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Protein

Protein tyrosine phosphatase type IVA 1

Gene

Ptp4a1

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. May play a role in the development and maintenance of differentiating epithelial tissues (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 sitei72 – 721Proton donorBy similarity
Active sitei104 – 1041Phosphocysteine intermediateBy similarity
Binding sitei110 – 1101SubstrateBy similarity

GO - Molecular functioni

  1. prenylated protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. multicellular organismal development Source: UniProtKB-KW
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. positive regulation of cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ptp4a1
Synonyms:Prl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1277096. Ptp4a1.

Subcellular locationi

Cell membrane 1 Publication. Early endosome 1 Publication. Endoplasmic reticulum 1 Publication. Cytoplasm 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
Note: And mitotic spindle.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic side of plasma membrane Source: MGI
  3. early endosome Source: UniProtKB-SubCell
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. endosome Source: UniProtKB
  6. extracellular vesicular exosome Source: MGI
  7. plasma membrane Source: UniProtKB
  8. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041C → S: Abolishes activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 1PRO_0000094782Add
BLAST
Propeptidei171 – 1733Removed in mature formCuratedPRO_0000396728

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 104By similarity
Modified residuei170 – 1701Cysteine methyl esterCurated
Lipidationi170 – 1701S-farnesyl cysteine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ63739.
PaxDbiQ63739.
PRIDEiQ63739.

PTM databases

PhosphoSiteiQ63739.

Expressioni

Developmental stagei

Expressed in all tissues except heart and skeletal muscle, from E10.5 to E18.5.1 Publication

Gene expression databases

BgeeiQ63739.
CleanExiMM_PTP4A1.
ExpressionAtlasiQ63739. baseline and differential.
GenevestigatoriQ63739.

Interactioni

Subunit structurei

Homotrimer. Interacts with tubulin (By similarity). Interacts with ATF5.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ63739.
SMRiQ63739. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 14867Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 13236Interaction with ATF5Add
BLAST
Regioni105 – 1106Phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ63739.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ63739.
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.

Q63739-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE
60 70 80 90 100
ATYDTTLVEK EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI
110 120 130 140 150
AVHCVAGLGR APVLVALALI EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE
160 170
KYRPKMRLRF KDSNGHRNNC CIQ
Length:173
Mass (Da):19,815
Last modified:November 1, 1996 - v1
Checksum:i702008013D3F3835
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14858.1.
RefSeqiNP_035330.1. NM_011200.2.
XP_006495861.1. XM_006495798.1.
XP_006495862.1. XM_006495799.1.
XP_006544159.1. XM_006544096.1.
UniGeneiMm.491181.

Genome annotation databases

EnsembliENSMUST00000027232; ENSMUSP00000027232; ENSMUSG00000026064.
ENSMUST00000076587; ENSMUSP00000110861; ENSMUSG00000026064.
GeneIDi102643131.
19243.
KEGGimmu:102643131.
mmu:19243.
UCSCiuc007anh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14858.1.
RefSeqiNP_035330.1. NM_011200.2.
XP_006495861.1. XM_006495798.1.
XP_006495862.1. XM_006495799.1.
XP_006544159.1. XM_006544096.1.
UniGeneiMm.491181.

3D structure databases

ProteinModelPortaliQ63739.
SMRiQ63739. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ63739.

PTM databases

PhosphoSiteiQ63739.

Proteomic databases

MaxQBiQ63739.
PaxDbiQ63739.
PRIDEiQ63739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027232; ENSMUSP00000027232; ENSMUSG00000026064.
ENSMUST00000076587; ENSMUSP00000110861; ENSMUSG00000026064.
GeneIDi102643131.
19243.
KEGGimmu:102643131.
mmu:19243.
UCSCiuc007anh.1. mouse.

Organism-specific databases

CTDi7803.
MGIiMGI:1277096. Ptp4a1.

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ63739.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ63739.
TreeFamiTF313384.

Miscellaneous databases

NextBioi296058.
PROiQ63739.
SOURCEiSearch...

Gene expression databases

BgeeiQ63739.
CleanExiMM_PTP4A1.
ExpressionAtlasiQ63739. baseline and differential.
GenevestigatoriQ63739.

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. 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.
    , 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.

Entry informationi

Entry nameiTP4A1_MOUSE
AccessioniPrimary (citable) accession number: Q63739
Secondary accession number(s): O09097, O09154, Q3UFU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 124 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.