Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Exocyst complex component 4  

UniProtKB / Swiss-Prot ID :  EXOC4_HUMAN

Gene Name (Synonyms) : 
EXOC4, KIAA1699, SEC8, SEC8L1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane (By similarity). 

Protein Sequence MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELT...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
220S -> F (in a colorectal cancer sample;somatic mutation).
599A -> T (in a colorectal cancer sample;somatic mutation).
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAEAA
---CCCCCC
17.63UniProtKB
Link-
9N6-acetyllysineAAGGKYRST
CCCCCCCCC
36.25HPRD
Link-
9N6-acetyllysineAAGGKYRST
CCCCCCCCC
36.25Phosphositeplus
Link-
9N6-acetyllysine.AAGGKYRST
CCCCCCCCC
36.25UniProtKB
Link-
30PhosphothreonineSVIRTLSTS
HHHHHHCCC
17.59Phosphositeplus
Link-
32PhosphoserineIRTLSTSDD
HHHHCCCCC
25.83Phosphositeplus
Link-
33PhosphothreonineRTLSTSDDV
HHHCCCCCH
39.01Phosphositeplus
Link-
34PhosphoserineTLSTSDDVE
HHCCCCCHH
28.56Phosphositeplus
Link-
223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSLVKDASV
EEEECCCCC
53.52Phosphositeplus
Link-
226PhosphoserineVKDASVPLI
ECCCCCCCC
34.11HPRD
Link-
226PhosphoserineVKDASVPLI
ECCCCCCCC
34.11Phosphositeplus
Link-
226Phosphoserine.VKDASVPLI
ECCCCCCCC
34.11UniProtKB
Link-
233PhosphothreonineLIDVTNLPT
CCCCCCCCH
27.56HPRD
Link-
233PhosphothreonineLIDVTNLPT
CCCCCCCCH
27.56Phosphositeplus
Link-
233Phosphothreonine.LIDVTNLPT
CCCCCCCCH
27.56UniProtKB
Link-
237PhosphothreonineTNLPTPRKF
CCCCHHHHH
38.60HPRD
Link-
237PhosphothreonineTNLPTPRKF
CCCCHHHHH
38.60PhosphoELM
Link-
237PhosphothreonineTNLPTPRKF
CCCCHHHHH
38.60Phosphositeplus
Link-
237PhosphothreonineTNLPTPRKF
CCCCHHHHH
38.60SysPTM
Link-
237Phosphothreonine.TNLPTPRKF
CCCCHHHHH
38.60UniProtKB
Link-
240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PTPRKFLDT
CHHHHHHHC
52.03Phosphositeplus
Link-
380PhosphotyrosineDIKLYDMAD
CCCCCCHHH
9.93Phosphositeplus
Link-
400PhosphotyrosineLLTEYLDMK
HHHHHCCCC
11.63Phosphositeplus
Link-
554PhosphothreonineGVTKTSDPL
HEEECCCCC
29.06HPRD
Link-
555PhosphoserineVTKTSDPLK
EEECCCCCE
38.49HPRD
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DTBP1_HUMANphysical interactionEBI-1106287
intact17043677
EXOC1_HUMANphysical interactionEBI-1106292
intact17043677
NMDE2_HUMANin vivoHPRD:12185HPRD12738960
DLG3_HUMANin vitro
yeast 2-hybrid
HPRD:12185HPRD12738960
RALA_HUMANin vitroHPRD:12185HPRD11406615
EXOC7_HUMANENSP00000253861STRING
- top -

Disease Reference
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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-9, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-237, AND MASSSPECTROMETRY.
"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-226; THR-233 ANDTHR-237, AND MASS 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 THR-237, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures