4F2_HUMAN - dbPTM
4F2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 4F2_HUMAN
UniProt AC P08195
Protein Name 4F2 cell-surface antigen heavy chain
Gene Name SLC3A2
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Apical cell membrane
Single-pass type II membrane protein. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localized to the plasma membrane when associated with SLC7A5 or SLC7A8. Localized to the placent
Protein Description Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also 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. 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. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier. 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 MELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
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
1Acetylation-------MELQPPEA
-------CCCCCCCC		11.9322814378
2Acetylation------MELQPPEAS
------CCCCCCCCE		56.9919691289
2Phosphorylation------MELQPPEAS
------CCCCCCCCE		56.9917081983
2 (in isoform 2)Acetylation-56.9919413330
2 (in isoform 2)Phosphorylation-56.9925849741
5Phosphorylation---MELQPPEASIAV
---CCCCCCCCEEEE		41.1217081983
5 (in isoform 2)Phosphorylation-41.1225159151
9PhosphorylationELQPPEASIAVVSIP
CCCCCCCEEEEEECC		14.9320068231
14PhosphorylationEASIAVVSIPRQLPG
CCEEEEEECCCCCCC		21.9224719451
22 (in isoform 3)Phosphorylation-23.1521955146
24 (in isoform 3)Phosphorylation-30.7321955146
32 (in isoform 3)Phosphorylation-36.7121955146
37PhosphorylationGLSAGDDSELGSHCV
CCCCCCCCHHHHHCH		39.1927251275
37 (in isoform 3)Phosphorylation-39.1921955146
39 (in isoform 3)Phosphorylation-11.1821955146
41AcetylationGDDSELGSHCVAQTG
CCCCHHHHHCHHHHH		26.7419691289
41PhosphorylationGDDSELGSHCVAQTG
CCCCHHHHHCHHHHH		26.7419691289
41 (in isoform 3)Phosphorylation-26.7419691289
44 (in isoform 3)Phosphorylation-3.5617081983
46 (in isoform 2)Ubiquitination-18.7221890473
49 (in isoform 3)Ubiquitination-4.81-
59 (in isoform 2)Ubiquitination-32.9821890473
65 (in isoform 2)Ubiquitination-10.4921890473
70PhosphorylationQNAEMIETGSDCVTQ
HCHHHHHHCCHHHHH		30.9422468782
70 (in isoform 2)Ubiquitination-30.9421890473
72AcetylationAEMIETGSDCVTQAG
HHHHHHCCHHHHHHH		34.94-
72PhosphorylationAEMIETGSDCVTQAG
HHHHHHCCHHHHHHH		34.9419691289
76PhosphorylationETGSDCVTQAGLQLL
HHCCHHHHHHHHHHH		21.0222468782
85 (in isoform 3)Ubiquitination-34.9321890473
98 (in isoform 3)Ubiquitination-5.7821890473
99PhosphorylationASKNAEVTGTMSQDT
HCCCCCCEECCCCCC		20.5921406692
101PhosphorylationKNAEVTGTMSQDTEV
CCCCCEECCCCCCCC		12.3221406692
103AcetylationAEVTGTMSQDTEVDM
CCCEECCCCCCCCCH		25.4119691289
103PhosphorylationAEVTGTMSQDTEVDM
CCCEECCCCCCCCCH		25.4125159151
104 (in isoform 3)Ubiquitination-51.3121890473
106PhosphorylationTGTMSQDTEVDMKEV
EECCCCCCCCCHHEE		30.2125159151
109 (in isoform 3)Ubiquitination-35.8821890473
111UbiquitinationQDTEVDMKEVELNEL
CCCCCCHHEEEHHHC		54.8921906983
122UbiquitinationLNELEPEKQPMNAAS
HHHCCCCCCCCCHHH		71.1120972266
125SulfoxidationLEPEKQPMNAASGAA
CCCCCCCCCHHHHHH		5.0228465586
129PhosphorylationKQPMNAASGAAMSLA
CCCCCHHHHHHHHHH		26.9330266825
133SulfoxidationNAASGAAMSLAGAEK
CHHHHHHHHHHHHHH		3.1528465586
134AcetylationAASGAAMSLAGAEKN
HHHHHHHHHHHHHHC		15.44-
134PhosphorylationAASGAAMSLAGAEKN
HHHHHHHHHHHHHHC		15.4430266825
134 (in isoform 4)Phosphorylation-15.4419691289
135PhosphorylationASGAAMSLAGAEKNG
HHHHHHHHHHHHHCC		3.0727251275
140UbiquitinationMSLAGAEKNGLVKIK
HHHHHHHHCCCEEEE		56.6421906983
145UbiquitinationAEKNGLVKIKVAEDE
HHHCCCEEEEECCCH		41.6821906983
147AcetylationKNGLVKIKVAEDEAE
HCCCEEEEECCCHHH		29.6726051181
147UbiquitinationKNGLVKIKVAEDEAE
HCCCEEEEECCCHHH		29.6718781797
147 (in isoform 1)Ubiquitination-29.6721890473
160AcetylationAEAAAAAKFTGLSKE
HHHHHHHHHHCCCHH		38.4427452117
160UbiquitinationAEAAAAAKFTGLSKE
HHHHHHHHHHCCCHH		38.4421890473
160 (in isoform 1)Ubiquitination-38.4421890473
162PhosphorylationAAAAAKFTGLSKEEL
HHHHHHHHCCCHHHH		36.1830266825
165PhosphorylationAAKFTGLSKEELLKV
HHHHHCCCHHHHHHH		39.0930266825
166AcetylationAKFTGLSKEELLKVA
HHHHCCCHHHHHHHH		61.3225825284
166SumoylationAKFTGLSKEELLKVA
HHHHCCCHHHHHHHH		61.32-
166UbiquitinationAKFTGLSKEELLKVA
HHHHCCCHHHHHHHH		61.3221890473
166 (in isoform 1)Ubiquitination-61.3221890473
171UbiquitinationLSKEELLKVAGSPGW
CCHHHHHHHHCCCHH		42.5422053931
171 (in isoform 1)Ubiquitination-42.5421890473
171 (in isoform 4)Ubiquitination-42.54-
175PhosphorylationELLKVAGSPGWVRTR
HHHHHHCCCHHHHHH		15.5321815630
178 (in isoform 4)Ubiquitination-4.6421890473
181PhosphorylationGSPGWVRTRWALLLL
CCCHHHHHHHHHHHH		22.42-
191 (in isoform 4)Ubiquitination-2.5021890473
197 (in isoform 4)Ubiquitination-3.6421890473
202 (in isoform 4)Ubiquitination-2.1521890473
217AcetylationCRELPAQKWWHTGAL
CCCCCCCCCEECCCE		55.1227452117
217UbiquitinationCRELPAQKWWHTGAL
CCCCCCCCCEECCCE		55.12-
245AcetylationAGNLAGLKGRLDYLS
CCHHCCHHHHHHHHH		40.8626051181
245UbiquitinationAGNLAGLKGRLDYLS
CCHHCCHHHHHHHHH		40.8621906983
248 (in isoform 4)Ubiquitination-7.47-
250PhosphorylationGLKGRLDYLSSLKVK
CHHHHHHHHHHCCCC		17.0528152594
252PhosphorylationKGRLDYLSSLKVKGL
HHHHHHHHHCCCCEE		27.6524719451
253PhosphorylationGRLDYLSSLKVKGLV
HHHHHHHHCCCCEEE		29.6121815630
255AcetylationLDYLSSLKVKGLVLG
HHHHHHCCCCEEEEC		43.8027452117
255UbiquitinationLDYLSSLKVKGLVLG
HHHHHHCCCCEEEEC		43.80-
257UbiquitinationYLSSLKVKGLVLGPI
HHHHCCCCEEEECCC		44.96-
266AcetylationLVLGPIHKNQKDDVA
EEECCCCCCCCCCCC		62.8927452117
266UbiquitinationLVLGPIHKNQKDDVA
EEECCCCCCCCCCCC		62.89-
269UbiquitinationGPIHKNQKDDVAQTD
CCCCCCCCCCCCCCC		66.3521906983
276 (in isoform 4)Ubiquitination-33.05-
286 (in isoform 4)Ubiquitination-28.83-
287AcetylationIDPNFGSKEDFDSLL
CCCCCCCHHHHHHHH		62.7826051181
287UbiquitinationIDPNFGSKEDFDSLL
CCCCCCCHHHHHHHH		62.7821906983
288 (in isoform 4)Ubiquitination-66.66-
292PhosphorylationGSKEDFDSLLQSAKK
CCHHHHHHHHHHHHH		30.8521712546
296PhosphorylationDFDSLLQSAKKKSIR
HHHHHHHHHHHCCEE		41.8625159151
298AcetylationDSLLQSAKKKSIRVI
HHHHHHHHHCCEEEE		67.0127452117
298SuccinylationDSLLQSAKKKSIRVI
HHHHHHHHHCCEEEE		67.0123954790
298UbiquitinationDSLLQSAKKKSIRVI
HHHHHHHHHCCEEEE		67.01-
300 (in isoform 4)Ubiquitination-50.86-
301PhosphorylationLQSAKKKSIRVILDL
HHHHHHCCEEEEEEC		25.2218452278
309PhosphorylationIRVILDLTPNYRGEN
EEEEEECCCCCCCCC		14.78-
312PhosphorylationILDLTPNYRGENSWF
EEECCCCCCCCCCCC		22.6218452278
317PhosphorylationPNYRGENSWFSTQVD
CCCCCCCCCCCCCHH		25.7921712546
320PhosphorylationRGENSWFSTQVDTVA
CCCCCCCCCCHHHHH		16.2121712546
321PhosphorylationGENSWFSTQVDTVAT
CCCCCCCCCHHHHHH		24.1221712546
329UbiquitinationQVDTVATKVKDALEF
CHHHHHHHHHHHHHH		37.2321906983
354UbiquitinationVRDIENLKDASSFLA
EECHHHCCCHHHHHH		63.9321906983
362 (in isoform 4)Ubiquitination-52.31-
365N-linked_GlycosylationSFLAEWQNITKGFSE
HHHHHHHHHCCCCCC		44.9912754519
368UbiquitinationAEWQNITKGFSEDRL
HHHHHHCCCCCCCCE		54.9121906983
381N-linked_GlycosylationRLLIAGTNSSDLQQI
CEEEEECCHHHHHHH		38.3012754519
385 (in isoform 4)Ubiquitination-4.33-
395N-linked_GlycosylationILSLLESNKDLLLTS
HHHHHHHCCCEEEEE		32.2719349973
402PhosphorylationNKDLLLTSSYLSDSG
CCCEEEEEEECCCCC		19.56-
403PhosphorylationKDLLLTSSYLSDSGS
CCEEEEEEECCCCCC		25.51-
404PhosphorylationDLLLTSSYLSDSGST
CEEEEEEECCCCCCC		15.25-
406PhosphorylationLLTSSYLSDSGSTGE
EEEEEECCCCCCCCH		22.8419065266
408PhosphorylationTSSYLSDSGSTGEHT
EEEECCCCCCCCHHH		31.1319065266
410PhosphorylationSYLSDSGSTGEHTKS
EECCCCCCCCHHHHH		36.8719065266
416UbiquitinationGSTGEHTKSLVTQYL
CCCCHHHHHHHHHHH		43.6421906983
424N-linked_GlycosylationSLVTQYLNATGNRWC
HHHHHHHHHCCCCCE		30.4412754519
428N-linked_GlycosylationQYLNATGNRWCSWSL
HHHHHCCCCCEECCH		29.8919349973
431S-palmitoylationNATGNRWCSWSLSQA
HHCCCCCEECCHHHH		2.4229575903
442PhosphorylationLSQARLLTSFLPAQL
HHHHHHHHHCCHHHH		23.25-
443PhosphorylationSQARLLTSFLPAQLL
HHHHHHHHCCHHHHH		25.42-
506N-linked_GlycosylationIPGAVSANMTVKGQS
CCCCEEECEEECCCC		21.103480538
513PhosphorylationNMTVKGQSEDPGSLL
CEEECCCCCCCHHHH		53.2721712546
518PhosphorylationGQSEDPGSLLSLFRR
CCCCCCHHHHHHHHH		31.3721712546
521PhosphorylationEDPGSLLSLFRRLSD
CCCHHHHHHHHHHHH		30.6521712546
527PhosphorylationLSLFRRLSDQRSKER
HHHHHHHHHHHHHHH		29.8619065266
531PhosphorylationRRLSDQRSKERSLLH
HHHHHHHHHHHHHHC		32.9819065266
545PhosphorylationHGDFHAFSAGPGLFS
CCCCHHHHCCCCHHH		32.8520068231
552PhosphorylationSAGPGLFSYIRHWDQ
HCCCCHHHHHEEECC		25.3724719451
581O-linked_GlycosylationLSAGLQASDLPASAS
CCCCCCHHCCCCCCC		27.07OGP
598PhosphorylationAKADLLLSTQPGREE
CCCCEEECCCCCCCC		25.6021712546
607PhosphorylationQPGREEGSPLELERL
CCCCCCCCCCCHHHC		29.5923403867
615AcetylationPLELERLKLEPHEGL
CCCHHHCCCCCCCCE		57.9626051181
615UbiquitinationPLELERLKLEPHEGL
CCCHHHCCCCCCCCE		57.962190698
625MethylationPHEGLLLRFPYAA--
CCCCEECCCCCCC--		30.39115917121
646 (in isoform 4)Ubiquitination--
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
406SPhosphorylationKinaseCSNK2A1P68400
GPS
408SPhosphorylationKinaseCSNK2A1P68400
GPS
410SPhosphorylationKinaseCSNK2A1P68400
GPS
527SPhosphorylationKinaseCSNK2A1P68400
GPS
531SPhosphorylationKinaseCSNK2A1P68400
GPS
-KUbiquitinationE3 ubiquitin ligaseMARCHF8Q5T0T0
PMID:21757542
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
406SPhosphorylation

19065266
408SPhosphorylation

19065266
410SPhosphorylation

19065266
527SPhosphorylation

19065266
531SPhosphorylation

19065266
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 4F2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAT1_HUMANSLC7A5physical
9829974
YLAT1_HUMANSLC7A7physical
9878049
YLAT1_MOUSESlc7a7physical
9878049
CD44_HUMANCD44physical
22939629
VAMP3_HUMANVAMP3physical
22939629
NDUS3_HUMANNDUFS3physical
22939629
RT09_HUMANMRPS9physical
22939629
AT2A2_HUMANATP2A2physical
22939629
LAT2_MOUSESlc7a8physical
10574970
BASI_HUMANBSGphysical
26344197
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 4F2_HUMAN

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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-365; ASN-381; ASN-424 ANDASN-506, AND MASS SPECTROMETRY.
"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-365; ASN-381 AND ASN-506,AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-381 AND ASN-424, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-365; ASN-381 AND ASN-424.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND THR-106, ANDMASS SPECTROMETRY.
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-147, AND MASSSPECTROMETRY.

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