CTR2_HUMAN - dbPTM
CTR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTR2_HUMAN
UniProt AC P52569
Protein Name Cationic amino acid transporter 2
Gene Name SLC7A2
Organism Homo sapiens (Human).
Sequence Length 658
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Functions as permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine); the affinity for its substrates differs between isoforms created by alternative splicing. Isoform 1 functions as permease that mediates the transport of the cationic amino acids (arginine, lysine and ornithine), and it has much higher affinity for arginine than isoform 2. Isoform 2 functions as low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine). [PubMed: 9174363 May play a role in classical or alternative activation of macrophages via its role in arginine transport.]
Protein Sequence MIPCRAALTFARCLIRRKIVTLDSLEDTKLCRCLSTMDLIALGVGSTLGAGVYVLAGEVAKADSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVTVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLSKQIGQFLRTYFRMNYTGLAEYPDFFAVCLILLLAGLLSFGVKESAWVNKVFTAVNILVLLFVMVAGFVKGNVANWKISEEFLKNISASAREPPSENGTSIYGAGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVTSLLVCFMAYFGVSAALTLMMPYYLLDEKSPLPVAFEYVGWGPAKYVVAAGSLCALSTSLLGSIFPMPRVIYAMAEDGLLFKCLAQINSKTKTPIIATLSSGAVAALMAFLFDLKALVDMMSIGTLMAYSLVAACVLILRYQPGLSYDQPKCSPEKDGLGSSPRVTSKSESQVTMLQRQGFSMRTLFCPSLLPTQQSASLVSFLVGFLAFLVLGLSVLTTYGVHAITRLEAWSLALLALFLVLFVAIVLTIWRQPQNQQKVAFMVPFLPFLPAFSILVNIYLMVQLSADTWVRFSIWMAIGFLIYFSYGIRHSLEGHLRDENNEEDAYPDNVHAAAEEKSAIQANDHHPRNLSSPFIFHEKTSEF
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
6 (in isoform 2)Phosphorylation-17.34-
6 (in isoform 3)Phosphorylation-17.34-
10 (in isoform 2)Phosphorylation-4.14-
10 (in isoform 3)Phosphorylation-4.14-
21PhosphorylationLIRRKIVTLDSLEDT
HHHCCCCCHHHCCHH		28.4623186163
24PhosphorylationRKIVTLDSLEDTKLC
CCCCCHHHCCHHCHH		36.4525849741
28PhosphorylationTLDSLEDTKLCRCLS
CHHHCCHHCHHHHHC		19.2821815630
29UbiquitinationLDSLEDTKLCRCLST
HHHCCHHCHHHHHCH		58.8933845483
35PhosphorylationTKLCRCLSTMDLIAL
HCHHHHHCHHCHHHH		25.8822210691
36PhosphorylationKLCRCLSTMDLIALG
CHHHHHCHHCHHHHC		11.1922210691
69 (in isoform 2)Ubiquitination-3.28-
69UbiquitinationADSGPSIVVSFLIAA
CCCCCHHHHHHHHHH		3.2833845483
157N-linked_GlycosylationLRTYFRMNYTGLAEY
HHHHHHCCCCCHHHC		27.27UniProtKB CARBOHYD
221PhosphorylationNVANWKISEEFLKNI
CCCCCCCCHHHHHHH		27.6127174698
226 (in isoform 1)Ubiquitination-58.5221906983
226UbiquitinationKISEEFLKNISASAR
CCCHHHHHHHCCCCC		58.5221906983
227N-linked_GlycosylationISEEFLKNISASARE
CCHHHHHHHCCCCCC		35.28UniProtKB CARBOHYD
229PhosphorylationEEFLKNISASAREPP
HHHHHHHCCCCCCCC		26.0927174698
231PhosphorylationFLKNISASAREPPSE
HHHHHCCCCCCCCCC		22.5227174698
239N-linked_GlycosylationAREPPSENGTSIYGA
CCCCCCCCCCEEECC		64.48UniProtKB CARBOHYD
266 (in isoform 3)Ubiquitination-10.9821906983
266 (in isoform 2)Ubiquitination-10.9821906983
376S-palmitoylationEDGLLFKCLAQINSK
CCCHHHHHHHHCCCC		2.7429575903
415PhosphorylationKALVDMMSIGTLMAY
HHHHHHHHHHHHHHH		15.95-
422PhosphorylationSIGTLMAYSLVAACV
HHHHHHHHHHHHHHH		6.64-
437 (in isoform 2)Phosphorylation-16.25-
440PhosphorylationRYQPGLSYDQPKCSP
HHCCCCCCCCCCCCC		24.5221712546
443UbiquitinationPGLSYDQPKCSPEKD
CCCCCCCCCCCCCCC		36.4023503661
444UbiquitinationGLSYDQPKCSPEKDG
CCCCCCCCCCCCCCC		41.5333845483
446PhosphorylationSYDQPKCSPEKDGLG
CCCCCCCCCCCCCCC		42.0720873877
