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Protein

Protein tyrosine phosphatase type IVA 2

Gene

PTP4A2

Organism
Homo sapiens (Human)
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. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Inhibited by sodium orthovanadate and pentamidine.2 Publications

Sites

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

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 2 (EC:3.1.3.48)
Alternative name(s):
HU-PP-1
OV-1
PTP(CAAXII)
Protein-tyrosine phosphatase 4a2
Protein-tyrosine phosphatase of regenerating liver 2
Short name:
PRL-2
Gene namesi
Name:PTP4A2
Synonyms:PRL2, PTPCAAX2
ORF Names:BM-008
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9635. PTP4A2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. early endosome Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: UniProtKB-SubCell
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 and cytosol. No interaction with RABGGTB. 1 Publication
Mutagenesisi165 – 1651C → S: No effect on interaction with RABGGTB. 1 Publication

Organism-specific databases

PharmGKBiPA33978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Protein tyrosine phosphatase type IVA 2PRO_0000094785Add
BLAST
Propeptidei165 – 1673Removed in mature formCuratedPRO_0000396731

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 101By similarity
Modified residuei164 – 1641Cysteine methyl esterCurated
Lipidationi164 – 1641S-farnesyl cysteine2 Publications

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB. Unfarnesylated forms are redirected to the nucleus and cytosol.

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ12974.
PaxDbiQ12974.
PeptideAtlasiQ12974.
PRIDEiQ12974.

PTM databases

DEPODiQ12974.
PhosphoSiteiQ12974.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in skeletal muscle, heart and thymus. Overexpressed in prostate tumor tissue.3 Publications

Gene expression databases

BgeeiQ12974.
CleanExiHS_PTP4A2.
ExpressionAtlasiQ12974. baseline and differential.
GenevestigatoriQ12974.

Organism-specific databases

HPAiCAB011204.
HPA003281.

Interactioni

Subunit structurei

In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB.1 Publication

Protein-protein interaction databases

BioGridi113747. 11 interactions.
IntActiQ12974. 2 interactions.
MINTiMINT-2806089.
STRINGi9606.ENSP00000344909.

Structurei

3D structure databases

ProteinModelPortaliQ12974.
SMRiQ12974. 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.
InParanoidiQ12974.
KOiK18041.
OMAiAPIEKEG.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ12974.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12974-1) [UniParc]FASTAAdd to basket

Also known as: Ptp-IV1a, Ptp-IV1b

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

        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:October 31, 1996 - v1
Checksum:iE97B88BF87B87943
GO
Isoform 2 (identifier: Q12974-2) [UniParc]FASTAAdd to basket

Also known as: PTP4Ar

The sequence of this isoform differs from the canonical sequence as follows:
     64-82: DWPFDDGAPPPNQIVDDWL → KKKGSVQFQTAALFGEIPT
     83-167: Missing.

Show »
Length:82
Mass (Da):9,241
Checksum:i9B230FA7EA3F8A57
GO
Isoform 3 (identifier: Q12974-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-63: Missing.

Note: No experimental confirmation available.

Show »
Length:136
Mass (Da):15,669
Checksum:i906A2AF8CDF7C2C5
GO
Isoform 4 (identifier: Q12974-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-132: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:142
Mass (Da):16,367
Checksum:i777A719A36214008
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131N → D in AAB39331 (PubMed:8661118).Curated
Sequence conflicti53 – 531A → D in AAB59575 (PubMed:7490091).Curated
Sequence conflicti102 – 1021V → F in BAG59751 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 6331Missing in isoform 3. 1 PublicationVSP_044813Add
BLAST
Alternative sequencei64 – 8219DWPFD…VDDWL → KKKGSVQFQTAALFGEIPT in isoform 2. CuratedVSP_014404Add
BLAST
Alternative sequencei83 – 16785Missing in isoform 2. CuratedVSP_014405Add
BLAST
Alternative sequencei108 – 13225Missing in isoform 4. CuratedVSP_055056Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14603 mRNA. Translation: AAA90979.1.
U48297 mRNA. Translation: AAB40598.1.
L48722 Genomic DNA. Translation: AAB42169.1.
L48723 Genomic DNA. Translation: AAB42170.1.
L48937 Genomic DNA. Translation: AAB39331.1.
AF208850 mRNA. Translation: AAF64264.1.
AK292703 mRNA. Translation: BAF85392.1.
AK297280 mRNA. Translation: BAG59751.1.
AL136115 Genomic DNA. Translation: CAI21726.1.
CH471059 Genomic DNA. Translation: EAX07578.1.
CH471059 Genomic DNA. Translation: EAX07579.1.
CH471059 Genomic DNA. Translation: EAX07582.1.
CH471059 Genomic DNA. Translation: EAX07583.1.
BC070182 mRNA. Translation: AAH70182.1.
L39000 mRNA. Translation: AAB59575.1.
CCDSiCCDS348.1. [Q12974-1]
CCDS53292.1. [Q12974-3]
CCDS59193.1. [Q12974-4]
PIRiI68523.
RefSeqiNP_001182029.1. NM_001195100.1. [Q12974-4]
NP_001182030.1. NM_001195101.1. [Q12974-3]
NP_536316.1. NM_080391.3. [Q12974-1]
XP_005271286.1. XM_005271229.1. [Q12974-1]
XP_005271287.1. XM_005271230.1. [Q12974-1]
XP_005271288.1. XM_005271231.1. [Q12974-4]
XP_005271289.1. XM_005271232.1. [Q12974-3]
XP_006710990.1. XM_006710927.1. [Q12974-1]
XP_006710991.1. XM_006710928.1. [Q12974-1]
UniGeneiHs.470477.
Hs.713025.

Genome annotation databases

EnsembliENST00000344035; ENSP00000344909; ENSG00000184007. [Q12974-1]
ENST00000457805; ENSP00000409260; ENSG00000184007. [Q12974-3]
ENST00000602683; ENSP00000473490; ENSG00000184007. [Q12974-4]
ENST00000602725; ENSP00000473259; ENSG00000184007. [Q12974-1]
GeneIDi8073.
KEGGihsa:8073.
UCSCiuc001btx.2. human. [Q12974-1]

Polymorphism databases

DMDMi68566159.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14603 mRNA. Translation: AAA90979.1.
U48297 mRNA. Translation: AAB40598.1.
L48722 Genomic DNA. Translation: AAB42169.1.
L48723 Genomic DNA. Translation: AAB42170.1.
L48937 Genomic DNA. Translation: AAB39331.1.
AF208850 mRNA. Translation: AAF64264.1.
AK292703 mRNA. Translation: BAF85392.1.
AK297280 mRNA. Translation: BAG59751.1.
AL136115 Genomic DNA. Translation: CAI21726.1.
CH471059 Genomic DNA. Translation: EAX07578.1.
CH471059 Genomic DNA. Translation: EAX07579.1.
CH471059 Genomic DNA. Translation: EAX07582.1.
CH471059 Genomic DNA. Translation: EAX07583.1.
BC070182 mRNA. Translation: AAH70182.1.
L39000 mRNA. Translation: AAB59575.1.
CCDSiCCDS348.1. [Q12974-1]
CCDS53292.1. [Q12974-3]
CCDS59193.1. [Q12974-4]
PIRiI68523.
RefSeqiNP_001182029.1. NM_001195100.1. [Q12974-4]
NP_001182030.1. NM_001195101.1. [Q12974-3]
NP_536316.1. NM_080391.3. [Q12974-1]
XP_005271286.1. XM_005271229.1. [Q12974-1]
XP_005271287.1. XM_005271230.1. [Q12974-1]
XP_005271288.1. XM_005271231.1. [Q12974-4]
XP_005271289.1. XM_005271232.1. [Q12974-3]
XP_006710990.1. XM_006710927.1. [Q12974-1]
XP_006710991.1. XM_006710928.1. [Q12974-1]
UniGeneiHs.470477.
Hs.713025.

3D structure databases

ProteinModelPortaliQ12974.
SMRiQ12974. Positions 6-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113747. 11 interactions.
IntActiQ12974. 2 interactions.
MINTiMINT-2806089.
STRINGi9606.ENSP00000344909.

Chemistry

BindingDBiQ12974.
ChEMBLiCHEMBL1075105.

PTM databases

DEPODiQ12974.
PhosphoSiteiQ12974.

Polymorphism databases

DMDMi68566159.

Proteomic databases

MaxQBiQ12974.
PaxDbiQ12974.
PeptideAtlasiQ12974.
PRIDEiQ12974.

Protocols and materials databases

DNASUi8073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344035; ENSP00000344909; ENSG00000184007. [Q12974-1]
ENST00000457805; ENSP00000409260; ENSG00000184007. [Q12974-3]
ENST00000602683; ENSP00000473490; ENSG00000184007. [Q12974-4]
ENST00000602725; ENSP00000473259; ENSG00000184007. [Q12974-1]
GeneIDi8073.
KEGGihsa:8073.
UCSCiuc001btx.2. human. [Q12974-1]

Organism-specific databases

CTDi8073.
GeneCardsiGC01M032372.
HGNCiHGNC:9635. PTP4A2.
HPAiCAB011204.
HPA003281.
MIMi601584. gene.
neXtProtiNX_Q12974.
PharmGKBiPA33978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG316886.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ12974.
KOiK18041.
OMAiAPIEKEG.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ12974.
TreeFamiTF313384.

Miscellaneous databases

GeneWikiiPTP4A2.
GenomeRNAii8073.
NextBioi30662.
PROiQ12974.
SOURCEiSearch...

Gene expression databases

BgeeiQ12974.
CleanExiHS_PTP4A2.
ExpressionAtlasiQ12974. baseline and differential.
GenevestigatoriQ12974.

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. "A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase."
    Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.
    Hum. Genet. 96:532-538(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Ovary.
  2. "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases."
    Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D., Randall S.K., Crowell P.L., Crowell D.N.
    Cancer Lett. 110:49-55(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-164, ENZYME REGULATION.
    Tissue: Mammary carcinoma.
  3. "Characterization and genomic mapping of genes and pseudogenes of a new human protein tyrosine phosphatase."
    Zhao Z., Lee C.-C., Monckton D.G., Yazdani A., Coolbaugh M.I., Li X., Bailey J., Shen Y., Caskey C.T.
    Genomics 35:172-181(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Ovary and Placenta.
  4. "A novel gene expressed in human bone marrow."
    Zhao M., Song H., Li N., Peng Y., Han Z., Chen Z.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain and Thymus.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  9. "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21."
    Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.
    Genomics 28:530-542(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-167 (ISOFORM 1).
    Tissue: Mammary gland.
  10. "Subcellular localization of intracellular protein tyrosine phosphatases in T cells."
    Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A., Renedo M., Oh P., Williams S., Schnitzer J., Mustelin T.
    Eur. J. Immunol. 30:2412-2421(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II."
    Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.
    J. Biol. Chem. 276:32875-32882(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABGGTB, ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION, MUTAGENESIS OF 164-CYS--GLN-167 AND CYS-165.
  12. "Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene."
    Wang Q., Holmes D.I.R., Powell S.M., Lu Q.L., Waxman J.
    Cancer Lett. 175:63-69(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, LACK OF INTERACTION WITH TUBULIN.
  14. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  15. "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases."
    Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K., Crowell P.L.
    Cancer Lett. 202:201-211(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTP4A2_HUMAN
AccessioniPrimary (citable) accession number: Q12974
Secondary accession number(s): A8K9I8
, B4DM39, D3DPP0, E9PGJ6, O00649, Q15197, Q15259, Q15260, Q15261, R4GN50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 4, 2005
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 138 of the entry and version 1 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

Miscellaneous

A processed pseudogene with 96% sequence identity was found in the BRCA1 (113705) region of 17q21.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.