CTL1_HUMAN - dbPTM
CTL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTL1_HUMAN
UniProt AC Q8WWI5
Protein Name Choline transporter-like protein 1
Gene Name SLC44A1
Organism Homo sapiens (Human).
Sequence Length 657
Subcellular Localization Cell membrane
Multi-pass membrane protein . Mitochondrion outer membrane
Multi-pass membrane protein .
Protein Description Choline transporter. May be involved in membrane synthesis and myelin production..
Protein Sequence MGCCSSASSAAQSSKREWKPLEDRSCTDIPWLLLFILFCIGMGFICGFSIATGAAARLVSGYDSYGNICGQKNTKLEAIPNSGMDHTQRKYVFFLDPCNLDLINRKIKSVALCVAACPRQELKTLSDVQKFAEINGSALCSYNLKPSEYTTSPKSSVLCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTILVILGSLGGTGVLWWLYAKQRRSPKETVTPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWVYWIMTLLFLGTTGSPVQNEQGFVEFKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDKRNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMILMYIHSQLKGKENACARCVLKSCICCLWCLEKCLNYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVATINTVGDFMLFLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLCFAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGVADSRELKPMASGASSA
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
2Myristoylation------MGCCSSASS
------CCCCCCHHH
22.5722223895
75UbiquitinationICGQKNTKLEAIPNS
CCCCCCCCEEECCCC
54.44-
98S-palmitoylationYVFFLDPCNLDLINR
EEEEECCCCHHHHCH
8.6829575903
123UbiquitinationACPRQELKTLSDVQK
HCCHHHHCCHHHHHH
46.82-
167PhosphorylationPKLPVPASAPIPFFH
CCCCCCCCCCCCCCC
28.62-
180N-linked_GlycosylationFHRCAPVNISCYAKF
CCCCCCCCHHHHHHH
21.2817660510
263PhosphorylationTGVLWWLYAKQRRSP
HHHHHHHHHCCCCCC
9.6822817900
447PhosphorylationLGTVAKGSFIITLVK
HCCCCCCCEEEEEEH
16.7426503514
462PhosphorylationIPRMILMYIHSQLKG
HHHHHHHHHHHHHCC
7.6426503514
465PhosphorylationMILMYIHSQLKGKEN
HHHHHHHHHHCCCCC
27.8726503514
468AcetylationMYIHSQLKGKENACA
HHHHHHHCCCCCHHH
61.3711688447
611PhosphorylationDTKYNDGSPGREFYM
CCCCCCCCCCHHCHH
27.3525159151
638UbiquitinationKAMKEAGKGGVADSR
HHHHHHCCCCCCCCH
60.58-
644PhosphorylationGKGGVADSRELKPMA
CCCCCCCCHHHCCCC
20.2323401153
648UbiquitinationVADSRELKPMASGAS
CCCCHHHCCCCCCCC
28.1721906983
648 (in isoform 1)Ubiquitination-28.1721906983
652PhosphorylationRELKPMASGASSA--
HHHCCCCCCCCCC--
28.7411698453
652O-linked_GlycosylationRELKPMASGASSA--
HHHCCCCCCCCCC--
28.7428657654
655PhosphorylationKPMASGASSA-----
CCCCCCCCCC-----
30.2629255136
656PhosphorylationPMASGASSA------
CCCCCCCCC------
37.1529255136

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 CTL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTL1_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 CTL1_HUMAN !!

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

Oops, there are no PPI records of CTL1_HUMAN !!

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 CTL1_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-652 AND SER-655, ANDMASS SPECTROMETRY.

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