448UbiquitinationDQPKCSPEKDGLGSS
CCCCCCCCCCCCCCC		47.7021987572
449UbiquitinationQPKCSPEKDGLGSSP
CCCCCCCCCCCCCCC		61.5521987572
454PhosphorylationPEKDGLGSSPRVTSK
CCCCCCCCCCCCCCC		42.0629255136
455PhosphorylationEKDGLGSSPRVTSKS
CCCCCCCCCCCCCCC		18.2229255136
459PhosphorylationLGSSPRVTSKSESQV
CCCCCCCCCCCHHHH		31.5529083192
460UbiquitinationGSSPRVTSKSESQVT
CCCCCCCCCCHHHHH		31.1821963094
460PhosphorylationGSSPRVTSKSESQVT
CCCCCCCCCCHHHHH		31.1824719451
461 (in isoform 1)Ubiquitination-49.2121906983
461UbiquitinationSSPRVTSKSESQVTM
CCCCCCCCCHHHHHH		49.2121963094
462PhosphorylationSPRVTSKSESQVTML
CCCCCCCCHHHHHHH		42.1025849741
464PhosphorylationRVTSKSESQVTMLQR
CCCCCCHHHHHHHHH		36.7225849741
467PhosphorylationSKSESQVTMLQRQGF
CCCHHHHHHHHHCCC		12.4325849741
483UbiquitinationMRTLFCPSLLPTQQS
HHHCCCCCCCCCHHH		43.6633845483
484UbiquitinationRTLFCPSLLPTQQSA
HHCCCCCCCCCHHHH		3.9233845483
486 (in isoform 3)Phosphorylation-33.1924719451
488UbiquitinationCPSLLPTQQSASLVS
CCCCCCCHHHHHHHH		33.0421987572
488 (in isoform 2)Ubiquitination-33.04-
489UbiquitinationPSLLPTQQSASLVSF
CCCCCCHHHHHHHHH		43.3621987572
494 (in isoform 3)Phosphorylation-3.3524719451
500UbiquitinationLVSFLVGFLAFLVLG
HHHHHHHHHHHHHHH		3.2921963094
500 (in isoform 2)Ubiquitination-3.2921906983
501 (in isoform 3)Ubiquitination-2.4421906983
501UbiquitinationVSFLVGFLAFLVLGL
HHHHHHHHHHHHHHH		2.4421963094
504 (in isoform 3)Phosphorylation-2.3024719451
621PhosphorylationENNEEDAYPDNVHAA
CCCCCCCCCCCHHHH		24.3629978859
631UbiquitinationNVHAAAEEKSAIQAN
CHHHHHHHHCHHCCC		47.8121963094
632UbiquitinationVHAAAEEKSAIQAND
HHHHHHHHCHHCCCC		36.3721963094
632 (in isoform 1)Ubiquitination-36.3721906983
633PhosphorylationHAAAEEKSAIQANDH
HHHHHHHCHHCCCCC		33.6128348404
646PhosphorylationDHHPRNLSSPFIFHE
CCCCCCCCCCCEEEC		39.2428355574
647PhosphorylationHHPRNLSSPFIFHEK
CCCCCCCCCCEEECC		27.3128355574
653UbiquitinationSSPFIFHEKTSEF--
CCCCEEECCCCCC--		47.4821987572
654UbiquitinationSPFIFHEKTSEF---
CCCEEECCCCCC---		49.1033845483
654SumoylationSPFIFHEKTSEF---
CCCEEECCCCCC---		49.10-
654 (in isoform 1)Ubiquitination-49.1021906983
655PhosphorylationPFIFHEKTSEF----
CCEEECCCCCC----		30.4223312004
656PhosphorylationFIFHEKTSEF-----
CEEECCCCCC-----		48.3423312004
661 (in isoform 3)Phosphorylation-27642862
671 (in isoform 2)Ubiquitination-21906983
671Ubiquitination--------------------
--------------------		21963094
672Ubiquitination---------------------
---------------------		21963094
672 (in isoform 3)Ubiquitination-21906983
673 (in isoform 3)Phosphorylation-27251275
686 (in isoform 3)Phosphorylation-24719451
687 (in isoform 3)Phosphorylation-24719451
693 (in isoform 2)Ubiquitination-21906983
693Ubiquitination------------------------------------------
------------------------------------------		33845483
694Ubiquitination-------------------------------------------
-------------------------------------------		33845483
694 (in isoform 3)Ubiquitination-21906983
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 CTR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTR2_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 CTR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CTR2_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
DB00123L-Lysine
DB00129L-Ornithine
Regulatory Network of CTR2_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-646, AND MASSSPECTROMETRY.

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