Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Gene

PPP2R5C

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

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.2 Publications

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: UniProtKB

GO - Biological processi

  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  • regulation of protein phosphatase type 2A activity Source: GOC
  • signal transduction Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ13362.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Alternative name(s):
PP2A B subunit isoform B'-gamma
PP2A B subunit isoform B56-gamma
PP2A B subunit isoform PR61-gamma
PP2A B subunit isoform R5-gamma
Renal carcinoma antigen NY-REN-29
Gene namesi
Name:PPP2R5C
Synonyms:KIAA0044
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9311. PPP2R5C.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33674.

Polymorphism and mutation databases

BioMutaiPPP2R5C.
DMDMi116241235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoformPRO_0000071457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13362.
PaxDbiQ13362.
PRIDEiQ13362.

PTM databases

PhosphoSiteiQ13362.

Miscellaneous databases

PMAP-CutDBQ13362.

Expressioni

Tissue specificityi

Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.

Inductioni

Up-regulated upon DNA damage.1 Publication

Gene expression databases

BgeeiQ13362.
CleanExiHS_PPP2R5C.
ExpressionAtlasiQ13362. baseline and differential.
GenevisibleiQ13362. HS.

Organism-specific databases

HPAiHPA027553.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with PPP2CA AND PPP2R1A; the interaction is direct. Interacts with SGOL1; the interaction is direct. Isoform 1 and isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK2O960174EBI-1266176,EBI-1180783
IER3P466952EBI-1266156,EBI-1748945
MDM2Q009875EBI-1266156,EBI-389668
PPP2CAP677757EBI-1266156,EBI-712311
PPP2R1AP301536EBI-1266156,EBI-302388
PPP2R1BP301542EBI-1266156,EBI-357094
TP53P046374EBI-1266156,EBI-366083

Protein-protein interaction databases

BioGridi111519. 27 interactions.
DIPiDIP-39401N.
IntActiQ13362. 18 interactions.
MINTiMINT-2835438.
STRINGi9606.ENSP00000412324.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 489Combined sources
Beta strandi55 – 584Combined sources
Beta strandi59 – 624Combined sources
Helixi63 – 8018Combined sources
Beta strandi83 – 853Combined sources
Helixi91 – 10313Combined sources
Beta strandi115 – 1184Combined sources
Helixi120 – 1223Combined sources
Helixi131 – 14616Combined sources
Helixi152 – 1554Combined sources
Turni156 – 1583Combined sources
Helixi161 – 17010Combined sources
Helixi176 – 19217Combined sources
Helixi194 – 1963Combined sources
Helixi197 – 21216Combined sources
Turni213 – 2153Combined sources
Helixi221 – 23313Combined sources
Helixi241 – 2499Combined sources
Helixi252 – 2554Combined sources
Helixi258 – 2625Combined sources
Helixi264 – 27714Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 29110Combined sources
Helixi301 – 31313Combined sources
Helixi317 – 33519Combined sources
Helixi340 – 3478Combined sources
Helixi348 – 3514Combined sources
Helixi353 – 3619Combined sources
Helixi363 – 3664Combined sources
Turni367 – 3693Combined sources
Turni372 – 3776Combined sources
Helixi384 – 39815Combined sources
Helixi409 – 43022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50B/E30-436[»]
2JAKX-ray2.60A11-380[»]
2NPPX-ray3.30B/E1-442[»]
2NYLX-ray3.80B/E38-425[»]
2NYMX-ray3.60B/E38-425[»]
3FGAX-ray2.70B34-436[»]
ProteinModelPortaliQ13362.
SMRiQ13362. Positions 34-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13362.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi416 – 4227Nuclear localization signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ13362.
KOiK11584.
OMAiRIANPNN.
PhylomeDBiQ13362.
TreeFamiTF105556.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gamma-3 (identifier: Q13362-1) [UniParc]FASTAAdd to basket

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
MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC
60 70 80 90 100
VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA
110 120 130 140 150
VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF
160 170 180 190 200
QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI
210 220 230 240 250
RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV
260 270 280 290 300
LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK
310 320 330 340 350
EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW
360 370 380 390 400
NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM
410 420 430 440 450
NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS
460 470 480 490 500
TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLARRKSELP
510 520
QDPHTKKALE AHCRADELAS QDGR
Length:524
Mass (Da):61,061
Last modified:October 17, 2006 - v3
Checksum:iB9CBF54550D713F8
GO
Isoform Gamma-1 (identifier: Q13362-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-524: YTVYSQASTM...ADELASQDGR → VLKKRIT

Show »
Length:449
Mass (Da):52,625
Checksum:i73CE22E378289FE8
GO
Isoform Gamma-2 (identifier: Q13362-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-481: Missing.

Show »
Length:485
Mass (Da):56,661
Checksum:i64F2D9D78F9D35B6
GO
Isoform 4 (identifier: Q13362-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR → MPNKNKKEKE...RELQKLPSLK
     443-481: Missing.

Note: No experimental confirmation available.
Show »
Length:540
Mass (Da):62,755
Checksum:i30B98C5AED1A4466
GO
Isoform 5 (identifier: Q13362-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MLTCNKAGSRMVVDAANSNGPFQPVVLLHI → MPNKNKKEKE...LVLIFGGLQG

Note: No experimental confirmation available.Curated
Show »
Length:555
Mass (Da):64,292
Checksum:i1C4C9780CF86FF71
GO

Sequence cautioni

The sequence AAC50387.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG63760.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti494 – 4941R → L in AAC50387 (PubMed:8617797).Curated
Isoform 5 (identifier: Q13362-5)
Sequence conflicti3 – 31N → K in BAG63760 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti515 – 5151A → P.
Corresponds to variant rs3742424 [ dbSNP | Ensembl ].
VAR_051745

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131MLTCN…LLHIR → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEQISVRKNSL VAVPSTVSAKIKVPVSQPIV KKDKRQNSSRFSASNNRELQ KLPSLK in isoform 4. 1 PublicationVSP_043645Add
BLAST
Alternative sequencei1 – 3030MLTCN…VLLHI → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEGTSPEEPSS PKVPPPLLPELLVLIFGGLQ G in isoform 5. CuratedVSP_046768Add
BLAST
Alternative sequencei443 – 52482YTVYS…SQDGR → VLKKRIT in isoform Gamma-1. 2 PublicationsVSP_005112Add
BLAST
Alternative sequencei443 – 48139Missing in isoform Gamma-2 and isoform 4. 2 PublicationsVSP_005113Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37352 mRNA. Translation: AAC50387.1. Different initiation.
Z69030 mRNA. Translation: CAA93154.1.
AK131391 mRNA. Translation: BAD18542.1.
AK302470 mRNA. Translation: BAG63760.1. Different initiation.
AB451341 mRNA. Translation: BAG70155.1.
AL118558 Genomic DNA. No translation available.
AL137779 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81756.1.
D26445 mRNA. Translation: BAA05465.1.
L42375 mRNA. Translation: AAC37603.1.
CCDSiCCDS45163.1. [Q13362-2]
CCDS53911.1. [Q13362-4]
CCDS53912.1. [Q13362-5]
CCDS9964.1. [Q13362-1]
CCDS9965.1. [Q13362-3]
RefSeqiNP_001155197.1. NM_001161725.1. [Q13362-5]
NP_001155198.1. NM_001161726.1. [Q13362-4]
NP_002710.2. NM_002719.3. [Q13362-1]
NP_848701.1. NM_178586.2. [Q13362-3]
NP_848702.1. NM_178587.2. [Q13362-2]
XP_005267884.1. XM_005267827.1.
XP_011535222.1. XM_011536920.1.
UniGeneiHs.368264.

Genome annotation databases

EnsembliENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
ENST00000334743; ENSP00000333905; ENSG00000078304.
ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneIDi5527.
KEGGihsa:5527.
UCSCiuc001ykk.3. human. [Q13362-4]
uc001ykn.3. human. [Q13362-2]
uc001yko.3. human. [Q13362-1]
uc001ykp.3. human. [Q13362-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37352 mRNA. Translation: AAC50387.1. Different initiation.
Z69030 mRNA. Translation: CAA93154.1.
AK131391 mRNA. Translation: BAD18542.1.
AK302470 mRNA. Translation: BAG63760.1. Different initiation.
AB451341 mRNA. Translation: BAG70155.1.
AL118558 Genomic DNA. No translation available.
AL137779 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81756.1.
D26445 mRNA. Translation: BAA05465.1.
L42375 mRNA. Translation: AAC37603.1.
CCDSiCCDS45163.1. [Q13362-2]
CCDS53911.1. [Q13362-4]
CCDS53912.1. [Q13362-5]
CCDS9964.1. [Q13362-1]
CCDS9965.1. [Q13362-3]
RefSeqiNP_001155197.1. NM_001161725.1. [Q13362-5]
NP_001155198.1. NM_001161726.1. [Q13362-4]
NP_002710.2. NM_002719.3. [Q13362-1]
NP_848701.1. NM_178586.2. [Q13362-3]
NP_848702.1. NM_178587.2. [Q13362-2]
XP_005267884.1. XM_005267827.1.
XP_011535222.1. XM_011536920.1.
UniGeneiHs.368264.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50B/E30-436[»]
2JAKX-ray2.60A11-380[»]
2NPPX-ray3.30B/E1-442[»]
2NYLX-ray3.80B/E38-425[»]
2NYMX-ray3.60B/E38-425[»]
3FGAX-ray2.70B34-436[»]
ProteinModelPortaliQ13362.
SMRiQ13362. Positions 34-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111519. 27 interactions.
DIPiDIP-39401N.
IntActiQ13362. 18 interactions.
MINTiMINT-2835438.
STRINGi9606.ENSP00000412324.

