TBC25_HUMAN - dbPTM
TBC25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC25_HUMAN
UniProt AC Q3MII6
Protein Name TBC1 domain family member 25
Gene Name TBC1D25
Organism Homo sapiens (Human).
Sequence Length 688
Subcellular Localization Cytoplasm . Cytoplasmic vesicle, autophagosome . It is dispersed in the cytoplasm under nutrient-rich conditions. Localizes at autophagosomes under cell starving conditions.
Protein Description Acts as a GTPase-activating protein specific for RAB33B. Involved in the regulation of autophagosome maturation, the process in which autophagosomes fuse with endosomes and lysosomes..
Protein Sequence MATASGASDLSGSGAPPPGVGAQAAAAAEEEEREVVRVRVKKCESFLPPEFRSFAVDPQITSLDVLQHILIRAFDLSGKKNFGISYLGRDRLGQEVYLSLLSDWDLSTAFATASKPYLQLRVDIRPSEDSPLLEDWDIISPKDVIGSDVLLAEKRSSLTTAALPFTQSILTQVGRTLSKVQQVLSWSYGEDVKPFKPPLSDAEFHTYLNHEGQLSRPEELRLRIYHGGVEPSLRKVVWRYLLNVYPDGLTGRERMDYMKRKSREYEQLKSEWAQRANPEDLEFIRSTVLKDVLRTDRAHPYYAGPEDGPHLRALHDLLTTYAVTHPQVSYCQGMSDLASPILAVMDHEGHAFVCFCGIMKRLAANFHPDGRAMATKFAHLKLLLRHADPDFYQYLQEAGADDLFFCYRWLLLELKREFAFDDALRMLEVTWSSLPPDPPEHEVELVGPPSQVADAGFGGHRGWPVRQRHMLRPAGGGGSTFEDAVDHLATASQGPGGGGRLLRQASLDGLQQLRDNMGSRRDPLVQLPHPAALISSKSLSEPLLNSPDPLLSSFSHPDSPSSSSPPSTQEASPTGDMAVGSPLMQEVGSPKDPGKSLPPVPPMGLPPPQEFGRGNPFMLFLCLAILLEHRDHIMRNGLDYNELAMHFDRLVRKHHLGRVLRRARALFADYLQSEVWDSEEGAEATAAS
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
3Phosphorylation-----MATASGASDL
-----CCCCCCCCCC		21.76-
5Phosphorylation---MATASGASDLSG
---CCCCCCCCCCCC		30.45-
8PhosphorylationMATASGASDLSGSGA
CCCCCCCCCCCCCCC		42.48-
127PhosphorylationLRVDIRPSEDSPLLE
EEEEECCCCCCCCCC		44.1627732954
130PhosphorylationDIRPSEDSPLLEDWD
EECCCCCCCCCCCCC		17.2527732954
140PhosphorylationLEDWDIISPKDVIGS
CCCCCCCCHHHHCCH		26.6529978859
147PhosphorylationSPKDVIGSDVLLAEK
CHHHHCCHHHHHHHH		17.2722210691
154UbiquitinationSDVLLAEKRSSLTTA
HHHHHHHHHCCCCHH		52.55-
156PhosphorylationVLLAEKRSSLTTAAL
HHHHHHHCCCCHHHH		40.5422617229
157PhosphorylationLLAEKRSSLTTAALP
HHHHHHCCCCHHHHH		33.4921712546
159PhosphorylationAEKRSSLTTAALPFT
HHHHCCCCHHHHHHH		19.1421712546
160O-linked_GlycosylationEKRSSLTTAALPFTQ
HHHCCCCHHHHHHHH		18.4130379171
160PhosphorylationEKRSSLTTAALPFTQ
HHHCCCCHHHHHHHH		18.4121712546
166PhosphorylationTTAALPFTQSILTQV
CHHHHHHHHHHHHHH		21.3328450419
168PhosphorylationAALPFTQSILTQVGR
HHHHHHHHHHHHHHH		19.2628450419
171PhosphorylationPFTQSILTQVGRTLS
HHHHHHHHHHHHHHH		21.3823090842
176PhosphorylationILTQVGRTLSKVQQV
HHHHHHHHHHHHHHH		29.4722210691
178PhosphorylationTQVGRTLSKVQQVLS
HHHHHHHHHHHHHHH		30.1222210691
262O-linked_GlycosylationMDYMKRKSREYEQLK
HHHHHHHHHHHHHHH		34.0830379171
269UbiquitinationSREYEQLKSEWAQRA
HHHHHHHHHHHHHHC		46.13-
290UbiquitinationFIRSTVLKDVLRTDR
HHHHHHHHHHHCCCC		41.26-
376UbiquitinationDGRAMATKFAHLKLL
CCHHHHHHHHHHHHH		30.89-
479PhosphorylationRPAGGGGSTFEDAVD
CCCCCCCCCHHHHHH		32.9528348404
480PhosphorylationPAGGGGSTFEDAVDH
CCCCCCCCHHHHHHH		34.0328348404
492PhosphorylationVDHLATASQGPGGGG
HHHHHHHCCCCCCHH		31.1726074081
506PhosphorylationGRLLRQASLDGLQQL
HHHHHHHCHHHHHHH		20.7519664994
535PhosphorylationPHPAALISSKSLSEP
CCHHHHHCCCCCCCC		32.3426074081
536PhosphorylationHPAALISSKSLSEPL
CHHHHHCCCCCCCCH		21.1926074081
538PhosphorylationAALISSKSLSEPLLN
HHHHCCCCCCCCHHC		38.7926074081
540PhosphorylationLISSKSLSEPLLNSP
HHCCCCCCCCHHCCC		44.2326074081
559PhosphorylationSSFSHPDSPSSSSPP
HHCCCCCCCCCCCCC		31.00-
564PhosphorylationPDSPSSSSPPSTQEA
CCCCCCCCCCCCCCC		42.66-
670PhosphorylationARALFADYLQSEVWD
HHHHHHHHHHHHCCC		11.8323879269
678PhosphorylationLQSEVWDSEEGAEAT
HHHHCCCCHHHHHHH		23.1023879269
688PhosphorylationGAEATAAS-------
HHHHHCCC-------		37.9923879269
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 TBC25_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC25_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 TBC25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBRAP_HUMANGABARAPphysical
21383079
GBRL2_HUMANGABARAPL2physical
21383079
MLP3B_HUMANMAP1LC3Bphysical
21383079
RAB2A_HUMANRAB2Aphysical
16923123
GBRL1_HUMANGABARAPL1physical
28514442
GBRAP_HUMANGABARAPphysical
28514442
GBRL2_HUMANGABARAPL2physical
28514442
OMA1_HUMANOMA1physical
28514442
F110A_HUMANFAM110Aphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
SYDE1_HUMANSYDE1physical
27173435
SRS12_HUMANSRSF12physical
27173435
DCLK1_HUMANDCLK1physical
27173435
TESK2_HUMANTESK2physical
27173435
MAGI1_HUMANMAGI1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
ZBT21_HUMANZBTB21physical
27173435
AFAD_HUMANMLLT4physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CBY1_HUMANCBY1physical
27173435
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 TBC25_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-140 AND SER-506, ANDMASS 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-506, AND MASSSPECTROMETRY.

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