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P81718 (PTN6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 6

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase SHP-1
Gene names
Name:Ptpn6
Synonyms:Ptph6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. UniProtKB P29351

Subunit structure

Monomer. Binds PTPNS1. Interacts with CDK2, FCRL2, FCRL3, FCRL4, CD300LF and CD84. Interacts with MILR1 (tyrosine-phosphorylated). Interacts with KIT. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation. Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with LYN By similarity. Interacts with MTUS1. Interacts with the tyrosine phosphorylated form of PDPK1 By similarity. Ref.2

Subcellular location

Cytoplasm. Nucleus. Note: In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK By similarity. Ref.2

Developmental stage

Highly expressed in embryonic cerebral cortex between day 18 and up to birth. Expression levels decrease after birth (at protein level). Ref.2

Domain

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

Post-translational modification

Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation By similarity. Phosphorylation at Tyr-566 enhances phosphatase activity By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.

Contains 2 SH2 domains.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Tyrosine-protein phosphatase non-receptor type 6
PRO_0000094760

Regions

Domain6 – 10297SH2 1
Domain112 – 215104SH2 2
Domain246 – 517272Tyrosine-protein phosphatase
Region455 – 4617Substrate binding By similarity

Sites

Active site4551Phosphocysteine intermediate By similarity UniProtKB P29350
Binding site4211Substrate By similarity
Binding site5021Substrate By similarity

Amino acid modifications

Modified residue661Phosphotyrosine By similarity
Modified residue3791Phosphotyrosine By similarity
Modified residue5381Phosphotyrosine By similarity
Modified residue5661Phosphotyrosine; by LYN By similarity

Sequences

Sequence LengthMass (Da)Tools
P81718 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 29364B22E8F45C87

FASTA61369,578
        10         20         30         40         50         60 
MLSRGWFHRD LSGPDAETLL KGRGVPGSFL ARPSRKNQGD FSLSVRVDDQ VTHIRIQNSG 

        70         80         90        100        110        120 
DFYDLYGGEK FATSTELVEY YTQQQGILQD RDGTIIHLKY PLNCSDPTSE RWYHGHMSGG 

       130        140        150        160        170        180 
QAESLLQAKG EPWTFLVRES LSQPGDFVLS VLNDQPKAAP GSPLRVTHIK VMCEGGRYTV 

       190        200        210        220        230        240 
GGSETFDSLT DLVEHFKKTG IEEASGAFVY LRQPYYATRV NAADIENRVL ELNKKQESED 

       250        260        270        280        290        300 
TAKAGFWEEF ESLQKQEAKN LHQRLEGQRP ENKSKNRYKN ILPFDHSRVI LQGRDSNIPG 

       310        320        330        340        350        360 
SDYINANYVK NQLLGPDENS KTYIASQGCL DATVNDFWQM AWQENTRVIV MTTREVEKGR 

       370        380        390        400        410        420 
NKCVPYWPEV GTQRVYGLYS VTNCKEHDTA EYKLRTLQIS PLDNGDLVRE IWHYQYLSWP 

       430        440        450        460        470        480 
DHGVPSEPGG VLSFLDQINQ RQESLPHAGP IIVHCSAGIG RTGTIIVIDM LMESVSTKGL 

       490        500        510        520        530        540 
DCDIDIQKTI QMVRAQRSGM VQTEAQYKFI YVAIAQFIET TKKKLEIIQS QRGQESEYGN 

       550        560        570        580        590        600 
ITYPPALRSA HAKASRTSSK HKEEVYENVH SKNKKEEKVK KQRSADKEKN KGSLKRNISL 

       610 
TPCRGLRWAD RDL 

« Hide

References

[1]"The rat SH2-containing protein-tyrosine phosphatase SHP-1 is a positive regulator of NGF-induced neuronal differentiation of PC12 cells."
Aoki N., Yamaguchi-Aoki Y., Ullrich A.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Angiotensin II-induced neural differentiation via angiotensin II type 2 (AT2) receptor-MMS2 cascade involving interaction between AT2 receptor-interacting protein and Src homology 2 domain-containing protein-tyrosine phosphatase 1."
Li J.-M., Mogi M., Tsukuda K., Tomochika H., Iwanami J., Min L.-J., Nahmias C., Iwai M., Horiuchi M.
Mol. Endocrinol. 21:499-511(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH MTUS1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U77038 mRNA. Translation: AAD00262.1.
RefSeqNP_446360.1. NM_053908.1.
UniGeneRn.18985.

3D structure databases

ProteinModelPortalP81718.
SMRP81718. Positions 6-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250571. 2 interactions.

PTM databases

PhosphoSiteP81718.

Proteomic databases

PaxDbP81718.
PRIDEP81718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116689.
KEGGrno:116689.
UCSCRGD:620660. rat.

Organism-specific databases

CTD5777.
RGD620660. Ptpn6.

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000273907.
HOVERGENHBG000223.
InParanoidP81718.
KOK05697.
PhylomeDBP81718.

Gene expression databases

GenevestigatorP81718.

Family and domain databases

Gene3D3.30.505.10. 2 hits.
InterProIPR000980. 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]
PfamPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619552.
PROP81718.

Entry information

Entry namePTN6_RAT
AccessionPrimary (citable) accession number: P81718
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families