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Protein

Tyrosine-protein phosphatase non-receptor type 9

Gene

PTPN9

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

Functioni

Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei470 – 4701SubstrateBy similarity
Active sitei515 – 5151Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei559 – 5591SubstrateBy similarity

GO - Molecular functioni

  • non-membrane spanning protein tyrosine phosphatase activity Source: ProtInc
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: GOC
  • protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PTPN9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9661. PTPN9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34005.

Polymorphism and mutation databases

DMDMi1172724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Tyrosine-protein phosphatase non-receptor type 9PRO_0000094764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP43378.
PaxDbiP43378.
PRIDEiP43378.

PTM databases

DEPODiP43378.
PhosphoSiteiP43378.

Expressioni

Gene expression databases

BgeeiP43378.
CleanExiHS_PTPN9.
ExpressionAtlasiP43378. baseline and differential.
GenevisibleiP43378. HS.

Organism-specific databases

HPAiHPA041922.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW134EBI-742898,EBI-741181
CMTM5Q96DZ94EBI-742898,EBI-2548702
GHRP109122EBI-742898,EBI-286316
MAL2Q969L23EBI-742898,EBI-944295
NSFP464592EBI-742898,EBI-712251
RTN3O951974EBI-742898,EBI-740467

Protein-protein interaction databases

BioGridi111744. 15 interactions.
IntActiP43378. 8 interactions.
MINTiMINT-1455219.
STRINGi9606.ENSP00000303554.

Structurei

Secondary structure

1
593
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi288 – 31225Combined sources
Helixi320 – 3234Combined sources
Turni325 – 3273Combined sources
Helixi328 – 3303Combined sources
Turni340 – 3423Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi359 – 3657Combined sources
Beta strandi368 – 3758Combined sources
Helixi380 – 3823Combined sources
Helixi383 – 39210Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi423 – 4264Combined sources
Beta strandi429 – 43810Combined sources
Beta strandi440 – 45112Combined sources
Turni452 – 4554Combined sources
Beta strandi456 – 46510Combined sources
Beta strandi470 – 4723Combined sources
Helixi478 – 49720Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi516 – 5194Combined sources
Helixi520 – 53819Combined sources
Beta strandi539 – 5413Combined sources
Helixi543 – 5508Combined sources
Turni551 – 5533Combined sources
Helixi561 – 57717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP43378.
SMRiP43378. Positions 48-237, 277-583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43378.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 243160CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST
Domaini303 – 574272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni515 – 5217Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000006971.
HOVERGENiHBG006880.
InParanoidiP43378.
KOiK18038.
OMAiVWEQNVL.
OrthoDBiEOG79GT5R.
PhylomeDBiP43378.
TreeFamiTF351975.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00194. PTPc. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF
60 70 80 90 100
LMARKFDVLR AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN
110 120 130 140 150
VRDPTGASIA LFTARLHHPH KSVQHVVLQA LFYLLDRAVD SFETQRNGLV
160 170 180 190 200
FIYDMCGSNY ANFELDLGKK VLNLLKGAFP ARLKKVLIVG APIWFRVPYS
210 220 230 240 250
IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK IDLATWNFQF
260 270 280 290 300
LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK
310 320 330 340 350
QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS
360 370 380 390 400
GHTQTDYINA SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM
410 420 430 440 450
TTRFEEGGRR KCGQYWPLEK DSRIRFGFLT VTNLGVENMN HYKKTTLEIH
460 470 480 490 500
NTEERQKRQV THFQFLSWPD YGVPSSAASL IDFLRVVRNQ QSLAVSNMGA
510 520 530 540 550
RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT LNVFQTVSRM
560 570 580 590
RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ
Length:593
Mass (Da):68,020
Last modified:November 1, 1995 - v1
Checksum:i9BD75A5A986DDA0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83738 mRNA. Translation: AAA60226.1.
BT007405 mRNA. Translation: AAP36073.1.
BC010863 mRNA. Translation: AAH10863.1.
CCDSiCCDS10280.1.
PIRiA42690.
RefSeqiNP_002824.1. NM_002833.3.
UniGeneiHs.445775.

Genome annotation databases

EnsembliENST00000618819; ENSP00000482732; ENSG00000169410.
GeneIDi5780.
KEGGihsa:5780.
UCSCiuc002bal.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83738 mRNA. Translation: AAA60226.1.
BT007405 mRNA. Translation: AAP36073.1.
BC010863 mRNA. Translation: AAH10863.1.
CCDSiCCDS10280.1.
PIRiA42690.
RefSeqiNP_002824.1. NM_002833.3.
UniGeneiHs.445775.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP43378.
SMRiP43378. Positions 48-237, 277-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111744. 15 interactions.
IntActiP43378. 8 interactions.
MINTiMINT-1455219.
STRINGi9606.ENSP00000303554.

Chemistry

BindingDBiP43378.
ChEMBLiCHEMBL6117.

PTM databases

DEPODiP43378.
PhosphoSiteiP43378.

Polymorphism and mutation databases

DMDMi1172724.

Proteomic databases

MaxQBiP43378.
PaxDbiP43378.
PRIDEiP43378.

Protocols and materials databases

DNASUi5780.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000618819; ENSP00000482732; ENSG00000169410.
GeneIDi5780.
KEGGihsa:5780.
UCSCiuc002bal.3. human.

Organism-specific databases

CTDi5780.
GeneCardsiGC15M075759.
HGNCiHGNC:9661. PTPN9.
HPAiHPA041922.
MIMi600768. gene.
neXtProtiNX_P43378.
PharmGKBiPA34005.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000006971.
HOVERGENiHBG006880.
InParanoidiP43378.
KOiK18038.
OMAiVWEQNVL.
OrthoDBiEOG79GT5R.
PhylomeDBiP43378.
TreeFamiTF351975.

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.

Miscellaneous databases

ChiTaRSiPTPN9. human.
EvolutionaryTraceiP43378.
GeneWikiiPTPN9.
GenomeRNAii5780.
NextBioi22478.
PROiP43378.
SOURCEiSearch...

Gene expression databases

BgeeiP43378.
CleanExiHS_PTPN9.
ExpressionAtlasiP43378. baseline and differential.
GenevisibleiP43378. HS.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00194. PTPc. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiPTN9_HUMAN
AccessioniPrimary (citable) accession number: P43378
Secondary accession number(s): Q53XR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 153 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 15
    Human chromosome 15: 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
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.