Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10852

- 4F2_MOUSE

UniProt

P10852 - 4F2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

4F2 cell-surface antigen heavy chain

Gene

Slc3a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. cation binding Source: InterPro
  3. double-stranded RNA binding Source: MGI
  4. neutral amino acid transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. leucine import Source: UniProtKB
  3. response to exogenous dsRNA Source: MGI
  4. tryptophan transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_211508. Basigin interactions.
REACT_230460. Amino acid transport across the plasma membrane.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
4F2 cell-surface antigen heavy chain
Short name:
4F2hc
Alternative name(s):
Solute carrier family 3 member 2
CD_antigen: CD98
Gene namesi
Name:Slc3a2
Synonyms:Mdu1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:96955. Slc3a2.

Subcellular locationi

Apical cell membrane; Single-pass type II membrane protein. Melanosome By similarity
Note: 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 similarity). Localized to the placental apical membrane (By similarity). Located selectively at cell-cell adhesion sites. Colocalized with SLC7A8/LAT2 at the basolateral membrane of kidney proximal tubules and small intestine epithelia. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7575CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei76 – 9924Helical; Signal-anchor for type II membrane proteinAdd
BLAST
Topological domaini100 – 526427ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031C → S: No effect on guidance of LAT1 to the plasma membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5265264F2 cell-surface antigen heavy chainPRO_0000064384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineBy similarity
Cross-linki42 – 42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei58 – 581Phosphoserine1 Publication
Disulfide bondi103 – 103Interchain (with light chain)Curated
Glycosylationi160 – 1601N-linked (GlcNAc...); atypical1 Publication
Glycosylationi166 – 1661N-linked (GlcNAc...)2 Publications
Glycosylationi249 – 2491N-linked (GlcNAc...); atypical1 Publication
Glycosylationi259 – 2591N-linked (GlcNAc...)2 Publications
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi385 – 3851N-linked (GlcNAc...)2 Publications
Glycosylationi399 – 3991N-linked (GlcNAc...)2 Publications
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10852.
PaxDbiP10852.
PRIDEiP10852.

PTM databases

PhosphoSiteiP10852.

Expressioni

Tissue specificityi

Observed in all adult tissues tested with strongest expression in kidney, small intestine, spleen, thymus and liver. Moderate expression in brain, stomach, heart, testis, lung, skin, pancreas and skeletal muscle. Expressed on the surface of epithelial cells of most embryonic tissues including epidermis, choroid plexus in the brain, retina, as well as intestinal, renal, and thymic epithelium. In brain expressed on capillary endothelia in cerebral cortex.3 Publications

Developmental stagei

Strong expression in the liver of 14 dpc embryo and in brain, spleen, liver, kidney and intestine of an 18 dpc embryo.1 Publication

Inductioni

Expression induced by concanavilin-A stimulation. Induced during cell activation but is subsequently maintained at constant levels throughout the cell cycle in exponentially growing cells.2 Publications

Gene expression databases

BgeeiP10852.
ExpressionAtlasiP10852. baseline and differential.
GenevestigatoriP10852.

Interactioni

Subunit structurei

Disulfide-linked heterodimer of a glycosylated heavy chain and a non-glycosylated light chain (SLC7A5, SLC7A6, SLCA7A7, SLC7A8, SLC7A10 or SLCA7A11). Colocalizes with cadherins (By similarity). Interacts with FAM57A/CT120 and ICAM1 (By similarity). Constitutively and specifically associates with beta-1 integrins (alpha-2/beta-1, alpha-3/beta-1, alpha-5/beta-1 and alpha-6/beta-1), but minimally with alpha-4/beta-1 (By similarity).By similarity

Protein-protein interaction databases

IntActiP10852. 4 interactions.
MINTiMINT-4996392.

Structurei

3D structure databases

ProteinModelPortaliP10852.
SMRiP10852. Positions 105-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SLC3A transporter family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00530000063127.
HOVERGENiHBG000023.
InParanoidiP10852.
KOiK06519.
OMAiNMTVKGQ.
OrthoDBiEOG7ZSHSV.
PhylomeDBiP10852.
TreeFamiTF314498.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P10852-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSQDTEVDMK DVELNELEPE KQPMNAADGA AAGEKNGLVK IKVAEDETEA
60 70 80 90 100
GVKFTGLSKE ELLKVAGSPG WVRTRWALLL LFWLGWLGML AGAVVIIVRA
110 120 130 140 150
PRCRELPVQR WWHKGALYRI GDLQAFVGRD AGGIAGLKSH LEYLSTLKVK
160 170 180 190 200
GLVLGPIHKN QKDEINETDL KQINPTLGSQ EDFKDLLQSA KKKSIHIILD
210 220 230 240 250
LTPNYQGQNA WFLPAQADIV ATKMKEALSS WLQDGVDGFQ FRDVGKLMNA
260 270 280 290 300
PLYLAEWQNI TKNLSEDRLL IAGTESSDLQ QIVNILESTS DLLLTSSYLS
310 320 330 340 350
NSTFTGERTE SLVTRFLNAT GSQWCSWSVS QAGLLADFIP DHLLRLYQLL
360 370 380 390 400
LFTLPGTPVF SYGDELGLQG ALPGQPAKAP LMPWNESSIF HIPRPVSLNM
410 420 430 440 450
TVKGQNEDPG SLLTQFRRLS DLRGKERSLL HGDFHALSSS PDLFSYIRHW
460 470 480 490 500
DQNERYLVVL NFRDSGRSAR LGASNLPAGI SLPASAKLLL STDSARQSRE
510 520
EDTSLKLENL SLNPYEGLLL QFPFVA
Length:526
Mass (Da):58,337
Last modified:July 1, 1989 - v1
Checksum:iAE6261F11C7D9468
GO
Isoform 2 (identifier: P10852-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPEPTEHSTDGVSVPRQPPSAQTGLDVQVVSAAGDSGTM

Note: No experimental confirmation available.

Show »
Length:565
Mass (Da):62,240
Checksum:i7CF0572C4E948451
GO

Sequence cautioni

The sequence BAE36291.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDPEPTEHSTDGVSVPRQPP SAQTGLDVQVVSAAGDSGTM in isoform 2. 1 PublicationVSP_054953

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14309 mRNA. Translation: CAA32490.1.
AB023408 mRNA. Translation: BAA90555.1.
AK161280 mRNA. Translation: BAE36291.1. Different initiation.
AK165417 mRNA. Translation: BAE38172.1.
AC025794 Genomic DNA. No translation available.
CH466612 Genomic DNA. Translation: EDL33352.1.
BC065173 mRNA. Translation: AAH65173.1.
CCDSiCCDS29540.1. [P10852-1]
CCDS50381.1. [P10852-2]
PIRiS03600.
RefSeqiNP_001154885.1. NM_001161413.1. [P10852-2]
NP_032603.3. NM_008577.4. [P10852-1]
XP_006526794.1. XM_006526731.1. [P10852-1]
XP_006526795.1. XM_006526732.1. [P10852-1]
UniGeneiMm.4114.

Genome annotation databases

EnsembliENSMUST00000010239; ENSMUSP00000010239; ENSMUSG00000010095. [P10852-1]
ENSMUST00000170157; ENSMUSP00000130194; ENSMUSG00000010095. [P10852-2]
GeneIDi17254.
KEGGimmu:17254.
UCSCiuc008gmi.2. mouse.
uc012bib.1. mouse. [P10852-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14309 mRNA. Translation: CAA32490.1 .
AB023408 mRNA. Translation: BAA90555.1 .
AK161280 mRNA. Translation: BAE36291.1 . Different initiation.
AK165417 mRNA. Translation: BAE38172.1 .
AC025794 Genomic DNA. No translation available.
CH466612 Genomic DNA. Translation: EDL33352.1 .
BC065173 mRNA. Translation: AAH65173.1 .
CCDSi CCDS29540.1. [P10852-1 ]
CCDS50381.1. [P10852-2 ]
PIRi S03600.
RefSeqi NP_001154885.1. NM_001161413.1. [P10852-2 ]
NP_032603.3. NM_008577.4. [P10852-1 ]
XP_006526794.1. XM_006526731.1. [P10852-1 ]
XP_006526795.1. XM_006526732.1. [P10852-1 ]
UniGenei Mm.4114.

3D structure databases

ProteinModelPortali P10852.
SMRi P10852. Positions 105-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P10852. 4 interactions.
MINTi MINT-4996392.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSitei P10852.

Proteomic databases

MaxQBi P10852.
PaxDbi P10852.
PRIDEi P10852.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000010239 ; ENSMUSP00000010239 ; ENSMUSG00000010095 . [P10852-1 ]
ENSMUST00000170157 ; ENSMUSP00000130194 ; ENSMUSG00000010095 . [P10852-2 ]
GeneIDi 17254.
KEGGi mmu:17254.
UCSCi uc008gmi.2. mouse.
uc012bib.1. mouse. [P10852-1 ]

Organism-specific databases

CTDi 6520.
MGIi MGI:96955. Slc3a2.

Phylogenomic databases

eggNOGi COG0366.
GeneTreei ENSGT00530000063127.
HOVERGENi HBG000023.
InParanoidi P10852.
KOi K06519.
OMAi NMTVKGQ.
OrthoDBi EOG7ZSHSV.
PhylomeDBi P10852.
TreeFami TF314498.

Enzyme and pathway databases

Reactomei REACT_211508. Basigin interactions.
REACT_230460. Amino acid transport across the plasma membrane.

Miscellaneous databases

NextBioi 291726.
PROi P10852.
SOURCEi Search...

Gene expression databases

Bgeei P10852.
ExpressionAtlasi P10852. baseline and differential.
Genevestigatori P10852.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, expression and regulation of the murine 4F2 heavy chain."
    Parmacek M.S., Karpinski B.A., Gottsdiener K.M., Thompson C.B., Leiden J.M.
    Nucleic Acids Res. 17:1915-1931(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6 X DBA/2 and ICR.
    Tissue: Macrophage and Pre-B cell.
  2. "Localization of expression of system L neutral amino acid transporter LAT1 in brain."
    Kanai Y., Watanabe M., Endou H.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ICR.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  7. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 43-53; 163-171; 456-463 AND 488-496, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  8. "4F2 (CD98) heavy chain is associated covalently with an amino acid transporter and controls intracellular trafficking and membrane topology of 4F2 heterodimer."
    Nakamura E., Sato M., Yang H., Miyagawa F., Harasaki M., Tomita K., Matsuoka S., Noma A., Iwai K., Minato N.
    J. Biol. Chem. 274:3009-3016(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, MUTAGENESIS OF CYS-103.
    Strain: BALB/c.
  9. "Identification of a membrane protein, LAT-2, that co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids."
    Pineda M., Fernandez E., Torrents D., Estevez R., Lopez C., Camps M., Lloberas J., Zorzano A., Palacin M.
    J. Biol. Chem. 274:19738-19744(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  10. "LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine."
    Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F., Kuehn L.C.
    J. Biol. Chem. 274:34948-34954(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. Cited for: FUNCTION.
  12. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-166; ASN-249; ASN-259; ASN-385 AND ASN-399.
    Tissue: Myoblast.
  14. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-259; ASN-385 AND ASN-399.

Entry informationi

Entry namei4F2_MOUSE
AccessioniPrimary (citable) accession number: P10852
Secondary accession number(s): G3UWA6, Q54AH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Leucine uptake was inhibited by ileum, valine histidine and phenylalanine as well as by 2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid (BCH) (a specific inhibitor of system L transport).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3