P35831 (PTN12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Ptpn12

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › podosome 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.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from direct assay Ref.3. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara podosome Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	phosphoprotein phosphatase activity Inferred from direct assay Ref.3. Source: MGI protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 775	775	Tyrosine-protein phosphatase non-receptor type 12		PRO_0000094772
Regions
	Domain	28 – 293	266	Tyrosine-protein phosphatase
	Region	231 – 237	7	Substrate binding By similarity
	Region	344 – 437	94	Interaction with TGFB1I1
Sites
	Active site	231	1	Phosphocysteine intermediate By similarity
	Binding site	199	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	186	1	Phosphoserine Ref.12
	Modified residue	331	1	Phosphoserine Ref.15
	Modified residue	434	1	Phosphoserine Ref.14
	Modified residue	448	1	Phosphoserine By similarity
	Modified residue	467	1	Phosphoserine By similarity
	Modified residue	519	1	Phosphothreonine By similarity
	Modified residue	567	1	Phosphoserine By similarity
	Modified residue	569	1	Phosphothreonine By similarity
	Modified residue	596	1	Phosphoserine Ref.13
	Modified residue	598	1	Phosphothreonine Ref.13
	Modified residue	603	1	Phosphoserine Ref.13
	Modified residue	606	1	Phosphoserine By similarity
	Modified residue	608	1	Phosphoserine Ref.13
	Modified residue	613	1	Phosphoserine By similarity
	Modified residue	673	1	Phosphoserine Ref.12
	Modified residue	748	1	Phosphoserine Ref.10
Experimental info
	Sequence conflict	110 – 111	2	LA → FR in CAA60477. Ref.3
	Sequence conflict	128	1	I → M in CAA60477. Ref.3
	Sequence conflict	296	1	K → N in CAA45037. Ref.1
	Sequence conflict	310	1	A → R in CAA60477. Ref.3
	Sequence conflict	328 – 332	5	KQDSP → DETS in CAA45037. Ref.1
	Sequence conflict	380	1	W → V in CAA45037. Ref.1
	Sequence conflict	414 – 415	2	PM → QW in CAA60477. Ref.3
	Sequence conflict	606 – 607	2	SD → WH in CAA60477. Ref.3
	Sequence conflict	642	1	T → H in CAA60477. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P35831 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: ED1A7A577CE4352C	FASTA	775	86,526
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-673, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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-596; THR-598; SER-603 AND SER-608, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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-434, MASS SPECTROMETRY. Tissue: Macrophage.
[15]	"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, MASS SPECTROMETRY. 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.
IPI	IPI00337948.
PIR	JH0609. S55345.
RefSeq	NP_035333.2. NM_011203.2.
UniGene	Mm.319117.
3D structure databases
ProteinModelPortal	P35831.
SMR	P35831. Positions 3-298.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35831. 1 interaction.
MINT	MINT-1486617.
STRING	10090.ENSMUSP00000030556.
PTM databases
PhosphoSite	P35831.
Proteomic databases
PaxDb	P35831.
PRIDE	P35831.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
GeneID	19248.
KEGG	mmu:19248.
Organism-specific databases
CTD	5782.
MGI	MGI:104673. Ptpn12.
Phylogenomic databases
eggNOG	COG5599.
GeneTree	ENSGT00700000104095.
HOGENOM	HOG000252955.
HOVERGEN	HBG007666.
InParanoid	Q80UM4.
KO	K01104.
OMA	ERYWPLY.
OrthoDB	EOG42BX89.
Gene expression databases
ArrayExpress	P35831.
Bgee	P35831.
Genevestigator	P35831.
GermOnline	ENSMUSG00000028771. Mus musculus.
Family and domain databases
InterPro	IPR012266. Ptpn_12. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00102. Y_phosphatase. 1 hit. [Graphical view]
PIRSF	PIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00194. PTPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PTPN12. mouse.
NextBio	296078.
SOURCE	Search...

Entry information

Entry name

PTN12_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program