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Protein

Protein tyrosine phosphatase type IVA 1

Gene

PTP4A1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

GO - Biological processi

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 1PRO_0000094783Add
BLAST
Propeptidei171 – 1733Removed in mature formBy similarityPRO_0000396729

Amino acid modifications

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

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Interactioni

Subunit structurei

Homotrimer. Interacts with ATF5 and tubulin (By similarity).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000018734.

Structurei

3D structure databases

ProteinModelPortaliQ5R7J8.
SMRiQ5R7J8. 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 ATF5By similarityAdd
BLAST
Regioni105 – 1106Phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG071295.
InParanoidiQ5R7J8.
KOiK18041.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PfamiPF00782. DSPc. 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.

Q5R7J8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE
60 70 80 90 100
ATYDTALVEK EGIHVLDWPF DDGAPPSNQI VDGWLSLVKI KFREEPGCCI
110 120 130 140 150
AVHCVAGLGR APVLVALALI EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE
160 170
KYRPKMRLRF KDSNGHRNNC CIQ
Length:173
Mass (Da):19,727
Last modified:December 21, 2004 - v1
Checksum:i5FF00B273E00A186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860117 mRNA. Translation: CAH92262.1.
RefSeqiNP_001126324.1. NM_001132852.1.
UniGeneiPab.863.

Genome annotation databases

GeneIDi100173305.
KEGGipon:100173305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860117 mRNA. Translation: CAH92262.1.
RefSeqiNP_001126324.1. NM_001132852.1.
UniGeneiPab.863.

3D structure databases

ProteinModelPortaliQ5R7J8.
SMRiQ5R7J8. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000018734.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173305.
KEGGipon:100173305.

Organism-specific databases

CTDi7803.

Phylogenomic databases

HOVERGENiHBG071295.
InParanoidiQ5R7J8.
KOiK18041.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiTP4A1_PONAB
AccessioniPrimary (citable) accession number: Q5R7J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 21, 2004
Last modified: June 24, 2015
This is version 64 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. 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.