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P29351

- PTN6_MOUSE

UniProt

P29351 - PTN6_MOUSE

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Protein

Tyrosine-protein phosphatase non-receptor type 6

Gene

Ptpn6

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

Functioni

Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei419 – 4191SubstrateBy similarity
Active sitei453 – 4531Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei500 – 5001SubstrateBy similarity

GO - Molecular functioni

  1. phosphotyrosine binding Source: MGI
  2. protein tyrosine phosphatase activity Source: MGI
  3. SH2 domain binding Source: MGI
  4. SH3 domain binding Source: MGI
  5. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. abortive mitotic cell cycle Source: MGI
  2. B cell receptor signaling pathway Source: MGI
  3. cell differentiation Source: UniProtKB
  4. cell proliferation Source: UniProtKB
  5. cytokine-mediated signaling pathway Source: MGI
  6. hematopoietic progenitor cell differentiation Source: MGI
  7. intracellular signal transduction Source: MGI
  8. megakaryocyte development Source: MGI
  9. natural killer cell mediated cytotoxicity Source: MGI
  10. negative regulation of B cell receptor signaling pathway Source: MGI
  11. negative regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
  12. negative regulation of MAPK cascade Source: MGI
  13. negative regulation of MAP kinase activity Source: MGI
  14. negative regulation of peptidyl-tyrosine phosphorylation Source: MGI
  15. negative regulation of T cell proliferation Source: MGI
  16. negative regulation of T cell receptor signaling pathway Source: MGI
  17. peptidyl-tyrosine dephosphorylation Source: GOC
  18. peptidyl-tyrosine phosphorylation Source: Ensembl
  19. platelet aggregation Source: MGI
  20. platelet formation Source: MGI
  21. positive regulation of cell adhesion mediated by integrin Source: MGI
  22. positive regulation of cell proliferation Source: Ensembl
  23. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  24. protein dephosphorylation Source: MGI
  25. regulation of B cell differentiation Source: MGI
  26. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  27. regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  28. regulation of release of sequestered calcium ion into cytosol Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_198614. Growth hormone receptor signaling.
REACT_198622. Interferon alpha/beta signaling.
REACT_198627. Regulation of IFNA signaling.
REACT_198645. Regulation of IFNG signaling.
REACT_198660. Interferon gamma signaling.
REACT_210793. Interleukin receptor SHC signaling.
REACT_215628. Signal regulatory protein (SIRP) family interactions.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_227425. Regulation of KIT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 6 (EC:3.1.3.48)
Alternative name(s):
70Z-SHP
Hematopoietic cell protein-tyrosine phosphatase
PTPTY-42
Protein-tyrosine phosphatase 1C
Short name:
PTP-1C
SH-PTP1
Short name:
SHP-1
Gene namesi
Name:Ptpn6
Synonyms:Hcp, Hcph, Ptp1C
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:96055. Ptpn6.

Subcellular locationi

Cytoplasm. Nucleus By similarity
Note: In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity).By similarity

GO - Cellular componenti

  1. alpha-beta T cell receptor complex Source: MGI
  2. cell-cell junction Source: MGI
  3. cytoplasm Source: MGI
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: Ensembl
  6. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in Ptpn6 are the cause of the motheaten (me) or viable motheaten (mev) phenotypes. Mice homozygous for the recessive allelic mutations develop severe defects in hematopoiesis.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Tyrosine-protein phosphatase non-receptor type 6PRO_0000094759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphotyrosineBy similarity
Modified residuei377 – 3771Phosphotyrosine1 Publication
Modified residuei536 – 5361Phosphotyrosine1 Publication
Modified residuei564 – 5641Phosphotyrosine; by LYNBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues. Phosphorylation at Tyr-564 enhances phosphatase activity (By similarity). Binding of KITLG/SCF to KIT increases tyrosine phosphorylation.By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29351.
PaxDbiP29351.
PRIDEiP29351.

PTM databases

PhosphoSiteiP29351.

Expressioni

Tissue specificityi

Expressed predominantly in hematopoietic cells.1 Publication

Gene expression databases

BgeeiP29351.
CleanExiMM_PTPN6.
ExpressionAtlasiP29351. baseline and differential.
GenevestigatoriP29351.

Interactioni

Subunit structurei

Monomer. Interacts with FCRL2, FCRL3, FCRL4, CD84 and MTUS1 (By similarity). Binds PTPNS1. Interacts with CD300LF and CDK2. Interacts with MILR1 (tyrosine-phosphorylated). Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (By similarity). Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation (By similarity). Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with LYN (By similarity). Interacts with KIT. Interacts with the tyrosine phosphorylated form of PDPK1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd22P353295EBI-2620699,EBI-300059
Stat1P422252EBI-2620699,EBI-647118
tirB7UM992EBI-2620699,EBI-2504426From a different organism.

Protein-protein interaction databases

BioGridi200256. 6 interactions.
DIPiDIP-41455N.
IntActiP29351. 8 interactions.
MINTiMINT-192591.

Structurei

3D structure databases

ProteinModelPortaliP29351.
SMRiP29351. Positions 1-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 10097SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 213104SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 515272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni453 – 4597Substrate bindingBy similarity

Domaini

The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation.By similarity

Sequence similaritiesi

Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118836.
HOVERGENiHBG000223.
InParanoidiP29351.
KOiK05697.
OMAiQAKGEPW.
OrthoDBiEOG7NPFST.
PhylomeDBiP29351.
TreeFamiTF351632.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000980. SH2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTiSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29351-1) [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
MVRWFHRDLS GPDAETLLKG RGVPGSFLAR PSRKNQGDFS LSVRVDDQVT
60 70 80 90 100
HIRIQNSGDF YDLYGGEKFA TLTELVEYYT QQQGILQDRD GTIIHLKYPL
110 120 130 140 150
NCSDPTSERW YHGHISGGQA ESLLQAKGEP WTFLVRESLS QPGDFVLSVL
160 170 180 190 200
NDQPKAGPGS PLRVTHIKVM CEGGRYTVGG SETFDSLTDL VEHFKKTGIE
210 220 230 240 250
EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA KAGFWEEFES
260 270 280 290 300
LQKQEVKNLH QRLEGQRPEN KSKNRYKNIL PFDHSRVILQ GRDSNIPGSD
310 320 330 340 350
YINANYVKNQ LLGPDENSKT YIASQGCLDA TVNDFWQMAW QENTRVIVMT
360 370 380 390 400
TREVEKGRNK CVPYWPEVGT QRVYGLYSVT NSREHDTAEY KLRTLQISPL
410 420 430 440 450
DNGDLVREIW HYQYLSWPDH GVPSEPGGVL SFLDQINQRQ ESLPHAGPII
460 470 480 490 500
VHCSAGIGRT GTIIVIDMLM ESISTKGLDC DIDIQKTIQM VRAQRSGMVQ
510 520 530 540 550
TEAQYKFIYV AIAQFIETTK KKLEIIQSQK GQESEYGNIT YPPAVRSAHA
560 570 580 590
KASRTSSKHK EEVYENVHSK SKKEEKVKKQ RSADKEKNKG SLKRK
Length:595
Mass (Da):67,559
Last modified:July 11, 2002 - v2
Checksum:iCF17300D032638D2
GO
Isoform 2 (identifier: P29351-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MVR → MLSRG

Show »
Length:597
Mass (Da):67,717
Checksum:iE8491CE77E06E989
GO
Isoform 3 (identifier: P29351-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-44: SLSVR → MLSRG

Show »
Length:556
Mass (Da):63,179
Checksum:iCACF025DF9D7BC2D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401A → R in AAA37796. (PubMed:1732748)Curated
Sequence conflicti572 – 5721K → Q in AAA37796. (PubMed:1732748)Curated
Sequence conflicti586 – 5861E → D in AAH12660. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 9923EYYTQ…HLKYP → VPRPHIWRAGGVTAAGQGRA LD in motheaten (me).
Add
BLAST
Natural varianti100 – 595496Missing in motheaten (me).
Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 3. CuratedVSP_005132Add
BLAST
Alternative sequencei1 – 33MVR → MLSRG in isoform 2. CuratedVSP_005131
Alternative sequencei40 – 445SLSVR → MLSRG in isoform 3. CuratedVSP_005133

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M68902 mRNA. Translation: AAA37796.1.
M90389 mRNA. Translation: AAA40007.1.
S63763 mRNA. No translation available.
S63764 mRNA. No translation available.
S63803 mRNA. No translation available.
AC002397 Genomic DNA. Translation: AAC36009.1.
AC002397 Genomic DNA. Translation: AAC36008.1.
U65955
, U65952, U65953, U65954 Genomic DNA. Translation: AAD00152.1.
U65955
, U65951, U65952, U65953, U65954 Genomic DNA. Translation: AAD00151.1.
BC012660 mRNA. Translation: AAH12660.1.
CCDSiCCDS39628.1. [P29351-1]
CCDS51908.1. [P29351-2]
PIRiA44390.
RefSeqiNP_001071173.1. NM_001077705.2. [P29351-2]
NP_038573.2. NM_013545.3. [P29351-1]
UniGeneiMm.271799.

Genome annotation databases

EnsembliENSMUST00000004377; ENSMUSP00000004377; ENSMUSG00000004266. [P29351-2]
ENSMUST00000112484; ENSMUSP00000108103; ENSMUSG00000004266. [P29351-1]
ENSMUST00000171549; ENSMUSP00000129124; ENSMUSG00000004266. [P29351-2]
ENSMUST00000174265; ENSMUSP00000133991; ENSMUSG00000004266. [P29351-3]
GeneIDi15170.
KEGGimmu:15170.
UCSCiuc009drk.1. mouse. [P29351-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M68902 mRNA. Translation: AAA37796.1 .
M90389 mRNA. Translation: AAA40007.1 .
S63763 mRNA. No translation available.
S63764 mRNA. No translation available.
S63803 mRNA. No translation available.
AC002397 Genomic DNA. Translation: AAC36009.1 .
AC002397 Genomic DNA. Translation: AAC36008.1 .
U65955
, U65952 , U65953 , U65954 Genomic DNA. Translation: AAD00152.1 .
U65955
, U65951 , U65952 , U65953 , U65954 Genomic DNA. Translation: AAD00151.1 .
BC012660 mRNA. Translation: AAH12660.1 .
CCDSi CCDS39628.1. [P29351-1 ]
CCDS51908.1. [P29351-2 ]
PIRi A44390.
RefSeqi NP_001071173.1. NM_001077705.2. [P29351-2 ]
NP_038573.2. NM_013545.3. [P29351-1 ]
UniGenei Mm.271799.

3D structure databases

ProteinModelPortali P29351.
SMRi P29351. Positions 1-529.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200256. 6 interactions.
DIPi DIP-41455N.
IntActi P29351. 8 interactions.
MINTi MINT-192591.

PTM databases

PhosphoSitei P29351.

Proteomic databases

MaxQBi P29351.
PaxDbi P29351.
PRIDEi P29351.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004377 ; ENSMUSP00000004377 ; ENSMUSG00000004266 . [P29351-2 ]
ENSMUST00000112484 ; ENSMUSP00000108103 ; ENSMUSG00000004266 . [P29351-1 ]
ENSMUST00000171549 ; ENSMUSP00000129124 ; ENSMUSG00000004266 . [P29351-2 ]
ENSMUST00000174265 ; ENSMUSP00000133991 ; ENSMUSG00000004266 . [P29351-3 ]
GeneIDi 15170.
KEGGi mmu:15170.
UCSCi uc009drk.1. mouse. [P29351-1 ]

Organism-specific databases

CTDi 5777.
MGIi MGI:96055. Ptpn6.

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118836.
HOVERGENi HBG000223.
InParanoidi P29351.
KOi K05697.
OMAi QAKGEPW.
OrthoDBi EOG7NPFST.
PhylomeDBi P29351.
TreeFami TF351632.

Enzyme and pathway databases

Reactomei REACT_198614. Growth hormone receptor signaling.
REACT_198622. Interferon alpha/beta signaling.
REACT_198627. Regulation of IFNA signaling.
REACT_198645. Regulation of IFNG signaling.
REACT_198660. Interferon gamma signaling.
REACT_210793. Interleukin receptor SHC signaling.
REACT_215628. Signal regulatory protein (SIRP) family interactions.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_227425. Regulation of KIT signaling.

Miscellaneous databases

ChiTaRSi PTPN6. mouse.
NextBioi 287680.
PROi P29351.
SOURCEi Search...

Gene expression databases

Bgeei P29351.
CleanExi MM_PTPN6.
ExpressionAtlasi P29351. baseline and differential.
Genevestigatori P29351.

Family and domain databases

Gene3Di 3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000980. SH2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTi SM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13."
    Yi T., Cleveland J.L., Ihle J.N.
    Mol. Cell. Biol. 12:836-846(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2.
  2. "Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences."
    Matthews R.J., Bowne D.B., Flores E., Thomas M.L.
    Mol. Cell. Biol. 12:2396-2405(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene."
    Schultz L.D., Schweitzer P.A., Rajan T.V., Yi T., Ihle J.N., Matthews R.J., Thomas M.L., Beier D.R.
    Cell 73:1445-1454(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MOTHEATEN AND VIABLE MOTHEATEN.
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  4. "Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
    Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
    Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
  5. "Murine SHP-1 splice variants with altered Src homology 2 (SH2) domains. Implications for the SH2-mediated intramolecular regulation of SHP-1."
    Martin A., Tsui H.W., Shulman M.J., Isenman D., Tsui F.W.
    J. Biol. Chem. 274:21725-21734(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), SUBUNIT.
    Strain: C3H.
    Tissue: Adrenal gland.
  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].
  7. "Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1."
    Yeung Y.-G., Berg K.L., Pixley F.J., Angeletti R.H., Stanley E.R.
    J. Biol. Chem. 267:23447-23450(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-68; 128-135; 137-151; 242-252; 278-285; 293-308 AND 373-382, PHOSPHORYLATION.
  8. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
    Yi T., Cleveland J.L., Ihle J.N.
    Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 342-451, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Myeloid leukemia cell.
  9. "High expression of inhibitory receptor SHPS-1 and its association with protein tyrosine phosphatase SHP-1 in macrophages."
    Veillette A., Thibaudeau E., Latour S.
    J. Biol. Chem. 273:22719-22728(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPNS1.
  10. "SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain."
    Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.
    Mol. Cell. Biol. 18:2089-2099(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIT, FUNCTION IN MODULATING KIT SIGNALING, PHOSPHORYLATION.
  11. "CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit osteoclast formation."
    Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G., Seaman W.E., Daws M.R.
    J. Immunol. 171:6541-6548(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD300LF.
    Strain: C57BL/6.
  12. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377 AND TYR-536, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-mediated immediate hypersensitivity reactions."
    Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H., Sugiyama T., Shibayama S., Shibuya K., Shibuya A.
    Nat. Immunol. 11:601-607(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MILR1.

Entry informationi

Entry nameiPTN6_MOUSE
AccessioniPrimary (citable) accession number: P29351
Secondary accession number(s): O35128
, Q63872, Q63873, Q63874, Q921G3, Q9QVA6, Q9QVA7, Q9QVA8, Q9R0V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 11, 2002
Last modified: October 29, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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