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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform

Gene

PPP3CB

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

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991IronBy similarity
Metal bindingi101 – 1011IronBy similarity
Metal bindingi127 – 1271IronBy similarity
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi159 – 1591ZincBy similarity
Active sitei160 – 1601Proton donorBy similarity
Metal bindingi208 – 2081ZincBy similarity
Metal bindingi290 – 2901ZincBy similarity

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  • axon extension Source: UniProtKB
  • calcineurin-NFAT signaling cascade Source: BHF-UCL
  • calcium ion regulated exocytosis Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • dephosphorylation Source: UniProtKB
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • heart development Source: Ensembl
  • innate immune response Source: Reactome
  • learning Source: UniProtKB
  • locomotion involved in locomotory behavior Source: Ensembl
  • lymphangiogenesis Source: Ensembl
  • memory Source: UniProtKB
  • negative regulation of T cell mediated cytotoxicity Source: Ensembl
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • positive regulation of NFAT protein import into nucleus Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein dephosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of synaptic plasticity Source: UniProtKB
  • response to cytokine Source: Ensembl
  • signal transduction Source: UniProtKB
  • social behavior Source: UniProtKB
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell activation Source: UniProtKB
  • T cell differentiation Source: Ensembl
  • T cell homeostasis Source: Ensembl
  • T cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-180024. DARPP-32 events.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
SIGNORiP16298.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC:3.1.3.16)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Gene namesi
Name:PPP3CB
Synonyms:CALNA2, CALNB, CNA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9315. PPP3CB.

Subcellular locationi

GO - Cellular componenti

  • calcineurin complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • plasma membrane Source: UniProtKB
  • T-tubule Source: Ensembl
  • Z disc Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33679.

Chemistry

ChEMBLiCHEMBL5278.

Polymorphism and mutation databases

BioMutaiPPP3CB.
DMDMi60659599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 524523Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformPRO_0000058825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei478 – 4781PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16298.
MaxQBiP16298.
PaxDbiP16298.
PRIDEiP16298.

PTM databases

DEPODiP16298.
iPTMnetiP16298.
PhosphoSiteiP16298.
SwissPalmiP16298.

Expressioni

Gene expression databases

BgeeiP16298.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevisibleiP16298. HS.

Organism-specific databases

HPAiHPA008233.

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q99J342EBI-1759540,EBI-6117042From a different organism.
IRF2P143162EBI-1759540,EBI-2866589

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111524. 34 interactions.
DIPiDIP-52337N.
IntActiP16298. 13 interactions.
STRINGi9606.ENSP00000378306.

Chemistry

BindingDBiP16298.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 233Combined sources
Helixi40 – 434Combined sources
Helixi52 – 609Combined sources
Helixi67 – 8216Combined sources
Beta strandi86 – 905Combined sources
Beta strandi92 – 976Combined sources
Helixi104 – 11411Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi129 – 1324Combined sources
Helixi135 – 14814Combined sources
Turni150 – 1523Combined sources
Beta strandi153 – 1553Combined sources
Helixi163 – 1686Combined sources
Helixi171 – 1788Combined sources
Helixi181 – 19212Combined sources
Beta strandi196 – 2005Combined sources
Turni201 – 2033Combined sources
Beta strandi204 – 2096Combined sources
Helixi218 – 2225Combined sources
Beta strandi232 – 2343Combined sources
Helixi235 – 2417Combined sources
Turni246 – 2494Combined sources
Beta strandi256 – 2594Combined sources
Turni261 – 2633Combined sources
Beta strandi264 – 2696Combined sources
Helixi271 – 28111Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi296 – 2994Combined sources
Turni304 – 3063Combined sources
Beta strandi308 – 3158Combined sources
Helixi320 – 3223Combined sources
Beta strandi328 – 3347Combined sources
Beta strandi337 – 3437Combined sources
Helixi353 – 3553Combined sources
Helixi358 – 37821Combined sources
Beta strandi381 – 3833Combined sources
Turni384 – 3863Combined sources
Helixi479 – 4857Combined sources
Helixi488 – 4903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OR9X-ray2.23A1-524[»]
4ORAX-ray2.75A1-524[»]
4ORCX-ray2.70A1-524[»]
ProteinModelPortaliP16298.
SMRiP16298. Positions 16-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 310309CatalyticAdd
BLAST
Regioni256 – 2627Calcineurin B binding-site 1Sequence analysis
Regioni305 – 3106Calcineurin B binding-site 2Sequence analysis
Regioni401 – 42323Calmodulin-bindingSequence analysisAdd
BLAST
Regioni474 – 49623Inhibitory domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2111Poly-ProAdd
BLAST

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

eggNOGiKOG0375. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiTREADND.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Calcineurin A beta isoform consists of at least two isoenzymes that may result from alternative splicing events.

Isoform 1 (identifier: P16298-1) [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
MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP
60 70 80 90 100
RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
110 120 130 140 150
HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
160 170 180 190 200
STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
210 220 230 240 250
NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
260 270 280 290 300
EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
310 320 330 340 350
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
360 370 380 390 400
WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA
410 420 430 440 450
RKEIIRNKIR AIGKMARVFS VLREESESVL TLKGLTPTGM LPSGVLAGGR
460 470 480 490 500
QTLQSATVEA IEAEKAIRGF SPPHRICSFE EAKGLDRINE RMPPRKDAVQ
510 520
QDGFNSLNTA HATENHGTGN HTAQ
Length:524
Mass (Da):59,024
Last modified:February 1, 2005 - v2
Checksum:i7661183F3C2362C8
GO
Isoform 2 (identifier: P16298-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-137: E → EHVLGTEDISINPHNNINE
     456-524: ATVEAIEAEK...NHGTGNHTAQ → GNDVMQLAVP...LLFFSSCLSS

Show »
Length:514
Mass (Da):58,013
Checksum:i1B0BFA63FB98E06D
GO
Isoform 3 (identifier: P16298-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV
     456-465: Missing.

Show »
Length:515
Mass (Da):58,081
Checksum:iA6762D9468A09B51
GO
Isoform 4 (identifier: P16298-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV

Note: No experimental confirmation available.
Show »
Length:525
Mass (Da):59,123
Checksum:iADB0ECB75371B574
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei137 – 1371E → EHVLGTEDISINPHNNINE in isoform 2. 1 PublicationVSP_005096
Alternative sequencei395 – 3951D → DV in isoform 3 and isoform 4. 2 PublicationsVSP_043803
Alternative sequencei456 – 52469ATVEA…NHTAQ → GNDVMQLAVPQMDWGTPHSF ANNSHNACREFLLFFSSCLS S in isoform 2. 1 PublicationVSP_005097Add
BLAST
Alternative sequencei456 – 46510Missing in isoform 3. 1 PublicationVSP_012617

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29551 mRNA. Translation: AAA35706.1.
M29550 mRNA. Translation: AAA35705.1.
AJ488506 mRNA. Translation: CAD32694.1.
AL353731, AL359074 Genomic DNA. Translation: CAI52487.1.
AL359074, AL353731 Genomic DNA. Translation: CAI52473.1.
CH471083 Genomic DNA. Translation: EAW54497.1.
CH471083 Genomic DNA. Translation: EAW54498.1.
BC028049 mRNA. Translation: AAH28049.1.
CCDSiCCDS44436.1. [P16298-3]
CCDS44437.1. [P16298-4]
CCDS7328.1. [P16298-1]
PIRiA36222.
B36222.
RefSeqiNP_001135825.1. NM_001142353.2. [P16298-4]
NP_001135826.1. NM_001142354.2. [P16298-3]
NP_001276897.1. NM_001289968.1. [P16298-2]
NP_001276898.1. NM_001289969.1.
NP_066955.1. NM_021132.3. [P16298-1]
UniGeneiHs.500067.

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.4. human. [P16298-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29551 mRNA. Translation: AAA35706.1.
M29550 mRNA. Translation: AAA35705.1.
AJ488506 mRNA. Translation: CAD32694.1.
AL353731, AL359074 Genomic DNA. Translation: CAI52487.1.
AL359074, AL353731 Genomic DNA. Translation: CAI52473.1.
CH471083 Genomic DNA. Translation: EAW54497.1.
CH471083 Genomic DNA. Translation: EAW54498.1.
BC028049 mRNA. Translation: AAH28049.1.
CCDSiCCDS44436.1. [P16298-3]
CCDS44437.1. [P16298-4]
CCDS7328.1. [P16298-1]
PIRiA36222.
B36222.
RefSeqiNP_001135825.1. NM_001142353.2. [P16298-4]
NP_001135826.1. NM_001142354.2. [P16298-3]
NP_001276897.1. NM_001289968.1. [P16298-2]
NP_001276898.1. NM_001289969.1.
NP_066955.1. NM_021132.3. [P16298-1]
UniGeneiHs.500067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OR9X-ray2.23A1-524[»]
4ORAX-ray2.75A1-524[»]
4ORCX-ray2.70A1-524[»]
ProteinModelPortaliP16298.
SMRiP16298. Positions 16-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111524. 34 interactions.
DIPiDIP-52337N.
IntActiP16298. 13 interactions.
STRINGi9606.ENSP00000378306.

Chemistry

BindingDBiP16298.
ChEMBLiCHEMBL5278.

PTM databases

DEPODiP16298.
iPTMnetiP16298.
PhosphoSiteiP16298.
SwissPalmiP16298.

Polymorphism and mutation databases

BioMutaiPPP3CB.
DMDMi60659599.

Proteomic databases

EPDiP16298.
MaxQBiP16298.
PaxDbiP16298.
PRIDEiP16298.

Protocols and materials databases

DNASUi5532.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.4. human. [P16298-1]

Organism-specific databases

CTDi5532.
GeneCardsiPPP3CB.
HGNCiHGNC:9315. PPP3CB.
HPAiHPA008233.
MIMi114106. gene.
neXtProtiNX_P16298.
PharmGKBiPA33679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0375. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiTREADND.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

Enzyme and pathway databases

ReactomeiR-HSA-180024. DARPP-32 events.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
SIGNORiP16298.

Miscellaneous databases

ChiTaRSiPPP3CB. human.
GeneWikiiPPP3CB.
GenomeRNAii5532.
NextBioi21430.
PROiP16298.
SOURCEiSearch...

Gene expression databases

BgeeiP16298.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevisibleiP16298. HS.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain."
    Guerini D., Klee C.B.
    Proc. Natl. Acad. Sci. U.S.A. 86:9183-9187(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Identification of a third alternatively spliced cDNA encoding the catalytic subunit of protein phosphatase 2B beta."
    McPartlin A.E., Barker H.M., Cohen P.T.W.
    Biochim. Biophys. Acta 1088:308-310(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Teratocarcinoma.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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 4).
    Tissue: Testis.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP2BB_HUMAN
AccessioniPrimary (citable) accession number: P16298
Secondary accession number(s): P16299
, Q5F2F9, Q8N1F0, Q8N3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: May 11, 2016
This is version 137 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.