Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

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

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceEvidence 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 1and isoform 2interact 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. Chromosomecentromere 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. Translation N-terminally extended.

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

Alternative products

This entry describes 5 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.
Isoform 5 (identifier: Q13362-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MLTCNKAGSRMVVDAANSNGPFQPVVLLHI → MPNKNKKEKE...LVLIFGGLQG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
PRO_0000071457

Regions

Motif416 – 4227Nuclear localization signal Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16

Natural variations

Alternative sequence1 – 3131MLTCN…LLHIR → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEQISVRKNSL VAVPSTVSAKIKVPVSQPIV KKDKRQNSSRFSASNNRELQ KLPSLK in isoform 4.
VSP_043645
Alternative sequence1 – 3030MLTCN…VLLHI → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEGTSPEEPSS PKVPPPLLPELLVLIFGGLQ G in isoform 5.
VSP_046768
Alternative sequence443 – 52482YTVYS…SQDGR → VLKKRIT in isoform Gamma-1.
VSP_005112
Alternative sequence443 – 48139Missing in isoform Gamma-2 and isoform 4.
VSP_005113
Natural variant5151A → P.
Corresponds to variant rs3742424 [ dbSNP | Ensembl ].
VAR_051745

Experimental info

Sequence conflict4941R → L in AAC50387. Ref.1
Isoform 5:
Sequence conflict31N → K in BAG63760. Ref.3

Secondary structure

........................................................... 524
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gamma-3 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: B9CBF54550D713F8

FASTA52461,061
        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 

« Hide

Isoform Gamma-1 [UniParc].

Checksum: 73CE22E378289FE8
Show »

FASTA44952,625
Isoform Gamma-2 [UniParc].

Checksum: 64F2D9D78F9D35B6
Show »

FASTA48556,661
Isoform 4 [UniParc].

Checksum: 30B98C5AED1A4466
Show »

FASTA54062,755
Isoform 5 [UniParc].

Checksum: 1C4C9780CF86FF71
Show »

FASTA55564,292

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+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.
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.
CCDSCCDS45163.1. [Q13362-2]
CCDS53911.1. [Q13362-4]
CCDS53912.1. [Q13362-5]
CCDS9964.1. [Q13362-1]
CCDS9965.1. [Q13362-3]
RefSeqNP_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.
UniGeneHs.368264.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ13362.
SMRQ13362. Positions 34-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111519. 26 interactions.
DIPDIP-39401N.
IntActQ13362. 18 interactions.
MINTMINT-2835438.
STRING9606.ENSP00000333905.

PTM databases

PhosphoSiteQ13362.

Polymorphism databases

DMDM116241235.

Proteomic databases

MaxQBQ13362.
PaxDbQ13362.
PRIDEQ13362.

Protocols and materials databases

DNASU5527.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1]
ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneID5527.
KEGGhsa:5527.
UCSCuc001ykk.3. human. [Q13362-4]
uc001ykn.3. human. [Q13362-2]
uc001yko.3. human. [Q13362-1]
uc001ykp.3. human. [Q13362-3]

Organism-specific databases

CTD5527.
GeneCardsGC14P102228.
HGNCHGNC:9311. PPP2R5C.
HPAHPA027553.
MIM601645. gene.
neXtProtNX_Q13362.
PharmGKBPA33674.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264925.
HOGENOMHOG000067326.
HOVERGENHBG000009.
KOK11584.
OMASERWEAD.
PhylomeDBQ13362.
TreeFamTF105556.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ13362.

Gene expression databases

ArrayExpressQ13362.
BgeeQ13362.
CleanExHS_PPP2R5C.
GenevestigatorQ13362.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERPTHR10257. PTHR10257. 1 hit.
PfamPF01603. B56. 1 hit.
[Graphical view]
PIRSFPIRSF028043. PP2A_B56. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPP2R5C. human.
EvolutionaryTraceQ13362.
GeneWikiPPP2R5C.
GenomeRNAi5527.
NextBio21400.
PMAP-CutDBQ13362.
PROQ13362.
SOURCESearch...

Entry information

Entry name2A5G_HUMAN
AccessionPrimary (citable) accession number: Q13362
Secondary accession number(s): B4DYJ8 expand/collapse secondary AC list , B5BUA5, F5GWP3, Q14391, Q15060, Q15174, Q6ZN33
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM