Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12974 (TP4A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PTP4A2
Synonyms:PRL2, PTPCAAX2
ORF Names:BM-008
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited by sodium orthovanadate and pentamidine. Ref.2 Ref.14

Subunit structure

In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB. Ref.11 Ref.13

Subcellular location

Cell membrane. Early endosome. Cytoplasm Ref.10 Ref.11 Ref.13.

Tissue specificity

Ubiquitously expressed, with highest levels in skeletal muscle, heart and thymus. Overexpressed in prostate tumor tissue. Ref.3 Ref.10 Ref.12

Post-translational modification

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

Miscellaneous

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

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12974-1)

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.
Isoform 2 (identifier: Q12974-2)

Also known as: PTP4Ar;

The sequence of this isoform differs from the canonical sequence as follows:
     64-82: DWPFDDGAPPPNQIVDDWL → KKKGSVQFQTAALFGEIPT
     83-167: Missing.
Isoform 3 (identifier: Q12974-3)

The sequence of this isoform differs from the canonical sequence as follows:
     33-63: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Protein tyrosine phosphatase type IVA 2
PRO_0000094785
Propeptide165 – 1673Removed in mature form Probable
PRO_0000396731

Regions

Domain79 – 14567Tyrosine-protein phosphatase
Region102 – 1076Phosphate binding By similarity

Sites

Active site691Proton donor By similarity
Active site1011Phosphocysteine intermediate
Binding site1071Substrate By similarity

Amino acid modifications

Modified residue1641Cysteine methyl ester Probable
Lipidation1641S-farnesyl cysteine Ref.2 Ref.11
Disulfide bond46 ↔ 101 By similarity

Natural variations

Alternative sequence33 – 6331Missing in isoform 3.
VSP_044813
Alternative sequence64 – 8219DWPFD…VDDWL → KKKGSVQFQTAALFGEIPT in isoform 2.
VSP_014404
Alternative sequence83 – 16785Missing in isoform 2.
VSP_014405

Experimental info

Mutagenesis164 – 1674Missing: Locates in the nucleus and cytosol. No interaction with RABGGTB. Ref.11
Mutagenesis1651C → S: No effect on interaction with RABGGTB. Ref.11
Sequence conflict131N → D in AAB39331. Ref.3
Sequence conflict531A → D in AAB59575. Ref.9
Sequence conflict1021V → F in BAG59751. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ptp-IV1a) (Ptp-IV1b) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E97B88BF87B87943

FASTA16719,127
        10         20         30         40         50         60 
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI 

        70         80         90        100        110        120 
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG 

       130        140        150        160 
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ 

« Hide

Isoform 2 (PTP4Ar) [UniParc].

Checksum: 9B230FA7EA3F8A57
Show »

FASTA829,241
Isoform 3 [UniParc].

Checksum: 906A2AF8CDF7C2C5
Show »

FASTA13615,669

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI68523.
RefSeqNP_001182029.1. NM_001195100.1.
NP_001182030.1. NM_001195101.1.
NP_536316.1. NM_080391.3.
XP_005271286.1. XM_005271229.1.
XP_005271287.1. XM_005271230.1.
XP_005271289.1. XM_005271232.1.
UniGeneHs.470477.
Hs.713025.

3D structure databases

ProteinModelPortalQ12974.
SMRQ12974. Positions 6-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113747. 10 interactions.
IntActQ12974. 2 interactions.
MINTMINT-2806089.
STRING9606.ENSP00000344909.

Chemistry

BindingDBQ12974.
ChEMBLCHEMBL1075105.

PTM databases

PhosphoSiteQ12974.

Polymorphism databases

DMDM68566159.

Proteomic databases

PaxDbQ12974.
PeptideAtlasQ12974.
PRIDEQ12974.

Protocols and materials databases

DNASU8073.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344035; ENSP00000344909; ENSG00000184007. [Q12974-1]
ENST00000356536; ENSP00000348932; ENSG00000184007. [Q12974-2]
ENST00000457805; ENSP00000409260; ENSG00000184007. [Q12974-3]
ENST00000602725; ENSP00000473259; ENSG00000184007. [Q12974-1]
GeneID8073.
KEGGhsa:8073.
UCSCuc001btx.2. human. [Q12974-1]

Organism-specific databases

CTD8073.
GeneCardsGC01M032372.
HGNCHGNC:9635. PTP4A2.
HPACAB011204.
HPA003281.
MIM601584. gene.
neXtProtNX_Q12974.
PharmGKBPA33978.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316886.
HOVERGENHBG071295.
InParanoidQ12974.
KOK18041.
OMALANMNRP.
OrthoDBEOG7C8GJD.
PhylomeDBQ12974.
TreeFamTF313384.

Gene expression databases

ArrayExpressQ12974.
BgeeQ12974.
CleanExHS_PTP4A2.
GenevestigatorQ12974.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPTP4A2.
GenomeRNAi8073.
NextBio30662.
PROQ12974.
SOURCESearch...

Entry information

Entry nameTP4A2_HUMAN
AccessionPrimary (citable) accession number: Q12974
Secondary accession number(s): A8K9I8 expand/collapse secondary AC list , B4DM39, D3DPP0, E9PGJ6, O00649, Q15197, Q15259, Q15260, Q15261
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM