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Q15257

- PTPA_HUMAN

UniProt

Q15257 - PTPA_HUMAN

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Protein

Serine/threonine-protein phosphatase 2A activator

Gene
PPP2R4, PTPA
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 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

  1. ATP binding Source: HGNC
  2. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
  3. protein heterodimerization activity Source: HGNC
  4. protein homodimerization activity Source: HGNC
  5. protein phosphatase 2A binding Source: HGNC
  6. protein phosphatase type 2A regulator activity Source: HGNC
  7. protein tyrosine phosphatase activator activity Source: HGNC
  8. receptor binding Source: BHF-UCL

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. mitotic spindle organization in nucleus Source: RefGenome
  3. negative regulation of phosphoprotein phosphatase activity Source: HGNC
  4. negative regulation of protein dephosphorylation Source: HGNC
  5. positive regulation of apoptotic process Source: UniProtKB
  6. positive regulation of phosphoprotein phosphatase activity Source: HGNC
  7. positive regulation of protein dephosphorylation Source: HGNC
  8. protein folding Source: UniProtKB-KW
  9. protein peptidyl-prolyl isomerization Source: GOC
  10. regulation of phosphoprotein phosphatase activity Source: HGNC
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:9308. PPP2R4.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. calcium channel complex Source: BHF-UCL
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProtKB
  5. protein phosphatase type 2A complex Source: HGNC
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.

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

ArrayExpressiQ15257.
BgeeiQ15257.
CleanExiHS_PPP2R4.
GenevestigatoriQ15257.

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.1 Publication

Protein-protein interaction databases

BioGridi111516. 54 interactions.
IntActiQ15257. 10 interactions.
MINTiMINT-3031079.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliQ15257.
SMRiQ15257. Positions 23-357.

Miscellaneous databases

EvolutionaryTraceiQ15257.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPA-type PPIase family.

Phylogenomic databases

eggNOGiCOG5057.
HOVERGENiHBG019168.
KOiK17605.
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. Align

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

MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG    50
FILTLNEGVK GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA 100
GHCAPSEAIE KLVALLNTLD RWIDETPPVD QPSRFGNKAY RTWYAKLDEE 150
AENLVATVVP THLAAAVPEV AVYLKESVGN STRIDYGTGH EAAFAAFLCC 200
LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG SQGVWGLDDF 250
QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT 300
GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL 350
PIHPVTSG 358
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

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. VSP_005122Add
BLAST
Alternative sequencei73 – 14977Missing in isoform 4. VSP_005124Add
BLAST
Alternative sequencei73 – 10735Missing in isoform 1. VSP_005123Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131V → L in CAA51873. 1 Publication
Sequence conflicti113 – 1131V → L in CAA60163. 1 Publication
Sequence conflicti113 – 1131V → L in CAB77601. 1 Publication
Sequence conflicti113 – 1131V → L in CAB77602. 1 Publication
Sequence conflicti297 – 2971Missing in CAA60163. 1 Publication
Sequence conflicti297 – 2971Missing in CAB77601. 1 Publication
Sequence conflicti297 – 2971Missing in CAB77602. 1 Publication
Sequence conflicti297 – 2971Missing in CAB77603. 1 Publication
Sequence conflicti357 – 3571S → V AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [Q15257-1]
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]

Polymorphism databases

DMDMi116242737.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS65156.1. [Q15257-3 ]
CCDS6920.1. [Q15257-2 ]
PIRi A54021.
RefSeqi NP_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 ]
UniGenei Hs.400740.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G62 X-ray 1.60 A 22-358 [» ]
2HV6 X-ray 1.90 A/B 1-358 [» ]
2HV7 X-ray 2.50 A/B/C/D/E/F/G/H 1-358 [» ]
2IXM X-ray 1.50 A 20-357 [» ]
4LAC X-ray 2.82 B 19-358 [» ]
ProteinModelPortali Q15257.
SMRi Q15257. Positions 23-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111516. 54 interactions.
IntActi Q15257. 10 interactions.
MINTi MINT-3031079.

Chemistry

BindingDBi Q15257.
ChEMBLi CHEMBL2505.

PTM databases

PhosphoSitei Q15257.

Polymorphism databases

DMDMi 116242737.

2D gel databases

OGPi Q15257.

Proteomic databases

MaxQBi Q15257.
PaxDbi Q15257.
PRIDEi Q15257.

Protocols and materials databases

DNASUi 5524.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337738 ; ENSP00000337448 ; ENSG00000119383 . [Q15257-1 ]
ENST00000355007 ; ENSP00000347109 ; ENSG00000119383 . [Q15257-4 ]
ENST00000357197 ; ENSP00000349726 ; ENSG00000119383 . [Q15257-3 ]
ENST00000358994 ; ENSP00000351885 ; ENSG00000119383 . [Q15257-2 ]
ENST00000393370 ; ENSP00000377036 ; ENSG00000119383 . [Q15257-2 ]
GeneIDi 5524.
KEGGi hsa:5524.
UCSCi uc004bxl.2. human. [Q15257-2 ]
uc004bxm.2. human. [Q15257-1 ]
uc004bxo.2. human. [Q15257-4 ]
uc011mbp.2. human. [Q15257-3 ]

Organism-specific databases

CTDi 5524.
GeneCardsi GC09P131873.
HGNCi HGNC:9308. PPP2R4.
HPAi CAB022068.
CAB035999.
HPA005695.
MIMi 600756. gene.
neXtProti NX_Q15257.
PharmGKBi PA33671.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5057.
HOVERGENi HBG019168.
KOi K17605.
OrthoDBi EOG7KQ21W.
PhylomeDBi Q15257.
TreeFami TF105555.

Miscellaneous databases

ChiTaRSi PPP2R4. human.
EvolutionaryTracei Q15257.
GeneWikii PPP2R4.
GenomeRNAii 5524.
NextBioi 21382.
PROi Q15257.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15257.
Bgeei Q15257.
CleanExi HS_PPP2R4.
Genevestigatori Q15257.

Family and domain databases

InterProi IPR004327. Phstyr_phstse_ac.
[Graphical view ]
PANTHERi PTHR10012. PTHR10012. 1 hit.
Pfami PF03095. PTPA. 1 hit.
[Graphical view ]
PIRSFi PIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 127 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

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