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Q5BIN5 (PIN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

EC=5.2.1.8
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name=PPIase Pin1
Rotamase Pin1
Gene names
Name:PIN1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subunit structure

Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML and BCL-6 By similarity.

Subcellular location

Nucleus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. Note: Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization By similarity.

Domain

The WW domain is required for the interaction with STIL and KIF20B By similarity.

Post-translational modification

Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation By similarity.

Sequence similarities

Contains 1 PpiC domain.

Contains 1 WW domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell motility

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho GTPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell proliferation

Inferred from sequence or structural similarity. Source: AgBase

regulation of cytokinesis

Inferred from electronic annotation. Source: Ensembl

regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Ensembl

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
PRO_0000236242

Regions

Domain5 – 3935WW
Domain52 – 163112PpiC

Amino acid modifications

Modified residue461N6-acetyllysine By similarity
Modified residue711Phosphoserine; by DAPK1 By similarity
Modified residue1081Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BIN5 [UniParc].

Last modified April 12, 2005. Version 1.
Checksum: 6CED0EF411C3AB0D

FASTA16318,273
        10         20         30         40         50         60 
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSGSGKNGQG EPTRVRCSHL 

        70         80         90        100        110        120 
LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG 

       130        140        150        160 
DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT021189 mRNA. Translation: AAX31371.1.
BC112583 mRNA. Translation: AAI12584.1.
RefSeqNP_001029804.1. NM_001034632.3.
UniGeneBt.5583.

3D structure databases

ProteinModelPortalQ5BIN5.
SMRQ5BIN5. Positions 1-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000022592.

Proteomic databases

PRIDEQ5BIN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022592; ENSBTAP00000022592; ENSBTAG00000016988.
GeneID535470.
KEGGbta:535470.

Organism-specific databases

CTD5300.

Phylogenomic databases

eggNOGCOG0760.
GeneTreeENSGT00640000091578.
HOGENOMHOG000275331.
HOVERGENHBG002101.
InParanoidQ5BIN5.
KOK09578.
OMAFALKVGD.
OrthoDBEOG7S4X82.
TreeFamTF101101.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20876760.

Entry information

Entry namePIN1_BOVIN
AccessionPrimary (citable) accession number: Q5BIN5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: April 12, 2005
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families