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P35831 (PTN12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 12

EC=3.1.3.48
Alternative name(s):
MPTP-PEST
Protein-tyrosine phosphatase P19
Short name=P19-PTP
Gene names
Name:Ptpn12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2 By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with PTK2B/PYK2. Interacts with PSTPIP1 and TGFB1I1. Interacts with LPXN. Ref.7 Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasm. Cell projectionpodosome Ref.9.

Post-translational modification

Phosphorylated by STK24/MST3 and this results in inhibition of its activity By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pstpip1P978145EBI-2642957,EBI-7484574
Shc1P980832EBI-2642957,EBI-300201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 775775Tyrosine-protein phosphatase non-receptor type 12
PRO_0000094772

Regions

Domain28 – 293266Tyrosine-protein phosphatase
Region231 – 2377Substrate binding By similarity
Region344 – 43794Interaction with TGFB1I1

Sites

Active site2311Phosphocysteine intermediate By similarity
Binding site1991Substrate By similarity
Binding site2781Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue191Phosphoserine By similarity
Modified residue3311Phosphoserine Ref.13 Ref.14
Modified residue4341Phosphoserine Ref.13
Modified residue4481Phosphoserine By similarity
Modified residue4671Phosphoserine By similarity
Modified residue5191Phosphothreonine By similarity
Modified residue5501Phosphoserine Ref.12
Modified residue5671Phosphoserine By similarity
Modified residue5691Phosphothreonine By similarity
Modified residue5961Phosphoserine Ref.12
Modified residue5981Phosphothreonine Ref.12
Modified residue6031Phosphoserine Ref.12
Modified residue6061Phosphoserine Ref.12
Modified residue6081Phosphoserine Ref.12
Modified residue6131Phosphoserine By similarity
Modified residue6731Phosphoserine By similarity
Modified residue7481Phosphoserine Ref.10

Experimental info

Sequence conflict110 – 1112LA → FR in CAA60477. Ref.3
Sequence conflict1281I → M in CAA60477. Ref.3
Sequence conflict2961K → N in CAA45037. Ref.1
Sequence conflict3101A → R in CAA60477. Ref.3
Sequence conflict328 – 3325KQDSP → DETS in CAA45037. Ref.1
Sequence conflict3801W → V in CAA45037. Ref.1
Sequence conflict414 – 4152PM → QW in CAA60477. Ref.3
Sequence conflict606 – 6072SD → WH in CAA60477. Ref.3
Sequence conflict6421T → H in CAA60477. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P35831 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: ED1A7A577CE4352C

FASTA77586,526
        10         20         30         40         50         60 
MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK 

        70         80         90        100        110        120 
KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM 

       130        140        150        160        170        180 
IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCENEQAR TDYFIRTLLL 

       190        200        210        220        230        240 
EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA 

       250        260        270        280        290        300 
ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 

       310        320        330        340        350        360 
YEIHGAQKIA DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE EILQPPEPHP 

       370        380        390        400        410        420 
VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH PADLNRSYDK SADPMGKSES 

       430        440        450        460        470        480 
AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD GNTLLNRGHA IKIKSASSSV VDRTSKPQEL 

       490        500        510        520        530        540 
SAGALKVDDV SQNSCADCSA AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG 

       550        560        570        580        590        600 
PENATPVPDS PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP 

       610        620        630        640        650        660 
LHSDDSDSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CTRRVLPMSI ARQEVAGTPH 

       670        680        690        700        710        720 
SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP NQEWSEQRES EGLTTSGNEK 

       730        740        750        760        770 
HDAGGIHTEA SADSPPAFSD KKDQITKSPA EVTDIGFGNR CGKPKGPREP PSEWT 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of a novel murine non-receptor protein tyrosine phosphatase during differentiation of P19 embryonal carcinoma cells."
den Hertog J., Pals C.E., Jonk L.J., Kruijer W.
Biochem. Biophys. Res. Commun. 184:1241-1249(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase."
Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M., Adachi M., Imai K., Yachi A.
Biochem. Biophys. Res. Commun. 189:1223-1230(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 297-416.
[3]"Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein tyrosine phosphatase."
Charest A., Wagner J., Shen S.H., Tremblay M.L.
Biochem. J. 308:425-432(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Strain: C57BL/6.
[7]"Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain."
Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L., Nose K.
J. Biol. Chem. 274:9847-9853(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[8]"PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-PEST toward a specific dephosphorylation of WASP."
Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S., Lasky L.A., Tremblay M.L.
J. Biol. Chem. 277:2973-2986(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSTPIP1.
[9]"Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LPXN AND PTK2B/PYK2.
[10]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[11]"Leupaxin binds to PEST domain tyrosine phosphatase PEP."
Watanabe N., Amano N., Ishizuka H., Mashima K.
Mol. Cell. Biochem. 269:13-17(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPXN.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-596; THR-598; SER-603; SER-606 AND SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63440 mRNA. Translation: CAA45037.1. Sequence problems.
X86781 Genomic DNA. Translation: CAA60477.1.
AK154107 mRNA. Translation: BAE32381.1.
CH466586 Genomic DNA. Translation: EDL03216.1.
BC051980 mRNA. Translation: AAH51980.1.
CCDSCCDS19102.1.
PIRJH0609.
S55345.
RefSeqNP_035333.2. NM_011203.2.
UniGeneMm.319117.

3D structure databases

ProteinModelPortalP35831.
SMRP35831. Positions 3-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202478. 2 interactions.
IntActP35831. 5 interactions.
MINTMINT-1618529.
STRING10090.ENSMUSP00000030556.

PTM databases

PhosphoSiteP35831.

Proteomic databases

MaxQBP35831.
PaxDbP35831.
PRIDEP35831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
GeneID19248.
KEGGmmu:19248.
UCSCuc008woh.1. mouse.

Organism-specific databases

CTD5782.
MGIMGI:104673. Ptpn12.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00750000117233.
HOGENOMHOG000252955.
HOVERGENHBG007666.
InParanoidQ80UM4.
KOK18024.
OMATWSFHGP.
OrthoDBEOG744T8Z.
TreeFamTF351977.

Gene expression databases

ArrayExpressP35831.
BgeeP35831.
GenevestigatorP35831.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN12. mouse.
NextBio296078.
PROP35831.
SOURCESearch...

Entry information

Entry namePTN12_MOUSE
AccessionPrimary (citable) accession number: P35831
Secondary accession number(s): Q80UM4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 130 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot