ACATN_MOUSE - dbPTM
ACATN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACATN_MOUSE
UniProt AC Q99J27
Protein Name Acetyl-coenzyme A transporter 1
Gene Name Slc33a1
Organism Mus musculus (Mouse).
Sequence Length 550
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides. [PubMed: 10570973 Negatively regulates BMP signaling (By similarity]
Protein Sequence MSPTISHKDSSRQRRSGMFSHALDMKSGPLPPGGWDDSRRDSVGGEGDREVLLGDAGPGDLPKAPRSYRSELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYFKNFGRRKSWLVPTQYTLGIFMIYLSTQVDRLLGNIDGRTPDVVALTVTFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENREASIVKEETQGITDTYKLLFSIIKMPAVLAFCLLILTSKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILPLLISKYTAGPQPLNIFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPLYYYIIVLLSYALHQVTLYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECVGASNQNCRTPDAIELCKKLGGSCVTALDGYYVESIICVLIGFGWWFFLGPKFKKLQDEGPSSWKCKRNN
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------MSPTISHKD
------CCCCCCCCC
30.6525777480
4Phosphorylation----MSPTISHKDSS
----CCCCCCCCCCH
28.0125777480
6Phosphorylation--MSPTISHKDSSRQ
--CCCCCCCCCCHHH
27.2825777480
10PhosphorylationPTISHKDSSRQRRSG
CCCCCCCCHHHHHCC
32.0225777480
11PhosphorylationTISHKDSSRQRRSGM
CCCCCCCHHHHHCCC
42.4325777480
16PhosphorylationDSSRQRRSGMFSHAL
CCHHHHHCCCHHHHH
36.4825521595
20PhosphorylationQRRSGMFSHALDMKS
HHHCCCHHHHHCCCC
10.0425521595
38PhosphorylationPPGGWDDSRRDSVGG
CCCCCCCCCCCCCCC
27.0923140645
42PhosphorylationWDDSRRDSVGGEGDR
CCCCCCCCCCCCCCC
22.3525521595
103N-linked_GlycosylationPLILQSKNVSYTDQA
HEEEECCCCCCCCHH
32.96-
160PhosphorylationIFMIYLSTQVDRLLG
HHHHHHHHHHHHHHC
29.9821183079
320PhosphorylationAFCLLILTSKIGFSA
HHHHHHHHHCCCCCH
22.45-
321PhosphorylationFCLLILTSKIGFSAA
HHHHHHHHCCCCCHH
20.87-
497S-palmitoylationTPDAIELCKKLGGSC
CHHHHHHHHHHCCCH
2.0728526873

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 ACATN_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACATN_MOUSE !!

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 ACATN_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACATN_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACATN_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.

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