AR6P6_HUMAN - dbPTM
AR6P6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AR6P6_HUMAN
UniProt AC Q8N6S5
Protein Name ADP-ribosylation factor-like protein 6-interacting protein 6
Gene Name ARL6IP6
Organism Homo sapiens (Human).
Sequence Length 226
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MSFAESGWRSALRRRGPGTPGPVARPSYSSFTQGDSWGEGEVDEEEGCDQVARDLRAEFSAGAWSEPRKRSVLPPDGNGSPVLPDKRNGIFPAAAGSRAQPRRWPVQVLSILCSLLFAILLAFLLAIAYLIVKELHAENLKNEDDVDTGLLGFWTLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM
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
2Phosphorylation------MSFAESGWR
------CCHHHHHHH
32.9123401153
6Phosphorylation--MSFAESGWRSALR
--CCHHHHHHHHHHH
39.9822199227
10PhosphorylationFAESGWRSALRRRGP
HHHHHHHHHHHHHCC
25.7522199227
19PhosphorylationLRRRGPGTPGPVARP
HHHHCCCCCCCCCCC
28.3623401153
27PhosphorylationPGPVARPSYSSFTQG
CCCCCCCCCCCCCCC
31.9028450419
28PhosphorylationGPVARPSYSSFTQGD
CCCCCCCCCCCCCCC
15.8328450419
29PhosphorylationPVARPSYSSFTQGDS
CCCCCCCCCCCCCCC
24.2628450419
30PhosphorylationVARPSYSSFTQGDSW
CCCCCCCCCCCCCCC
24.8728450419
32PhosphorylationRPSYSSFTQGDSWGE
CCCCCCCCCCCCCCC
33.3228450419
36PhosphorylationSSFTQGDSWGEGEVD
CCCCCCCCCCCCCCC
43.7523927012
48S-palmitoylationEVDEEEGCDQVARDL
CCCCCCCHHHHHHHH
3.6029575903
60PhosphorylationRDLRAEFSAGAWSEP
HHHHHHHHCCCCCCC
19.8030266825
65PhosphorylationEFSAGAWSEPRKRSV
HHHCCCCCCCCCCCC
36.8730266825
71PhosphorylationWSEPRKRSVLPPDGN
CCCCCCCCCCCCCCC
30.9230266825
80PhosphorylationLPPDGNGSPVLPDKR
CCCCCCCCCCCCCCC
18.8123401153

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 AR6P6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AR6P6_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 AR6P6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
YKT6_HUMANYKT6physical
26186194
DUS3_HUMANDUSP3physical
26186194
PNPO_HUMANPNPOphysical
26186194
BLVRB_HUMANBLVRBphysical
26186194
GSTM1_HUMANGSTM1physical
26186194
PEBB_HUMANCBFBphysical
26186194
PMVK_HUMANPMVKphysical
26186194
NAA50_HUMANNAA50physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
PYGB_HUMANPYGBphysical
26186194
SNX3_HUMANSNX3physical
26186194
PNPO_HUMANPNPOphysical
28514442
DUS3_HUMANDUSP3physical
28514442
PMVK_HUMANPMVKphysical
28514442
SNX3_HUMANSNX3physical
28514442
GSTM1_HUMANGSTM1physical
28514442
NAA50_HUMANNAA50physical
28514442
CHM4A_HUMANCHMP4Aphysical
28514442
PEBB_HUMANCBFBphysical
28514442
YKT6_HUMANYKT6physical
28514442
BLVRB_HUMANBLVRBphysical
28514442
BID_HUMANBIDphysical
28514442

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 AR6P6_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-60 AND SER-65, AND MASSSPECTROMETRY.
"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-2; SER-36; SER-65 ANDSER-80, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, AND MASSSPECTROMETRY.

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