CTL2_HUMAN - dbPTM
CTL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTL2_HUMAN
UniProt AC Q8IWA5
Protein Name Choline transporter-like protein 2
Gene Name SLC44A2
Organism Homo sapiens (Human).
Sequence Length 706
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Isoform 1, but not isoform 3, exhibits some choline transporter activity..
Protein Sequence MGDERPHYYGKHGTPQKYDPTFKGPIYNRGCTDIICCVFLLLAIVGYVAVGIIAWTHGDPRKVIYPTDSRGEFCGQKGTKNENKPYLFYFNIVKCASPLVLLEFQCPTPQICVEKCPDRYLTYLNARSSRDFEYYKQFCVPGFKNNKGVAEVLQDGDCPAVLIPSKPLARRCFPAIHAYKGVLMVGNETTYEDGHGSRKNITDLVEGAKKANGVLEARQLAMRIFEDYTVSWYWIIIGLVIAMAMSLLFIILLRFLAGIMVWVMIIMVILVLGYGIFHCYMEYSRLRGEAGSDVSLVDLGFQTDFRVYLHLRQTWLAFMIILSILEVIIILLLIFLRKRILIAIALIKEASRAVGYVMCSLLYPLVTFFLLCLCIAYWASTAVFLSTSNEAVYKIFDDSPCPFTAKTCNPETFPSSNESRQCPNARCQFAFYGGESGYHRALLGLQIFNAFMFFWLANFVLALGQVTLAGAFASYYWALRKPDDLPAFPLFSAFGRALRYHTGSLAFGALILAIVQIIRVILEYLDQRLKAAENKFAKCLMTCLKCCFWCLEKFIKFLNRNAYIMIAIYGTNFCTSARNAFFLLMRNIIRVAVLDKVTDFLFLLGKLLIVGSVGILAFFFFTHRIRIVQDTAPPLNYYWVPILTVIVGSYLIAHGFFSVYGMCVDTLFLCFLEDLERNDGSAERPYFMSSTLKKLLNKTNKKAAES
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
8PhosphorylationMGDERPHYYGKHGTP
CCCCCCCCCCCCCCC		19.3228152594
9PhosphorylationGDERPHYYGKHGTPQ
CCCCCCCCCCCCCCC		19.3628152594
10 (in isoform 3)Phosphorylation-14.3329978859
12 (in isoform 3)Phosphorylation-40.7829978859
14PhosphorylationHYYGKHGTPQKYDPT
CCCCCCCCCCCCCCC		23.4325159151
16 (in isoform 3)Phosphorylation-57.7029978859
17 (in isoform 1)Ubiquitination-53.4721906983
17UbiquitinationGKHGTPQKYDPTFKG
CCCCCCCCCCCCCCC		53.4721906983
18PhosphorylationKHGTPQKYDPTFKGP
CCCCCCCCCCCCCCC		23.1628176443
21PhosphorylationTPQKYDPTFKGPIYN
CCCCCCCCCCCCCCC		34.7728152594
27PhosphorylationPTFKGPIYNRGCTDI
CCCCCCCCCCCHHHH		11.26-
115AcetylationTPQICVEKCPDRYLT
CCCEEHHHCCHHHHH		30.587925323
120PhosphorylationVEKCPDRYLTYLNAR
HHHCCHHHHHHHHCC		15.69-
165PhosphorylationCPAVLIPSKPLARRC
CCEEEECCCHHHHHH		39.6524719451
187N-linked_GlycosylationKGVLMVGNETTYEDG
CEEEEECCCCCCCCC		31.8419349973
199UbiquitinationEDGHGSRKNITDLVE
CCCCCCCCCHHHHHH		55.16-
200N-linked_GlycosylationDGHGSRKNITDLVEG
CCCCCCCCHHHHHHH		41.0817660510
202PhosphorylationHGSRKNITDLVEGAK
CCCCCCHHHHHHHHH		32.45-
207 (in isoform 2)Ubiquitination-34.9121906983
209UbiquitinationTDLVEGAKKANGVLE
HHHHHHHHHCCCHHH		64.3721906983
209 (in isoform 1)Ubiquitination-64.3721906983
303PhosphorylationLVDLGFQTDFRVYLH
EEECCCCCCHHHHHH		34.54-
404 (in isoform 2)Ubiquitination-16.6421906983
406UbiquitinationSPCPFTAKTCNPETF
CCCCCCCCCCCCCCC		51.0221906983
406 (in isoform 1)Ubiquitination-51.0221906983
417N-linked_GlycosylationPETFPSSNESRQCPN
CCCCCCCCCCCCCCC		56.4517660510
479 (in isoform 2)Ubiquitination-4.4721906983
481 (in isoform 1)Ubiquitination-54.3621906983
481UbiquitinationSYYWALRKPDDLPAF
HHHHHHCCCCCCCCC		54.3621906983
492PhosphorylationLPAFPLFSAFGRALR
CCCCHHHHHHHHHHH		30.30-
500PhosphorylationAFGRALRYHTGSLAF
HHHHHHHHHHHHHHH		12.4628270605
502PhosphorylationGRALRYHTGSLAFGA
HHHHHHHHHHHHHHH		21.3828270605
504PhosphorylationALRYHTGSLAFGALI
HHHHHHHHHHHHHHH		20.0628270605
563PhosphorylationKFLNRNAYIMIAIYG
HHHCCCCEEEEEECC		8.45-
681PhosphorylationDLERNDGSAERPYFM
HHHHCCCCCCCCHHH		29.8028060719
686PhosphorylationDGSAERPYFMSSTLK
CCCCCCCHHHHHHHH		20.3828060719
689PhosphorylationAERPYFMSSTLKKLL
CCCCHHHHHHHHHHH		15.4020873877
690PhosphorylationERPYFMSSTLKKLLN
CCCHHHHHHHHHHHH		26.4320873877
691PhosphorylationRPYFMSSTLKKLLNK
CCHHHHHHHHHHHHH		34.9825849741
693 (in isoform 1)Ubiquitination-41.2721906983
693UbiquitinationYFMSSTLKKLLNKTN
HHHHHHHHHHHHHHH		41.272190698
698UbiquitinationTLKKLLNKTNKKAAE
HHHHHHHHHHHHHHC		54.14-
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 CTL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTL2_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 CTL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CTL2_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
DB00122Choline
Regulatory Network of CTL2_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-200, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-200, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory