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Q12974

- TP4A2_HUMAN

UniProt

Q12974 - TP4A2_HUMAN

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Protein
Protein tyrosine phosphatase type IVA 2
Gene
PTP4A2, PRL2, PTPCAAX2, BM-008
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. 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 donor By similarity
Active sitei101 – 1011Phosphocysteine intermediate
Binding sitei107 – 1071Substrate By similarity

GO - Molecular functioni

  1. phosphatase activity Source: InterPro
  2. 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:9635. PTP4A2.

Subcellular locationi

Cell membrane. Early endosome. Cytoplasm 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. early endosome Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProt
  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 2
PRO_0000094785Add
BLAST
Propeptidei165 – 1673Removed in mature form Inferred
PRO_0000396731

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 101 By similarity
Modified residuei164 – 1641Cysteine methyl ester Inferred
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

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

ArrayExpressiQ12974.
BgeeiQ12974.
CleanExiHS_PTP4A2.
GenevestigatoriQ12974.

Organism-specific databases

HPAiCAB011204.
HPA003281.

Interactioni

Subunit structurei

In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB.2 Publications

Protein-protein interaction databases

BioGridi113747. 10 interactions.
IntActiQ12974. 2 interactions.
MINTiMINT-2806089.
STRINGi9606.ENSP00000344909.

Structurei

3D structure databases

ProteinModelPortaliQ12974.
SMRiQ12974. Positions 6-157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 14567Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 1076Phosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG316886.
HOVERGENiHBG071295.
InParanoidiQ12974.
KOiK18041.
OMAiNGHNCCV.
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. Align

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

MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY    50
DKAPVEKEGI HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH 100
CVAGLGRAPV LVALALIECG MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR 150
PKMRLRFRDT NGHCCVQ 167
Length:167
Mass (Da):19,127
Last modified:November 1, 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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 6331Missing in isoform 3.
VSP_044813Add
BLAST
Alternative sequencei64 – 8219DWPFD…VDDWL → KKKGSVQFQTAALFGEIPT in isoform 2.
VSP_014404Add
BLAST
Alternative sequencei83 – 16785Missing in isoform 2.
VSP_014405Add
BLAST
Alternative sequencei108 – 13225Missing in isoform 4.
VSP_055056Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131N → D in AAB39331. 1 Publication
Sequence conflicti53 – 531A → D in AAB59575. 1 Publication
Sequence conflicti102 – 1021V → F in BAG59751. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
PIRiI68523.
RefSeqiNP_001182029.1. NM_001195100.1.
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.
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]
ENST00000356536; ENSP00000348932; ENSG00000184007. [Q12974-2]
ENST00000457805; ENSP00000409260; ENSG00000184007. [Q12974-3]
ENST00000602683; ENSP00000473490; ENSG00000184007.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS348.1. [Q12974-1 ]
CCDS53292.1. [Q12974-3 ]
PIRi I68523.
RefSeqi NP_001182029.1. NM_001195100.1.
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.
XP_005271289.1. XM_005271232.1. [Q12974-3 ]
XP_006710990.1. XM_006710927.1. [Q12974-1 ]
XP_006710991.1. XM_006710928.1. [Q12974-1 ]
UniGenei Hs.470477.
Hs.713025.

3D structure databases

ProteinModelPortali Q12974.
SMRi Q12974. Positions 6-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113747. 10 interactions.
IntActi Q12974. 2 interactions.
MINTi MINT-2806089.
STRINGi 9606.ENSP00000344909.

Chemistry

BindingDBi Q12974.
ChEMBLi CHEMBL1075105.

PTM databases

PhosphoSitei Q12974.

Polymorphism databases

DMDMi 68566159.

Proteomic databases

MaxQBi Q12974.
PaxDbi Q12974.
PeptideAtlasi Q12974.
PRIDEi Q12974.

Protocols and materials databases

DNASUi 8073.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344035 ; ENSP00000344909 ; ENSG00000184007 . [Q12974-1 ]
ENST00000356536 ; ENSP00000348932 ; ENSG00000184007 . [Q12974-2 ]
ENST00000457805 ; ENSP00000409260 ; ENSG00000184007 . [Q12974-3 ]
ENST00000602683 ; ENSP00000473490 ; ENSG00000184007 .
ENST00000602725 ; ENSP00000473259 ; ENSG00000184007 . [Q12974-1 ]
GeneIDi 8073.
KEGGi hsa:8073.
UCSCi uc001btx.2. human. [Q12974-1 ]

Organism-specific databases

CTDi 8073.
GeneCardsi GC01M032372.
HGNCi HGNC:9635. PTP4A2.
HPAi CAB011204.
HPA003281.
MIMi 601584. gene.
neXtProti NX_Q12974.
PharmGKBi PA33978.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316886.
HOVERGENi HBG071295.
InParanoidi Q12974.
KOi K18041.
OMAi NGHNCCV.
OrthoDBi EOG7C8GJD.
PhylomeDBi Q12974.
TreeFami TF313384.

Miscellaneous databases

GeneWikii PTP4A2.
GenomeRNAii 8073.
NextBioi 30662.
PROi Q12974.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12974.
Bgeei Q12974.
CleanExi HS_PTP4A2.
Genevestigatori Q12974.

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. "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(1995) [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(1996) [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(1996) [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 (NOV-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(2004) [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(2006) [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(2004) [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(1995) [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(2000) [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(2001) [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(2002) [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(2002) [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(2002) [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(2003) [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 5, 2005
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 134 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

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