SubmitCancel

Skip Header

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

O75688

- PPM1B_HUMAN

UniProt

O75688 - PPM1B_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Protein phosphatase 1B
Gene
PPM1B, PP2CB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.2 Publications

Catalytic activityi

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

Cofactori

Binds 2 magnesium or manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Manganese 1 By similarity
Metal bindingi60 – 601Manganese 2 By similarity
Metal bindingi61 – 611Manganese 1; via carbonyl oxygen By similarity
Metal bindingi243 – 2431Manganese 2 By similarity
Metal bindingi286 – 2861Manganese 2 By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. manganese ion binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. N-terminal protein myristoylation Source: UniProtKB
  2. cytokine-mediated signaling pathway Source: Reactome
  3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  4. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  5. negative regulation of defense response to virus Source: UniProtKB
  6. negative regulation of interferon-beta production Source: UniProtKB
  7. peptidyl-threonine dephosphorylation Source: UniProtKB
  8. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1B (EC:3.1.3.16)
Alternative name(s):
Protein phosphatase 2C isoform beta
Short name:
PP2C-beta
Gene namesi
Name:PPM1B
Synonyms:PP2CB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9276. PPM1B.

Subcellular locationi

Cytoplasmcytosol. Membrane By similarity
Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization By similarity.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti163693. 2p21 microdeletion syndrome.
PharmGKBiPA33604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 479478Protein phosphatase 1B
PRO_0000057746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Cross-linki12 – 12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication

Post-translational modificationi

Isgylation negatively regulates its activity.
N-myristoylation is essential for the recognition of its substrates for dephosphorylation By similarity.

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Ubl conjugation

Proteomic databases

MaxQBiO75688.
PaxDbiO75688.
PRIDEiO75688.

PTM databases

PhosphoSiteiO75688.

Expressioni

Tissue specificityi

Highly expressed in heart and skeletal muscle.

Gene expression databases

ArrayExpressiO75688.
BgeeiO75688.
CleanExiHS_PPM1B.
GenevestigatoriO75688.

Organism-specific databases

HPAiHPA016745.

Interactioni

Subunit structurei

Monomer By similarity. Interacts with PAK6. Interacts with the phosphorylated form of IKBKB/IKKB.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494074EBI-1047039,EBI-743313
ARRB2P321213EBI-1047039,EBI-714559
ISG15P051612EBI-1047039,EBI-746466

Protein-protein interaction databases

BioGridi111490. 35 interactions.
IntActiO75688. 11 interactions.
MINTiMINT-2841839.
STRINGi9606.ENSP00000282412.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1911
Beta strandi22 – 3110
Beta strandi33 – 353
Beta strandi38 – 469
Turni47 – 493
Beta strandi50 – 6314
Helixi66 – 8015
Turni83 – 853
Helixi99 – 11820
Turni121 – 1233
Beta strandi134 – 1396
Beta strandi141 – 15111
Beta strandi153 – 1586
Beta strandi161 – 1655
Helixi174 – 1829
Turni193 – 1953
Helixi205 – 2073
Helixi215 – 2173
Beta strandi218 – 2214
Beta strandi225 – 2306
Beta strandi235 – 2417
Helixi243 – 2464
Helixi251 – 26212
Helixi268 – 28114
Beta strandi288 – 2947

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P8EX-ray1.82A/B2-297[»]
ProteinModelPortaliO75688.
SMRiO75688. Positions 4-295.

Miscellaneous databases

EvolutionaryTraceiO75688.

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiO75688.
KOiK04461.
OMAiVMISPEH.
PhylomeDBiO75688.
TreeFamiTF313590.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PP2C. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Beta-1 (identifier: O75688-1) [UniParc]FASTAAdd to Basket

Also known as: Beta-X, PPM1B2

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

MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL    50
EDWSFFAVYD GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE 100
NVKNGIRTGF LKIDEYMRNF SDLRNGMDRS GSTAVGVMIS PKHIYFINCG 150
DSRAVLYRNG QVCFSTQDHK PCNPREKERI QNAGGSVMIQ RVNGSLAVSR 200
ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL ACDGIWDVMS 250
NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 300
VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL 350
PPGGGLAGKR NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR 400
INHRGNYRQL LEEMLTSYRL AKVEGEESPA EPAATATSSN SDAGNPVTMQ 450
ESHTESESGL AELDSSNEDA GTKMSGEKI 479
Length:479
Mass (Da):52,643
Last modified:November 1, 1998 - v1
Checksum:iA3A5797AD263DFBD
GO
Isoform Beta-2 (identifier: O75688-2) [UniParc]FASTAAdd to Basket

Also known as: PPM1B1

The sequence of this isoform differs from the canonical sequence as follows:
     379-387: ASDEAEESG → GAGDLEDPW
     388-479: Missing.

Show »
Length:387
Mass (Da):42,771
Checksum:i56A644A4E5E2B12B
GO
Isoform Beta-X (identifier: O75688-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-287: Missing.

Show »
Length:193
Mass (Da):20,884
Checksum:iE655DD15842CA329
GO
Isoform 4 (identifier: O75688-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     379-380: AS → QK
     381-387: Missing.
     388-479: Missing.

Show »
Length:380
Mass (Da):42,086
Checksum:iE5C00B5FF4278013
GO
Isoform 5 (identifier: O75688-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     322-327: EIMEKS → GKTNAF
     328-380: Missing.
     381-387: Missing.
     388-479: Missing.

Show »
Length:327
Mass (Da):36,313
Checksum:iE38A263FCF7F1692
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 287286Missing in isoform Beta-X.
VSP_041085Add
BLAST
Alternative sequencei322 – 3276EIMEKS → GKTNAF in isoform 5.
VSP_043641
Alternative sequencei328 – 38053Missing in isoform 5.
VSP_043642Add
BLAST
Alternative sequencei379 – 3879ASDEAEESG → GAGDLEDPW in isoform Beta-2.
VSP_005087
Alternative sequencei379 – 3802AS → QK in isoform 4.
VSP_043643
Alternative sequencei381 – 3877Missing in isoform 4 and isoform 5.
VSP_043644
Alternative sequencei388 – 47992Missing in isoform Beta-2, isoform 4 and isoform 5.
VSP_005088Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ005801 mRNA. Translation: CAA06704.1.
AF294792 mRNA. Translation: AAG02232.1.
AJ271832 mRNA. Translation: CAC27992.1.
AJ271835 mRNA. Translation: CAC27993.1.
DQ023508 mRNA. Translation: AAY89639.1.
DQ023509 mRNA. Translation: AAY89640.1.
DQ023510 mRNA. Translation: AAY89641.1.
AF136972 mRNA. Translation: AAG49433.1.
AL833035 mRNA. Translation: CAH56319.1.
AC013717 Genomic DNA. Translation: AAX88954.1.
AC019129 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00282.1.
CH471053 Genomic DNA. Translation: EAX00283.1.
BC012002 mRNA. Translation: AAH12002.1.
BC064381 mRNA. Translation: AAH64381.1.
CCDSiCCDS1816.1. [O75688-2]
CCDS1817.1. [O75688-1]
CCDS46271.1. [O75688-4]
CCDS46272.1. [O75688-5]
RefSeqiNP_001028728.1. NM_001033556.1. [O75688-5]
NP_001028729.1. NM_001033557.1. [O75688-4]
NP_002697.1. NM_002706.4. [O75688-1]
NP_808907.1. NM_177968.2. [O75688-2]
NP_808908.1. NM_177969.2.
UniGeneiHs.416769.

Genome annotation databases

EnsembliENST00000282412; ENSP00000282412; ENSG00000138032. [O75688-1]
ENST00000345249; ENSP00000326089; ENSG00000138032. [O75688-3]
ENST00000378551; ENSP00000367813; ENSG00000138032. [O75688-2]
ENST00000409432; ENSP00000387287; ENSG00000138032. [O75688-4]
ENST00000409895; ENSP00000387341; ENSG00000138032. [O75688-5]
GeneIDi5495.
KEGGihsa:5495.
UCSCiuc002rts.3. human. [O75688-5]
uc002rtt.3. human. [O75688-1]
uc002rtu.3. human. [O75688-4]
uc002rtv.3. human. [O75688-3]
uc002rtw.3. human. [O75688-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ005801 mRNA. Translation: CAA06704.1 .
AF294792 mRNA. Translation: AAG02232.1 .
AJ271832 mRNA. Translation: CAC27992.1 .
AJ271835 mRNA. Translation: CAC27993.1 .
DQ023508 mRNA. Translation: AAY89639.1 .
DQ023509 mRNA. Translation: AAY89640.1 .
DQ023510 mRNA. Translation: AAY89641.1 .
AF136972 mRNA. Translation: AAG49433.1 .
AL833035 mRNA. Translation: CAH56319.1 .
AC013717 Genomic DNA. Translation: AAX88954.1 .
AC019129 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00282.1 .
CH471053 Genomic DNA. Translation: EAX00283.1 .
BC012002 mRNA. Translation: AAH12002.1 .
BC064381 mRNA. Translation: AAH64381.1 .
CCDSi CCDS1816.1. [O75688-2 ]
CCDS1817.1. [O75688-1 ]
CCDS46271.1. [O75688-4 ]
CCDS46272.1. [O75688-5 ]
RefSeqi NP_001028728.1. NM_001033556.1. [O75688-5 ]
NP_001028729.1. NM_001033557.1. [O75688-4 ]
NP_002697.1. NM_002706.4. [O75688-1 ]
NP_808907.1. NM_177968.2. [O75688-2 ]
NP_808908.1. NM_177969.2.
UniGenei Hs.416769.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P8E X-ray 1.82 A/B 2-297 [» ]
ProteinModelPortali O75688.
SMRi O75688. Positions 4-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111490. 35 interactions.
IntActi O75688. 11 interactions.
MINTi MINT-2841839.
STRINGi 9606.ENSP00000282412.

