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Protein

Serine/threonine-protein phosphatase 2A activator

Gene

PPP2R4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg2+ (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg2+ (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.By similarity2 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1897ATP
Nucleotide bindingi240 – 2423ATP
Nucleotide bindingi342 – 3432ATP

GO - Molecular functioni

  • ATP binding Source: HGNC
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central
  • protein heterodimerization activity Source: HGNC
  • protein homodimerization activity Source: HGNC
  • protein phosphatase 2A binding Source: HGNC
  • protein phosphatase type 2A regulator activity Source: HGNC
  • protein tyrosine phosphatase activator activity Source: HGNC
  • receptor binding Source: BHF-UCL

GO - Biological processi

  • metabolic process Source: GOC
  • mitotic spindle organization in nucleus Source: GO_Central
  • negative regulation of phosphoprotein phosphatase activity Source: HGNC
  • negative regulation of protein dephosphorylation Source: HGNC
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of phosphoprotein phosphatase activity Source: HGNC
  • positive regulation of protein dephosphorylation Source: HGNC
  • protein peptidyl-prolyl isomerization Source: GOC
  • regulation of phosphoprotein phosphatase activity Source: HGNC
  • regulation of protein phosphatase type 2A activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A activator (EC:5.2.1.8)
Alternative name(s):
PP2A, subunit B', PR53 isoform
Phosphotyrosyl phosphatase activator
Short name:
PTPA
Serine/threonine-protein phosphatase 2A regulatory subunit 4
Serine/threonine-protein phosphatase 2A regulatory subunit B'
Gene namesi
Name:PPP2R4
Synonyms:PTPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9308. PPP2R4.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein phosphatase type 2A complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1851D → A: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi239 – 2391A → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi240 – 2401G → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi244 – 2441V → D: Impairs interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi305 – 3051E → A: Abolishes interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi316 – 3161V → D: Impairs interaction with the PP2A(D) complex.
Mutagenesisi325 – 3251G → D: Abolishes interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi329 – 3291M → D: Abolishes interaction with the PP2A(D) complex. 1 Publication
Mutagenesisi337 – 3371K → G: Impairs interaction with the PP2A(D) complex. 1 Publication

Organism-specific databases

PharmGKBiPA33671.

Polymorphism and mutation databases

BioMutaiPPP2R4.
DMDMi116242737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 358357Serine/threonine-protein phosphatase 2A activatorPRO_0000071524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15257.
PaxDbiQ15257.
PRIDEiQ15257.

2D gel databases

OGPiQ15257.

PTM databases

PhosphoSiteiQ15257.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ15257.
CleanExiHS_PPP2R4.
ExpressionAtlasiQ15257. baseline and differential.
GenevisibleiQ15257. HS.

Organism-specific databases

HPAiCAB022068.
CAB035999.
HPA005695.

Interactioni

Subunit structurei

Associates with PP2A heterodimeric core enzyme PP2A(D), composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A). Interacts with PPP2CB (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTQ4VCS5-23EBI-1774121,EBI-3891843

Protein-protein interaction databases

BioGridi111516. 58 interactions.
IntActiQ15257. 11 interactions.
MINTiMINT-3031079.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 407Combined sources
Helixi43 – 5816Combined sources
Turni59 – 613Combined sources
Helixi107 – 12418Combined sources
Beta strandi134 – 1363Combined sources
Helixi139 – 15618Combined sources
Helixi161 – 1666Combined sources
Helixi167 – 1759Combined sources
Turni181 – 1844Combined sources
Helixi188 – 20316Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 2176Combined sources
Helixi219 – 23315Combined sources
Beta strandi237 – 2404Combined sources
Helixi243 – 2453Combined sources
Beta strandi247 – 2504Combined sources
Helixi253 – 2619Combined sources
Turni262 – 2643Combined sources
Helixi270 – 2745Combined sources
Helixi276 – 2827Combined sources
Helixi283 – 2853Combined sources
Helixi287 – 29812Combined sources
Helixi303 – 3064Combined sources
Helixi308 – 3136Combined sources
Helixi319 – 33315Combined sources
Turni334 – 3363Combined sources
Helixi338 – 3414Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G62X-ray1.60A22-358[»]
2HV6X-ray1.90A/B1-358[»]
2HV7X-ray2.50A/B/C/D/E/F/G/H1-358[»]
2IXMX-ray1.50A20-357[»]
4LACX-ray2.82B19-358[»]
4NY3X-ray1.80A/B22-358[»]
ProteinModelPortaliQ15257.
SMRiQ15257. Positions 23-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15257.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPA-type PPIase family.Curated

