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Protein

Linker for activation of T-cells family member 2

Gene

LAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.3 Publications

GO - Molecular functioni

  • SH2 domain binding Source: HGNC

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • B cell activation Source: HGNC
  • B cell receptor signaling pathway Source: HGNC
  • calcium-mediated signaling Source: HGNC
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • intracellular signal transduction Source: HGNC
  • mast cell degranulation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity, Mast cell degranulation

Enzyme and pathway databases

ReactomeiR-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
SignaLinkiQ9GZY6.

Names & Taxonomyi

Protein namesi
Recommended name:
Linker for activation of T-cells family member 2
Alternative name(s):
Linker for activation of B-cells
Membrane-associated adapter molecule
Non-T-cell activation linker
Williams-Beuren syndrome chromosomal region 15 protein
Williams-Beuren syndrome chromosomal region 5 protein
Gene namesi
Name:LAT2
Synonyms:LAB, NTAL, WBS15, WBSCR15, WBSCR5
ORF Names:HSPC046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:12749. LAT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55ExtracellularSequence analysis
Transmembranei6 – 2621Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini27 – 243217CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • mast cell granule Source: GOC
  • membrane raft Source: HGNC
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

LAT2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of LAT2 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581Y → F: No change in phosphorylation upon BCR activation. 1 Publication
Mutagenesisi84 – 841Y → F: No change in phosphorylation upon BCR activation. 1 Publication
Mutagenesisi95 – 951Y → F: Slightly reduces phosphorylation upon BCR activation. 1 Publication
Mutagenesisi110 – 1101Y → F: No change in phosphorylation upon BCR activation. 1 Publication
Mutagenesisi118 – 1181Y → F: No change in phosphorylation upon BCR activation. 1 Publication
Mutagenesisi136 – 1361Y → F: Slightly reduces phosphorylation upon BCR activation. 1 Publication
Mutagenesisi193 – 1931Y → F: Reduces phosphorylation upon BCR activation. 1 Publication
Mutagenesisi233 – 2331Y → F: Strongly reduces phosphorylation upon BCR activation. 1 Publication

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

PharmGKBiPA37356.

Polymorphism and mutation databases

BioMutaiLAT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Linker for activation of T-cells family member 2PRO_0000083334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi25 – 251S-palmitoyl cysteine1 Publication
Lipidationi28 – 281S-palmitoyl cysteine1 Publication
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei58 – 581PhosphotyrosineBy similarity
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei136 – 1361Phosphotyrosine2 Publications
Modified residuei193 – 1931Phosphotyrosine2 Publications
Modified residuei233 – 2331Phosphotyrosine2 Publications

Post-translational modificationi

Phosphorylated on tyrosines following cross-linking of BCR in B-cells, FCGR1 in myeloid cells, or FCER1 in mast cells; which induces the recruitment of GRB2.3 Publications
May be polyubiquitinated.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9GZY6.
MaxQBiQ9GZY6.
PaxDbiQ9GZY6.
PRIDEiQ9GZY6.

PTM databases

iPTMnetiQ9GZY6.
PhosphoSiteiQ9GZY6.
SwissPalmiQ9GZY6.

Expressioni

Tissue specificityi

Highly expressed in spleen, peripheral blood lymphocytes, and germinal centers of lymph nodes. Also expressed in placenta, lung, pancreas and small intestine. Present in B-cells, NK cells and monocytes. Absent from T-cells (at protein level).4 Publications

Gene expression databases

BgeeiQ9GZY6.
CleanExiHS_LAT2.
ExpressionAtlasiQ9GZY6. baseline and differential.
GenevisibleiQ9GZY6. HS.

Organism-specific databases

HPAiHPA003462.

Interactioni

Subunit structurei

When phosphorylated, interacts with GRB2. May also interact with SOS1, GAB1 and CBL.3 Publications

GO - Molecular functioni

  • SH2 domain binding Source: HGNC

Protein-protein interaction databases

BioGridi113301. 4 interactions.
IntActiQ9GZY6. 1 interaction.
MINTiMINT-2864124.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MAZX-ray1.90B133-141[»]
ProteinModelPortaliQ9GZY6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GZY6.

Family & Domainsi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZVX. Eukaryota.
ENOG4111816. LUCA.
GeneTreeiENSGT00390000006821.
HOVERGENiHBG082063.
InParanoidiQ9GZY6.
OMAiEDGEPDY.
PhylomeDBiQ9GZY6.
TreeFamiTF336203.

Family and domain databases

InterProiIPR031428. LAT2.
[Graphical view]
PfamiPF15703. LAT2. 2 hits.
[Graphical view]
ProDomiPD332876. PD332876. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9GZY6-1) [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
MSSGTELLWP GAALLVLLGV AASLCVRCSR PGAKRSEKIY QQRSLREDQQ
60 70 80 90 100
SFTGSRTYSL VGQAWPGPLA DMAPTRKDKL LQFYPSLEDP ASSRYQNFSK
110 120 130 140 150
GSRHGSEEAY IDPIAMEYYN WGRFSKPPED DDANSYENVL ICKQKTTETG
160 170 180 190 200
AQQEGIGGLC RGDLSLSLAL KTGPTSGLCP SASPEEDEES EDYQNSASIH
210 220 230 240
QWRESRKVMG QLQREASPGP VGSPDEEDGE PDYVNGEVAA TEA
Length:243
Mass (Da):26,550
Last modified:March 1, 2001 - v1
Checksum:i222D2CCF3C71C503
GO
Isoform 2 (identifier: Q9GZY6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     112-243: Missing.

Note: No experimental confirmation available.
Show »
Length:111
Mass (Da):12,255
Checksum:i09540AE67B44F485
GO

Sequence cautioni

The sequence AAF29018.1 differs from that shown. Reason: Frameshift at positions 82, 86, 130 and 221. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391I → M in BAF82763 (PubMed:14702039).Curated
Sequence conflicti82 – 821Q → A in AAF29018 (PubMed:11042152).Curated
Sequence conflicti101 – 1011G → R in AAF29018 (PubMed:11042152).Curated
Sequence conflicti221 – 2211V → M in AAF29018 (PubMed:11042152).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei112 – 243132Missing in isoform 2. 1 PublicationVSP_016643Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF257135 mRNA. Translation: AAF91352.1.
AF045555 Genomic DNA. Translation: AAF74978.1.
AY190023 mRNA. Translation: AAO63155.1.
AF252611 mRNA. Translation: AAK37429.1.
AF252612 mRNA. Translation: AAK37430.1.
AF252613 mRNA. Translation: AAK37633.1.
AF252614 mRNA. Translation: AAK37431.1.
AF161531 mRNA. Translation: AAF29018.1. Frameshift.
AK002099 mRNA. Translation: BAA92084.1.
AK092904 mRNA. Translation: BAG52627.1.
AK290074 mRNA. Translation: BAF82763.1.
AK290916 mRNA. Translation: BAF83605.1.
AC005081 Genomic DNA. Translation: AAS07404.1.
AC005081 Genomic DNA. Translation: AAS07405.1.
CH471200 Genomic DNA. Translation: EAW69610.1.
CH471200 Genomic DNA. Translation: EAW69611.1.
CH471200 Genomic DNA. Translation: EAW69612.1.
CH471200 Genomic DNA. Translation: EAW69613.1.
BC001609 mRNA. Translation: AAH01609.1.
BC009204 mRNA. Translation: AAH09204.1.
CCDSiCCDS5566.2. [Q9GZY6-1]
RefSeqiNP_054865.2. NM_014146.3. [Q9GZY6-1]
NP_115852.1. NM_032463.2. [Q9GZY6-1]
NP_115853.2. NM_032464.2. [Q9GZY6-1]
XP_011514860.1. XM_011516558.1. [Q9GZY6-1]
UniGeneiHs.741249.

Genome annotation databases

EnsembliENST00000275635; ENSP00000275635; ENSG00000086730. [Q9GZY6-1]
ENST00000344995; ENSP00000344881; ENSG00000086730. [Q9GZY6-1]
ENST00000398475; ENSP00000381492; ENSG00000086730. [Q9GZY6-1]
ENST00000460943; ENSP00000420494; ENSG00000086730. [Q9GZY6-1]
ENST00000488266; ENSP00000433807; ENSG00000086730. [Q9GZY6-2]
GeneIDi7462.
KEGGihsa:7462.
UCSCiuc003uag.4. human. [Q9GZY6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF257135 mRNA. Translation: AAF91352.1.
AF045555 Genomic DNA. Translation: AAF74978.1.
AY190023 mRNA. Translation: AAO63155.1.
AF252611 mRNA. Translation: AAK37429.1.
AF252612 mRNA. Translation: AAK37430.1.
AF252613 mRNA. Translation: AAK37633.1.
AF252614 mRNA. Translation: AAK37431.1.
AF161531 mRNA. Translation: AAF29018.1. Frameshift.
AK002099 mRNA. Translation: BAA92084.1.
AK092904 mRNA. Translation: BAG52627.1.
AK290074 mRNA. Translation: BAF82763.1.
AK290916 mRNA. Translation: BAF83605.1.
AC005081 Genomic DNA. Translation: AAS07404.1.
AC005081 Genomic DNA. Translation: AAS07405.1.
CH471200 Genomic DNA. Translation: EAW69610.1.
CH471200 Genomic DNA. Translation: EAW69611.1.
CH471200 Genomic DNA. Translation: EAW69612.1.
CH471200 Genomic DNA. Translation: EAW69613.1.
BC001609 mRNA. Translation: AAH01609.1.
BC009204 mRNA. Translation: AAH09204.1.
CCDSiCCDS5566.2. [Q9GZY6-1]
RefSeqiNP_054865.2. NM_014146.3. [Q9GZY6-1]
NP_115852.1. NM_032463.2. [Q9GZY6-1]
NP_115853.2. NM_032464.2. [Q9GZY6-1]
XP_011514860.1. XM_011516558.1. [Q9GZY6-1]
UniGeneiHs.741249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MAZX-ray1.90B133-141[»]
ProteinModelPortaliQ9GZY6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113301. 4 interactions.
IntActiQ9GZY6. 1 interaction.
MINTiMINT-2864124.

