VTA1_HUMAN - dbPTM
VTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTA1_HUMAN
UniProt AC Q9NP79
Protein Name Vacuolar protein sorting-associated protein VTA1 homolog
Gene Name VTA1
Organism Homo sapiens (Human).
Sequence Length 307
Subcellular Localization Cytoplasm . Endosome membrane
Peripheral membrane protein .
Protein Description Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding..
Protein Sequence MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFLSKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNDIEENEDAGAASLPTQPTQPSSSSTYDPSNMPSGNYTGIQIPPGAHAPANTPAEVPHSTGVASNTIQPTPQTIPAIDPALFNTISQGDVRLTPEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLTTGRE
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
2Acetylation------MAALAPLPP
------CCCCCCCCC
15.9322223895
15AcetylationPPLPAQFKSIQHHLR
CCCCHHHHHHHHHHH
34.2725953088
22MethylationKSIQHHLRTAQEHDK
HHHHHHHHHHHHHCC
24.53115919869
43SulfoxidationYYCRLYAMQTGMKID
HHHHHHHHHHCCCCC
2.0130846556
47SulfoxidationLYAMQTGMKIDSKTP
HHHHHHCCCCCCCCH
3.7930846556
522-HydroxyisobutyrylationTGMKIDSKTPECRKF
HCCCCCCCCHHHHHH
65.44-
62AcetylationECRKFLSKLMDQLEA
HHHHHHHHHHHHHHH
50.4025953088
64SulfoxidationRKFLSKLMDQLEALK
HHHHHHHHHHHHHHH
3.3821406390
71AcetylationMDQLEALKKQLGDNE
HHHHHHHHHHHCCCH
45.5925953088
712-HydroxyisobutyrylationMDQLEALKKQLGDNE
HHHHHHHHHHHCCCH
45.59-
72UbiquitinationDQLEALKKQLGDNEA
HHHHHHHHHHCCCHH
52.16-
150PhosphorylationKYARWKATYIHNCLK
HHHHHHHHHHHHHHH
21.2028152594
151PhosphorylationYARWKATYIHNCLKN
HHHHHHHHHHHHHHC
12.6828152594
155S-nitrosocysteineKATYIHNCLKNGETP
HHHHHHHHHHCCCCC
3.37-
155S-nitrosylationKATYIHNCLKNGETP
HHHHHHHHHHCCCCC
3.3719483679
242O-linked_GlycosylationASNTIQPTPQTIPAI
CCCCCCCCCCCCCCC
16.20OGP
258O-linked_GlycosylationPALFNTISQGDVRLT
HHHHCCCCCCCCCCC
26.5230379171
265PhosphorylationSQGDVRLTPEDFARA
CCCCCCCCHHHHHHH
17.6721815630
277UbiquitinationARAQKYCKYAGSALQ
HHHHHHHHHCCCCCC
34.74-
277MalonylationARAQKYCKYAGSALQ
HHHHHHHHHCCCCCC
34.7426320211
277AcetylationARAQKYCKYAGSALQ
HHHHHHHHHCCCCCC
34.7425953088
278PhosphorylationRAQKYCKYAGSALQY
HHHHHHHHCCCCCCH
16.7821945579
281PhosphorylationKYCKYAGSALQYEDV
HHHHHCCCCCCHHCH
20.0321945579
285PhosphorylationYAGSALQYEDVSTAV
HCCCCCCHHCHHHHH
18.2321945579
289PhosphorylationALQYEDVSTAVQNLQ
CCCHHCHHHHHHHHH
23.9921945579
290PhosphorylationLQYEDVSTAVQNLQK
CCHHCHHHHHHHHHH
30.6021945579
300AcetylationQNLQKALKLLTTGRE
HHHHHHHHHHHCCCC
46.4325953088

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 VTA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTA1_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 VTA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BACD1_HUMANKCTD13physical
16189514
NECA2_HUMANNECAB2physical
16189514
MBIP1_HUMANMBIPphysical
16189514
KLH12_HUMANKLHL12physical
16189514
DPPA2_HUMANDPPA2physical
16189514
CHMP5_HUMANCHMP5physical
21543490
CHM2A_HUMANCHMP2Aphysical
21543490
CHMP3_HUMANCHMP3physical
21543490
A4_HUMANAPPphysical
21832049
XPP1_HUMANXPNPEP1physical
22939629
VATC1_HUMANATP6V1C1physical
22863883
SRC8_HUMANCTTNphysical
22863883
MAOX_HUMANME1physical
22863883
SYDC_HUMANDARSphysical
26344197
DLDH_HUMANDLDphysical
26344197
MK03_HUMANMAPK3physical
26344197
XPP1_HUMANXPNPEP1physical
26344197

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 VTA1_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 ALA-2, AND MASS SPECTROMETRY.

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