PIAS3_HUMAN - dbPTM
PIAS3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIAS3_HUMAN
UniProt AC Q9Y6X2
Protein Name E3 SUMO-protein ligase PIAS3
Gene Name PIAS3
Organism Homo sapiens (Human).
Sequence Length 628
Subcellular Localization Cytoplasm . Nucleus . Nucleus speckle . Colocalizes with MITF in the nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1 in nuclear granules.
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 and the steroid hormone signaling pathway. Involved in regulating STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. [PubMed: 21965678]
Protein Sequence MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLAPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQVQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILSSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSPVQGGDPSENKKKVEVIDLTIESSSDEEDLPPTKKHCSVTSAAIPALPGSKGVLTSGHQPSSVLRSPAMGTLGGDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDALGHFFQYRGTPSHFLGPLAPTLGSSHCSATPAPPPGRVSSIVAPGGALREGHGGPLPSGPSLTGCRSDIISLD
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 Orthologous
Protein Cluster
2Acetylation------MAELGELKH
------CCCHHHHHH		22.26-
8UbiquitinationMAELGELKHMVMSFR
CCCHHHHHHHHHHCC		25.92-
13PhosphorylationELKHMVMSFRVSELQ
HHHHHHHHCCHHHHH		9.8624719451
34UbiquitinationGRNKSGRKHELLAKA
CCCCCCCHHHHHHHH		44.98-
46SumoylationAKALHLLKSSCAPSV
HHHHHHHHHCCCCHH		46.84-
46SumoylationAKALHLLKSSCAPSV
HHHHHHHHHCCCCHH		46.8428112733
56SumoylationCAPSVQMKIKELYRR
CCCHHHHHHHHHHHH		33.27-
56UbiquitinationCAPSVQMKIKELYRR
CCCHHHHHHHHHHHH		33.27-
56SumoylationCAPSVQMKIKELYRR
CCCHHHHHHHHHHHH		33.2728112733
58SumoylationPSVQMKIKELYRRRF
CHHHHHHHHHHHHHC		35.83-
58SumoylationPSVQMKIKELYRRRF
CHHHHHHHHHHHHHC		35.83-
58UbiquitinationPSVQMKIKELYRRRF
CHHHHHHHHHHHHHC		35.83-
84PhosphorylationLLSLPPGTSPVGSPG
HHCCCCCCCCCCCCC		35.3128348404
85PhosphorylationLSLPPGTSPVGSPGP
HCCCCCCCCCCCCCC		24.4128348404
89PhosphorylationPGTSPVGSPGPLAPI
CCCCCCCCCCCCCCC		27.2428348404
165PhosphorylationAHFTFALTPQQVQQI
CCEEEECCHHHHHHH		18.6722210691
174PhosphorylationQQVQQILTSREVLPG
HHHHHHHHCCCCCCC		27.6322210691
183AcetylationREVLPGAKCDYTIQV
CCCCCCCCCCEEEEE		33.2926051181
183UbiquitinationREVLPGAKCDYTIQV
CCCCCCCCCCEEEEE		33.29-
230SumoylationPGYLPPTKNGAEPKR
CCCCCCCCCCCCCCC		60.19-
230SumoylationPGYLPPTKNGAEPKR
CCCCCCCCCCCCCCC		60.1928112733
236UbiquitinationTKNGAEPKRPSRPIN
CCCCCCCCCCCCCCC		69.33-
288SumoylationTAGTLLQKLRAKGIR
HHHHHHHHHHHCCCC		39.65-
288UbiquitinationTAGTLLQKLRAKGIR
HHHHHHHHHHHCCCC		39.65-
288SumoylationTAGTLLQKLRAKGIR
HHHHHHHHHHHCCCC		39.65-
295Asymmetric dimethylarginineKLRAKGIRNPDHSRA
HHHHCCCCCCHHHHH		58.24-
300PhosphorylationGIRNPDHSRALIKEK
CCCCCHHHHHHHHHH		26.9922964224
305UbiquitinationDHSRALIKEKLTADP
HHHHHHHHHHHCCCC		50.04-
307UbiquitinationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.2521906983
307SumoylationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.25-
307SumoylationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.2528112733
331SumoylationSLMCPLGKMRLTVPC
EEECCCCCCEEECCC		28.64-
331UbiquitinationSLMCPLGKMRLTVPC
EEECCCCCCEEECCC		28.64-
331SumoylationSLMCPLGKMRLTVPC
EEECCCCCCEEECCC		28.64-
361SumoylationYLQMNEKKPTWTCPV
HHHCCCCCCCEECCC		41.31-
361SumoylationYLQMNEKKPTWTCPV
HHHCCCCCCCEECCC		41.31-
372UbiquitinationTCPVCDKKAPYESLI
ECCCCCCCCCHHHEE		41.15-
415PhosphorylationMKPKKEASEVCPPPG
CCCCCCHHCCCCCCC		31.4923312004
423PhosphorylationEVCPPPGYGLDGLQY
CCCCCCCCCCCCCCC		21.9329978859
430PhosphorylationYGLDGLQYSPVQGGD
CCCCCCCCCCCCCCC		21.7125159151
431PhosphorylationGLDGLQYSPVQGGDP
CCCCCCCCCCCCCCC		12.9725849741
439PhosphorylationPVQGGDPSENKKKVE
CCCCCCCCCCCCEEE		59.5529978859
442UbiquitinationGGDPSENKKKVEVID
CCCCCCCCCEEEEEE		50.33-
443UbiquitinationGDPSENKKKVEVIDL
CCCCCCCCEEEEEEE		73.89-
451PhosphorylationKVEVIDLTIESSSDE
EEEEEEEEEECCCCC		20.9628102081
454PhosphorylationVIDLTIESSSDEEDL
EEEEEEECCCCCCCC		31.1528102081
455PhosphorylationIDLTIESSSDEEDLP
EEEEEECCCCCCCCC		29.0828102081
456PhosphorylationDLTIESSSDEEDLPP
EEEEECCCCCCCCCC		59.3228102081
464PhosphorylationDEEDLPPTKKHCSVT
CCCCCCCCCCCCCCC		51.2728102081
466SumoylationEDLPPTKKHCSVTSA
CCCCCCCCCCCCCCC		52.9328112733
466UbiquitinationEDLPPTKKHCSVTSA
CCCCCCCCCCCCCCC		52.93-
469PhosphorylationPPTKKHCSVTSAAIP
CCCCCCCCCCCCCCC		28.3123532336
471PhosphorylationTKKHCSVTSAAIPAL
CCCCCCCCCCCCCCC		9.0623532336
472PhosphorylationKKHCSVTSAAIPALP
CCCCCCCCCCCCCCC		17.3423532336
482UbiquitinationIPALPGSKGVLTSGH
CCCCCCCCCCCCCCC		59.98-
482SumoylationIPALPGSKGVLTSGH
CCCCCCCCCCCCCCC		59.9828112733
492PhosphorylationLTSGHQPSSVLRSPA
CCCCCCCCHHHCCCC		26.89-
497PhosphorylationQPSSVLRSPAMGTLG
CCCHHHCCCCCCCCC		16.9223532336
595PhosphorylationPPPGRVSSIVAPGGA
CCCCCEEEEEECCCC		20.4428857561
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
-KUbiquitinationE3 ubiquitin ligaseTRIM32Q13049
PMID:17987106
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIAS3_HUMAN !!
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 PIAS3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
15140884
SMAD2_HUMANSMAD2physical
14691252
SMAD3_HUMANSMAD3physical
14691252
SMAD4_HUMANSMAD4physical
14691252
MITF_HUMANMITFphysical
11709556
HMGA2_HUMANHMGA2physical
11390395
GFI1_HUMANGFI1physical
11060035
TRI32_HUMANTRIM32physical
17987106
ZMIZ2_HUMANZMIZ2physical
20159969
CHSP1_HUMANCARHSP1physical
21900206
UBA1_HUMANUBA1physical
21900206
PRS4_HUMANPSMC1physical
21900206
CS060_HUMANC19orf60physical
21900206
RAC1_HUMANRAC1physical
20935639
STAT3_HUMANSTAT3physical
12804609
STAT3_MOUSEStat3physical
9388184
STAT3_HUMANSTAT3physical
9724754
ZPI_HUMANSERPINA10physical
21988832
STAT3_HUMANSTAT3physical
21988832
UBC9_HUMANUBE2Iphysical
21988832
TAB2_HUMANTAB2physical
24096733
HIC1_HUMANHIC1physical
23704280
TF65_HUMANRELAphysical
22649547
BC11A_HUMANBCL11Aphysical
18681895
SMUF2_HUMANSMURF2physical
26679521
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIAS3_HUMAN

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Related Literatures of Post-Translational Modification

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