dbPTM

PIAS1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PIAS1_MOUSE
UniProt AC	O88907
Protein Name	E3 SUMO-protein ligase PIAS1
Gene Name	Pias1
Organism	Mus musculus (Mouse).
Sequence Length	651
Subcellular Localization	Nucleus speckle. Nucleus, PML body . Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton..
Protein Description	Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA (By similarity). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB. [PubMed: 24061474]
Protein Sequence	MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPPTLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSAELKQ ------CCCHHHHHH	21.33	-
90	Phosphorylation	SPMPPTLSPSTIPQL CCCCCCCCCCCCCCC	21.20	17540171
105	Phosphorylation	TYDGHPASSPLLPVS CCCCCCCCCCCCCHH	36.62	25338131
229	Phosphorylation	KVNTKPCSLPGYLPP EECCEECCCCCCCCC	46.24	22942356
303	Asymmetric dimethylarginine	RLRAKGIRNPDHSRA HHHHCCCCCCHHHHH	58.24	-
463	Phosphorylation	KVEVIDLTIDSSSDE CEEEEEEEECCCCCC	20.99	25293948
466	Phosphorylation	VIDLTIDSSSDEEEE EEEEEECCCCCCCCC	28.08	26824392
467	Phosphorylation	IDLTIDSSSDEEEEE EEEEECCCCCCCCCC	37.75	26824392
468	Phosphorylation	DLTIDSSSDEEEEEP EEEECCCCCCCCCCC	53.66	26824392
480	Phosphorylation	EEPPAKRTCPSLSPT CCCCCCCCCCCCCCC	28.23	25619855
483	Phosphorylation	PAKRTCPSLSPTSPL CCCCCCCCCCCCCCC	43.56	25521595
485	Phosphorylation	KRTCPSLSPTSPLSN CCCCCCCCCCCCCCC	30.39	25521595
487	Phosphorylation	TCPSLSPTSPLSNKG CCCCCCCCCCCCCCC	39.33	22942356
488	Phosphorylation	CPSLSPTSPLSNKGI CCCCCCCCCCCCCCC	27.51	26824392
491	Phosphorylation	LSPTSPLSNKGILSL CCCCCCCCCCCCCCC	39.62	22942356
497	Phosphorylation	LSNKGILSLPHQASP CCCCCCCCCCCCCCC	37.62	26239621
503	Phosphorylation	LSLPHQASPVSRTPS CCCCCCCCCCCCCCC	21.18	25521595
506	Phosphorylation	PHQASPVSRTPSLPA CCCCCCCCCCCCCCC	33.54	22942356
508	Phosphorylation	QASPVSRTPSLPAVD CCCCCCCCCCCCCCC	15.10	25266776
510	Phosphorylation	SPVSRTPSLPAVDTS CCCCCCCCCCCCCCC	46.50	27180971
516	Phosphorylation	PSLPAVDTSYINTSL CCCCCCCCCCCCHHH	19.48	25293948
517	Phosphorylation	SLPAVDTSYINTSLI CCCCCCCCCCCHHHH	21.39	25293948
518	Phosphorylation	LPAVDTSYINTSLIQ CCCCCCCCCCHHHHC	10.57	23970565
521	Phosphorylation	VDTSYINTSLIQDYR CCCCCCCHHHHCCCC	18.49	26643407
522	Phosphorylation	DTSYINTSLIQDYRH CCCCCCHHHHCCCCC	20.98	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
90	S	Phosphorylation	Kinase	CHUK	O15111	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PIAS1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PIAS1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAP18_MOUSE	Sap18	physical	14611647
GLI1_HUMAN	GLI1	physical	14611647
GLI3_HUMAN	GLI3	physical	14611647
CI_DROME	ci	physical	14611647
SAP18_DROME	Bin1	physical	14611647
PDIA6_HUMAN	PDIA6	physical	15280358
TIM50_HUMAN	TIMM50	physical	15280358
DNJA1_HUMAN	DNAJA1	physical	15280358
ANRA2_HUMAN	ANKRA2	physical	15280358
GRP78_HUMAN	HSPA5	physical	15280358
ZNF76_HUMAN	ZNF76	physical	15280358
TBP_MOUSE	Tbp	physical	16522640
NECD_MOUSE	Ndn	physical	24911587
HECD2_MOUSE	Hectd2	physical	26157031

Drug and Disease Associations

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

Regulatory Network of PIAS1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-485 ANDTHR-487, AND MASS SPECTROMETRY.	17242355 [Abstract]