Phylogenomic databases

eggNOGiCOG5057.
GeneTreeiENSGT00390000011500.
HOVERGENiHBG019168.
InParanoidiQ15257.
KOiK17605.
OMAiHPNLEPR.
OrthoDBiEOG7KQ21W.
PhylomeDBiQ15257.
TreeFamiTF105555.

Family and domain databases

InterProiIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.

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 2 (identifier: Q15257-1) [UniParc]FASTAAdd to basket

Also known as: Beta

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
MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG
60 70 80 90 100
FILTLNEGVK GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA
110 120 130 140 150
GHCAPSEAIE KLVALLNTLD RWIDETPPVD QPSRFGNKAY RTWYAKLDEE
160 170 180 190 200
AENLVATVVP THLAAAVPEV AVYLKESVGN STRIDYGTGH EAAFAAFLCC
210 220 230 240 250
LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG SQGVWGLDDF
260 270 280 290 300
QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT
310 320 330 340 350
GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL

PIHPVTSG
Length:358
Mass (Da):40,668
Last modified:October 17, 2006 - v3
Checksum:i2A962521AF5B4CF7
GO
Isoform 1 (identifier: Q15257-2) [UniParc]FASTAAdd to basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     73-107: Missing.

Show »
Length:323
Mass (Da):36,775
Checksum:iEA0D7B96FB88CC01
GO
Isoform 3 (identifier: Q15257-3) [UniParc]FASTAAdd to basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     45-108: Missing.

Show »
Length:294
Mass (Da):33,467
Checksum:i12C8B0D3D96A490B
GO
Isoform 4 (identifier: Q15257-4) [UniParc]FASTAAdd to basket

Also known as: Epsilon

The sequence of this isoform differs from the canonical sequence as follows:
     73-149: Missing.

Show »
Length:281
Mass (Da):31,859
Checksum:i9C554DF39A3436B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131V → L in CAA51873 (PubMed:8195217).Curated
Sequence conflicti113 – 1131V → L in CAA60163 (PubMed:8530035).Curated
Sequence conflicti113 – 1131V → L in CAB77601 (PubMed:10880964).Curated
Sequence conflicti113 – 1131V → L in CAB77602 (PubMed:10880964).Curated
Sequence conflicti297 – 2971Missing in CAA60163 (PubMed:8530035).Curated
Sequence conflicti297 – 2971Missing in CAB77601 (PubMed:10880964).Curated
Sequence conflicti297 – 2971Missing in CAB77602 (PubMed:10880964).Curated
Sequence conflicti297 – 2971Missing in CAB77603 (PubMed:10880964).Curated
Sequence conflicti357 – 3571S → V AA sequence (PubMed:8195217).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281K → R.
Corresponds to variant rs17481693 [ dbSNP | Ensembl ].
VAR_028101
Natural varianti208 – 2081R → Q.
Corresponds to variant rs4836639 [ dbSNP | Ensembl ].
VAR_028102
Natural varianti357 – 3571S → L.1 Publication
Corresponds to variant rs2480452 [ dbSNP | Ensembl ].
VAR_028103

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei45 – 10864Missing in isoform 3. 1 PublicationVSP_005122Add
BLAST
Alternative sequencei73 – 14977Missing in isoform 4. CuratedVSP_005124Add
BLAST
Alternative sequencei73 – 10735Missing in isoform 1. 4 PublicationsVSP_005123Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73478 mRNA. Translation: CAA51873.1.
X86428
, X86429, X86430, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAA60163.1.
X86428
, X86429, X86430, X86431, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77601.1.
X86428
, X86429, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77602.1.
X86428
, X86429, X86430, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77603.1.
AK302043 mRNA. Translation: BAG63436.1.
BT020119 mRNA. Translation: AAV38922.1.
AK222788 mRNA. Translation: BAD96508.1.
AL158151 Genomic DNA. Translation: CAM14695.1.
AL158151 Genomic DNA. Translation: CAP58847.2.
CH471090 Genomic DNA. Translation: EAW87876.1.
CH471090 Genomic DNA. Translation: EAW87882.1.
BC002545 mRNA. Translation: AAH02545.1.
BC011605 mRNA. Translation: AAH11605.1.
CCDSiCCDS65156.1. [Q15257-3]
CCDS6920.1. [Q15257-2]
PIRiA54021.
RefSeqiNP_001180326.1. NM_001193397.1.
NP_001258761.1. NM_001271832.1. [Q15257-3]
NP_066954.2. NM_021131.4. [Q15257-2]
NP_821067.1. NM_178000.2. [Q15257-2]
NP_821068.1. NM_178001.2. [Q15257-1]
NP_821070.1. NM_178003.2. [Q15257-4]
UniGeneiHs.400740.

Genome annotation databases

EnsembliENST00000337738; ENSP00000337448; ENSG00000119383.
ENST00000355007; ENSP00000347109; ENSG00000119383. [Q15257-4]
ENST00000357197; ENSP00000349726; ENSG00000119383. [Q15257-3]
ENST00000358994; ENSP00000351885; ENSG00000119383. [Q15257-2]
ENST00000393370; ENSP00000377036; ENSG00000119383. [Q15257-2]
GeneIDi5524.
KEGGihsa:5524.
UCSCiuc004bxl.2. human. [Q15257-2]
uc004bxm.2. human. [Q15257-1]
uc004bxo.2. human. [Q15257-4]
uc011mbp.2. human. [Q15257-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73478 mRNA. Translation: CAA51873.1.
X86428
, X86429, X86430, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAA60163.1.
X86428
, X86429, X86430, X86431, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77601.1.
X86428
, X86429, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77602.1.
X86428
, X86429, X86430, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77603.1.
AK302043 mRNA. Translation: BAG63436.1.
BT020119 mRNA. Translation: AAV38922.1.
AK222788 mRNA. Translation: BAD96508.1.
AL158151 Genomic DNA. Translation: CAM14695.1.
AL158151 Genomic DNA. Translation: CAP58847.2.
CH471090 Genomic DNA. Translation: EAW87876.1.
CH471090 Genomic DNA. Translation: EAW87882.1.
BC002545 mRNA. Translation: AAH02545.1.
BC011605 mRNA. Translation: AAH11605.1.
CCDSiCCDS65156.1. [Q15257-3]
CCDS6920.1. [Q15257-2]
PIRiA54021.
RefSeqiNP_001180326.1. NM_001193397.1.
NP_001258761.1. NM_001271832.1. [Q15257-3]
NP_066954.2. NM_021131.4. [Q15257-2]
NP_821067.1. NM_178000.2. [Q15257-2]
NP_821068.1. NM_178001.2. [Q15257-1]
NP_821070.1. NM_178003.2. [Q15257-4]
UniGeneiHs.400740.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G62X-ray1.60A22-358[»]
2HV6X-ray1.90A/B1-358[»]
2HV7X-ray2.50A/B/C/D/E/F/G/H1-358[»]
2IXMX-ray1.50A20-357[»]
4LACX-ray2.82B19-358[»]
4NY3X-ray1.80A/B22-358[»]
ProteinModelPortaliQ15257.
SMRiQ15257. Positions 23-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111516. 58 interactions.
IntActiQ15257. 11 interactions.
MINTiMINT-3031079.

Chemistry

BindingDBiQ15257.
ChEMBLiCHEMBL2505.

PTM databases

PhosphoSiteiQ15257.

Polymorphism and mutation databases

BioMutaiPPP2R4.
DMDMi116242737.

