TBCD4_MOUSE - dbPTM
TBCD4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBCD4_MOUSE
UniProt AC Q8BYJ6
Protein Name TBC1 domain family member 4
Gene Name Tbc1d4
Organism Mus musculus (Mouse).
Sequence Length 1307
Subcellular Localization Cytoplasm . Cytoplasmic perinuclear..
Protein Description May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake (By similarity)..
Protein Sequence MESPSCIQDEPFPHPLEPEPSAPAQPGATKPGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRRSQKPDAGGCGAPAAREVILVLSAPFLRCVPAPGAGVGGGAGSGAVQPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPNQVPDVISSIRQLSKAAMKEDSKPSKDNEDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKLQGERGGDPGDEMGVLEVESPVSPDDSLPEKADGTVNSPRALPSLASLPALASQPALASSRVCFPERILEDCGFDEQQEFRSRCSSVTGVMQKKVHENNQKTQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCANESLVDEVMLTLKQAFSTAAALQSAKTQIKLCETCPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPISDQEENELVILHLRQLCEAKQRTHVHIGEGPAIISNSTIPENVTSGGRFKLDVLKNKAKRSLTSSLENIFSRGANRMRGRLGSMDSFERANSLASEKDFSPGDSPPGTPPASPLSSAWHAFPEEDSDSPQFRRRAHTFSHPPSSSRRKLNLQDGKAHGLRSPLLRQSSSEQCSIVPSARRMYKESNSSCSLPSLHTSFSAPSFTAPSFLKSFYQNSGRLSPQYENEIRQDTASESSDGEGRKRTSSTCSNESLNAGGTPVTPRRVSWRQRIFLRVASPVNKSPSAMQQQKDGLDRTELLPLSPLSPTMEEEPLIIFLSGDEDTEKVEEKKKSKELKSLWKKAIHQQILLLRMEKENQKLEEARRDELQSRKVKLDYEEVGTCQKEILIAWDKKLLNCRTKIRCDMEDIHTSLKEGVPKSRRGEIWQFLALQYRLRHRLPNKHQPPDTSYKELLKQLTAQQHAILVDLGRTFPTHPYFSVQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRELYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALIMECENFENIVEFLKSTLPDMNTTEMEKIITQVFEMDISKQLHAYEVEYHVLQDELLESSYACEDNESLEKLERANNQLKRQNMDLLEKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVEQIRKLLPADALANCELLLKDLTHPTNDKAKAGNKP
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-------MESPSCIQ
-------CCCCCCCC		47.68-
3Phosphorylation-----MESPSCIQDE
-----CCCCCCCCCC		33.6926239621
5Phosphorylation---MESPSCIQDEPF
---CCCCCCCCCCCC		32.8826239621
21PhosphorylationHPLEPEPSAPAQPGA
CCCCCCCCCCCCCCC		45.2626239621
137PhosphorylationIHNSHDLTYFAYLIK
HHCCCCHHHEEEEEC		23.7325338131
172PhosphorylationNQVPDVISSIRQLSK
CCCHHHHHHHHHHHH		21.4025367039
173PhosphorylationQVPDVISSIRQLSKA
CCHHHHHHHHHHHHH		15.6325367039
230PhosphorylationDDCKDKFSLHEQQRL
HHCCCCCCHHHHHHH		34.2622802335
258PhosphorylationMGVLEVESPVSPDDS
CCEEEEECCCCCCCC		35.4624925903
261PhosphorylationLEVESPVSPDDSLPE
EEEECCCCCCCCCCC		26.4624925903
265PhosphorylationSPVSPDDSLPEKADG
CCCCCCCCCCCCCCC		53.8824925903
273PhosphorylationLPEKADGTVNSPRAL
CCCCCCCCCCCCCHH		19.6328066266
276PhosphorylationKADGTVNSPRALPSL
CCCCCCCCCCHHHCH		16.0726239621
282PhosphorylationNSPRALPSLASLPAL
CCCCHHHCHHHCHHH		37.1026745281
297PhosphorylationASQPALASSRVCFPE
HCCCHHHHCCCCCCH		21.3726060331
298PhosphorylationSQPALASSRVCFPER
CCCHHHHCCCCCCHH		24.1126060331
320PhosphorylationDEQQEFRSRCSSVTG
CHHHHHHHHHHHHHH		42.8521183079
323PhosphorylationQEFRSRCSSVTGVMQ
HHHHHHHHHHHHHHH		27.0826745281
324PhosphorylationEFRSRCSSVTGVMQK
HHHHHHHHHHHHHHH		27.5916935857
326PhosphorylationRSRCSSVTGVMQKKV
HHHHHHHHHHHHHHH		26.4628464351
348PhosphorylationQPRRRHASAPSHVQP
CCCCCCCCCCCCCCC		34.2926824392
351PhosphorylationRRHASAPSHVQPSDS
CCCCCCCCCCCCCCC		35.6927742792
356PhosphorylationAPSHVQPSDSEKNRT
CCCCCCCCCCCCCCE		36.3625619855
358PhosphorylationSHVQPSDSEKNRTML
CCCCCCCCCCCCEEE		55.6025619855
377PhosphorylationRFEINLISPDTKSVV
EEEEEEECCCCCCEE		21.6426239621
484AcetylationGLYPPRAKLVIQRHL
CCCCCHHHHHHHHHH		44.5623236377
492PhosphorylationLVIQRHLSSLTDNEQ
HHHHHHHHHCCCHHH		19.7121183079
573PhosphorylationLKNKAKRSLTSSLEN
HCHHHHHHHHHHHHH		34.9823527152
575PhosphorylationNKAKRSLTSSLENIF
HHHHHHHHHHHHHHH		19.9521082442
576PhosphorylationKAKRSLTSSLENIFS
HHHHHHHHHHHHHHH		37.9127742792
577PhosphorylationAKRSLTSSLENIFSR
HHHHHHHHHHHHHHH		34.1723527152
583PhosphorylationSSLENIFSRGANRMR
HHHHHHHHHCHHHHC		26.4723649490
584MethylationSLENIFSRGANRMRG
HHHHHHHHCHHHHCC		37.1824129315
595PhosphorylationRMRGRLGSMDSFERA
HHCCCCCCCCHHHHH		24.8216935857
598PhosphorylationGRLGSMDSFERANSL
CCCCCCCHHHHHHHH		21.9923527152
604PhosphorylationDSFERANSLASEKDF
CHHHHHHHHHCCCCC		25.0721659605
607PhosphorylationERANSLASEKDFSPG
HHHHHHHCCCCCCCC		50.9324899341
612PhosphorylationLASEKDFSPGDSPPG
HHCCCCCCCCCCCCC		37.8027180971
616PhosphorylationKDFSPGDSPPGTPPA
CCCCCCCCCCCCCCC		38.6224925903
620PhosphorylationPGDSPPGTPPASPLS
CCCCCCCCCCCCCCC		31.6926239621
624PhosphorylationPPGTPPASPLSSAWH
CCCCCCCCCCCCCCC		31.9526239621
627PhosphorylationTPPASPLSSAWHAFP
CCCCCCCCCCCCCCC		22.7626239621
628PhosphorylationPPASPLSSAWHAFPE
CCCCCCCCCCCCCCC		42.9626239621
638PhosphorylationHAFPEEDSDSPQFRR
CCCCCCCCCCHHHHH		43.1825293948
640PhosphorylationFPEEDSDSPQFRRRA
CCCCCCCCHHHHHHH		25.26-
649PhosphorylationQFRRRAHTFSHPPSS
HHHHHHHHHCCCCCH		26.3316935857
651PhosphorylationRRRAHTFSHPPSSSR
HHHHHHHCCCCCHHC		35.9226239621
672 (in isoform 4)Phosphorylation-40.6029514104
673PhosphorylationGKAHGLRSPLLRQSS
CCCCCCCCHHHHCCC		25.5826824392
673 (in isoform 2)Phosphorylation-25.5829514104
678 (in isoform 4)Phosphorylation-47.8623608596
679 (in isoform 3)Phosphorylation-29.4229899451
679 (in isoform 2)Phosphorylation-29.4223608596
679 (in isoform 4)Phosphorylation-29.4230352176
679PhosphorylationRSPLLRQSSSEQCSI
CCHHHHCCCCCCCCC		29.4223737553
680 (in isoform 4)Phosphorylation-29.5623608596
680 (in isoform 2)Phosphorylation-29.5630352176
680 (in isoform 3)Phosphorylation-29.5629899451
680PhosphorylationSPLLRQSSSEQCSIV
CHHHHCCCCCCCCCC		29.5623737553
681PhosphorylationPLLRQSSSEQCSIVP
HHHHCCCCCCCCCCH		36.6123737553
681 (in isoform 3)Phosphorylation-36.6129899451
681 (in isoform 2)Phosphorylation-36.6123608596
684 (in isoform 4)Phosphorylation-2.3523608596
685 (in isoform 2)Phosphorylation-26.7323608596
694 (in isoform 4)Phosphorylation-15.1429514104
695 (in isoform 2)Phosphorylation-45.3729514104
697 (in isoform 4)Phosphorylation-37.5529514104
