISWRQRIFL
ECCCCCCCHHHHHHH
17.8824719451
782PhosphorylationRIFLRVASPMNKSPS
HHHHHHCCCCCCCHH
23.0926055452
787PhosphorylationVASPMNKSPSAMQQQ
HCCCCCCCHHHHHHC
21.0523401153
789PhosphorylationSPMNKSPSAMQQQDG
CCCCCCHHHHHHCCC
43.3929255136
791SulfoxidationMNKSPSAMQQQDGLD
CCCCHHHHHHCCCCC
4.3021406390
806PhosphorylationRNELLPLSPLSPTME
HHHCCCCCCCCCCCC
23.1220068231
809PhosphorylationLLPLSPLSPTMEEEP
CCCCCCCCCCCCCCC
23.0028387310
811PhosphorylationPLSPLSPTMEEEPLV
CCCCCCCCCCCCCEE
33.5628464451
822PhosphorylationEPLVVFLSGEDDPEK
CCEEEEECCCCCHHH
28.7722468782
841PhosphorylationKKSKELRSLWRKAIH
HHHHHHHHHHHHHHH
44.9324719451
866PhosphorylationENQKLEASRDELQSR
HHHHHHHCHHHHHHC
30.7827251275
872PhosphorylationASRDELQSRKVKLDY
HCHHHHHHCCCCCCH
46.8527251275
892PhosphorylationCQKEVLITWDKKLLN
CCEEEEEEECHHHHC
24.3728509920
951PhosphorylationKQQPPDISYKELLKQ
CCCCCCCCHHHHHHH
37.2223828894
952PhosphorylationQQPPDISYKELLKQL
CCCCCCCHHHHHHHH
14.6023828894
1044PhosphorylationDLGFRKQYRPDMMSL
HHCCCHHHCCCHHHH
27.4423663014
1050PhosphorylationQYRPDMMSLQIQMYQ
HHCCCHHHHHHHHHH
15.5223401153
1056PhosphorylationMSLQIQMYQLSRLLH
HHHHHHHHHHHHHHH
7.0223663014
1059PhosphorylationQIQMYQLSRLLHDYH
HHHHHHHHHHHHHHH
12.8323663014
1065PhosphorylationLSRLLHDYHRDLYNH
HHHHHHHHHHHHHHH
6.4923401153
1122PhosphorylationVIFKVALSLLSSQET
HHHHHHHHHHCCCCC
19.9523401153
1125PhosphorylationKVALSLLSSQETLIM
HHHHHHHCCCCCEEH
34.9623401153
1126PhosphorylationVALSLLSSQETLIME
HHHHHHCCCCCEEHH
31.8223401153
1153PhosphorylationNTLPDMNTSEMEKII
HHCCCCCHHHHHHHH
21.3022210691
1154PhosphorylationTLPDMNTSEMEKIIT
HCCCCCHHHHHHHHH
29.9122210691
1189PhosphorylationLQDELQESSYSCEDS
HHHHHHHCCCCCCCH
22.9328122231
1190PhosphorylationQDELQESSYSCEDSE
HHHHHHCCCCCCCHH
21.9528122231
1191PhosphorylationDELQESSYSCEDSET
HHHHHCCCCCCCHHH
26.9822817900
1192PhosphorylationELQESSYSCEDSETL
HHHHCCCCCCCHHHH
16.9928122231
1196PhosphorylationSSYSCEDSETLEKLE
CCCCCCCHHHHHHHH
15.3627690223
1198PhosphorylationYSCEDSETLEKLERA
CCCCCHHHHHHHHHH
44.1427690223
1207PhosphorylationEKLERANSQLKRQNM
HHHHHHHHHHHHHCH
35.5925159151
1246PhosphorylationTRETKMKSLIRTLEQ
CHHHHHHHHHHHHHH
26.0623917254
1250PhosphorylationKMKSLIRTLEQEKMA
HHHHHHHHHHHHHHH
27.8723186163
1255UbiquitinationIRTLEQEKMAYQKTV
HHHHHHHHHHHHHHH
28.64-
1267UbiquitinationKTVEQLRKLLPADAL
HHHHHHHHHCCHHHH
64.07-

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
318SPhosphorylationKinaseAKT1P31749
Uniprot
318SPhosphorylationKinaseSGK1O00141
PSP
318SPhosphorylationKinaseRPS6KA1Q15418
GPS
318SPhosphorylationKinaseAKT-FAMILY-GPS
341SPhosphorylationKinaseAKT1P31749
PSP
341SPhosphorylationKinaseSGK1O00141
PSP
341SPhosphorylationKinaseRPS6KA1Q15418
GPS
485SPhosphorylationKinaseCHEK1O14757
GPS
568TPhosphorylationKinaseAKT1P31749
PSP
568TPhosphorylationKinaseSGK1O00141
PSP
568TPhosphorylationKinaseRPS6KA1Q15418
GPS
570SPhosphorylationKinaseAKT1P31749
PSP
570SPhosphorylationKinaseP90RSKQ15418
PSP
570SPhosphorylationKinaseSGK1O00141
PSP
570SPhosphorylationKinaseAMPK-FAMILY-GPS
588SPhosphorylationKinaseAMPK-FAMILY-GPS
588SPhosphorylationKinaseAKT-FAMILY-GPS
588SPhosphorylationKinaseSGK1O00141
PSP
588SPhosphorylationKinaseAKT1P31749
Uniprot
588SPhosphorylationKinaseRPS6KA1Q15418
GPS
588SPhosphorylationKinaseCHEK1O14757
GPS
595SPhosphorylationKinaseAKT-FAMILY-GPS
642TPhosphorylationKinaseSGK1O00141
PSP
642TPhosphorylationKinaseRPS6KA1Q15418
GPS
642TPhosphorylationKinaseAKT-FAMILY-GPS
642TPhosphorylationKinaseAMPK-FAMILY-GPS
642TPhosphorylationKinaseAKT1P31749
Uniprot
642TPhosphorylationKinasePKB_GROUP-PhosphoELM
650TPhosphorylationKinaseAKT-FAMILY-GPS
666SPhosphorylationKinaseP90RSKQ15418
PSP
666SPhosphorylationKinaseSGK1O00141
PSP
666SPhosphorylationKinaseAKT1P31749
PSP
751SPhosphorylationKinaseSGK1O00141
PSP
751SPhosphorylationKinaseRPS6KA1Q15418
GPS
751SPhosphorylationKinaseAKT1P31749
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:25515538

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBCD4_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 TBCD4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SR140_HUMANU2SURPphysical
12421765
RBM12_HUMANRBM12physical
12421765
EP400_HUMANEP400physical
12421765
TET2_HUMANTET2physical
12421765
TBD2A_HUMANTBC1D2physical
22863883
TLE3_HUMANTLE3physical
22863883
MEP50_HUMANWDR77physical
22863883
RAB14_MOUSERab14physical
21454505
1433Z_HUMANYWHAZphysical
25770209

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616087Diabetes mellitus, non-insulin-dependent, 5 (NIDDM5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBCD4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-570; SER-588; SER-591; THR-749; SER-751;THR-752; SER-754 AND THR-766, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-477, AND MASS SPECTROMETRY.
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-566; THR-568; SER-570;SER-588 AND SER-591, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-570; SER-588; SER-591; THR-749; SER-751;THR-752; SER-754 AND THR-766, AND MASS SPECTROMETRY.
"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-341; SER-566; SER-570;SER-588; SER-591; SER-666; THR-752; SER-754 AND SER-757, 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-551; SER-566; SER-570AND SER-588, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-591, ANDMASS SPECTROMETRY.
"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-344 AND SER-588, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASSSPECTROMETRY.
"A method to identify serine kinase substrates. Akt phosphorylates anovel adipocyte protein with a Rab GTPase-activating protein (GAP)domain.";
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,Lienhard G.E.;
J. Biol. Chem. 277:22115-22118(2002).
Cited for: PHOSPHORYLATION AT SER-588 AND THR-642.
"Identification of a novel AS160 splice variant that regulates GLUT4translocation and glucose-uptake in rat muscle cells.";
Baus D., Heermeier K., De Hoop M., Metz-Weidmann C., Gassenhuber J.,Dittrich W., Welte S., Tennagels N.;
Cell. Signal. 20:2237-2246(2008).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULARLOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-642.

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