2D gel databases

OGPiQ15257.

Proteomic databases

MaxQBiQ15257.
PaxDbiQ15257.
PRIDEiQ15257.

Protocols and materials databases

DNASUi5524.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337738; ENSP00000337448; ENSG00000119383.
ENST00000355007; ENSP00000347109; ENSG00000119383. [Q15257-4]
ENST00000357197; ENSP00000349726; ENSG00000119383. [Q15257-3]
ENST00000358994; ENSP00000351885; ENSG00000119383. [Q15257-2]
ENST00000393370; ENSP00000377036; ENSG00000119383. [Q15257-2]
GeneIDi5524.
KEGGihsa:5524.
UCSCiuc004bxl.2. human. [Q15257-2]
uc004bxm.2. human. [Q15257-1]
uc004bxo.2. human. [Q15257-4]
uc011mbp.2. human. [Q15257-3]

Organism-specific databases

CTDi5524.
GeneCardsiGC09P131873.
HGNCiHGNC:9308. PPP2R4.
HPAiCAB022068.
CAB035999.
HPA005695.
MIMi600756. gene.
neXtProtiNX_Q15257.
PharmGKBiPA33671.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5057.
GeneTreeiENSGT00390000011500.
HOVERGENiHBG019168.
InParanoidiQ15257.
KOiK17605.
OMAiHPNLEPR.
OrthoDBiEOG7KQ21W.
PhylomeDBiQ15257.
TreeFamiTF105555.

Miscellaneous databases

ChiTaRSiPPP2R4. human.
EvolutionaryTraceiQ15257.
GeneWikiiPPP2R4.
GenomeRNAii5524.
NextBioi21382.
PROiQ15257.
SOURCEiSearch...

Gene expression databases

BgeeiQ15257.
CleanExiHS_PPP2R4.
ExpressionAtlasiQ15257. baseline and differential.
GenevisibleiQ15257. HS.

Family and domain databases

InterProiIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A."
    Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B., Merlevede W., Goris J.
    J. Biol. Chem. 269:15668-15675(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Heart.
  2. "Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A."
    Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J., Merlevede W., Goris J.
    Genomics 28:261-272(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Blood.
  3. "Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene."
    Janssens V., van Hoof C., Martens E., de Baere I., Merlevede W., Goris J.
    Eur. J. Biochem. 267:4406-4413(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3 AND 4).
  4. "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] (ISOFORM 3).
    Tissue: Testis.
  5. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-357.
    Tissue: Liver.
  7. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Placenta.
  10. "Overexpression of the cis/trans isomerase PTPA triggers caspase 3-dependent apoptosis."
    Azam S., Drobetsky E., Ramotar D.
    Apoptosis 12:1243-1255(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions."
    Magnusdottir A., Stenmark P., Flodin S., Nyman T., Hammarstroem M., Ehn M., Bakali H M.A., Berglund H., Nordlund P.
    J. Biol. Chem. 281:22434-22438(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-358.
  15. "Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity."
    Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S., Schiltz M., Barford D., van Tilbeurgh H., Goris J.
    Mol. Cell 23:413-424(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 20-357.
  16. "Structure and mechanism of the phosphotyrosyl phosphatase activator."
    Chao Y., Xing Y., Chen Y., Xu Y., Lin Z., Li Z., Jeffrey P.D., Stock J.B., Shi Y.
    Mol. Cell 23:535-546(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION IN MODULATION OF PP2A SUBSTRATE SPECIFICITY, ATP-BINDING, MUTAGENESIS OF ASP-185; ALA-239; GLY-240; VAL-244; GLU-305; GLY-325; MET-329 AND LYS-337, INTERACTION WITH THE PP2A(D) COMPLEX.

Entry informationi

Entry nameiPTPA_HUMAN
AccessioniPrimary (citable) accession number: Q15257
Secondary accession number(s): A2A347
, A9IZU4, B4DXM4, Q15258, Q53GZ3, Q5TZQ2, Q9BUK1, Q9NNZ7, Q9NNZ8, Q9NNZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 137 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.