Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Vacuolar protein sorting-associated protein VTA1 homolog  

UniProtKB / Swiss-Prot ID :  VTA1_HUMAN

Gene Name (Synonyms) : 
VTA1, C6orf55 HSPC228, My012  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Endosome membrane; Peripheral membrane protein (Probable). 

Protein Function :  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 MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFLSKLMDQLEAL...
Predicted Secondary Structure CCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
239I -> M (in dbSNP:rs2232307). VAR_053917
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAALAP
---CCCCCC
15.93UniProtKB
Link
155S-nitrosocysteineYIHNCLKNG
HHHHHHHCC
3.37dbSNO
Link
278PhosphotyrosineKYCKYAGSA
HHHHHHHHH
16.78Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CBS_HUMANphysical interactionMINT-66058MINT16189514
Q5J7Q8_HUMANphysical interactionMINT-66288MINT16189514
NECA2_HUMANphysical interactionMINT-66658MINT16189514
ZBT16_HUMANphysical interactionMINT-67258MINT16189514
KLH12_HUMANphysical interactionMINT-67365MINT16189514
RPIA_HUMANphysical interactionEBI-754579
intact16189514
MBIP1_HUMANphysical interactionEBI-756817
intact16189514
KLH12_HUMANphysical interactionEBI-756823
intact16189514
DPPA2_HUMANphysical interactionEBI-756946
intact16189514
KCD13_HUMANphysical interactionEBI-754417
intact16189514
ZBT16_HUMANyeast 2-hybridHPRD:09855HPRD16189514
KCD13_HUMANyeast 2-hybridHPRD:09855HPRD16189514
DPPA2_HUMANyeast 2-hybridHPRD:09855HPRD16189514
KLH12_HUMANyeast 2-hybridHPRD:09855HPRD16189514
MBIP1_HUMANyeast 2-hybridHPRD:09855HPRD16189514
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures