ACATN_HUMAN - dbPTM
ACATN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACATN_HUMAN
UniProt AC O00400
Protein Name Acetyl-coenzyme A transporter 1
Gene Name SLC33A1
Organism Homo sapiens (Human).
Sequence Length 549
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides. [PubMed: 9096318 Negatively regulates BMP signaling]
Protein Sequence MSPTISHKDSSRQRRPGNFSHSLDMKSGPLPPGGWDDSHLDSAGREGDREALLGDTGTGDFLKAPQSFRAELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYVKNFGRRKSWLVPTQYILGLFMIYLSTQVDRLLGNTDDRTPDVIALTVAFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENEVSVVKEETQGITDTYKLLFAIIKMPAVLTFCLLILTAKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILPLIISKYTAGPQPLNTFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPIYYYIVVLLSYALHQVTVYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECVGASNQNCRTPDAVELCKKLGGSCVTALDGYYVESIICVFIGFGWWFFLGPKFKKLQDEGSSSWKCKRNN
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		30.6529255136
4Phosphorylation----MSPTISHKDSS
----CCCCCCCCCCC		28.0129514088
6Phosphorylation--MSPTISHKDSSRQ
--CCCCCCCCCCCCC		27.2825404012
20PhosphorylationQRRPGNFSHSLDMKS
CCCCCCCCCCCCCCC		19.0321406692
22PhosphorylationRPGNFSHSLDMKSGP
CCCCCCCCCCCCCCC		25.5125159151
38PhosphorylationPPGGWDDSHLDSAGR
CCCCCCHHHHHCCCC		24.3928555341
42PhosphorylationWDDSHLDSAGREGDR
CCHHHHHCCCCCCCH		38.70-
63UbiquitinationTGTGDFLKAPQSFRA
CCCCHHHHCCHHHHH		59.0021906983
103N-linked_GlycosylationPLILQSKNVSYTDQA
HEEEECCCCCCCCHH		32.96UniProtKB CARBOHYD
133PhosphorylationAPLVDAVYVKNFGRR
HHHCCEEEEECCCCC		13.87-
135UbiquitinationLVDAVYVKNFGRRKS
HCCEEEEECCCCCCC		28.9521963094
288UbiquitinationENEVSVVKEETQGIT
HCCCEEEECCCCCCC		47.9129967540
325PhosphorylationLTAKIGFSAADAVTG
HHHHHCCCHHHHHHC		19.82-
331PhosphorylationFSAADAVTGLKLVEE
CCHHHHHHCCCHHHC		38.22-
364PhosphorylationIILPLIISKYTAGPQ
HHHHHHHHHCCCCCC		16.77-
366PhosphorylationLPLIISKYTAGPQPL
HHHHHHHCCCCCCCC		8.6023663014
367PhosphorylationPLIISKYTAGPQPLN
HHHHHHCCCCCCCCH		28.9523663014
375PhosphorylationAGPQPLNTFYKAMPY
CCCCCCHHHHHHHHH		35.7023663014
377PhosphorylationPQPLNTFYKAMPYRL
CCCCHHHHHHHHHHH		8.8723663014
378UbiquitinationQPLNTFYKAMPYRLL
CCCHHHHHHHHHHHH		33.74-
382PhosphorylationTFYKAMPYRLLLGLE
HHHHHHHHHHHHHHH		10.7823663014
496S-palmitoylationTPDAVELCKKLGGSC
CHHHHHHHHHHCCCH		2.0129575903
497UbiquitinationPDAVELCKKLGGSCV
HHHHHHHHHHCCCHH		64.7529967540
498UbiquitinationDAVELCKKLGGSCVT
HHHHHHHHHCCCHHH		51.90-
534UbiquitinationFLGPKFKKLQDEGSS
HHCHHHHHHCCCCCC		55.2929967540
541PhosphorylationKLQDEGSSSWKCKRN
HHCCCCCCCCCCCCC		51.58-
544UbiquitinationDEGSSSWKCKRNN--
CCCCCCCCCCCCC--		31.6529967540
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACATN_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 ACATN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT2A2_HUMANATP2A2physical
26496610
ATPA_HUMANATP5A1physical
26496610
ATP5E_HUMANATP5Ephysical
26496610
ATPO_HUMANATP5Ophysical
26496610
CALX_HUMANCANXphysical
26496610
CLCN7_HUMANCLCN7physical
26496610
CLIC1_HUMANCLIC1physical
26496610
EF1D_HUMANEEF1Dphysical
26496610
EF1G_HUMANEEF1Gphysical
26496610
HS90B_HUMANHSP90AB1physical
26496610
METK2_HUMANMAT2Aphysical
26496610
KI67_HUMANMKI67physical
26496610
RON_HUMANMST1Rphysical
26496610
MYO1E_HUMANMYO1Ephysical
26496610
MERL_HUMANNF2physical
26496610
PROF1_HUMANPFN1physical
26496610
RAD51_HUMANRAD51physical
26496610
CTR1_HUMANSLC7A1physical
26496610
TAP1_HUMANTAP1physical
26496610
ELOB_HUMANTCEB2physical
26496610
TPM4_HUMANTPM4physical
26496610
ENPL_HUMANHSP90B1physical
26496610
SEM3B_HUMANSEMA3Bphysical
26496610
TAGL2_HUMANTAGLN2physical
26496610
ARHG7_HUMANARHGEF7physical
26496610
ZW10_HUMANZW10physical
26496610
SPN1_HUMANSNUPNphysical
26496610
RAD50_HUMANRAD50physical
26496610
INADL_HUMANINADLphysical
26496610
CEPT1_HUMANCEPT1physical
26496610
HAX1_HUMANHAX1physical
26496610
CKAP4_HUMANCKAP4physical
26496610
MIC60_HUMANIMMTphysical
26496610
S27A2_HUMANSLC27A2physical
26496610
UBP24_HUMANUSP24physical
26496610
ECM29_HUMANKIAA0368physical
26496610
SERA_HUMANPHGDHphysical
26496610
CKAP2_HUMANCKAP2physical
26496610
FABD_HUMANMCATphysical
26496610
GIT1_HUMANGIT1physical
26496610
RAB14_HUMANRAB14physical
26496610
MACOI_HUMANTMEM57physical
26496610
NCLN_HUMANNCLNphysical
26496610
DOCK6_HUMANDOCK6physical
26496610
DEFM_HUMANPDFphysical
26496610
CS043_HUMANC19orf43physical
26496610
ELMO3_HUMANELMO3physical
26496610
NUD18_HUMANNUDT18physical
26496610
ZN598_HUMANZNF598physical
26496610
MSL1_HUMANMSL1physical
26496610
RBM42_HUMANRBM42physical
28514442
Drug and Disease Associations
Kegg Disease
H00266 Hereditary spastic paraplegia (SPG)
OMIM Disease
612539Spastic paraplegia 42, autosomal dominant (SPG42)
614482Congenital cataracts, hearing loss, and neurodegeneration (CCHLND)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACATN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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, AND MASSSPECTROMETRY.

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