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Q63739 (TP4A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 1
EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 4a1
Protein-tyrosine phosphatase of regenerating liver 1
Short name=PRL-1
Gene names
Name:Ptp4a1
Synonyms:Prl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length173 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. May play a role in the development and maintenance of differentiating epithelial tissues By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited by sodium orthovanadate and pentamidine By similarity.

Subunit structure

Homotrimer. Interacts with tubulin By similarity. Interacts with ATF5. Ref.6

Subcellular location

Cell membrane. Early endosome. Endoplasmic reticulum. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Note: And mitotic spindle. Ref.5

Developmental stage

Expressed in all tissues except heart and skeletal muscle, from E10.5 to E18.5. Ref.4

Post-translational modification

Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170Protein tyrosine phosphatase type IVA 1
PRO_0000094782
Propeptide171 – 1733Removed in mature form Probable
PRO_0000396728

Regions

Domain82 – 14867Tyrosine-protein phosphatase
Region97 – 13236Interaction with ATF5
Region105 – 1106Phosphate binding By similarity

Sites

Active site721Proton donor By similarity
Active site1041Phosphocysteine intermediate By similarity
Binding site1101Substrate By similarity

Amino acid modifications

Modified residue1701Cysteine methyl ester Probable
Lipidation1701S-farnesyl cysteine Ref.5
Disulfide bond49 ↔ 104 By similarity

Experimental info

Mutagenesis1041C → S: Abolishes activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q63739 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 702008013D3F3835

FASTA17319,815
        10         20         30         40         50         60 
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTTLVEK 

        70         80         90        100        110        120 
EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI 

       130        140        150        160        170 
EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ

« Hide

References

« Hide 'large scale' references
[1]Oh B., Hwang S.-Y., Knowles B.B.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Bone marrow and Head.
[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: FVB/N.
Tissue: Colon and Eye.
[4]"Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene."
Rundle C.H., Kappen C.
J. Exp. Zool. 283:612-617(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-23, DEVELOPMENTAL STAGE.
[5]"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-170, SUBCELLULAR LOCATION.
[6]"ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase."
Peters C.S., Liang X., Li S., Kannan S., Peng Y., Taub R., Diamond R.H.
J. Biol. Chem. 276:13718-13726(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF5, MUTAGENESIS OF CYS-104.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U84411 mRNA. Translation: AAB58913.1.
AK081491 mRNA. Translation: BAC38233.1.
AK148288 mRNA. Translation: BAE28460.1.
AK150506 mRNA. Translation: BAE29619.1.
AK151533 mRNA. Translation: BAE30480.1.
BC055039 mRNA. Translation: AAH55039.1.
BC086787 mRNA. Translation: AAH86787.1.
BC094447 mRNA. Translation: AAH94447.1.
AF064943 mRNA. No translation available.
IPIIPI00133490.
RefSeqNP_035330.1. NM_011200.2.
XP_001472631.1. XM_001472581.3.
UniGeneMm.374437.

3D structure databases

ProteinModelPortalQ63739.
ModBaseSearch...

PTM databases

PhosphoSiteQ63739.

Proteomic databases

PaxDbQ63739.
PRIDEQ63739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027232; ENSMUSP00000027232; ENSMUSG00000026064.
ENSMUST00000076587; ENSMUSP00000110861; ENSMUSG00000026064.
GeneID100044742.
19243.
KEGGmmu:100044742.
mmu:19243.

Organism-specific databases

CTD7803.
MGIMGI:1277096. Ptp4a1.

Phylogenomic databases

eggNOGNOG265664.
GeneTreeENSGT00390000009788.
HOGENOMHOG000231265.
HOVERGENHBG071295.
InParanoidQ63739.
KOK01104.
OMACEATYDA.
OrthoDBEOG4ZCT5N.

Gene expression databases

ArrayExpressQ63739.
BgeeQ63739.
CleanExMM_PTP4A1.
GenevestigatorQ63739.
GermOnlineENSMUSG00000026064. Mus musculus.
ENSMUSG00000071558. Mus musculus.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. False negative.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ63739.
NextBio296058.
SOURCESearch...

Entry information

Entry nameTP4A1_MOUSE
AccessionPrimary (citable) accession number: Q63739
Secondary accession number(s): O09097, O09154, Q3UFU9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents