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cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | lld:cellmap |
cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | lld:imid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PIN1_HUMAN | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PIN1_HUMAN | lld:cellmap |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PIN1_HUMAN | lld:imid |
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cpath:CPATH-58969 | http://www.biopax.org/relea... | 5.2.1.8 | lld:biogrid |
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cpath:CPATH-58969 | http://www.biopax.org/relea... | Rotamase Pin1 | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | Rotamase Pin1 | lld:cellmap |
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cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase Pin1 | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase Pin1 | lld:cellmap |
cpath:CPATH-58969 | http://www.biopax.org/relea... | Peptidyl-prolyl cis-trans isomerase Pin1 | lld:imid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PPIase Pin1 | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PPIase Pin1 | lld:cellmap |
cpath:CPATH-58969 | http://www.biopax.org/relea... | PPIase Pin1 | lld:imid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | 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. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License. | lld:biogrid |
cpath:CPATH-58969 | http://www.biopax.org/relea... | 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. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License. | lld:cellmap |
cpath:CPATH-58969 | http://www.biopax.org/relea... | 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. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License. | lld:imid |
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