Skip Header

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

Q7SZ10

- PP1GB_XENLA

UniProt

Q7SZ10 - PP1GB_XENLA

(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

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B

Gene

ppp1cc-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1By similarity
Metal bindingi66 – 661Manganese 1By similarity
Metal bindingi92 – 921Manganese 1By similarity
Metal bindingi92 – 921Manganese 2By similarity
Metal bindingi124 – 1241Manganese 2By similarity
Active sitei125 – 1251Proton donorBy similarity
Metal bindingi173 – 1731Manganese 2By similarity
Metal bindingi248 – 2481Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. glycogen metabolic process Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
  3. mitotic nuclear envelope reassembly Source: UniProtKB
  4. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism, Mitosis

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B
Short name:
PP-1G-B
Alternative name(s):
Protein phosphatase 1 zeta1 Publication (EC:3.1.3.16)
Short name:
xPP1-zeta1 Publication
Gene namesi
Name:ppp1cc-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromerekinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. kinetochore Source: UniProtKB-KW
  2. mitochondrion Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Serine/threonine-protein phosphatase PP1-gamma catalytic subunit BPRO_0000365635Add
BLAST

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, ppp1c1, ppp1cb or ppp1cc, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then is complexed to one or several targeting or regulatory subunits.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7SZ10.
SMRiQ7SZ10. Positions 6-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Sequence Analysis

Phylogenomic databases

HOVERGENiHBG000216.
KOiK06269.

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]

Sequencei

Sequence statusi: Complete.

Q7SZ10-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320
KKKPNASRPV TPPRGIITKQ AKK
Length:323
Mass (Da):36,938
Last modified:October 1, 2003 - v1
Checksum:i38D4C5DE036A8C2D
GO

Sequence cautioni

The sequence BAF51555.1 differs from that shown. Reason: Frameshift at position 301. Curated
The sequence BAF51555.1 differs from that shown. Reason: Erroneous termination at position 249. Translated as Gln.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB106882 mRNA. Translation: BAF51555.1. Sequence problems.
BC054188 mRNA. Translation: AAH54188.1.
RefSeqiNP_001080904.1. NM_001087435.1.
UniGeneiXl.83313.

Genome annotation databases

GeneIDi380598.
KEGGixla:380598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB106882 mRNA. Translation: BAF51555.1 . Sequence problems.
BC054188 mRNA. Translation: AAH54188.1 .
RefSeqi NP_001080904.1. NM_001087435.1.
UniGenei Xl.83313.

3D structure databases

ProteinModelPortali Q7SZ10.
SMRi Q7SZ10. Positions 6-300.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 380598.
KEGGi xla:380598.

Organism-specific databases

CTDi 5501.

Phylogenomic databases

HOVERGENi HBG000216.
KOi K06269.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts."
    Ito H., Koyama Y., Takano M., Ishii K., Maeno M., Furukawa K., Horigome T.
    Exp. Cell Res. 313:1897-1910(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: OocyteImported.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: TadpoleImported.

Entry informationi

Entry nameiPP1GB_XENLA
AccessioniPrimary (citable) accession number: Q7SZ10
Secondary accession number(s): A4PB28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3