PRAF3_HUMAN - dbPTM
PRAF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRAF3_HUMAN
UniProt AC O75915
Protein Name PRA1 family protein 3
Gene Name ARL6IP5
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein . Cytoplasm . Cytoplasm, cytoskeleton . Also exists as a soluble form in the cytoplasm. Associated with microtubules.
Protein Description Regulates intracellular concentrations of taurine and glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner. May be involved in membrane traffic..
Protein Sequence MDVNIAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISIVGFLSPFNMILGGIVVVLVFTGFVWAAHNKDVLRRMKKRYPTTFVMVVMLASYFLISMFGGVMVFVFGITFPLLLMFIHASLRLRNLKNKLENKMEGIGLKRTPMGIVLDALEQQEEGINRLTDYISKVKE
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
1Acetylation-------MDVNIAPL
-------CCCCCCCC
13.4922223895
18PhosphorylationWDDFFPGSDRFARPD
CCCCCCCCCCCCCCC
26.3321712546
31UbiquitinationPDFRDISKWNNRVVS
CCCCCHHHHCHHHHH
55.0321890473
31AcetylationPDFRDISKWNNRVVS
CCCCCHHHHCHHHHH
55.0325953088
31MalonylationPDFRDISKWNNRVVS
CCCCCHHHHCHHHHH
55.0326320211
31UbiquitinationPDFRDISKWNNRVVS
CCCCCHHHHCHHHHH
55.0321890473
151AcetylationLKNKLENKMEGIGLK
HHHHHHHHCCCCCCC
29.0227452117
151UbiquitinationLKNKLENKMEGIGLK
HHHHHHHHCCCCCCC
29.0221890473
152SulfoxidationKNKLENKMEGIGLKR
HHHHHHHCCCCCCCC
9.5821406390
1582-HydroxyisobutyrylationKMEGIGLKRTPMGIV
HCCCCCCCCCCCCHH
49.35-
158UbiquitinationKMEGIGLKRTPMGIV
HCCCCCCCCCCCCHH
49.3521890473
180PhosphorylationEEGINRLTDYISKVK
HHHHHHHHHHHHHHC
24.4226552605
182PhosphorylationGINRLTDYISKVKE-
HHHHHHHHHHHHCC-
11.2329978859
184PhosphorylationNRLTDYISKVKE---
HHHHHHHHHHCC---
25.7630108239
185UbiquitinationRLTDYISKVKE----
HHHHHHHHHCC----
48.0121890473
185MalonylationRLTDYISKVKE----
HHHHHHHHHCC----
48.0126320211
185UbiquitinationRLTDYISKVKE----
HHHHHHHHHCC----
48.0121890473

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 PRAF3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRAF3_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 PRAF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC1_HUMANXRCC1physical
19208635
RL5_HUMANRPL5physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
RN185_HUMANRNF185physical
25416956

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 PRAF3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-9, AND ACETYLATION AT MET-1.

TOP