698 (in isoform 2)Phosphorylation-38.7529514104
698PhosphorylationRRMYKESNSSCSLPS
HHHHHHCCCCCCCCC		38.7524719451
711PhosphorylationPSLHTSFSAPSFTAP
CCCCCCCCCCCCCCH		38.7519923418
743PhosphorylationENEIRQDTASESSDG
HHHHHHCCCCCCCCC		24.6020531401
745PhosphorylationEIRQDTASESSDGEG
HHHHCCCCCCCCCCC		39.8520531401
747PhosphorylationRQDTASESSDGEGRK
HHCCCCCCCCCCCCC		31.1020531401
748PhosphorylationQDTASESSDGEGRKR
HCCCCCCCCCCCCCC		45.6520531401
756PhosphorylationDGEGRKRTSSTCSNE
CCCCCCCCCCCCCCC		30.0223527152
757PhosphorylationGEGRKRTSSTCSNES
CCCCCCCCCCCCCCC		27.9027742792
758PhosphorylationEGRKRTSSTCSNESL
CCCCCCCCCCCCCCC		32.5916935857
759PhosphorylationGRKRTSSTCSNESLN
CCCCCCCCCCCCCCC		21.5227742792
761PhosphorylationKRTSSTCSNESLNAG
CCCCCCCCCCCCCCC		43.6625521595
764PhosphorylationSSTCSNESLNAGGTP
CCCCCCCCCCCCCCC		31.0427742792
770PhosphorylationESLNAGGTPVTPRRV
CCCCCCCCCCCCCCC		17.4216141072
773PhosphorylationNAGGTPVTPRRVSWR
CCCCCCCCCCCCCHH		16.57-
789PhosphorylationRIFLRVASPVNKSPS
HHHHEECCCCCCCHH		26.9023737553
794PhosphorylationVASPVNKSPSAMQQQ
ECCCCCCCHHHHHHH		20.9126239621
796PhosphorylationSPVNKSPSAMQQQKD
CCCCCCHHHHHHHCC		43.3923684622
808PhosphorylationQKDGLDRTELLPLSP
HCCCCCCHHCEECCC		30.5626643407
814PhosphorylationRTELLPLSPLSPTME
CHHCEECCCCCCCCC		23.1226239621
817PhosphorylationLLPLSPLSPTMEEEP
CEECCCCCCCCCCCC		23.0026239621
819PhosphorylationPLSPLSPTMEEEPLI
ECCCCCCCCCCCCEE		33.5626239621
830PhosphorylationEPLIIFLSGDEDTEK
CCEEEEECCCCCHHH		33.1926239621
835PhosphorylationFLSGDEDTEKVEEKK
EECCCCCHHHHHHHH		35.3426643407
931PhosphorylationLKEGVPKSRRGEIWQ
HHCCCCCHHCHHHHH		22.5723832136
1068PhosphorylationQIQMYQLSRLLHDYH
HHHHHHHHHHHHHHH		12.8319740738
1135PhosphorylationVALSLLSSQEALIME
HHHHHHCCCHHHHHH		31.8219923418
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
324SPhosphorylationKinaseAKT1P31750
Uniprot
348SPhosphorylationKinaseAKT1P31750
Uniprot
577SPhosphorylationKinaseAKT1P31750
Uniprot
595SPhosphorylationKinaseAKT1P31750
Uniprot
595SPhosphorylationKinasePRKCZQ02956
GPS
649TPhosphorylationKinaseAKT1P31750
Uniprot
711SPhosphorylationKinaseAMPKA2P54646
PSP
711SPhosphorylationKinasePRKAA2Q8BRK8
GPS
758SPhosphorylationKinaseAKT1P31750
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBCD4_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TBCD4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBCD4_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASSSPECTROMETRY.
"Insulin-stimulated phosphorylation of a Rab GTPase-activating proteinregulates GLUT4 translocation.";
Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S.,Garner C.W., Lienhard G.E.;
J. Biol. Chem. 278:14599-14602(2003).
Cited for: PHOSPHORYLATION AT SER-324; SER-348; SER-577; SER-595; THR-649 ANDSER-758.
"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-595 AND THR-649, SUBCELLULAR LOCATION, ANDTISSUE SPECIFICITY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory