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

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Q7SZ10 (PP1GB_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B
Short name=PP-1G-B

Alternative name(s):
Protein phosphatase 1 zeta
Short name=xPP1-zeta
EC=3.1.3.16

Gene names

Name:

ppp1cc-b

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate. UniProtKB P36874
Cofactor	Binds 1 iron ion per subunit By similarity. UniProtKB P36873 Binds 1 manganese ion per subunit By similarity. UniProtKB P36873
Subunit structure	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. UniProtKB P63088
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleus › nucleolus By similarity. Nucleus › nucleoplasm By similarity. Chromosome › centromere › kinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.
Sequence caution	The sequence BAF51555.1 differs from that shown. Reason: Erroneous termination at position 249. Translated as Gln. The sequence BAF51555.1 differs from that shown. Reason: Frameshift at position 301.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism Mitosis
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Mitochondrion Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic nuclear envelope reassembly Inferred from sequence or structural similarity. Source: UniProtKB protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 323

323

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

PRO_0000365635

Sites

Active site

125

Proton donor By similarity UniProtKB P36873

Metal binding

Iron By similarity UniProtKB P36873

Metal binding

Iron By similarity UniProtKB P36873

Metal binding

Iron By similarity UniProtKB P36873

Metal binding

Manganese By similarity UniProtKB P36873

Metal binding

124

Manganese By similarity UniProtKB P36873

Metal binding

173

Manganese By similarity UniProtKB P36873

Metal binding

248

Manganese By similarity UniProtKB P36873

Sequences

Sequence

Length

Mass (Da)

Tools

Q7SZ10 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 38D4C5DE036A8C2D
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FASTA

323

36,938

        10         20         30         40         50         60 
MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 

       130        140        150        160        170        180 
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 

       190        200        210        220        230        240 
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 

       250        260        270        280        290        300 
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 

       310        320 
KKKPNASRPV TPPRGIITKQ AKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: Oocyte.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tadpole.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB106882 mRNA. Translation: BAF51555.1. Sequence problems. BC054188 mRNA. Translation: AAH54188.1.
RefSeq	NP_001080904.1. NM_001087435.1.
UniGene	Xl.83313.
3D structure databases
HSSP	HSSP built from PDB template 1JK7 based on UniProtKB P36873.
ProteinModelPortal	Q7SZ10.
SMR	Q7SZ10. Positions 6-300.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380598.
KEGG	xla:380598.
Organism-specific databases
CTD	5501.
Phylogenomic databases
HOVERGEN	HBG000216.
KO	K06269.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PP1GB_XENLA

Accession

Primary (citable) accession number: Q7SZ10
Secondary accession number(s): A4PB28

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	October 1, 2003
Last modified:	November 28, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents