VPS53_HUMAN - dbPTM
VPS53_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS53_HUMAN
UniProt AC Q5VIR6
Protein Name Vacuolar protein sorting-associated protein 53 homolog
Gene Name VPS53
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein. Endosome membrane
Peripheral membrane protein. Recycling endosome . Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endos
Protein Description Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. [PubMed: 15878329]
Protein Sequence MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDRADFNAVEYINTLFPTEQSLANIDEVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWIKRQLVDYEEKYGRMFPREWCMAERIAVEFCHVTRAELAKIMRTRAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDEPTPEMEELATEKGDLDQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLGELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTTTSSGGLTISSLLKEKEGSEVAKFTLEELCLICNILSTAEYCLATTQQLEEKLKEKVDVSLIERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALTAMSKMQWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCVKFANSFIPKFITHLFKCKPISMVGAEQVRWT
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
102UbiquitinationQALEEAQKAIQQLFG
HHHHHHHHHHHHHHH		55.2821890473
102 (in isoform 3)Ubiquitination-55.2821890473
102 (in isoform 1)Ubiquitination-55.2821890473
102UbiquitinationQALEEAQKAIQQLFG
HHHHHHHHHHHHHHH		55.2821890473
102 (in isoform 4)Ubiquitination-55.28-
110AcetylationAIQQLFGKIKDIKDK
HHHHHHHHHHHHHHH		38.9719608861
110 (in isoform 4)Ubiquitination-38.97-
133 (in isoform 4)Ubiquitination-49.44-
143PhosphorylationDHAKRHLTTSITTLN
HHHHHHHHHHHHHHH		16.6324043423
144PhosphorylationHAKRHLTTSITTLNH
HHHHHHHHHHHHHHH		25.2124043423
145PhosphorylationAKRHLTTSITTLNHL
HHHHHHHHHHHHHHH		16.8324043423
147PhosphorylationRHLTTSITTLNHLHM
HHHHHHHHHHHHHHH		25.6224043423
148PhosphorylationHLTTSITTLNHLHML
HHHHHHHHHHHHHHH		24.7224043423
161PhosphorylationMLAGGVDSLEAMTRR
HHHCCCCHHHHHHHH		26.2124043423
166PhosphorylationVDSLEAMTRRRQYGE
CCHHHHHHHHHHHHH		28.2424043423
171PhosphorylationAMTRRRQYGEVANLL
HHHHHHHHHHHHHHH		17.2824043423
191PhosphorylationVLEHFHKYMGIPQIR
HHHHHHHHCCCHHHH		7.6324043423
292 (in isoform 4)Ubiquitination-24.32-
301 (in isoform 4)Ubiquitination-40.85-
324PhosphorylationAVEFCHVTRAELAKI
HHHHHHCCHHHHHHH		10.6524719451
360 (in isoform 4)Ubiquitination-57.00-
360MalonylationNFEGFLAKRFSGCTL
CCCCHHHHHCCCCEE		57.0026320211
360AcetylationNFEGFLAKRFSGCTL
CCCCHHHHHCCCCEE		57.0019608861
371PhosphorylationGCTLTDGTLKKLESP
CCEECCCCCCCCCCC		37.9128857561
374 (in isoform 4)Ubiquitination-61.68-
377PhosphorylationGTLKKLESPPPSTNP
CCCCCCCCCCCCCCC		53.8225159151
381PhosphorylationKLESPPPSTNPFLED
CCCCCCCCCCCCCCC		46.7428102081
382PhosphorylationLESPPPSTNPFLEDE
CCCCCCCCCCCCCCC		53.3228102081
391PhosphorylationPFLEDEPTPEMEELA
CCCCCCCCHHHHHHH		29.8125159151
520PhosphorylationLSGNLPKTTTSSGGL
HHCCCCCCEECCCCE		33.1121406692
521PhosphorylationSGNLPKTTTSSGGLT
HCCCCCCEECCCCEE		30.7021406692
522PhosphorylationGNLPKTTTSSGGLTI
CCCCCCEECCCCEEH		26.5727251275
523PhosphorylationNLPKTTTSSGGLTIS
CCCCCEECCCCEEHH		25.5427251275
524PhosphorylationLPKTTTSSGGLTISS
CCCCEECCCCEEHHH		34.4827251275
528PhosphorylationTTSSGGLTISSLLKE
EECCCCEEHHHHHHH		23.3027251275
530PhosphorylationSSGGLTISSLLKEKE
CCCCEEHHHHHHHCC		15.0821406692
531PhosphorylationSGGLTISSLLKEKEG
CCCEEHHHHHHHCCC		33.5921406692
539PhosphorylationLLKEKEGSEVAKFTL
HHHHCCCCHHHCHHH		29.9529083192
580PhosphorylationLKEKVDVSLIERINL
HHHHCCHHHHHHHCC		21.1118367545
689PhosphorylationLFKCKPISMVGAEQV
HHCCCCCCCCCCCCC		18.8821406692
699PhosphorylationGAEQVRWT-------
CCCCCCCC-------		20.4021406692
712 (in isoform 4)Phosphorylation-22210691
714 (in isoform 4)Phosphorylation--
715 (in isoform 4)Phosphorylation--
734 (in isoform 4)Phosphorylation--
771 (in isoform 4)Ubiquitination--
776 (in isoform 4)Ubiquitination--
784 (in isoform 4)Phosphorylation-26471730
785 (in isoform 4)Phosphorylation-26471730
803 (in isoform 4)Phosphorylation-27251275
804 (in isoform 4)Phosphorylation-27251275
806 (in isoform 4)Phosphorylation-27251275
808 (in isoform 4)Phosphorylation-27251275
810 (in isoform 4)Phosphorylation-27251275
818 (in isoform 4)Phosphorylation-24719451
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 VPS53_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS53_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 VPS53_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS52_HUMANVPS52physical
20685960
VPS51_HUMANVPS51physical
20685960
EXOC2_HUMANEXOC2physical
20685960
VPS53_HUMANVPS53physical
20685960
VPS51_HUMANVPS51physical
26344197
VPS50_HUMANCCDC132physical
28514442
VPS54_HUMANVPS54physical
28514442
SNP29_HUMANSNAP29physical
28514442
BASI_HUMANBSGphysical
28514442
PRAF2_HUMANPRAF2physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
VPS51_HUMANVPS51physical
27173435
EIPR1_HUMANTSSC1physical
27173435
RABE1_HUMANRABEP1physical
27173435
VPS52_HUMANVPS52physical
28542518
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615851Pontocerebellar hypoplasia 2E (PCH2E)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPS53_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-110 AND LYS-360, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND THR-391, ANDMASS SPECTROMETRY.

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