Chemistry

BindingDBi O75688.
ChEMBLi CHEMBL2845.

PTM databases

PhosphoSitei O75688.

Proteomic databases

MaxQBi O75688.
PaxDbi O75688.
PRIDEi O75688.

Protocols and materials databases

DNASUi 5495.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282412 ; ENSP00000282412 ; ENSG00000138032 . [O75688-1 ]
ENST00000345249 ; ENSP00000326089 ; ENSG00000138032 . [O75688-3 ]
ENST00000378551 ; ENSP00000367813 ; ENSG00000138032 . [O75688-2 ]
ENST00000409432 ; ENSP00000387287 ; ENSG00000138032 . [O75688-4 ]
ENST00000409895 ; ENSP00000387341 ; ENSG00000138032 . [O75688-5 ]
GeneIDi 5495.
KEGGi hsa:5495.
UCSCi uc002rts.3. human. [O75688-5 ]
uc002rtt.3. human. [O75688-1 ]
uc002rtu.3. human. [O75688-4 ]
uc002rtv.3. human. [O75688-3 ]
uc002rtw.3. human. [O75688-2 ]

Organism-specific databases

CTDi 5495.
GeneCardsi GC02P044307.
HGNCi HGNC:9276. PPM1B.
HPAi HPA016745.
MIMi 603770. gene.
neXtProti NX_O75688.
Orphaneti 163693. 2p21 microdeletion syndrome.
PharmGKBi PA33604.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0631.
HOGENOMi HOG000233895.
HOVERGENi HBG053647.
InParanoidi O75688.
KOi K04461.
OMAi VMISPEH.
PhylomeDBi O75688.
TreeFami TF313590.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.

Miscellaneous databases

EvolutionaryTracei O75688.
GeneWikii PPM1B.
GenomeRNAii 5495.
NextBioi 21250.
PROi O75688.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75688.
Bgeei O75688.
CleanExi HS_PPM1B.
Genevestigatori O75688.

Family and domain databases

Gene3Di 1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The cloning expression and tissue distribution of human PP2Cbeta."
    Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.
    FEBS Lett. 431:121-124(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
    Tissue: Liver.
  2. "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms."
    Cheng A., Kaldis P., Solomon M.J.
    J. Biol. Chem. 275:34744-34749(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
  3. "Protein phosphatase 1B. Cloning and characterization of two major transcripts generated by alternative use of 3' exons."
    Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I., Smorodinsky N.I., Lavi S.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
  4. "The 2p21 deletion syndrome: characterization of the transcription content."
    Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E.
    Genomics 86:195-211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
    Tissue: Adrenal gland.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
    Tissue: Stomach.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS BETA-1 AND BETA-X).
    Tissue: Brain and Urinary bladder.
  10. "Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation."
    Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.
    FEBS Lett. 580:4521-4526(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION AT LYS-12 AND LYS-142.
  11. "Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins."
    Kaur R., Yuan X., Lu M.L., Balk S.P.
    Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAK6.
  12. "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
    Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
    Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKB.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
    Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
    Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "PPM1B negatively regulates antiviral response via dephosphorylating TBK1."
    Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W., Sun W., Mori-Akiyama Y., Zhang H., Fu S., Yang J.
    Cell. Signal. 24:2197-2204(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.

Entry informationi

Entry nameiPPM1B_HUMAN
AccessioniPrimary (citable) accession number: O75688
Secondary accession number(s): Q461Q2
, Q4J6C1, Q4J6C2, Q658R4, Q96ER6, Q9HAY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 151 of the entry and version 1 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 2
    Human chromosome 2: 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

External Data

Dasty 3

Similar proteinsi