Q00005 (2ABB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform

Alternative name(s):
PP2A subunit B isoform B55-beta
PP2A subunit B isoform PR55-beta
PP2A subunit B isoform R2-beta
PP2A subunit B isoform beta

Gene names

Name:

PPP2R2B

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	443 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. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity By similarity. Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance By similarity.
Subunit structure	PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and 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.
Subcellular location	Isoform 1: Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Membrane By similarity. Isoform 2: Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion outer membrane By similarity. Note: Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity By similarity.
Tissue specificity	Brain.
Domain	The N-terminal 26 residues of isoform 2 constitute a cryptic mitochondrial matrix import signal with critical basic and hydrophobic residues, that is necessary and sufficient for targeting the PP2A holoenzyme to the outer mitochondrial membrane (OMM) and does not affect holoenzyme formation or catalytic activity By similarity. The last WD repeat of isoform 2 constitutes a mitochondrial stop-transfer domain that confers resistance to the unfolding step process required for import and therefore prevents PPP2R2B matrix translocation and signal sequence cleavage By similarity.
Involvement in disease	Spinocerebellar ataxia 12 (SCA12) [MIM:604326]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar ataxia (ADCA). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7
Sequence similarities	Belongs to the phosphatase 2A regulatory subunit B family. Contains 7 WD repeats.
Sequence caution	The sequence AAH31790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG51642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG51642.1 differs from that shown. Reason: Erroneous termination at position 116. Translated as Lys.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Cytoskeleton Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Neurodegeneration Spinocerebellar ataxia
Domain	Repeat WD repeat
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from electronic annotation. Source: Compara cellular response to stress Inferred from electronic annotation. Source: Compara mitochondrial fragmentation involved in apoptotic process Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara protein targeting to mitochondrion Inferred from electronic annotation. Source: Compara regulation of protein phosphatase type 2A activity Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: InterPro spermatid development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase type 2A complex Inferred from electronic annotation. Source: Compara
Molecular_function	protein phosphatase type 2A regulator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDPK1	O15530	8	EBI-1052159,EBI-717097
PPP2R1A	P30153	5	EBI-1052159,EBI-302388
RPS6KB1	P23443	2	EBI-1052159,EBI-1775921

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q00005-1)

Also known as: Bbeta; Bbeta1;

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.

Note: Conserved additional ATG codons are found 5' of the putative initiator codon in transcripts supporting isoform 1. They may initiate the translation of upstream short open reading frames altering the expression of that isoform as described in PubMed=1849734.

Isoform 2 (identifier: Q00005-2)

Also known as: Bbeta2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MKCFSRYLPYIFRPPNTILSSSCH

Note: Contains a cryptic mitochondrial transit peptide at positions 1-26 (By similarity).

Isoform 3 (identifier: Q00005-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MIPGIGTLTQDTLWCFSQVKGTIEIGT

Isoform 4 (identifier: Q00005-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

Isoform 5 (identifier: Q00005-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

Isoform 6 (identifier: Q00005-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEEDIDTRKINNSFLRDHSYATE → MNYPDENTYGNK

Isoform 7 (identifier: Q00005-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHQPPPASCS...VPTQVSLLSM

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform		PRO_0000071421
Regions
	Repeat	22 – 61	40	WD 1
	Repeat	87 – 128	42	WD 2
	Repeat	171 – 209	39	WD 3
	Repeat	220 – 260	41	WD 4
	Repeat	279 – 317	39	WD 5
	Repeat	334 – 375	42	WD 6
	Repeat	410 – 442	33	WD 7
Natural variations
	Alternative sequence	1 – 23	23	MEEDI…SYATE → MNYPDENTYGNK in isoform 6.		VSP_044923
	Alternative sequence	1 – 21	21	MEEDI…DHSYA → MKCFSRYLPYIFRPPNTILS SSCH in isoform 2.		VSP_037976
	Alternative sequence	1 – 21	21	MEEDI…DHSYA → MIPGIGTLTQDTLWCFSQVK GTIEIGT in isoform 3.		VSP_037977
	Alternative sequence	1	1	M → MVLQPSERHYRDWNHRRLGP WCSPTGSPAPLSCETGCGEG SWILVCRLLVPTQVSLLSM in isoform 4.		VSP_037978
	Alternative sequence	1	1	M → MLLSLPALHLQTSEHHPFFQ LPHRRLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 5.		VSP_037979
	Alternative sequence	1	1	M → MHQPPPASCSSSSSSSSSSC ECARVGVRVSALAPAAAPCP APRQLPYPRLPEPPSRGTST LIPARLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 7.		VSP_045748
	Natural variant	36	1	G → V. Corresponds to variant rs11547494 [ dbSNP | Ensembl ].		VAR_051738
Experimental info
	Sequence conflict	22	1	T → A in BAH11838. Ref.2
	Sequence conflict	62	1	H → N in BI669304. Ref.5
	Sequence conflict	109	1	S → F in BAH12040. Ref.2
	Sequence conflict	163	1	T → S in BI490027. Ref.6
	Sequence conflict	164	1	P → S in BAF82406. Ref.2
	Sequence conflict	292	1	S → R in BAH12040. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Bbeta) (Bbeta1) [UniParc]. Last modified April 1, 1993. Version 1. Checksum: C383C834B2852B8F	FASTA	443	51,710
	10 20 30 40 50 60 MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ 70 80 90 100 110 120 VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV 130 140 150 160 170 180 SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS 190 200 210 220 230 240 VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY 250 260 270 280 290 300 SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD 310 320 330 340 350 360 YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN 370 380 390 400 410 420 FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW 430 440 HPSENIIAVA ATNNLYIFQD KVN
	Isoform 2 (Bbeta2) [UniParc]. Checksum: D5BDD8D10F79CF0B	FASTA	446	52,017
	10 20 30 40 50 60 MKCFSRYLPY IFRPPNTILS SSCHTEADII STVEFNHTGE LLATGDKGGR VVIFQREQES 70 80 90 100 110 120 KNQVHRRGEY NVYSTFQSHE PEFDYLKSLE IEEKINKIRW LPQQNAAYFL LSTNDKTVKL 130 140 150 160 170 180 WKVSERDKRP EGYNLKDEEG RLRDPATITT LRVPVLRPMD LMVEATPRRV FANAHTYHIN 190 200 210 220 230 240 SISVNSDYET YMSADDLRIN LWNFEITNQS FNIVDIKPAN MEELTEVITA AEFHPHHCNT 250 260 270 280 290 300 FVYSSSKGTI RLCDMRASAL CDRHTKFFEE PEDPSNRSFF SEIISSISDV KFSHSGRYIM 310 320 330 340 350 360 TRDYLTVKVW DLNMENRPIE TYQVHDYLRS KLCSLYENDC IFDKFECVWN GSDSVIMTGS 370 380 390 400 410 420 YNNFFRMFDR NTKRDVTLEA SRENSKPRAI LKPRKVCVGG KRRKDEISVD SLDFSKKILH 430 440 TAWHPSENII AVAATNNLYI FQDKVN
	Isoform 3 [UniParc]. Checksum: 6773D04E733403B1	FASTA	449	52,066
	10 20 30 40 50 60 MIPGIGTLTQ DTLWCFSQVK GTIEIGTTEA DIISTVEFNH TGELLATGDK GGRVVIFQRE 70 80 90 100 110 120 QESKNQVHRR GEYNVYSTFQ SHEPEFDYLK SLEIEEKINK IRWLPQQNAA YFLLSTNDKT 130 140 150 160 170 180 VKLWKVSERD KRPEGYNLKD EEGRLRDPAT ITTLRVPVLR PMDLMVEATP RRVFANAHTY 190 200 210 220 230 240 HINSISVNSD YETYMSADDL RINLWNFEIT NQSFNIVDIK PANMEELTEV ITAAEFHPHH 250 260 270 280 290 300 CNTFVYSSSK GTIRLCDMRA SALCDRHTKF FEEPEDPSNR SFFSEIISSI SDVKFSHSGR 310 320 330 340 350 360 YIMTRDYLTV KVWDLNMENR PIETYQVHDY LRSKLCSLYE NDCIFDKFEC VWNGSDSVIM 370 380 390 400 410 420 TGSYNNFFRM FDRNTKRDVT LEASRENSKP RAILKPRKVC VGGKRRKDEI SVDSLDFSKK 430 440 ILHTAWHPSE NIIAVAATNN LYIFQDKVN
	Isoform 4 [UniParc]. Checksum: 3FE3DD278143364A	FASTA	501	58,171
	10 20 30 40 50 60 MVLQPSERHY RDWNHRRLGP WCSPTGSPAP LSCETGCGEG SWILVCRLLV PTQVSLLSME 70 80 90 100 110 120 EDIDTRKINN SFLRDHSYAT EADIISTVEF NHTGELLATG DKGGRVVIFQ REQESKNQVH 130 140 150 160 170 180 RRGEYNVYST FQSHEPEFDY LKSLEIEEKI NKIRWLPQQN AAYFLLSTND KTVKLWKVSE 190 200 210 220 230 240 RDKRPEGYNL KDEEGRLRDP ATITTLRVPV LRPMDLMVEA TPRRVFANAH TYHINSISVN 250 260 270 280 290 300 SDYETYMSAD DLRINLWNFE ITNQSFNIVD IKPANMEELT EVITAAEFHP HHCNTFVYSS 310 320 330 340 350 360 SKGTIRLCDM RASALCDRHT KFFEEPEDPS NRSFFSEIIS SISDVKFSHS GRYIMTRDYL 370 380 390 400 410 420 TVKVWDLNME NRPIETYQVH DYLRSKLCSL YENDCIFDKF ECVWNGSDSV IMTGSYNNFF 430 440 450 460 470 480 RMFDRNTKRD VTLEASRENS KPRAILKPRK VCVGGKRRKD EISVDSLDFS KKILHTAWHP 490 500 SENIIAVAAT NNLYIFQDKV N
	Isoform 5 [UniParc]. Checksum: D47AFC5DD1629FDB	FASTA	509	58,897
	10 20 30 40 50 60 MLLSLPALHL QTSEHHPFFQ LPHRRLGPWC SPTGSPAPLS CETGCGEGSW ILVCRLLVPT 70 80 90 100 110 120 QVSLLSMEED IDTRKINNSF LRDHSYATEA DIISTVEFNH TGELLATGDK GGRVVIFQRE 130 140 150 160 170 180 QESKNQVHRR GEYNVYSTFQ SHEPEFDYLK SLEIEEKINK IRWLPQQNAA YFLLSTNDKT 190 200 210 220 230 240 VKLWKVSERD KRPEGYNLKD EEGRLRDPAT ITTLRVPVLR PMDLMVEATP RRVFANAHTY 250 260 270 280 290 300 HINSISVNSD YETYMSADDL RINLWNFEIT NQSFNIVDIK PANMEELTEV ITAAEFHPHH 310 320 330 340 350 360 CNTFVYSSSK GTIRLCDMRA SALCDRHTKF FEEPEDPSNR SFFSEIISSI SDVKFSHSGR 370 380 390 400 410 420 YIMTRDYLTV KVWDLNMENR PIETYQVHDY LRSKLCSLYE NDCIFDKFEC VWNGSDSVIM 430 440 450 460 470 480 TGSYNNFFRM FDRNTKRDVT LEASRENSKP RAILKPRKVC VGGKRRKDEI SVDSLDFSKK 490 500 ILHTAWHPSE NIIAVAATNN LYIFQDKVN
	Isoform 6 [UniParc]. Checksum: B63F511DEF9670CA	FASTA	432	50,371
	10 20 30 40 50 60 MNYPDENTYG NKADIISTVE FNHTGELLAT GDKGGRVVIF QREQESKNQV HRRGEYNVYS 70 80 90 100 110 120 TFQSHEPEFD YLKSLEIEEK INKIRWLPQQ NAAYFLLSTN DKTVKLWKVS ERDKRPEGYN 130 140 150 160 170 180 LKDEEGRLRD PATITTLRVP VLRPMDLMVE ATPRRVFANA HTYHINSISV NSDYETYMSA 190 200 210 220 230 240 DDLRINLWNF EITNQSFNIV DIKPANMEEL TEVITAAEFH PHHCNTFVYS SSKGTIRLCD 250 260 270 280 290 300 MRASALCDRH TKFFEEPEDP SNRSFFSEII SSISDVKFSH SGRYIMTRDY LTVKVWDLNM 310 320 330 340 350 360 ENRPIETYQV HDYLRSKLCS LYENDCIFDK FECVWNGSDS VIMTGSYNNF FRMFDRNTKR 370 380 390 400 410 420 DVTLEASREN SKPRAILKPR KVCVGGKRRK DEISVDSLDF SKKILHTAWH PSENIIAVAA 430 TNNLYIFQDK VN
	Isoform 7 [UniParc]. Checksum: DFACDC3C235450D7	FASTA	549	62,505
	10 20 30 40 50 60 MHQPPPASCS SSSSSSSSSC ECARVGVRVS ALAPAAAPCP APRQLPYPRL PEPPSRGTST 70 80 90 100 110 120 LIPARLGPWC SPTGSPAPLS CETGCGEGSW ILVCRLLVPT QVSLLSMEED IDTRKINNSF 130 140 150 160 170 180 LRDHSYATEA DIISTVEFNH TGELLATGDK GGRVVIFQRE QESKNQVHRR GEYNVYSTFQ 190 200 210 220 230 240 SHEPEFDYLK SLEIEEKINK IRWLPQQNAA YFLLSTNDKT VKLWKVSERD KRPEGYNLKD 250 260 270 280 290 300 EEGRLRDPAT ITTLRVPVLR PMDLMVEATP RRVFANAHTY HINSISVNSD YETYMSADDL 310 320 330 340 350 360 RINLWNFEIT NQSFNIVDIK PANMEELTEV ITAAEFHPHH CNTFVYSSSK GTIRLCDMRA 370 380 390 400 410 420 SALCDRHTKF FEEPEDPSNR SFFSEIISSI SDVKFSHSGR YIMTRDYLTV KVWDLNMENR 430 440 450 460 470 480 PIETYQVHDY LRSKLCSLYE NDCIFDKFEC VWNGSDSVIM TGSYNNFFRM FDRNTKRDVT 490 500 510 520 530 540 LEASRENSKP RAILKPRKVC VGGKRRKDEI SVDSLDFSKK ILHTAWHPSE NIIAVAATNN LYIFQDKVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform." Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., Merlevede W., Hofsteenge J., Hemmings B.A. Biochemistry 30:3589-3597(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	"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] (ISOFORMS 1; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7). Tissue: Brain and Corpus callosum.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6). Tissue: Brain and Hypothalamus.
[6]	Strausberg R.L. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2).
[7]	"Expansion of a novel CAG trinucleotide repeat in the 5' region of PPP2R2B is associated with SCA12." Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A., Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G., Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A., Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L. Nat. Genet. 23:391-392(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCA12.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64930 mRNA. Translation: AAA36493.1. AK056192 mRNA. Translation: BAG51642.1. Sequence problems. AK289717 mRNA. Translation: BAF82406.1. AK294659 mRNA. Translation: BAH11838.1. AK295347 mRNA. Translation: BAH12040.1. AC008728 Genomic DNA. No translation available. AC009186 Genomic DNA. No translation available. AC010251 Genomic DNA. No translation available. AC011386 Genomic DNA. No translation available. AC011357 Genomic DNA. No translation available. AC091919 Genomic DNA. No translation available. AC091924 Genomic DNA. No translation available. CH471062 Genomic DNA. Translation: EAW61829.1. CH471062 Genomic DNA. Translation: EAW61831.1. CH471062 Genomic DNA. Translation: EAW61832.1. CH471062 Genomic DNA. Translation: EAW61833.1. CH471062 Genomic DNA. Translation: EAW61834.1. CH471062 Genomic DNA. Translation: EAW61835.1. BC031790 mRNA. Translation: AAH31790.1. Different initiation. BI490027 mRNA. No translation available. BI669304 mRNA. No translation available.
IPI	IPI00020850. IPI00376972. IPI00376973. IPI00944548. IPI00944557.
PIR	B38351.
RefSeq	NP_001258828.1. NM_001271899.1. NP_001258829.1. NM_001271900.1. NP_001258877.1. NM_001271948.1. NP_858060.2. NM_181674.2. NP_858061.2. NM_181675.3. NP_858062.1. NM_181676.2. NP_858063.1. NM_181677.2. NP_858064.1. NM_181678.2.
UniGene	Hs.655213.
3D structure databases
ProteinModelPortal	Q00005.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q00005. 167 interactions.
STRING	9606.ENSP00000336591.
PTM databases
PhosphoSite	Q00005.
Polymorphism databases
DMDM	231446.
Proteomic databases
PaxDb	Q00005.
PRIDE	Q00005.
Protocols and materials databases
DNASU	5521.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336640; ENSP00000336591; ENSG00000156475. ENST00000356826; ENSP00000349283; ENSG00000156475. ENST00000394409; ENSP00000377931; ENSG00000156475. ENST00000394410; ENSP00000377932; ENSG00000156475. ENST00000394411; ENSP00000377933; ENSG00000156475. ENST00000394413; ENSP00000377935; ENSG00000156475. ENST00000394414; ENSP00000377936; ENSG00000156475. ENST00000453001; ENSP00000398779; ENSG00000156475. ENST00000504198; ENSP00000421396; ENSG00000156475. ENST00000508545; ENSP00000431320; ENSG00000156475.
GeneID	5521.
KEGG	hsa:5521.
UCSC	uc003loe.3. human. uc003loi.4. human. uc011dbu.2. human. uc011dbv.2. human.
Organism-specific databases
CTD	5521.
GeneCards	GC05M145969.
HGNC	HGNC:9305. PPP2R2B.
HPA	HPA038118.
MIM	604325. gene. 604326. phenotype.
neXtProt	NX_Q00005.
Orphanet	98762. Spinocerebellar ataxia type 12.
PharmGKB	PA33669.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5170.
HOVERGEN	HBG000012.
InParanoid	Q00005.
KO	K04354.
OMA	NYATEAD.
OrthoDB	EOG4M0F1K.
Gene expression databases
ArrayExpress	Q00005.
Bgee	Q00005.
CleanEx	HS_PPP2R2B.
Genevestigator	Q00005.
GermOnline	ENSG00000156475. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 3 hits.
InterPro	IPR000009. PP2A_PR55. IPR018067. PP2A_PR55_CS. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
PANTHER	PTHR11871. PTHR11871. 1 hit.
PIRSF	PIRSF037309. PP2A_PR55. 1 hit.
PRINTS	PR00600. PP2APR55.
SMART	SM00320. WD40. 6 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS01024. PR55_1. 1 hit. PS01025. PR55_2. 1 hit. PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPP2R2B. human.
GenomeRNAi	5521.
NextBio	21356.
SOURCE	Search...

Entry information

Entry name

2ABB_HUMAN

Accession

Primary (citable) accession number: Q00005
Secondary accession number(s): A6NEJ2 , A8K102, B3KPD0, B7Z2F2, B7Z304, D3DQF7, D3DQF8, G3V149

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 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.