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Protein

Protein tyrosine phosphatase type IVA 2

Gene

Ptp4a2

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

Functioni

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).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Inhibited by sodium orthovanadate and pentamidine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Proton donorBy similarity
Active sitei101 – 1011Phosphocysteine intermediateBy similarity
Binding sitei107 – 1071SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ptp4a2
Synonyms:Prl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1277117. Ptp4a2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1674Missing : Locates in the nucleus. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Protein tyrosine phosphatase type IVA 2PRO_0000094786Add
BLAST
Propeptidei165 – 1673Removed in mature formCuratedPRO_0000396732

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 101By similarity
Modified residuei164 – 1641Cysteine methyl esterCurated
Lipidationi164 – 1641S-farnesyl cysteine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiO70274.
PaxDbiO70274.
PRIDEiO70274.

PTM databases

PhosphoSiteiO70274.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO70274.
CleanExiMM_PTP4A2.
ExpressionAtlasiO70274. baseline and differential.
GenevestigatoriO70274.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiO70274. 1 interaction.
MINTiMINT-4105284.

Structurei

3D structure databases

ProteinModelPortaliO70274.
SMRiO70274. Positions 6-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 14567Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 1076Phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG316886.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiO70274.
KOiK18041.
OMAiAPIEKEG.
OrthoDBiEOG7C8GJD.
PhylomeDBiO70274.
TreeFamiTF313384.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY
60 70 80 90 100
DKAPVEKEGI HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH
110 120 130 140 150
CVAGLGRAPV LVALALIECG MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR
160
PKMRLRFRDT NGHCCVQ
Length:167
Mass (Da):19,127
Last modified:August 1, 1998 - v1
Checksum:iE97B88BF87B87943
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18704.1.
PIRiJC5981.
RefSeqiNP_001158217.1. NM_001164745.1.
NP_033000.1. NM_008974.4.
UniGeneiMm.193688.

Genome annotation databases

EnsembliENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
GeneIDi19244.
KEGGimmu:19244.
UCSCiuc008uyf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18704.1.
PIRiJC5981.
RefSeqiNP_001158217.1. NM_001164745.1.
NP_033000.1. NM_008974.4.
UniGeneiMm.193688.

3D structure databases

ProteinModelPortaliO70274.
SMRiO70274. Positions 6-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70274. 1 interaction.
MINTiMINT-4105284.

Chemistry

BindingDBiO70274.

PTM databases

PhosphoSiteiO70274.

Proteomic databases

MaxQBiO70274.
PaxDbiO70274.
PRIDEiO70274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
GeneIDi19244.
KEGGimmu:19244.
UCSCiuc008uyf.2. mouse.

Organism-specific databases

CTDi8073.
MGIiMGI:1277117. Ptp4a2.

Phylogenomic databases

eggNOGiNOG316886.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiO70274.
KOiK18041.
OMAiAPIEKEG.
OrthoDBiEOG7C8GJD.
PhylomeDBiO70274.
TreeFamiTF313384.

Miscellaneous databases

ChiTaRSiPtp4a2. mouse.
NextBioi296062.
PROiO70274.
SOURCEiSearch...

Gene expression databases

BgeeiO70274.
CleanExiMM_PTP4A2.
ExpressionAtlasiO70274. baseline and differential.
GenevestigatoriO70274.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTP4A2_MOUSE
AccessioniPrimary (citable) accession number: O70274
Secondary accession number(s): Q3U1K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: August 1, 1998
Last modified: May 27, 2015
This is version 121 of the entry and version 1 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.