PTM databases

PhosphoSiteiQ13362.

Polymorphism and mutation databases

BioMutaiPPP2R5C.
DMDMi116241235.

Proteomic databases

MaxQBiQ13362.
PaxDbiQ13362.
PRIDEiQ13362.

Protocols and materials databases

DNASUi5527.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
ENST00000334743; ENSP00000333905; ENSG00000078304.
ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneIDi5527.
KEGGihsa:5527.
UCSCiuc001ykk.3. human. [Q13362-4]
uc001ykn.3. human. [Q13362-2]
uc001yko.3. human. [Q13362-1]
uc001ykp.3. human. [Q13362-3]

Organism-specific databases

CTDi5527.
GeneCardsiGC14P102228.
HGNCiHGNC:9311. PPP2R5C.
HPAiHPA027553.
MIMi601645. gene.
neXtProtiNX_Q13362.
PharmGKBiPA33674.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ13362.
KOiK11584.
OMAiRIANPNN.
PhylomeDBiQ13362.
TreeFamiTF105556.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ13362.

Miscellaneous databases

ChiTaRSiPPP2R5C. human.
EvolutionaryTraceiQ13362.
GeneWikiiPPP2R5C.
GenomeRNAii5527.
NextBioi21400.
PMAP-CutDBQ13362.
PROiQ13362.
SOURCEiSearch...

Gene expression databases

BgeeiQ13362.
CleanExiHS_PPP2R5C.
ExpressionAtlasiQ13362. baseline and differential.
GenevisibleiQ13362. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel protein phosphatase 2A regulatory subunit highly expressed in muscle."
    Tehrani M.A., Mumby M.C., Kamibayashi C.
    J. Biol. Chem. 271:5164-5170(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-3).
    Tissue: Umbilical vein.
  2. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
    Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
    Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
    Tissue: Fetal retina.
  3. "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 4), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Hippocampus and Testis.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-3).
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2).
    Tissue: Bone marrow.
  8. "Identification of a new family of protein phosphatase 2A regulatory subunits."
    McCright B., Virshup D.M.
    J. Biol. Chem. 270:26123-26128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1).
  9. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
    McCright B., Rivers A.M., Audlin S., Virshup D.M.
    J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  11. "PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
    Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
    Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGOL1, SUBCELLULAR LOCATION.
  12. "B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK."
    Letourneux C., Rocher G., Porteu F.
    EMBO J. 25:727-738(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IER3 AND ERK KINASES, PHOSPHORYLATION.
  13. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL1.
  14. "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
    Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
    EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, INDUCTION.
  15. "Serine 15 phosphorylation of p53 directs its interaction with B56gamma and the tumor suppressor activity of B56gamma-specific protein phosphatase 2A."
    Shouse G.P., Cai X., Liu X.
    Mol. Cell. Biol. 28:448-456(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53.
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure of the protein phosphatase 2A holoenzyme."
    Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S., Jeffrey P.D., Shi Y.
    Cell 127:1239-1251(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-442 IN COMPLEX WITH PPP2CA AND PPP2R1A.
  18. "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme."
    Cho U.S., Xu W.
    Nature 445:53-57(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-436 IN COMPLEX WITH PPP2CA AND PPP2R1A.
  19. "Structure and function of the PP2A-shugoshin interaction."
    Xu Z., Cetin B., Anger M., Cho U.S., Helmhart W., Nasmyth K., Xu W.
    Mol. Cell 35:426-441(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-436 IN COMPLEX WITH PPP2CA; PPP2R1A AND SGOL1.
  20. "The structure of the PP2A regulatory subunit B56 gamma: the remaining piece of the PP2A jigsaw puzzle."
    Magnusdottir A., Stenmark P., Flodin S., Nyman T., Kotenyova T., Graeslund S., Ogg D., Nordlund P.
    Proteins 74:212-221(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-380.

Entry informationi

Entry namei2A5G_HUMAN
AccessioniPrimary (citable) accession number: Q13362
Secondary accession number(s): B4DYJ8
, B5BUA5, F5GWP3, Q14391, Q15060, Q15174, Q6ZN33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 156 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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.