TBC23_HUMAN - dbPTM
TBC23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC23_HUMAN
UniProt AC Q9NUY8
Protein Name TBC1 domain family member 23
Gene Name TBC1D23
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Golgi apparatus, trans-Golgi network . Localization to the trans-Golgi is regulated by ARL1 and ARL5B/ARL8. ARL1 increases Golgi localization, while ARL5B decreases it. Recruitment to the trans-Golgi network requires the presence of GOLGA1 and GOLGA4
Protein Description Putative Rab GTPase-activating protein which plays a role in vesicular trafficking. [PubMed: 28823707 Involved in endosome-to-Golgi trafficking. Acts as a bridging protein by binding simultaneously to golgins, including GOLGA1 and GOLGA4, located at the trans-Golgi, and to the WASH complex, located on endosome-derived vesicles]
Protein Sequence MAEGEDVPPLPTSSGDGWEKDLEEALEAGGCDLETLRNIIQGRPLPADLRAKVWKIALNVAGKGDSLASWDGILDLPEQNTIHKDCLQFIDQLSVPEEKAAELLLDIESVITFYCKSRNIKYSTSLSWIHLLKPLVHLQLPRSDLYNCFYAIMNKYIPRDCSQKGRPFHLFRLLIQYHEPELCSYLDTKKITPDSYALNWLGSLFACYCSTEVTQAIWDGYLQQADPFFIYFLMLIILVNAKEVILTQESDSKEEVIKFLENTPSSLNIEDIEDLFSLAQYYCSKTPASFRKDNHHLFGSTLLGIKDDDADLSQALCLAISVSEILQANQLQGEGVRFFVVDCRPAEQYNAGHLSTAFHLDSDLMLQNPSEFAQSVKSLLEAQKQSIESGSIAGGEHLCFMGSGREEEDMYMNMVLAHFLQKNKEYVSIASGGFMALQQHLADINVDGPENGYGHWIASTSGSRSSINSVDGESPNGSSDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSCTERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHLLVTATHMYCLREIVSRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYLIPNAGDATKAIKQQIMKVLDALES
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
84UbiquitinationPEQNTIHKDCLQFID
CCCCCCCHHHHHHHH		46.4129967540
122PhosphorylationCKSRNIKYSTSLSWI
HHCCCCCEEECCHHH		17.2428985074
125PhosphorylationRNIKYSTSLSWIHLL
CCCCEEECCHHHHHH		17.9228985074
146PhosphorylationQLPRSDLYNCFYAIM
CCCHHHHHHHHHHHH		18.1818083107
150PhosphorylationSDLYNCFYAIMNKYI
HHHHHHHHHHHHCCC		9.4518083107
251UbiquitinationVILTQESDSKEEVIK
HEECCCCCCHHHHHH		64.0823000965
256UbiquitinationESDSKEEVIKFLENT
CCCCHHHHHHHHHCC		6.3823000965
262UbiquitinationEVIKFLENTPSSLNI
HHHHHHHCCCCCCCH		60.4823000965
271UbiquitinationPSSLNIEDIEDLFSL
CCCCCHHHHHHHHHH		45.8623000965
296UbiquitinationSFRKDNHHLFGSTLL
HHCCCCCCCCCCCCC		29.1623000965
300PhosphorylationDNHHLFGSTLLGIKD
CCCCCCCCCCCCCCC		14.4625849741
301PhosphorylationNHHLFGSTLLGIKDD
CCCCCCCCCCCCCCC		26.7827732954
301UbiquitinationNHHLFGSTLLGIKDD
CCCCCCCCCCCCCCC		26.7823000965
307UbiquitinationSTLLGIKDDDADLSQ
CCCCCCCCCCCCHHH		58.0423000965
316UbiquitinationDADLSQALCLAISVS
CCCHHHHHHHHHHHH		1.5823000965
378PhosphorylationEFAQSVKSLLEAQKQ
HHHHHHHHHHHHHHH		35.7121406692
384UbiquitinationKSLLEAQKQSIESGS
HHHHHHHHHHHHCCC		53.7329901268
411PhosphorylationGREEEDMYMNMVLAH
CCCHHHHHHHHHHHH		9.5429978859
415UbiquitinationEDMYMNMVLAHFLQK
HHHHHHHHHHHHHHH		3.4721139048
427UbiquitinationLQKNKEYVSIASGGF
HHHCCCEEEEECCHH		3.3223000965
432UbiquitinationEYVSIASGGFMALQQ
CEEEEECCHHHHHHH		25.0823000965
438UbiquitinationSGGFMALQQHLADIN
CCHHHHHHHHHHCCC		21.0723000965
447UbiquitinationHLADINVDGPENGYG
HHHCCCCCCCCCCCC		63.5423000965
459PhosphorylationGYGHWIASTSGSRSS
CCCCEEEECCCCCCC		17.6128348404
460UbiquitinationYGHWIASTSGSRSSI
CCCEEEECCCCCCCC		28.2521139048
460PhosphorylationYGHWIASTSGSRSSI
CCCEEEECCCCCCCC		28.2528348404
461PhosphorylationGHWIASTSGSRSSIN
CCEEEECCCCCCCCC		32.0728348404
463PhosphorylationWIASTSGSRSSINSV
EEEECCCCCCCCCCC		28.8528348404
465PhosphorylationASTSGSRSSINSVDG
EECCCCCCCCCCCCC		36.9522617229
466PhosphorylationSTSGSRSSINSVDGE
ECCCCCCCCCCCCCC		25.3628348404
469PhosphorylationGSRSSINSVDGESPN
CCCCCCCCCCCCCCC		21.6625159151
474 (in isoform 2)Phosphorylation-29.24-
474PhosphorylationINSVDGESPNGSSDR
CCCCCCCCCCCCCHH		29.2423401153
478PhosphorylationDGESPNGSSDRGMKS
CCCCCCCCCHHHHHH		35.3930278072
479PhosphorylationGESPNGSSDRGMKSL
CCCCCCCCHHHHHHH		32.5025850435
484UbiquitinationGSSDRGMKSLVNKMT
CCCHHHHHHHHHHHH		43.3823000965
485PhosphorylationSSDRGMKSLVNKMTV
CCHHHHHHHHHHHHH		28.7624670416
489UbiquitinationGMKSLVNKMTVALKT
HHHHHHHHHHHHHHC		28.5923000965
495UbiquitinationNKMTVALKTKSVNVR
HHHHHHHHCCCCCHH		44.1423000965
495 (in isoform 2)Ubiquitination-44.1420972266
497AcetylationMTVALKTKSVNVREK
HHHHHHCCCCCHHHH		51.3112439387
504AcetylationKSVNVREKVISFIEN
CCCCHHHHHHHHHHC		34.0112439399
504UbiquitinationKSVNVREKVISFIEN
CCCCHHHHHHHHHHC		34.0123000965
507 (in isoform 2)Phosphorylation-24.14-
507PhosphorylationNVREKVISFIENTST
CHHHHHHHHHHCCCC		24.1428355574
512 (in isoform 2)Phosphorylation-22.6122210691
512PhosphorylationVISFIENTSTPVDRM
HHHHHHCCCCCCCCC		22.6129255136
513PhosphorylationISFIENTSTPVDRMS
HHHHHCCCCCCCCCC		42.1529255136
513 (in isoform 2)Phosphorylation-42.1522210691
514 (in isoform 2)Phosphorylation-25.8716964243
514PhosphorylationSFIENTSTPVDRMSF
HHHHCCCCCCCCCCC		25.8729255136
520PhosphorylationSTPVDRMSFNLPWPD
CCCCCCCCCCCCCCC		16.3326657352
529PhosphorylationNLPWPDRSCTERHVS
CCCCCCCCCCCCCCC		32.5425627689
531PhosphorylationPWPDRSCTERHVSSS
CCCCCCCCCCCCCCC		36.9825159151
536PhosphorylationSCTERHVSSSDRVGK
CCCCCCCCCCCCCCC		20.2824719451
537PhosphorylationCTERHVSSSDRVGKP
CCCCCCCCCCCCCCC		34.8628555341
545PhosphorylationSDRVGKPYRGVKPVF
CCCCCCCCCCCCCCE		24.3926657352
552 (in isoform 2)Phosphorylation-6.29-
553PhosphorylationRGVKPVFSIGDEEEY
CCCCCCEECCCHHHC		26.3728796482
560PhosphorylationSIGDEEEYDTDEIDS
ECCCHHHCCCCCCCC		27.6728796482
562PhosphorylationGDEEEYDTDEIDSSS
CCHHHCCCCCCCCCC		34.3323927012
567PhosphorylationYDTDEIDSSSMSDDD
CCCCCCCCCCCCHHH		29.9423927012
568PhosphorylationDTDEIDSSSMSDDDR
CCCCCCCCCCCHHHH		26.7223927012
569PhosphorylationTDEIDSSSMSDDDRK
CCCCCCCCCCHHHHH		26.6823927012
571PhosphorylationEIDSSSMSDDDRKEV
CCCCCCCCHHHHHHH		39.5723927012
572UbiquitinationIDSSSMSDDDRKEVV
CCCCCCCHHHHHHHE		53.8629967540
582UbiquitinationRKEVVNIQTWINKPD
HHHHEEHHHHHCCCC		26.1129967540
583PhosphorylationKEVVNIQTWINKPDV
HHHEEHHHHHCCCCC		25.23-
587UbiquitinationNIQTWINKPDVKHHF
EHHHHHCCCCCCCCC		33.2029967540
591UbiquitinationWINKPDVKHHFPCKE
HHCCCCCCCCCCCCC		38.4521139048
597UbiquitinationVKHHFPCKEVKESGH
CCCCCCCCCHHHHCC		66.8229967540
612UbiquitinationMFPSHLLVTATHMYC
CCCHHHHHHHHHHHH		4.2729967540
627UbiquitinationLREIVSRKGLAYIQS
HHHHHHHHCHHHHHH		51.2529967540
631PhosphorylationVSRKGLAYIQSRQAL
HHHHCHHHHHHHHHH		12.4418083107
633UbiquitinationRKGLAYIQSRQALNS
HHCHHHHHHHHHHHH		21.6421139048
634UbiquitinationKGLAYIQSRQALNSV
HCHHHHHHHHHHHHH		19.4633845483
634PhosphorylationKGLAYIQSRQALNSV
HCHHHHHHHHHHHHH		19.4624247654
648UbiquitinationVVKITSKKKHPELIT
HHHHHCCCCCCCCEE		56.9621139048
649UbiquitinationVKITSKKKHPELITF
HHHHCCCCCCCCEEE		69.0433845483
664PhosphorylationKYGNSSASGIEILAI
ECCCCCCCCEEEEEE		42.1027251275
669UbiquitinationSASGIEILAIERYLI
CCCCEEEEEEEEEEC		2.2629967540
674PhosphorylationEILAIERYLIPNAGD
EEEEEEEEECCCCCH		9.01-
684UbiquitinationPNAGDATKAIKQQIM
CCCCHHHHHHHHHHH		50.2429967540
699PhosphorylationKVLDALES-------
HHHHHHHC-------		46.5024670416
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

Oops, there are no upstream regulatory protein records of TBC23_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC23_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 TBC23_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
25416956
WDR62_HUMANWDR62physical
25416956
CAGE1_HUMANCAGE1physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
GLRX3_HUMANGLRX3physical
26344197
OSGEP_HUMANOSGEPphysical
26344197
STK11_HUMANSTK11physical
21516116
HSP7C_HUMANHSPA8physical
28514442
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 TBC23_HUMAN

loading...

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-474, 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-507 AND THR-514, ANDMASS SPECTROMETRY.
"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-474 AND THR-514, ANDMASS SPECTROMETRY.

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