| Tag | Content |
|---|---|
| UniProt Accession | PIN1_HUMAN; Q13526; |
| Entrez ID | 5300 |
| GenBank Protein ID | |
| GenBank Nucleotide ID | |
| Protein Name | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1) |
| Gene Name | PIN1 |
| Organism | Homo sapiens |
| NCBI Taxa ID | 9606 |
| Functional Description | Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, Ref. 21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BT(view all) |
| Sequence (Fasta) | MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL 60 LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG 120 DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE 164 |
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| Database | Annotation |
|---|---|
| CTD (Curated) (count: 1) | MESH:D001943 ; Breast Neoplasms |
| HGMD (count: 1) | CR072323; Alzheimer disease, association with; Regulatory
|
| PTM | Modification Sites |
|---|---|
| Phosphorylation (count: 14) (view all) | 105 SGEEDFESLASQFSD dbPAF
108 EDFESLASQFSDCSS dbPAF 114 ASQFSDCSSAKARGD dbPAF 115 SQFSDCSSAKARGDL dbPAF 138 QKPFEDASFALRTGE dbPAF 154 SGPVFTDSGIHIILR dbPAF |
| Acetylation (count: 3) | 117 FSDCSSAKARGDLGA PLMD
46 GNSSSGGKNGQGEPA PLMD 63 RCSHLLVKHSQSRRP PLMD |
| Ubiquitination (count: 6) | 117 FSDCSSAKARGDLGA PLMD
13 KLPPGWEKRMSRSSG PLMD 132 FSRGQMQKPFEDASF PLMD 82 QEKITRTKEEALELI PLMD 95 LINGYIQKIKSGEED PLMD 97 NGYIQKIKSGEEDFE PLMD |
| Sumoylation (count: 3) | 6 **MADEEKLPPGWEK PLMD
63 RCSHLLVKHSQSRRP PLMD 82 QEKITRTKEEALELI PLMD |