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O75365

- TP4A3_HUMAN

UniProt

O75365 - TP4A3_HUMAN

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Protein
Protein tyrosine phosphatase type IVA 3
Gene
PTP4A3, PRL3
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Enzyme regulationi

Inhibited by sodium orthovanadate and peroxovanadium compounds, and by pentamidine.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Proton donor Inferred
Active sitei104 – 1041Phosphocysteine intermediate
Binding sitei110 – 1101Substrate

GO - Molecular functioni

  1. prenylated protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein tyrosine phosphatase type IVA 3 (EC:3.1.3.48)
Alternative name(s):
PRL-R
Protein-tyrosine phosphatase 4a3
Protein-tyrosine phosphatase of regenerating liver 3
Short name:
PRL-3
Gene namesi
Name:PTP4A3
Synonyms:PRL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9636. PTP4A3.

Subcellular locationi

Cell membrane. Early endosome 1 Publication

GO - Cellular componenti

  1. early endosome Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491C → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi71 – 711D → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi72 – 721D → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi104 – 1041C → A or S: 95% loss of enzymatic activity. 2 Publications
Mutagenesisi104 – 1041C → S: Reduces migration-promoting activity. 2 Publications
Mutagenesisi111 – 1111A → S: Enhances catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA33979.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 3
PRO_0000094788Add
BLAST
Propeptidei171 – 1733Removed in mature form By similarity
PRO_0000396735

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 1041 Publication
Modified residuei170 – 1701Cysteine methyl ester By similarity
Lipidationi170 – 1701S-farnesyl cysteine By similarity

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting By similarity.

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiO75365.
PaxDbiO75365.
PRIDEiO75365.

PTM databases

PhosphoSiteiO75365.

Expressioni

Tissue specificityi

Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis.1 Publication

Gene expression databases

ArrayExpressiO75365.
BgeeiO75365.
CleanExiHS_PTP4A3.
GenevestigatoriO75365.

Organism-specific databases

HPAiHPA003281.

Interactioni

Subunit structurei

Interacts with tubulin.1 Publication

Protein-protein interaction databases

BioGridi116327. 37 interactions.
IntActiO75365. 4 interactions.
STRINGi9606.ENSP00000332274.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145
Beta strandi17 – 226
Beta strandi23 – 264
Turni27 – 293
Helixi30 – 4011
Beta strandi45 – 495
Helixi55 – 617
Beta strandi65 – 684
Beta strandi69 – 713
Helixi79 – 9416
Beta strandi99 – 1035
Beta strandi107 – 1104
Helixi111 – 1199
Helixi120 – 1223
Helixi125 – 13511
Beta strandi137 – 1393
Helixi144 – 1529
Turni156 – 1583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R6HNMR-A1-169[»]
1V3ANMR-A1-173[»]
2MBCNMR-A1-162[»]
DisProtiDP00254.
ProteinModelPortaliO75365.
SMRiO75365. Positions 1-169.

Miscellaneous databases

EvolutionaryTraceiO75365.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265664.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiO75365.
KOiK18041.
OMAiKAKFCDD.
OrthoDBiEOG7C8GJD.
PhylomeDBiO75365.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O75365-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MARMNRPAPV EVSYKHMRFL ITHNPTNATL STFIEDLKKY GATTVVRVCE    50
VTYDKTPLEK DGITVVDWPF DDGAPPPGKV VEDWLSLVKA KFCEAPGSCV 100
AVHCVAGLGR APVLVALALI ESGMKYEDAI QFIRQKRRGA INSKQLTYLE 150
KYRPKQRLRF KDPHTHKTRC CVM 173
Length:173
Mass (Da):19,535
Last modified:July 5, 2005 - v2
Checksum:i15DF01999A9A3573
GO
Isoform 2 (identifier: O75365-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-135: Missing.

Note: Unstructured and inactive.

Show »
Length:148
Mass (Da):16,777
Checksum:iE9B7DB82575DF7CD
GO
Isoform 3 (identifier: O75365-3) [UniParc]FASTAAdd to Basket

Also known as: short

The sequence of this isoform differs from the canonical sequence as follows:
     39-124: Missing.

Show »
Length:87
Mass (Da):10,494
Checksum:iDE4A4D64102DC8CF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 12486Missing in isoform 3.
VSP_014406Add
BLAST
Alternative sequencei111 – 13525Missing in isoform 2.
VSP_014407Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401A → R in AAC29314. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041434 mRNA. Translation: AAC29314.1.
AJ276554 mRNA. Translation: CAC81757.1.
BT007303 mRNA. Translation: AAP35967.1.
BC003105 mRNA. Translation: AAH03105.1.
U87168 mRNA. Translation: AAB47560.1.
CCDSiCCDS6382.1. [O75365-2]
CCDS6383.1. [O75365-1]
RefSeqiNP_009010.2. NM_007079.3. [O75365-2]
NP_116000.1. NM_032611.2. [O75365-1]
XP_005250819.1. XM_005250762.2. [O75365-1]
XP_005250820.1. XM_005250763.1. [O75365-1]
XP_005250821.1. XM_005250764.1. [O75365-1]
XP_005250824.1. XM_005250767.2. [O75365-2]
XP_006716562.1. XM_006716499.1. [O75365-1]
XP_006725163.1. XM_006725100.1. [O75365-1]
XP_006725164.1. XM_006725101.1. [O75365-1]
XP_006725165.1. XM_006725102.1. [O75365-1]
XP_006725166.1. XM_006725103.1. [O75365-1]
UniGeneiHs.43666.
Hs.744870.

Genome annotation databases

EnsembliENST00000329397; ENSP00000332274; ENSG00000184489. [O75365-1]
ENST00000349124; ENSP00000331730; ENSG00000184489. [O75365-2]
ENST00000520105; ENSP00000428758; ENSG00000184489. [O75365-2]
ENST00000521578; ENSP00000428976; ENSG00000184489. [O75365-1]
GeneIDi11156.
KEGGihsa:11156.
UCSCiuc003ywg.1. human. [O75365-1]
uc003ywh.1. human. [O75365-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041434 mRNA. Translation: AAC29314.1 .
AJ276554 mRNA. Translation: CAC81757.1 .
BT007303 mRNA. Translation: AAP35967.1 .
BC003105 mRNA. Translation: AAH03105.1 .
U87168 mRNA. Translation: AAB47560.1 .
CCDSi CCDS6382.1. [O75365-2 ]
CCDS6383.1. [O75365-1 ]
RefSeqi NP_009010.2. NM_007079.3. [O75365-2 ]
NP_116000.1. NM_032611.2. [O75365-1 ]
XP_005250819.1. XM_005250762.2. [O75365-1 ]
XP_005250820.1. XM_005250763.1. [O75365-1 ]
XP_005250821.1. XM_005250764.1. [O75365-1 ]
XP_005250824.1. XM_005250767.2. [O75365-2 ]
XP_006716562.1. XM_006716499.1. [O75365-1 ]
XP_006725163.1. XM_006725100.1. [O75365-1 ]
XP_006725164.1. XM_006725101.1. [O75365-1 ]
XP_006725165.1. XM_006725102.1. [O75365-1 ]
XP_006725166.1. XM_006725103.1. [O75365-1 ]
UniGenei Hs.43666.
Hs.744870.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R6H NMR - A 1-169 [» ]
1V3A NMR - A 1-173 [» ]
2MBC NMR - A 1-162 [» ]
DisProti DP00254.
ProteinModelPortali O75365.
SMRi O75365. Positions 1-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116327. 37 interactions.
IntActi O75365. 4 interactions.
STRINGi 9606.ENSP00000332274.

Chemistry

BindingDBi O75365.
ChEMBLi CHEMBL4162.

PTM databases

PhosphoSitei O75365.

Proteomic databases

MaxQBi O75365.
PaxDbi O75365.
PRIDEi O75365.

Protocols and materials databases

DNASUi 11156.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329397 ; ENSP00000332274 ; ENSG00000184489 . [O75365-1 ]
ENST00000349124 ; ENSP00000331730 ; ENSG00000184489 . [O75365-2 ]
ENST00000520105 ; ENSP00000428758 ; ENSG00000184489 . [O75365-2 ]
ENST00000521578 ; ENSP00000428976 ; ENSG00000184489 . [O75365-1 ]
GeneIDi 11156.
KEGGi hsa:11156.
UCSCi uc003ywg.1. human. [O75365-1 ]
uc003ywh.1. human. [O75365-2 ]

Organism-specific databases

CTDi 11156.
GeneCardsi GC08P142432.
HGNCi HGNC:9636. PTP4A3.
HPAi HPA003281.
MIMi 606449. gene.
neXtProti NX_O75365.
PharmGKBi PA33979.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265664.
HOGENOMi HOG000231265.
HOVERGENi HBG071295.
InParanoidi O75365.
KOi K18041.
OMAi KAKFCDD.
OrthoDBi EOG7C8GJD.
PhylomeDBi O75365.
TreeFami TF313384.

Miscellaneous databases

EvolutionaryTracei O75365.
GeneWikii PTP4A3.
GenomeRNAii 11156.
NextBioi 42423.
PROi O75365.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75365.
Bgeei O75365.
CleanExi HS_PTP4A3.
Genevestigatori O75365.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Zeng Q., Tan Y.H., Hong W.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Full-length of some muscular transcripts, Telethon (Italy) project B41."
    Ievolella C., Stanchi F., Pacchioni B., Silvia T., Frigimelica E., Scannapieco P., Corso V., Biasio B., Lanfranchi G.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Skeletal muscle.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "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] (ISOFORM 2).
    Tissue: Eye.
  5. "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38."
    Dayton M.A., Knobloch T.J.
    Recept. Signal Transduct. 7:241-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-148 (ISOFORM 1).
    Tissue: Lung fibroblast.
  6. Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF CYS-104, ENZYME REGULATION, FUNCTION.
  7. Cited for: OVEREXPRESSION IN COLON CANCER.
  8. "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis."
    Wang J., Kirby C.E., Herbst R.
    J. Biol. Chem. 277:46659-46668(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TUBULIN.
  9. "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity."
    Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.
    Mol. Cancer Ther. 1:1255-1264(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis."
    Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J., Manser E., Hong W.
    Cancer Res. 63:2716-2722(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-104.
  11. "Structure of human PRL-3, the phosphatase associated with cancer metastasis."
    Kim K.-A., Song J.-S., Jee J., Sheen M.R., Lee C., Lee T.G., Ro S., Cho J.M., Lee W., Yamazaki T., Jeon Y.H., Cheong C.
    FEBS Lett. 565:181-187(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-173 (ISOFORM 1).
  12. "Structural insights into molecular function of the metastasis-associated phosphatase PRL-3."
    Kozlov G., Cheng J., Ziomek E., Banville D., Gehring K., Ekiel I.
    J. Biol. Chem. 279:11882-11889(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-169 (ISOFORM 1), DISULFIDE BOND, ENZYME ACTIVITY (ISOFORMS 1 AND 2), MUTAGENESIS OF CYS-49; ASP-71; ASP-72 AND ALA-111.

Entry informationi

Entry nameiTP4A3_HUMAN
AccessioniPrimary (citable) accession number: O75365
Secondary accession number(s): Q8IVN5, Q99849, Q9BTW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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