PTM databases

iPTMnetiQ9GZY6.
PhosphoSiteiQ9GZY6.
SwissPalmiQ9GZY6.

Polymorphism and mutation databases

BioMutaiLAT2.

Proteomic databases

EPDiQ9GZY6.
MaxQBiQ9GZY6.
PaxDbiQ9GZY6.
PRIDEiQ9GZY6.

Protocols and materials databases

DNASUi7462.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275635; ENSP00000275635; ENSG00000086730. [Q9GZY6-1]
ENST00000344995; ENSP00000344881; ENSG00000086730. [Q9GZY6-1]
ENST00000398475; ENSP00000381492; ENSG00000086730. [Q9GZY6-1]
ENST00000460943; ENSP00000420494; ENSG00000086730. [Q9GZY6-1]
ENST00000488266; ENSP00000433807; ENSG00000086730. [Q9GZY6-2]
GeneIDi7462.
KEGGihsa:7462.
UCSCiuc003uag.4. human. [Q9GZY6-1]

Organism-specific databases

CTDi7462.
GeneCardsiLAT2.
HGNCiHGNC:12749. LAT2.
HPAiHPA003462.
MIMi605719. gene.
neXtProtiNX_Q9GZY6.
PharmGKBiPA37356.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZVX. Eukaryota.
ENOG4111816. LUCA.
GeneTreeiENSGT00390000006821.
HOVERGENiHBG082063.
InParanoidiQ9GZY6.
OMAiEDGEPDY.
PhylomeDBiQ9GZY6.
TreeFamiTF336203.

Enzyme and pathway databases

ReactomeiR-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
SignaLinkiQ9GZY6.

Miscellaneous databases

ChiTaRSiLAT2. human.
EvolutionaryTraceiQ9GZY6.
GeneWikiiLAT2.
GenomeRNAii7462.
PROiQ9GZY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZY6.
CleanExiHS_LAT2.
ExpressionAtlasiQ9GZY6. baseline and differential.
GenevisibleiQ9GZY6. HS.

Family and domain databases

InterProiIPR031428. LAT2.
[Graphical view]
PfamiPF15703. LAT2. 2 hits.
[Graphical view]
ProDomiPD332876. PD332876. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Divergent human and mouse orthologs of a novel gene (WBSCR15/Wbscr15) reside within the genomic interval commonly deleted in Williams syndrome."
    Doyle J.L., DeSilva U., Miller W., Green E.D.
    Cytogenet. Cell Genet. 90:285-290(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE, TISSUE SPECIFICITY.
  2. "Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23."
    Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V., Koop B.F.
    Mamm. Genome 11:890-898(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH GRB2; SOS1; GAB1 AND CBL, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-25 AND CYS-28, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233, UBIQUITINATION, FUNCTION.
    Tissue: Leukocyte.
  4. "LAB: a new membrane-associated adaptor molecule in B cell activation."
    Janssen E., Zhu M., Zhang W., Koonpaew S., Zhang W.
    Nat. Immunol. 4:117-123(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH GRB2, FUNCTION.
    Tissue: B-cell.
  5. "A novel gene, WBS15, is deleted in patients with Williams syndrome."
    Tassabehji M., Heather L., Gladwin A., Metcalfe K., Donnai D., Read A., Wilmot C.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DISEASE.
  6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Neutrophil, Placenta, Spleen and Substantia nigra.
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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).
    Tissue: B-cell and Lymph.
  11. "NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation."
    Tkaczyk C., Horejsi V., Iwaki S., Draber P., Samelson L.E., Satterthwaite A.B., Nahm D.H., Metcalfe D.D., Gilfillan A.M.
    Blood 104:207-214(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The importance of three membrane-distal tyrosines in the adaptor protein NTAL/LAB."
    Koonpaew S., Janssen E., Zhu M., Zhang W.
    J. Biol. Chem. 279:11229-11235(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-58; TYR-84; TYR-95; TYR-110; TYR-118; TYR-136; TYR-193 AND TYR-233, PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233, INTERACTION WITH GRB2.
  13. Cited for: TISSUE SPECIFICITY.
  14. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNTAL_HUMAN
AccessioniPrimary (citable) accession number: Q9GZY6
Secondary accession number(s): A6NFK6
, A8K209, A8K4F1, D3DXF9, Q9BXX8, Q9NZY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.