dbPTM

4F2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	4F2_MOUSE
UniProt AC	P10852
Protein Name	4F2 cell-surface antigen heavy chain
Gene Name	Slc3a2
Organism	Mus musculus (Mouse).
Sequence Length	526
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 (By similarity). Localized to the plasma membrane when associated with SLC7A5 or SLC7A8 (By simil
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 (By similarity)..
Protein Sequence	MSQDTEVDMKDVELNELEPEKQPMNAADGAAAGEKNGLVKIKVAEDETEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALYRIGDLQAFVGRDAGGIAGLKSHLEYLSTLKVKGLVLGPIHKNQKDEINETDLKQINPTLGSQEDFKDLLQSAKKKSIHIILDLTPNYQGQNAWFLPAQADIVATKMKEALSSWLQDGVDGFQFRDVGKLMNAPLYLAEWQNITKNLSEDRLLIAGTESSDLQQIVNILESTSDLLLTSSYLSNSTFTGERTESLVTRFLNATGSQWCSWSVSQAGLLADFIPDHLLRLYQLLLFTLPGTPVFSYGDELGLQGALPGQPAKAPLMPWNESSIFHIPRPVSLNMTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHGDFHALSSSPDLFSYIRHWDQNERYLVVLNFRDSGRSARLGASNLPAGISLPASAKLLLSTDSARQSREEDTSLKLENLSLNPYEGLLLQFPFVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSQDTEVDM ------CCCCCCCCH	36.44	23375375
5	Phosphorylation	---MSQDTEVDMKDV ---CCCCCCCCHHHC	30.21	25266776
6 (in isoform 2)	Phosphorylation	-	44.82	24759943
9 (in isoform 2)	Phosphorylation	-	4.89	25293948
10 (in isoform 2)	Phosphorylation	-	54.91	24759943
35	Ubiquitination	DGAAAGEKNGLVKIK CCCCCCCCCCEEEEE	56.23	-
42	Ubiquitination	KNGLVKIKVAEDETE CCCEEEEEEEECCCH	29.67	-
48	Phosphorylation	IKVAEDETEAGVKFT EEEEECCCHHCCEEC	43.38	28066266
53	Ubiquitination	DETEAGVKFTGLSKE CCCHHCCEECCCCHH	35.97	-
55	Phosphorylation	TEAGVKFTGLSKEEL CHHCCEECCCCHHHH	31.34	25159016
58	Phosphorylation	GVKFTGLSKEELLKV CCEECCCCHHHHHHH	39.09	26824392
59	Ubiquitination	VKFTGLSKEELLKVA CEECCCCHHHHHHHH	61.32	-
74	Ubiquitination	GSPGWVRTRWALLLL CCCHHHHHHHHHHHH	22.42	22790023
81	Ubiquitination	TRWALLLLFWLGWLG HHHHHHHHHHHHHHH	2.67	22790023
92	Ubiquitination	GWLGMLAGAVVIIVR HHHHHHHCCEEEEEC	18.23	22790023
97	Phosphorylation	LAGAVVIIVRAPRCR HHCCEEEEECCCCCC	0.86	24719451
98	Ubiquitination	AGAVVIIVRAPRCRE HCCEEEEECCCCCCC	2.68	22790023
160	N-linked_Glycosylation	VLGPIHKNQKDEINE EECCCCCCCCCCCCC	39.72	19656770
166	N-linked_Glycosylation	KNQKDEINETDLKQI CCCCCCCCCCHHHHH	44.03	19656770
176	Phosphorylation	DLKQINPTLGSQEDF HHHHHCCCCCCHHHH	38.98	28066266
179	Phosphorylation	QINPTLGSQEDFKDL HHCCCCCCHHHHHHH	33.24	28066266
249	N-linked_Glycosylation	RDVGKLMNAPLYLAE CCHHHHHCCCCHHHH	49.17	19656770
259	N-linked_Glycosylation	LYLAEWQNITKNLSE CHHHHHHHHCCCCCC	44.99	19656770
262	Ubiquitination	AEWQNITKNLSEDRL HHHHHHCCCCCCCCE	52.69	-
263	N-linked_Glycosylation	EWQNITKNLSEDRLL HHHHHCCCCCCCCEE	39.90	-
300	Phosphorylation	LLTSSYLSNSTFTGE HHHHHHHCCCCCCCC	22.09	-
301	N-linked_Glycosylation	LTSSYLSNSTFTGER HHHHHHCCCCCCCCC	42.34	-
302	Phosphorylation	TSSYLSNSTFTGERT HHHHHCCCCCCCCCH	22.86	-
318	N-linked_Glycosylation	SLVTRFLNATGSQWC HHHHHHHHCCCCCCC	32.51	-
385	N-linked_Glycosylation	KAPLMPWNESSIFHI CCCCCCCCCCCCEEC	33.14	19656770
399	N-linked_Glycosylation	IPRPVSLNMTVKGQN CCCCEEECEEECCCC	19.30	19656770
420	Phosphorylation	LTQFRRLSDLRGKER HHHHHHHHHCCCCHH	32.56	24704852
498	Phosphorylation	STDSARQSREEDTSL CCHHHHHCHHHCCCC	35.79	25338131
509	N-linked_Glycosylation	DTSLKLENLSLNPYE CCCCEEECCCCCCCC	45.42	-

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 4F2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
300	S	Phosphorylation	-
Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions.
302	S	Phosphorylation	-
Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions.
420	S	Phosphorylation	-
Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of 4F2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of 4F2_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-166; ASN-259; ASN-385 ANDASN-399, AND MASS SPECTROMETRY.	19349973 [Abstract]
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-166; ASN-249;ASN-259; ASN-385 AND ASN-399, AND MASS SPECTROMETRY.	19656770 [Abstract]

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