Serine/threonine-protein phosphatase 2A regulatory subunit B'

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer in presence of ATP and Mg²⁺ (in vitro).
Subunit structure	Associates with PP2A heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A).
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the PTPA-type PPIase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of phosphoprotein phosphatase activity Inferred from direct assay. Source: HGNC negative regulation of protein amino acid dephosphorylation Inferred from direct assay. Source: HGNC positive regulation of phosphoprotein phosphatase activity Inferred from direct assay. Source: HGNC positive regulation of protein amino acid dephosphorylation Inferred from direct assay. Source: HGNC
Cellular component	calcium channel complex Inferred from direct assay. Source: UniProtKB protein phosphatase type 2A complex Traceable author statement. Source: HGNC soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from direct assay. Source: HGNC protein heterodimerization activity Traceable author statement. Source: HGNC protein homodimerization activity Inferred from direct assay. Source: HGNC protein phosphatase 2A binding Inferred from direct assay. Source: HGNC protein phosphatase type 2A regulator activity Inferred from direct assay. Source: HGNC protein tyrosine phosphatase activator activity Ref.1 Inferred from direct assay. Source: HGNC receptor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q15257-1) 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.

Isoform 1 (identifier: Q15257-2) Also known as: Alpha; The sequence of this isoform differs from the canonical sequence as follows: 73-107: Missing.

Isoform 3 (identifier: Q15257-3) Also known as: Delta; The sequence of this isoform differs from the canonical sequence as follows: 45-108: Missing.

Isoform 4 (identifier: Q15257-4) Also known as: Epsilon; The sequence of this isoform differs from the canonical sequence as follows: 73-149: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 358

357

Serine/threonine-protein phosphatase 2A regulatory subunit B'

PRO_0000071524

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

62

1

N6-acetyllysine Ref.12

Modified residue

337

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

45 – 108

64

Missing in isoform 3.

VSP_005122

Alternative sequence

73 – 149

77

Missing in isoform 4.

VSP_005124

Alternative sequence

73 – 107

35

Missing in isoform 1.

VSP_005123

Natural variant

28

1

K → R: dbSNP rs17481693.

VAR_028101

Natural variant

208

1

R → Q: dbSNP rs4836639.

VAR_028102

Natural variant

357

1

S → L: dbSNP rs2480452. Ref.6

VAR_028103

Experimental info

Sequence conflict

1

V → L in CAA51873. Ref.1

Sequence conflict

1

V → L in CAA60163. Ref.2

Sequence conflict

1

V → L in CAB77601. Ref.3

Sequence conflict

1

V → L in CAB77602. Ref.3

Sequence conflict

1

Missing in CAA60163. Ref.2

Sequence conflict

1

Missing in CAB77601. Ref.3

Sequence conflict

1

Missing in CAB77602. Ref.3

Sequence conflict

1

Missing in CAB77603. Ref.3

Sequence conflict

357

1

S → V AA sequence Ref.1

Secondary structure

1

.

358

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 2 (Beta) [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 2A962521AF5B4CF7 Show »	FASTA	358	40,668
10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA GHCAPSEAIE KLVALLNTLD 130 140 150 160 170 180 RWIDETPPVD QPSRFGNKAY RTWYAKLDEE AENLVATVVP THLAAAVPEV AVYLKESVGN 190 200 210 220 230 240 STRIDYGTGH EAAFAAFLCC LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG 250 260 270 280 290 300 SQGVWGLDDF QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT 310 320 330 340 350 GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL PIHPVTSG « Hide
Isoform 1 (Alpha). Checksum: EA0D7B96FB88CC01 Show »	FASTA	323	36,775
10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEAIEKLVAL LNTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDEEAENLV 130 140 150 160 170 180 ATVVPTHLAA AVPEVAVYLK ESVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQIAI 190 200 210 220 230 240 VFKVFNRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PYLEPRHFVD 250 260 270 280 290 300 EKAVNENHKD YMFLECILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL 310 320 EKFPVIQHFK FGSLLPIHPV TSG « Hide
Isoform 3 (Delta). Checksum: 12C8B0D3D96A490B Show »	FASTA	294	33,467
10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAIEKLVA LLNTLDRWID 70 80 90 100 110 120 ETPPVDQPSR FGNKAYRTWY AKLDEEAENL VATVVPTHLA AAVPEVAVYL KESVGNSTRI 130 140 150 160 170 180 DYGTGHEAAF AAFLCCLCKI GVLRVDDQIA IVFKVFNRYL EVMRKLQKTY RMEPAGSQGV 190 200 210 220 230 240 WGLDDFQFLP FIWGSSQLID HPYLEPRHFV DEKAVNENHK DYMFLECILF ITEMKTGPFA 250 260 270 280 290 EHSNQLWNIS AVPSWSKVNQ GLIRMYKAEC LEKFPVIQHF KFGSLLPIHP VTSG « Hide
Isoform 4 (Epsilon). Checksum: 9C554DF39A3436B1 Show »	FASTA	281	31,859
10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEEAENLVAT VVPTHLAAAV PEVAVYLKES VGNSTRIDYG TGHEAAFAAF 130 140 150 160 170 180 LCCLCKIGVL RVDDQIAIVF KVFNRYLEVM RKLQKTYRME PAGSQGVWGL DDFQFLPFIW 190 200 210 220 230 240 GSSQLIDHPY LEPRHFVDEK AVNENHKDYM FLECILFITE MKTGPFAEHS NQLWNISAVP 250 260 270 280 SWSKVNQGLI RMYKAECLEK FPVIQHFKFG SLLPIHPVTS G « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8195217] [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: 8530035] [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: 10880964] [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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62 AND LYS-337, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73478 mRNA. Translation: CAA51873.1.
X86428

X86439 Genomic DNA. Translation: CAA60163.1.
X86428

X86439 Genomic DNA. Translation: CAB77601.1.
X86428

X86439 Genomic DNA. Translation: CAB77602.1.
X86428

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.

IPI

IPI00217296.
IPI00217297.
IPI00293102.
IPI00893197.

PIR

A54021.

RefSeq

NP_066954.2.
NP_821067.1.
NP_821068.1.
NP_821070.1.

UniGene

Hs.400740

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Protein-protein interaction databases

STRING

Q15257.

PTM databases

PhosphoSite

Q15257.

2-D gel databases

OGP

Q15257.

Proteomic databases

PRIDE

Q15257.

Genome annotation databases

Ensembl

ENST00000337738; ENSP00000337448; ENSG00000119383; Homo sapiens. [Genome view]

GeneID

5524.

KEGG

hsa:5524.

UCSC

uc004bxl.1. human.
uc004bxm.1. human.
uc004bxo.1. human.

Organism-specific databases

CTD

5524.

GeneCards

GC09P130913.

HGNC

HGNC:9308. PPP2R4.

HPA

CAB022068.
HPA005695.

MIM

600756. gene.

PharmGKB

PA33671.

GenAtlas

Phylogenomic databases

HOVERGEN

Q15257.

PhylomeDB

Q15257.

Gene expression databases

ArrayExpress

Q15257.

Bgee

Q15257.

CleanEx

HS_PPP2R4.

Genevestigator

Q15257.

GermOnline

ENSG00000119383. Homo sapiens.

Family and domain databases

InterPro

IPR004327. Phstyr_phstse_ac.
[Graphical view]

PANTHER

PTHR10012. Phstyr_phstse_ac. 1 hit.

Pfam

PF03095. PTPA. 1 hit.
[Graphical view]

PIRSF

PIRSF016325. Phstyr_phstse_ac. 1 hit.

ProtoNet

Other Resources

NextBio

21382.

SOURCE

Entry information

Entry name

PTPA_HUMAN

Accession

Primary (citable) accession number: Q15257
Secondary accession number(s): A2A347

Q9NNZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	October 17, 2006
Last modified:	January 19, 2010
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.