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P43378 (PTN9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 9

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase MEG2
Short name=PTPase MEG2
Gene names
Name:PTPN9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus. Ref.7

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 3 subfamily.

Contains 1 CRAL-TRIO domain.

Contains 1 tyrosine-protein phosphatase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Tyrosine-protein phosphatase non-receptor type 9
PRO_0000094764

Regions

Domain84 – 243160CRAL-TRIO
Domain303 – 574272Tyrosine-protein phosphatase
Region515 – 5217Substrate binding By similarity

Sites

Active site5151Phosphocysteine intermediate By similarity
Binding site4701Substrate By similarity
Binding site5591Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5

Secondary structure

............................................... 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43378 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 9BD75A5A986DDA0B

FASTA59368,020
        10         20         30         40         50         60 
MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR 

        70         80         90        100        110        120 
AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH 

       130        140        150        160        170        180 
KSVQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP 

       190        200        210        220        230        240 
ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK 

       250        260        270        280        290        300 
IDLATWNFQF LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK 

       310        320        330        340        350        360 
QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA 

       370        380        390        400        410        420 
SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK 

       430        440        450        460        470        480 
DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL 

       490        500        510        520        530        540 
IDFLRVVRNQ QSLAVSNMGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT 

       550        560        570        580        590 
LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p."
Gu M., Warshawsky I., Majerus P.W.
Proc. Natl. Acad. Sci. U.S.A. 89:2980-2984(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
Tissue: Pancreas.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-582, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83738 mRNA. Translation: AAA60226.1.
BT007405 mRNA. Translation: AAP36073.1.
BC010863 mRNA. Translation: AAH10863.1.
PIRA42690.
RefSeqNP_002824.1. NM_002833.3.
UniGeneHs.445775.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA5X-ray1.60A/B277-582[»]
4GE2X-ray1.80A/B277-582[»]
4GE5X-ray2.00A/B277-582[»]
4GE6X-ray1.40A/B277-582[»]
4ICZX-ray1.90A277-582[»]
ProteinModelPortalP43378.
SMRP43378. Positions 48-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111744. 6 interactions.
IntActP43378. 7 interactions.
MINTMINT-1455219.
STRING9606.ENSP00000303554.

Chemistry

BindingDBP43378.
ChEMBLCHEMBL6117.

PTM databases

PhosphoSiteP43378.

Polymorphism databases

DMDM1172724.

Proteomic databases

PaxDbP43378.
PRIDEP43378.

Protocols and materials databases

DNASU5780.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306726; ENSP00000303554; ENSG00000169410.
GeneID5780.
KEGGhsa:5780.
UCSCuc002bal.3. human.

Organism-specific databases

CTD5780.
GeneCardsGC15M075759.
HGNCHGNC:9661. PTPN9.
HPAHPA041922.
MIM600768. gene.
neXtProtNX_P43378.
PharmGKBPA34005.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000006971.
HOVERGENHBG006880.
InParanoidP43378.
KOK18038.
OMAMTTRFEE.
OrthoDBEOG79GT5R.
PhylomeDBP43378.
TreeFamTF351975.

Gene expression databases

ArrayExpressP43378.
BgeeP43378.
CleanExHS_PTPN9.
GenevestigatorP43378.

Family and domain databases

Gene3D3.40.525.10. 1 hit.
InterProIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM01100. CRAL_TRIO_N. 1 hit.
SM00194. PTPc. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN9. human.
EvolutionaryTraceP43378.
GeneWikiPTPN9.
GenomeRNAi5780.
NextBio22478.
PROP43378.
SOURCESearch...

Entry information

Entry namePTN9_HUMAN
AccessionPrimary (citable) accession number: P43378
Secondary accession number(s): Q53XR9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM