4F2_RAT - dbPTM
4F2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 4F2_RAT
UniProt AC Q794F9
Protein Name 4F2 cell-surface antigen heavy chain
Gene Name Slc3a2 {ECO:0000312|RGD:3073}
Organism Rattus norvegicus (Rat).
Sequence Length 527
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 sim
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 MSQDTEVDMKDVELNELEPEKQPMNAADGAAAGEKNGLVKIKVAEDEAEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALYRIGDLQAFVGPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKGQNAWFLPPQADIVATKMKEALSSWLQDGVDGFQVRDVGKLANASLYLAEWQNITKNFSEDRLLIAGTASSDLQQIVNILESTSDLLLTSSYLSQPVFTGEHAELLVIKYLNATGSRWCSWSVSQAGLLTSFIPAQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAPFMLWNESSNSQTSSPVSLNMTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHGDFDALSSSSGLFSYVRHWDQNERYLVVLNFQDVGLSARVGASNLPAGISLPASANLLLSTDSTRLSREEGTSLSLENLSLNPYEGLLLQFPFVA
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
2Phosphorylation------MSQDTEVDM
------CCCCCCCCH
36.4427097102
5Phosphorylation---MSQDTEVDMKDV
---CCCCCCCCHHHC
30.2127097102
10AcetylationQDTEVDMKDVELNEL
CCCCCCHHHCCHHHC
54.9183034461
21UbiquitinationLNELEPEKQPMNAAD
HHHCCCCCCCCCHHC
71.11-
21AcetylationLNELEPEKQPMNAAD
HHHCCCCCCCCCHHC
71.1155699617
35UbiquitinationDGAAAGEKNGLVKIK
CCCCCCCCCCEEEEE
56.23-
42UbiquitinationKNGLVKIKVAEDEAE
CCCEEEEEEECCHHH
29.67-
53UbiquitinationDEAEAGVKFTGLSKE
CHHHHCCEECCCCHH
35.97-
55PhosphorylationAEAGVKFTGLSKEEL
HHHCCEECCCCHHHH
31.3428432305
58PhosphorylationGVKFTGLSKEELLKV
CCEECCCCHHHHHHH
39.0930240740
59AcetylationVKFTGLSKEELLKVA
CEECCCCHHHHHHHH
61.3222902405
59UbiquitinationVKFTGLSKEELLKVA
CEECCCCHHHHHHHH
61.32-
148AcetylationLEYLSTLKVKGLVLG
HHHHHHCCCCEEEEC
41.8222902405
162AcetylationGPIHKNQKDEVNETD
CCCCCCCCCCCCHHH
66.3122902405
166N-linked_GlycosylationKNQKDEVNETDLKQI
CCCCCCCCHHHHHHC
44.39-
179PhosphorylationQIDPDLGSQEDFKDL
HCCCCCCCHHHHHHH
37.3828689409
184AcetylationLGSQEDFKDLLQSAK
CCCHHHHHHHHHHHH
60.8422902405
191AcetylationKDLLQSAKKKSIHII
HHHHHHHHHCCEEEE
67.0122902405
249N-linked_GlycosylationRDVGKLANASLYLAE
ECHHHHHCHHHHHHH
40.26-
259N-linked_GlycosylationLYLAEWQNITKNFSE
HHHHHHHHHCCCCCC
44.99-
263N-linked_GlycosylationEWQNITKNFSEDRLL
HHHHHCCCCCCCCEE
36.71-
300PhosphorylationLLTSSYLSQPVFTGE
HHCHHHHCCCCCCCC
24.97-
318N-linked_GlycosylationLLVIKYLNATGSRWC
EEEEEECCCCCCCCC
32.16-
386N-linked_GlycosylationEAPFMLWNESSNSQT
CCCEEEEECCCCCCC
35.00-
400N-linked_GlycosylationTSSPVSLNMTVKGQN
CCCCEEEEEEEECCC
19.30-
421PhosphorylationLTQFRRLSDLRGKER
HHHHHHHHHCCCCCH
32.5622673903
510N-linked_GlycosylationGTSLSLENLSLNPYE
CCCCEEECCCCCCCC
39.98-

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
300SPhosphorylation

-
421SPhosphorylation

-

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of 4F2_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 4F2_RAT

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Related Literatures of Post-Translational Modification

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