LAT1_HUMAN - dbPTM
LAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAT1_HUMAN
UniProt AC Q01650
Protein Name Large neutral amino acids transporter small subunit 1
Gene Name SLC7A5
Organism Homo sapiens (Human).
Sequence Length 507
Subcellular Localization Cytoplasm, cytosol. Apical cell membrane
Multi-pass membrane protein. Located to the plasma membrane by SLC3A2/4F2hc. Localized to the apical membrane of placental syncytiophoblastic cells. Expressed in both luminal and abluminal membranes of brain
Protein Description Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L-leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. When associated with LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation. [PubMed: 25998567]
Protein Sequence MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
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
72-Hydroxyisobutyrylation-MAGAGPKRRALAAP
-CCCCCHHHHCCCCC		54.31-
7Ubiquitination-MAGAGPKRRALAAP
-CCCCCHHHHCCCCC		54.3133845483
19UbiquitinationAAPAAEEKEEAREKM
CCCCHHHHHHHHHHH		52.9727667366
19AcetylationAAPAAEEKEEAREKM
CCCCHHHHHHHHHHH		52.9726051181
192-HydroxyisobutyrylationAAPAAEEKEEAREKM
CCCCHHHHHHHHHHH		52.97-
25UbiquitinationEKEEAREKMLAAKSA
HHHHHHHHHHHHHHC		33.3923000965
252-HydroxyisobutyrylationEKEEAREKMLAAKSA
HHHHHHHHHHHHHHC		33.39-
30UbiquitinationREKMLAAKSADGSAP
HHHHHHHHHCCCCCC		40.3421890473
30AcetylationREKMLAAKSADGSAP
HHHHHHHHHCCCCCC		40.3426051181
302-HydroxyisobutyrylationREKMLAAKSADGSAP
HHHHHHHHHCCCCCC		40.34-
30UbiquitinationREKMLAAKSADGSAP
HHHHHHHHHCCCCCC		40.3423000965
31PhosphorylationEKMLAAKSADGSAPA
HHHHHHHHCCCCCCC		27.1919664994
35PhosphorylationAAKSADGSAPAGEGE
HHHHCCCCCCCCCCC		31.4619664994
45PhosphorylationAGEGEGVTLQRNITL
CCCCCCCCHHHCCEE		28.2023927012
49N-linked_GlycosylationEGVTLQRNITLLNGV
CCCCHHHCCEEECCC		20.73UniProtKB CARBOHYD
225PhosphorylationQIGKGDVSNLDPNFS
HCCCCCHHHCCCCCC		36.0921712546
230N-linked_GlycosylationDVSNLDPNFSFEGTK
CHHHCCCCCCCCCCC		44.88UniProtKB CARBOHYD
245UbiquitinationLDVGNIVLALYSGLF
CCHHHHHHHHHHHHH		2.1127667366
267UbiquitinationLNFVTEEMINPYRNL
HHCCCHHHCCCCCCC		2.6727667366
302UbiquitinationAYFTTLSTEQMLSSE
HHHHCCCHHHHHCCC		33.0922817900
304UbiquitinationFTTLSTEQMLSSEAV
HHCCCHHHHHCCCEE		37.9022817900
306UbiquitinationTLSTEQMLSSEAVAV
CCCHHHHHCCCEEEE		5.2122817900
324UbiquitinationNYHLGVMSWIIPVFV
CHHHHHHHHHHHHHH		16.8422817900
326UbiquitinationHLGVMSWIIPVFVGL
HHHHHHHHHHHHHCH		1.6822817900
328UbiquitinationGVMSWIIPVFVGLSC
HHHHHHHHHHHCHHC		12.3621963094
340N-linked_GlycosylationLSCFGSVNGSLFTSS
HHCCCCCCCCEECCC		35.71UniProtKB CARBOHYD
354PhosphorylationSRLFFVGSREGHLPS
CEEEEECCCCCCHHH		23.1221712546
380UbiquitinationPVPSLVFTCVMTLLY
CCHHHHHHHHHHHHH		9.1927667366
422UbiquitinationMIWLRHRKPELERPI
HHHHHCCCCCCCCCC		36.4033845483
437UbiquitinationKVNLALPVFFILACL
CCCCHHHHHHHHHHH		6.7722817900
439UbiquitinationNLALPVFFILACLFL
CCHHHHHHHHHHHHH		4.5622817900
441UbiquitinationALPVFFILACLFLIA
HHHHHHHHHHHHHHH		2.0222817900
479UbiquitinationYFFGVWWKNKPKWLL
EEEEEECCCCCHHHH		39.1122817900
481UbiquitinationFGVWWKNKPKWLLQG
EEEECCCCCHHHHHH		44.2222817900
483UbiquitinationVWWKNKPKWLLQGIF
EECCCCCHHHHHHHH		52.6721963094
507PhosphorylationMQVVPQET-------
HHHCCCCC-------		38.3716097034
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 LAT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAT1_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 LAT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LAT1_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
DB00509Dextrothyroxine
DB01235L-DOPA
DB00451Levothyroxine
DB00279Liothyronine
DB01042Melphalan
Regulatory Network of LAT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-30, AND MASSSPECTROMETRY.

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