PIAS2_HUMAN - dbPTM
PIAS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIAS2_HUMAN
UniProt AC O75928
Protein Name E3 SUMO-protein ligase PIAS2
Gene Name PIAS2
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Nucleus speckle . Nucleus, PML body . Nucleus . Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (PubMed:22406621). Colocalizes with SUMO1 in nuclear granules (By similarity).
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 coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'..
Protein Sequence MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGGSSPVEPDLAVAGIHSLPSTSVTPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVSSQPCTKIESSSVLSKPCSVTVASEASKKKVDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPISSMSSDLPGLDFLSLIPVDPQYCPPMFLDSLTSPLTASSTSVTTTSSHESSTHVSSSSSRSETGVITSSGSNIPDIISLD
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
12PhosphorylationEELRNMVSSFRVSEL
HHHHHHHHHHCHHHH		17.0029414761
17PhosphorylationMVSSFRVSELQVLLG
HHHHHCHHHHHHHHH		28.47-
34UbiquitinationGRNKSGRKHDLLMRA
CCCCCCCHHHHHHHH		45.02-
46SumoylationMRALHLLKSGCSPAV
HHHHHHHHCCCCHHH		51.6828112733
46UbiquitinationMRALHLLKSGCSPAV
HHHHHHHHCCCCHHH		51.68-
50PhosphorylationHLLKSGCSPAVQIKI
HHHHCCCCHHHHHHH		21.3021815630
76PhosphorylationLEGLSDLSTIKSSVF
CCCCCCHHHHCCCEE		32.8328555341
103PhosphorylationLAVAGIHSLPSTSVT
EEEEECCCCCCCCCC		39.8026074081
106PhosphorylationAGIHSLPSTSVTPHS
EECCCCCCCCCCCCC		38.3126074081
107PhosphorylationGIHSLPSTSVTPHSP
ECCCCCCCCCCCCCC		25.8526074081
108PhosphorylationIHSLPSTSVTPHSPS
CCCCCCCCCCCCCCC		28.4726074081
110PhosphorylationSLPSTSVTPHSPSSP
CCCCCCCCCCCCCCC		18.3026074081
113PhosphorylationSTSVTPHSPSSPVGS
CCCCCCCCCCCCCCC		27.9026074081
115PhosphorylationSVTPHSPSSPVGSVL
CCCCCCCCCCCCCEE		50.7326074081
116PhosphorylationVTPHSPSSPVGSVLL
CCCCCCCCCCCCEEE		27.3026074081
120PhosphorylationSPSSPVGSVLLQDTK
CCCCCCCCEEEECCC		15.1526074081
127SumoylationSVLLQDTKPTFEMQQ
CEEEECCCCCCCCCC		50.80-
129PhosphorylationLLQDTKPTFEMQQPS
EEECCCCCCCCCCCC		33.5128122231
136PhosphorylationTFEMQQPSPPIPPVH
CCCCCCCCCCCCCCC		38.6826074081
162SumoylationDVLDVLIKPTSLVQS
HHHHHHHCCCHHHHH		37.77-
162SumoylationDVLDVLIKPTSLVQS
HHHHHHHCCCHHHHH		37.77-
162UbiquitinationDVLDVLIKPTSLVQS
HHHHHHHCCCHHHHH		37.77-
205PhosphorylationLPGGRRDYTVQVQLR
CCCCCCCEEEEEHEE		13.6522985185
206PhosphorylationPGGRRDYTVQVQLRL
CCCCCCEEEEEHEEH		14.5722985185
244PhosphorylationKLFPLPGYAPPPKNG
EEECCCCCCCCCCCC		17.6228152594
249UbiquitinationPGYAPPPKNGIEQKR
CCCCCCCCCCCCCCC		73.84-
249SumoylationPGYAPPPKNGIEQKR
CCCCCCCCCCCCCCC		73.8428112733
249SumoylationPGYAPPPKNGIEQKR
CCCCCCCCCCCCCCC		73.84-
264PhosphorylationPGRPLNITSLVRLSS
CCCCCCHHHEEEHHH		18.2222210691
265PhosphorylationGRPLNITSLVRLSSA
CCCCCHHHEEEHHHC		22.5222210691
292PhosphorylationIGKNYSMSVYLVRQL
CCCCCCCHHHHHHHH		11.1530631047
301PhosphorylationYLVRQLTSAMLLQRL
HHHHHHHHHHHHHHH		21.9230631047
319PhosphorylationGIRNPDHSRALIKEK
CCCCCHHHHHHHHHH		26.9922964224
324UbiquitinationDHSRALIKEKLTADP
HHHHHHHHHHHCCCC		50.04-
326SumoylationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.25-
326UbiquitinationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.25-
326 (in isoform 1)Ubiquitination-46.2521906983
326 (in isoform 2)Ubiquitination-46.2521906983
326SumoylationSRALIKEKLTADPDS
HHHHHHHHHCCCCCC		46.25-
330 (in isoform 3)Ubiquitination-42.1621906983
338PhosphorylationPDSEIATTSLRVSLM
CCCHHHCCEEEEEEE		19.42-
339PhosphorylationDSEIATTSLRVSLMC
CCHHHCCEEEEEEEC		15.15-
350SumoylationSLMCPLGKMRLTIPC
EEECCCCCCEEEECC		28.64-
350SumoylationSLMCPLGKMRLTIPC
EEECCCCCCEEEECC		28.64-
350UbiquitinationSLMCPLGKMRLTIPC
EEECCCCCCEEEECC		28.64-
380SumoylationYLQMNEKKPTWICPV
HHHCCCCCCCEEECC		41.31-
380SumoylationYLQMNEKKPTWICPV
HHHCCCCCCCEEECC		41.31-
430SumoylationSWCPMRPKKEAMKVS
CCCCCCCHHHHCCCC		53.5328112733
430SumoylationSWCPMRPKKEAMKVS
CCCCCCCHHHHCCCC		53.53-
430UbiquitinationSWCPMRPKKEAMKVS
CCCCCCCHHHHCCCC		53.53-
435UbiquitinationRPKKEAMKVSSQPCT
CCHHHHCCCCCCCCC		46.11-
435SumoylationRPKKEAMKVSSQPCT
CCHHHHCCCCCCCCC		46.1128112733
437PhosphorylationKKEAMKVSSQPCTKI
HHHHCCCCCCCCCEE		20.1030622161
438PhosphorylationKEAMKVSSQPCTKIE
HHHCCCCCCCCCEEC		40.9230622161
443UbiquitinationVSSQPCTKIESSSVL
CCCCCCCEECCCCCC		51.71-
443SumoylationVSSQPCTKIESSSVL
CCCCCCCEECCCCCC		51.7128112733
443SumoylationVSSQPCTKIESSSVL
CCCCCCCEECCCCCC		51.71-
446PhosphorylationQPCTKIESSSVLSKP
CCCCEECCCCCCCCC		31.2430622161
447PhosphorylationPCTKIESSSVLSKPC
CCCEECCCCCCCCCE		16.2130622161
448PhosphorylationCTKIESSSVLSKPCS
CCEECCCCCCCCCEE		36.0330622161
451PhosphorylationIESSSVLSKPCSVTV
ECCCCCCCCCEEEEE		32.1830622161
452SumoylationESSSVLSKPCSVTVA
CCCCCCCCCEEEEEC		45.9728112733
452UbiquitinationESSSVLSKPCSVTVA
CCCCCCCCCEEEEEC		45.97-
452SumoylationESSSVLSKPCSVTVA
CCCCCCCCCEEEEEC		45.97-
452AcetylationESSSVLSKPCSVTVA
CCCCCCCCCEEEEEC		45.9725953088
455PhosphorylationSVLSKPCSVTVASEA
CCCCCCEEEEECCHH		29.3830622161
457PhosphorylationLSKPCSVTVASEASK
CCCCEEEEECCHHHC		8.2830622161
460PhosphorylationPCSVTVASEASKKKV
CEEEEECCHHHCCCE		29.3825693802
463PhosphorylationVTVASEASKKKVDVI
EEECCHHHCCCEEEE		40.7425693802
464SumoylationTVASEASKKKVDVID
EECCHHHCCCEEEEE		64.76-
464UbiquitinationTVASEASKKKVDVID
EECCHHHCCCEEEEE		64.76-
464AcetylationTVASEASKKKVDVID
EECCHHHCCCEEEEE		64.7625953088
464SumoylationTVASEASKKKVDVID
EECCHHHCCCEEEEE		64.76-
465UbiquitinationVASEASKKKVDVIDL
ECCHHHCCCEEEEEE		56.38-
473PhosphorylationKVDVIDLTIESSSDE
CEEEEEEEECCCCCC		20.9629514088
476PhosphorylationVIDLTIESSSDEEED
EEEEEECCCCCCCCC		31.1520363803
477PhosphorylationIDLTIESSSDEEEDP
EEEEECCCCCCCCCC		29.0820363803
478PhosphorylationDLTIESSSDEEEDPP
EEEECCCCCCCCCCC		59.3220363803
489SumoylationEDPPAKRKCIFMSET
CCCCCCCEEEEEECC		30.86-
489SumoylationEDPPAKRKCIFMSET
CCCCCCCEEEEEECC		30.8628112733
494PhosphorylationKRKCIFMSETQSSPT
CCEEEEEECCCCCCC		27.0923401153
496PhosphorylationKCIFMSETQSSPTKG
EEEEEECCCCCCCCC		26.8323401153
498PhosphorylationIFMSETQSSPTKGVL
EEEECCCCCCCCCEE		45.7830266825
499PhosphorylationFMSETQSSPTKGVLM
EEECCCCCCCCCEEE		27.1123401153
501PhosphorylationSETQSSPTKGVLMYQ
ECCCCCCCCCEEEEC		42.2430266825
502SumoylationETQSSPTKGVLMYQP
CCCCCCCCCEEEECC		50.8628112733
507PhosphorylationPTKGVLMYQPSSVRV
CCCCEEEECCCCEEC		17.0827642862
539PhosphorylationYSVPFHHTPISSMSS
CCCCCCCCCCHHHCC		17.4725627689
539 (in isoform 2)Phosphorylation-17.4725159151
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 ligaseHUWE1Q7Z6Z7
PMID:20624960
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIAS2_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 PIAS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAV2_HUMANNAV2physical
16189514
DNM3A_HUMANDNMT3Aphysical
14752048
STAT4_HUMANSTAT4physical
12716907
ANDR_HUMANARphysical
9920921
ANDR_HUMANARphysical
11117529
ESR1_HUMANESR1physical
11117529
ESR2_HUMANESR2physical
11117529
GCR_HUMANNR3C1physical
11117529
PRGR_HUMANPGRphysical
11117529
GT2D1_HUMANGTF2IRD1physical
12193603
MITF_HUMANMITFphysical
16029420
JUN_HUMANJUNphysical
11867732
P53_HUMANTP53physical
11867732
HIC1_HUMANHIC1physical
17283066
HUWE1_HUMANHUWE1physical
20624960
MK08_HUMANMAPK8physical
19815509
TRAF2_HUMANTRAF2physical
22184250
PML_HUMANPMLphysical
21779164
IFIH1_HUMANIFIH1physical
21156324
PML_HUMANPMLphysical
22406621
FLI1_HUMANFLI1physical
16148010
CDN2A_HUMANCDKN2Aphysical
20308430
ARF_HUMANCDKN2Aphysical
20308430
SMAD3_HUMANSMAD3physical
16777850
SMAD4_HUMANSMAD4physical
16777850
MSX2_HUMANMSX2physical
9256341
PLAG1_HUMANPLAG1physical
15208321
PLAL1_HUMANPLAGL1physical
15208321
RUFY1_HUMANRUFY1physical
21988832
SUMO1_HUMANSUMO1physical
21988832
UBC9_HUMANUBE2Iphysical
21988832
PIAS4_HUMANPIAS4physical
21988832
TCAM2_HUMANTICAM2physical
21988832
HIC1_HUMANHIC1physical
23704280
P53_HUMANTP53physical
19339993
PIAS2_HUMANPIAS2physical
25416956
ZBED1_HUMANZBED1physical
25416956
CCDB1_HUMANCCNDBP1physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
NAV2_HUMANNAV2physical
25416956
TSR2_HUMANTSR2physical
25416956
ACY3_HUMANACY3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
ARNT_HUMANARNTphysical
24618291
UBC9_HUMANUBE2Iphysical
16148010
UBC9_HUMANUBE2Iphysical
11867732
PIAS2_HUMANPIAS2physical
11867732
CDN2B_HUMANCDKN2Bphysical
25241761
PIAS1_HUMANPIAS1physical
25241761
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 PIAS2_HUMAN

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