PIN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIN1_MOUSE
• UniProt AC: Q9QUR7
• Protein Name: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
• Gene Name: Pin1
• Organism: Mus musculus (Mouse).
• Sequence Length: 165
• Subcellular Localization: Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization.
• Protein 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. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. 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 (By similarity). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. [PubMed: 17828269 Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (By similarity May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (By similarity]
• Protein Sequence: MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGGSTVGGSSKNGQGEPAKVRCSHLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGPFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Ubiquitination	KLPPGWEKRMSRSSG CCCCCHHHHCCCCCC	47.06	-
16	Phosphorylation	PGWEKRMSRSSGRVY CCHHHHCCCCCCCEE	32.80	20215645
23	Phosphorylation	SRSSGRVYYFNHITN CCCCCCEEEEECCCC	10.86	29514104
24	Phosphorylation	RSSGRVYYFNHITNA CCCCCEEEEECCCCH	8.61	-
48	Acetylation	STVGGSSKNGQGEPA CCCCCCCCCCCCCCC	67.79	-
73	Phosphorylation	HSQSRRPSSWRQEKI CCCCCCCCCHHHHHH	40.50	29514104
74	Phosphorylation	SQSRRPSSWRQEKIT CCCCCCCCHHHHHHH	29.03	29514104
81	Phosphorylation	SWRQEKITRSKEEAL CHHHHHHHCCHHHHH	39.70	29899451
83	Phosphorylation	RQEKITRSKEEALEL HHHHHHCCHHHHHHH	35.45	29899451
100	Phosphorylation	GYIQKIKSGEEDFES HHHHHHHCCHHHHHH	55.71	29899451
110	Phosphorylation	EDFESLASQFSDCSS HHHHHHHHHHCCCHH	36.73	-
113	Phosphorylation	ESLASQFSDCSSAKA HHHHHHHCCCHHCHH	30.03	26525534
115	S-nitrosocysteine	LASQFSDCSSAKARG HHHHHCCCHHCHHCC	3.16	-
115	Glutathionylation	LASQFSDCSSAKARG HHHHHCCCHHCHHCC	3.16	24333276
115	S-nitrosylation	LASQFSDCSSAKARG HHHHHCCCHHCHHCC	3.16	22178444
119	Ubiquitination	FSDCSSAKARGDLGP HCCCHHCHHCCCCCC	40.33	-
154	Phosphorylation	EMSGPVFTDSGIHII CCCCCEECCCEEEEE	29.50	26643407
156	Phosphorylation	SGPVFTDSGIHIILR CCCEECCCEEEEEEE	36.27	26643407

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
16	S	Phosphorylation	Kinase	PRKCZ	Q02956	GPS
73	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
73	S	Phosphorylation	Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PIN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NANOG_MOUSE	Nanog	physical	20622153
CTNB1_MOUSE	Ctnnb1	physical	19995909
EGR1_MOUSE	Egr1	physical	19995909
PITX1_MOUSE	Pitx1	physical	19995909
FBXW7_MOUSE	Fbxw7	physical	22608923
IRAK1_MOUSE	Irak1	physical	21743479

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.