Q13362 (2A5G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PPP2R5C
Synonyms:	KIAA0044

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12 Ref.14
Subunit structure	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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Subcellular location	Nucleus. Chromosome › centromere Ref.9 Ref.11.
Tissue specificity	Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.
Induction	Up-regulated upon DNA damage. Ref.14
Post-translational modification	Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C. Ref.9 Ref.12
Sequence similarities	Belongs to the phosphatase 2A regulatory subunit B56 family.
Sequence caution	The sequence AAC50387.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Centromere Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from direct assay Ref.14. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from mutant phenotype Ref.14. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.14. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype PubMed 16717086. Source: MGI signal transduction Non-traceable author statement Ref.9. Source: UniProtKB
Cellular_component	chromosome, centromeric region Inferred from direct assay Ref.11. Source: UniProtKB nucleus Inferred from direct assay Ref.9. Source: UniProtKB protein phosphatase type 2A complex Inferred from direct assay Ref.16Ref.14. Source: UniProtKB
Molecular_function	protein phosphatase type 2A regulator activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHEK2	O96017	4	EBI-1266176,EBI-1180783
PPP2R1A	P30153	3	EBI-1266170,EBI-302388

Alternative products

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

Isoform Gamma-3 (identifier: Q13362-1)

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 Gamma-1 (identifier: Q13362-2)

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

Isoform Gamma-2 (identifier: Q13362-3)

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

Isoform 4 (identifier: Q13362-4)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 524

524

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

PRO_0000071457

Regions

Motif

416 – 422

7

Nuclear localization signal Potential

Amino acid modifications

Modified residue

497

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 31

31

MLTCN…LLHIR → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEQISVRKNSL VAVPSTVSAKIKVPVSQPIV KKDKRQNSSRFSASNNRELQ KLPSLK in isoform 4.

VSP_043645

Alternative sequence

443 – 524

82

YTVYS…SQDGR → VLKKRIT in isoform Gamma-1.

VSP_005112

Alternative sequence

443 – 481

39

Missing in isoform Gamma-2 and isoform 4.

VSP_005113

Natural variant

515

1

A → P.
Corresponds to variant rs3742424 [ dbSNP | Ensembl ].

VAR_051745

Experimental info

Sequence conflict

494

1

R → L in AAC50387. Ref.1

Secondary structure

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524

Helix Strand Turn

Details...

Helix

40 – 48

9

Beta strand

55 – 58

4

Beta strand

59 – 62

4

Helix

63 – 80

18

Beta strand

83 – 85

3

Helix

91 – 103

13

Beta strand

115 – 118

4

Helix

120 – 122

3

Helix

131 – 146

16

Helix

152 – 155

4

Turn

156 – 158

3

Helix

161 – 170

10

Helix

176 – 192

17

Helix

194 – 196

3

Helix

197 – 212

16

Turn

213 – 215

3

Helix

221 – 233

13

Helix

241 – 249

9

Helix

252 – 255

4

Helix

258 – 262

5

Helix

264 – 277

14

Helix

279 – 281

3

Helix

282 – 291

10

Helix

301 – 313

13

Helix

317 – 335

19

Helix

340 – 347

8

Helix

348 – 351

4

Helix

353 – 361

9

Helix

363 – 366

4

Turn

367 – 369

3

Turn

372 – 377

6

Helix

384 – 398

15

Helix

409 – 430

22

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gamma-3 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: B9CBF54550D713F8	FASTA	524	61,061
	10 20 30 40 50 60 MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL 70 80 90 100 110 120 SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP 130 140 150 160 170 180 EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD 190 200 210 220 230 240 FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK 250 260 270 280 290 300 EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK 310 320 330 340 350 360 EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS 370 380 390 400 410 420 DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK 430 440 450 460 470 480 LKMKEREEAW VKIENLAKAN PQYTVYSQAS TMSIPVAMET DGPLFEDVQM LRKTVKDEAH 490 500 510 520 QAQKDPKKDR PLARRKSELP QDPHTKKALE AHCRADELAS QDGR
	Isoform Gamma-1 [UniParc]. Checksum: 73CE22E378289FE8	FASTA	449	52,625
	10 20 30 40 50 60 MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL 70 80 90 100 110 120 SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP 130 140 150 160 170 180 EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD 190 200 210 220 230 240 FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK 250 260 270 280 290 300 EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK 310 320 330 340 350 360 EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS 370 380 390 400 410 420 DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK 430 440 LKMKEREEAW VKIENLAKAN PQVLKKRIT
	Isoform Gamma-2 [UniParc]. Checksum: 64F2D9D78F9D35B6	FASTA	485	56,661
	10 20 30 40 50 60 MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL 70 80 90 100 110 120 SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP 130 140 150 160 170 180 EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD 190 200 210 220 230 240 FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK 250 260 270 280 290 300 EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK 310 320 330 340 350 360 EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS 370 380 390 400 410 420 DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK 430 440 450 460 470 480 LKMKEREEAW VKIENLAKAN PQAQKDPKKD RPLARRKSEL PQDPHTKKAL EAHCRADELA SQDGR
	Isoform 4 [UniParc]. Checksum: 30B98C5AED1A4466	FASTA	540	62,755
	10 20 30 40 50 60 MPNKNKKEKE SPKAGKSGKS SKEGQDTVES EQISVRKNSL VAVPSTVSAK IKVPVSQPIV 70 80 90 100 110 120 KKDKRQNSSR FSASNNRELQ KLPSLKDVPP ADQEKLFIQK LRQCCVLFDF VSDPLSDLKW 130 140 150 160 170 180 KEVKRAALSE MVEYITHNRN VITEPIYPEV VHMFAVNMFR TLPPSSNPTG AEFDPEEDEP 190 200 210 220 230 240 TLEAAWPHLQ LVYEFFLRFL ESPDFQPNIA KKYIDQKFVL QLLELFDSED PRERDFLKTT 250 260 270 280 290 300 LHRIYGKFLG LRAYIRKQIN NIFYRFIYET EHHNGIAELL EILGSIINGF ALPLKEEHKI 310 320 330 340 350 360 FLLKVLLPLH KVKSLSVYHP QLAYCVVQFL EKDSTLTEPV VMALLKYWPK THSPKEVMFL 370 380 390 400 410 420 NELEEILDVI EPSEFVKIME PLFRQLAKCV SSPHFQVAER ALYYWNNEYI MSLISDNAAK 430 440 450 460 470 480 ILPIMFPSLY RNSKTHWNKT IHGLIYNALK LFMEMNQKLF DDCTQQFKAE KLKEKLKMKE 490 500 510 520 530 540 REEAWVKIEN LAKANPQAQK DPKKDRPLAR RKSELPQDPH TKKALEAHCR ADELASQDGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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). Tissue: Hippocampus.
[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]	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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U37352 mRNA. Translation: AAC50387.1. Different initiation.
Z69030 mRNA. Translation: CAA93154.1.
AK131391 mRNA. Translation: BAD18542.1.
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.

IPI

IPI00012834.
IPI00185637.
IPI00220145.
IPI00442098.

RefSeq

NP_001155197.1. NM_001161725.1.
NP_001155198.1. NM_001161726.1.
NP_002710.2. NM_002719.3.
NP_848701.1. NM_178586.2.
NP_848702.1. NM_178587.2.

UniGene

Hs.368264.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IAE	X-ray	3.50	B/E	30-436	[»]
2JAK	X-ray	2.60	A	11-380	[»]
2NPP	X-ray	3.30	B/E	1-442	[»]
2NYL	X-ray	3.80	B/E	38-425	[»]
2NYM	X-ray	3.60	B/E	38-425	[»]
3FGA	X-ray	2.70	B	34-436	[»]

ProteinModelPortal

Q13362.

ModBase

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Protein-protein interaction databases

DIP

DIP-29396N.
DIP-39401N.

IntAct

Q13362. 9 interactions.

MINT

MINT-2835438.

STRING

9606.ENSP00000333905.

PTM databases

PhosphoSite

Q13362.

Polymorphism databases

DMDM

116241235.

Proteomic databases

PaxDb

Q13362.

PRIDE

Q13362.

Protocols and materials databases

DNASU

5527.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000328724; ENSP00000329009; ENSG00000078304.
ENST00000334743; ENSP00000333905; ENSG00000078304.
ENST00000350249; ENSP00000262239; ENSG00000078304.
ENST00000445439; ENSP00000408389; ENSG00000078304.

GeneID

5527.

KEGG

hsa:5527.

UCSC

uc001ykn.3. human.
uc001yko.3. human.
uc001ykp.3. human.

Organism-specific databases

CTD

5527.

GeneCards

GC14P102228.

HGNC

HGNC:9311. PPP2R5C.

HPA

HPA027553.

MIM

601645. gene.

neXtProt

NX_Q13362.

PharmGKB

PA33674.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

NOG264925.

HOGENOM

HOG000067326.

HOVERGEN

HBG000009.

KO

K11584.

OMA

ESHCRAD.

PhylomeDB

Q13362.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13362.

Bgee

Q13362.

CleanEx

HS_PPP2R5C.

Genevestigator

Q13362.

GermOnline

ENSG00000078304. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]

PANTHER

PTHR10257. PTHR10257. 1 hit.

Pfam

PF01603. B56. 1 hit.
[Graphical view]

PIRSF

PIRSF028043. PP2A_B56. 1 hit.

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

ProtoNet

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Other

ChiTaRS

PPP2R5C. human.

EvolutionaryTrace

Q13362.

GenomeRNAi

5527.

NextBio

21400.

PMAP-CutDB

Q13362.

SOURCE

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Entry information

Entry name

2A5G_HUMAN

Accession

Primary (citable) accession number: Q13362
Secondary accession number(s): B5BUA5 , Q14391, Q15060, Q15174, Q6ZN33

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.