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O70274 (TP4A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein tyrosine phosphatase type IVA 2

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 4a2
Protein-tyrosine phosphatase of regenerating liver 2
Short name=PRL-2
Gene names
Name:Ptp4a2
Synonyms:Prl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited by sodium orthovanadate and pentamidine By similarity.

Subunit structure

In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB By similarity.

Subcellular location

Cell membrane. Early endosome. Cytoplasm Ref.4.

Tissue specificity

Expressed in skeletal muscle, and at lower levels in liver, lung, heart, kidney, brain, testis and spleen. Ref.1

Post-translational modification

Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Protein tyrosine phosphatase type IVA 2
PRO_0000094786
Propeptide165 – 1673Removed in mature form Probable
PRO_0000396732

Regions

Domain79 – 14567Tyrosine-protein phosphatase
Region102 – 1076Phosphate binding By similarity

Sites

Active site691Proton donor By similarity
Active site1011Phosphocysteine intermediate By similarity
Binding site1071Substrate By similarity

Amino acid modifications

Modified residue1641Cysteine methyl ester Probable
Lipidation1641S-farnesyl cysteine Ref.4
Disulfide bond46 ↔ 101 By similarity

Experimental info

Mutagenesis164 – 1674Missing: Locates in the nucleus. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O70274 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E97B88BF87B87943

FASTA16719,127
        10         20         30         40         50         60 
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI 

        70         80         90        100        110        120 
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG 

       130        140        150        160 
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ 

« Hide

References

« Hide 'large scale' references
[1]"Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1."
Zeng Q., Hong W., Tan Y.H.
Biochem. Biophys. Res. Commun. 244:421-427(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"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: C57BL/6J.
Tissue: Testis.
[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].
Strain: C57BL/6.
Tissue: Brain and Embryo.
[4]"Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome."
Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.
J. Biol. Chem. 275:21444-21452(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION, MUTAGENESIS OF 164-CYS--GLN-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035644 mRNA. Translation: AAC15874.1.
AK033092 mRNA. Translation: BAC28149.1.
AK045093 mRNA. Translation: BAC32217.1.
AK155895 mRNA. Translation: BAE33489.1.
BC086794 mRNA. Translation: AAH86794.1.
BC087551 mRNA. Translation: AAH87551.1.
PIRJC5981.
RefSeqNP_001158217.1. NM_001164745.1.
NP_033000.1. NM_008974.4.
UniGeneMm.193688.

3D structure databases

ProteinModelPortalO70274.
SMRO70274. Positions 6-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO70274. 1 interaction.
MINTMINT-4105284.

Chemistry

BindingDBO70274.

PTM databases

PhosphoSiteO70274.

Proteomic databases

PaxDbO70274.
PRIDEO70274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
GeneID19244.
KEGGmmu:19244.
UCSCuc008uyf.2. mouse.

Organism-specific databases

CTD8073.
MGIMGI:1277117. Ptp4a2.

Phylogenomic databases

eggNOGNOG316886.
GeneTreeENSGT00390000009788.
HOGENOMHOG000231265.
HOVERGENHBG071295.
InParanoidO70274.
KOK18041.
OMALANMNRP.
OrthoDBEOG7C8GJD.
PhylomeDBO70274.
TreeFamTF313384.

Gene expression databases

ArrayExpressO70274.
BgeeO70274.
CleanExMM_PTP4A2.
GenevestigatorO70274.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTP4A2. mouse.
NextBio296062.
PROO70274.
SOURCESearch...

Entry information

Entry nameTP4A2_MOUSE
AccessionPrimary (citable) accession number: O70274
Secondary accession number(s): Q3U1K7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 112 of the entry and version 1 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