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Protein

Tyrosine-protein phosphatase non-receptor type 12

Gene

Ptpn12

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

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei199 – 1991SubstrateBy similarity
Active sitei231 – 2311Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei278 – 2781SubstrateBy similarity

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: MGI
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC
  3. SH3 domain binding Source: MGI

GO - Biological processi

  1. protein dephosphorylation Source: MGI
  2. tissue regeneration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ptpn12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:104673. Ptpn12.

Subcellular locationi

Cytoplasm 1 Publication. Cell projectionpodosome 1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: MGI
  4. cytosol Source: MGI
  5. plasma membrane Source: MGI
  6. podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Tyrosine-protein phosphatase non-receptor type 12PRO_0000094772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei331 – 3311Phosphoserine2 Publications
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei448 – 4481PhosphoserineBy similarity
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei519 – 5191PhosphothreonineBy similarity
Modified residuei550 – 5501Phosphoserine1 Publication
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei569 – 5691PhosphothreonineBy similarity
Modified residuei596 – 5961Phosphoserine1 Publication
Modified residuei598 – 5981Phosphothreonine1 Publication
Modified residuei603 – 6031Phosphoserine1 Publication
Modified residuei606 – 6061Phosphoserine1 Publication
Modified residuei608 – 6081Phosphoserine1 Publication
Modified residuei613 – 6131PhosphoserineBy similarity
Modified residuei673 – 6731PhosphoserineBy similarity
Modified residuei748 – 7481Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35831.
PaxDbiP35831.
PRIDEiP35831.

PTM databases

PhosphoSiteiP35831.

Expressioni

Gene expression databases

BgeeiP35831.
ExpressionAtlasiP35831. baseline and differential.
GenevestigatoriP35831.

Interactioni

Subunit structurei

Interacts with PTK2B/PYK2. Interacts with PSTPIP1 and TGFB1I1. Interacts with LPXN.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pstpip1P978145EBI-2642957,EBI-7484574
Shc1P980832EBI-2642957,EBI-300201

Protein-protein interaction databases

BioGridi202478. 2 interactions.
IntActiP35831. 5 interactions.
MINTiMINT-1618529.
STRINGi10090.ENSMUSP00000030556.

Structurei

3D structure databases

ProteinModelPortaliP35831.
SMRiP35831. Positions 3-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 293266Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 2377Substrate bindingBy similarity
Regioni344 – 43794Interaction with TGFB1I1Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000252955.
HOVERGENiHBG007666.
InParanoidiP35831.
KOiK18024.
OMAiTWSFHGP.
OrthoDBiEOG744T8Z.
TreeFamiTF351977.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35831-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT
60 70 80 90 100
ATGEKEENVK KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP
110 120 130 140 150
KAYVATQGPL ANTVIDFWRM IWEYNVVIIV MACREFEMGR KKCERYWPLY
160 170 180 190 200
GEDPITFAPF KISCENEQAR TDYFIRTLLL EFQNESRRLY QFHYVNWPDH
210 220 230 240 250
DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA ICAIDYTWNL
260 270 280 290 300
LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL
310 320 330 340 350
YEIHGAQKIA DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE
360 370 380 390 400
EILQPPEPHP VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH
410 420 430 440 450
PADLNRSYDK SADPMGKSES AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD
460 470 480 490 500
GNTLLNRGHA IKIKSASSSV VDRTSKPQEL SAGALKVDDV SQNSCADCSA
510 520 530 540 550
AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG PENATPVPDS
560 570 580 590 600
PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP
610 620 630 640 650
LHSDDSDSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CTRRVLPMSI
660 670 680 690 700
ARQEVAGTPH SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP
710 720 730 740 750
NQEWSEQRES EGLTTSGNEK HDAGGIHTEA SADSPPAFSD KKDQITKSPA
760 770
EVTDIGFGNR CGKPKGPREP PSEWT
Length:775
Mass (Da):86,526
Last modified:July 27, 2011 - v3
Checksum:iED1A7A577CE4352C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1112LA → FR in CAA60477. (PubMed:7772023)Curated
Sequence conflicti128 – 1281I → M in CAA60477. (PubMed:7772023)Curated
Sequence conflicti296 – 2961K → N in CAA45037. (PubMed:1590786)Curated
Sequence conflicti310 – 3101A → R in CAA60477. (PubMed:7772023)Curated
Sequence conflicti328 – 3325KQDSP → DETS in CAA45037. (PubMed:1590786)Curated
Sequence conflicti380 – 3801W → V in CAA45037. (PubMed:1590786)Curated
Sequence conflicti414 – 4152PM → QW in CAA60477. (PubMed:7772023)Curated
Sequence conflicti606 – 6072SD → WH in CAA60477. (PubMed:7772023)Curated
Sequence conflicti642 – 6421T → H in CAA60477. (PubMed:7772023)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19102.1.
PIRiJH0609.
S55345.
RefSeqiNP_035333.2. NM_011203.2.
UniGeneiMm.319117.

Genome annotation databases

EnsembliENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
GeneIDi19248.
KEGGimmu:19248.
UCSCiuc008woh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19102.1.
PIRiJH0609.
S55345.
RefSeqiNP_035333.2. NM_011203.2.
UniGeneiMm.319117.

3D structure databases

ProteinModelPortaliP35831.
SMRiP35831. Positions 3-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202478. 2 interactions.
IntActiP35831. 5 interactions.
MINTiMINT-1618529.
STRINGi10090.ENSMUSP00000030556.

PTM databases

PhosphoSiteiP35831.

Proteomic databases

MaxQBiP35831.
PaxDbiP35831.
PRIDEiP35831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
GeneIDi19248.
KEGGimmu:19248.
UCSCiuc008woh.1. mouse.

Organism-specific databases

CTDi5782.
MGIiMGI:104673. Ptpn12.

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000252955.
HOVERGENiHBG007666.
InParanoidiP35831.
KOiK18024.
OMAiTWSFHGP.
OrthoDBiEOG744T8Z.
TreeFamiTF351977.

Miscellaneous databases

ChiTaRSiPtpn12. mouse.
NextBioi296078.
PROiP35831.
SOURCEiSearch...

Gene expression databases

BgeeiP35831.
ExpressionAtlasiP35831. baseline and differential.
GenevestigatoriP35831.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. 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. "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.
    , 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. 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. 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.

Entry informationi

Entry nameiPTN12_MOUSE
AccessioniPrimary (citable) accession number: P35831
Secondary accession number(s): Q80UM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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.