PIAS4_HUMAN - dbPTM
PIAS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIAS4_HUMAN
UniProt AC Q8N2W9
Protein Name E3 SUMO-protein ligase PIAS4
Gene Name PIAS4
Organism Homo sapiens (Human).
Sequence Length 510
Subcellular Localization Nucleus, PML body . Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.
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/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation..
Protein Sequence MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKNSEPAPQPHRPLDPLTMHSTYDRAGAVPRTPLAGPNIDYPVLYGKYLNGLGRLPAKTLKPEVRLVKLPFFNMLDELLKPTELVPQNNEKLQESPCIFALTPRQVELIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSELLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAPYDQLIIDGLLSKILSECEDADEIEYLVDGSWCPIRAEKERSCSPQGAILVLGPSDANGLLPAPSVNGSGALGSTGGGGPVGSMENGKPGADVVDLTLDSSSSSEDEEEEEEEEEDEDEEGPRPKRRCPFQKGLVPAC
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------MAAELVEAK
------CCHHHHHHH		15.0519413330
9SumoylationAAELVEAKNMVMSFR
CHHHHHHHHHHEEEE		31.88-
9UbiquitinationAAELVEAKNMVMSFR
CHHHHHHHHHHEEEE		31.88-
9SumoylationAAELVEAKNMVMSFR
CHHHHHHHHHHEEEE		31.8828112733
14PhosphorylationEAKNMVMSFRVSDLQ
HHHHHHEEEEHHHHH		9.8624719451
18PhosphorylationMVMSFRVSDLQMLLG
HHEEEEHHHHHHHHH		28.48-
31UbiquitinationLGFVGRSKSGLKHEL
HHHHCCCCCCCCHHH		47.37-
35SumoylationGRSKSGLKHELVTRA
CCCCCCCCHHHHHHH		38.26-
35UbiquitinationGRSKSGLKHELVTRA
CCCCCCCCHHHHHHH		38.26-
35SumoylationGRSKSGLKHELVTRA
CCCCCCCCHHHHHHH		38.2628112733
51PhosphorylationQLVQFDCSPELFKKI
HHHHCCCCHHHHHHH		24.2126714015
56UbiquitinationDCSPELFKKIKELYE
CCCHHHHHHHHHHHH		67.24-
56SumoylationDCSPELFKKIKELYE
CCCHHHHHHHHHHHH		67.2428112733
57UbiquitinationCSPELFKKIKELYET
CCHHHHHHHHHHHHH		52.23-
59SumoylationPELFKKIKELYETRY
HHHHHHHHHHHHHHH		51.01-
59UbiquitinationPELFKKIKELYETRY
HHHHHHHHHHHHHHH		51.01-
59SumoylationPELFKKIKELYETRY
HHHHHHHHHHHHHHH		51.0128112733
68UbiquitinationLYETRYAKKNSEPAP
HHHHHHHHHCCCCCC		43.48-
68SumoylationLYETRYAKKNSEPAP
HHHHHHHHHCCCCCC		43.4828112733
69SumoylationYETRYAKKNSEPAPQ
HHHHHHHHCCCCCCC		58.4928112733
69UbiquitinationYETRYAKKNSEPAPQ
HHHHHHHHCCCCCCC		58.49-
69SumoylationYETRYAKKNSEPAPQ
HHHHHHHHCCCCCCC		58.49-
99PhosphorylationRAGAVPRTPLAGPNI
CCCCCCCCCCCCCCC		19.3129978859
108PhosphorylationLAGPNIDYPVLYGKY
CCCCCCCCCHHHHHH		7.4617360941
112PhosphorylationNIDYPVLYGKYLNGL
CCCCCHHHHHHHCCC		16.2924260401
114UbiquitinationDYPVLYGKYLNGLGR
CCCHHHHHHHCCCCC		32.7621906983
114AcetylationDYPVLYGKYLNGLGR
CCCHHHHHHHCCCCC		32.7619608861
125AcetylationGLGRLPAKTLKPEVR
CCCCCCCCCCCCCEE		53.0723749302
125SumoylationGLGRLPAKTLKPEVR
CCCCCCCCCCCCCEE		53.0728112733
125UbiquitinationGLGRLPAKTLKPEVR
CCCCCCCCCCCCCEE		53.0719608861
128SumoylationRLPAKTLKPEVRLVK
CCCCCCCCCCEEEEE		44.35-
128SumoylationRLPAKTLKPEVRLVK
CCCCCCCCCCEEEEE		44.35-
128UbiquitinationRLPAKTLKPEVRLVK
CCCCCCCCCCEEEEE		44.35-
135SumoylationKPEVRLVKLPFFNML
CCCEEEEECHHHHHH		55.84-
135SumoylationKPEVRLVKLPFFNML
CCCEEEEECHHHHHH		55.84-
158UbiquitinationLVPQNNEKLQESPCI
CCCCCCHHHCCCCCE		58.56-
187UbiquitinationRELQPGVKAVQVVLR
CCCCCCCCHHHHHHH		49.07-
219PhosphorylationIAVKVNHSYCSVPGY
EEEEECCCCCCCCCC		23.7228348404
222PhosphorylationKVNHSYCSVPGYYPS
EECCCCCCCCCCCCC		24.1028348404
229PhosphorylationSVPGYYPSNKPGVEP
CCCCCCCCCCCCCCC		41.1728348404
231SumoylationPGYYPSNKPGVEPKR
CCCCCCCCCCCCCCC		47.70-
231SumoylationPGYYPSNKPGVEPKR
CCCCCCCCCCCCCCC		47.70-
231UbiquitinationPGYYPSNKPGVEPKR
CCCCCCCCCCCCCCC		47.70-
274PhosphorylationKSYSVALYLVRQLTS
CHHHHHHHHHHHCCC		8.0719413330
294UbiquitinationRLKTIGVKHPELCKA
HHHHHCCCCHHHHHH		48.51-
300UbiquitinationVKHPELCKALVKEKL
CCCHHHHHHHHHHHH		58.33-
306SumoylationCKALVKEKLRLDPDS
HHHHHHHHHCCCCCC		32.94-
306SumoylationCKALVKEKLRLDPDS
HHHHHHHHHCCCCCC		32.94-
306UbiquitinationCKALVKEKLRLDPDS
HHHHHHHHHCCCCCC		32.94-
330UbiquitinationSLICPLVKMRLSVPC
ECCCCHHCCCCCCCC		26.45-
360UbiquitinationYLQMNEKKPTWMCPV
HHHCCCCCCCEEECC		41.31-
384PhosphorylationLIIDGLLSKILSECE
HHHHHHHHHHHHHCC		23.7724719451
403PhosphorylationIEYLVDGSWCPIRAE
CEEEECCCCCCCHHH		22.5026074081
411UbiquitinationWCPIRAEKERSCSPQ
CCCCHHHCCCCCCCC		58.40-
414PhosphorylationIRAEKERSCSPQGAI
CHHHCCCCCCCCCCE		21.7526074081
416PhosphorylationAEKERSCSPQGAILV
HHCCCCCCCCCCEEE		22.8526074081
427PhosphorylationAILVLGPSDANGLLP
CEEEECCCCCCCCCC		47.7826074081
504AcetylationKRRCPFQKGLVPAC-
CCCCCCCCCCCCCC-		55.3725953088
504UbiquitinationKRRCPFQKGLVPAC-
CCCCCCCCCCCCCC-		55.37-
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
18SPhosphorylationKinasePRKCZQ05513
GPS
-KUbiquitinationE3 ubiquitin ligaseTRIM32Q13049
PMID:16816390
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
35KSumoylation

12727872
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 PIAS4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEF1_HUMANLEF1physical
11731474
SMAD7_HUMANSMAD7physical
12815042
SMAD6_HUMANSMAD6physical
12815042
SMAD2_HUMANSMAD2physical
12815042
SMAD3_HUMANSMAD3physical
12815042
SMAD4_HUMANSMAD4physical
12815042
ZMIZ2_HUMANZMIZ2physical
20159969
BRCA1_HUMANBRCA1physical
20016594
PARP1_HUMANPARP1physical
19779455
SMAD1_HUMANSMAD1physical
12904571
SMAD2_HUMANSMAD2physical
12904571
SMAD3_HUMANSMAD3physical
12904571
SMAD4_HUMANSMAD4physical
12904571
SMAD4_HUMANSMAD4physical
12740389
ANDR_HUMANARphysical
14981544
HDAC1_HUMANHDAC1physical
14981544
HDAC2_HUMANHDAC2physical
14981544
TGM2_HUMANTGM2physical
19625650
KNTC1_HUMANKNTC1physical
20696768
ZW10_HUMANZW10physical
20696768
KPCZ_HUMANPRKCZphysical
21624955
ETS1_HUMANETS1physical
16862185
HERC2_HUMANHERC2physical
22508508
MDC1_HUMANMDC1physical
22661230
VHL_HUMANVHLphysical
20300531
NEMO_HUMANIKBKGphysical
16906147
HD_HUMANHTTphysical
15383276
MLP3A_HUMANMAP1LC3Aphysical
15383276
LRIF1_HUMANLRIF1physical
15383276
PR40A_HUMANPRPF40Aphysical
15383276
ITF2_HUMANTCF4physical
15831457
PLAG1_HUMANPLAG1physical
15208321
TCAM1_HUMANTICAM1physical
15251447
IRF3_HUMANIRF3physical
15251447
IRF7_HUMANIRF7physical
15251447
IPSP_HUMANSERPINA5physical
21988832
UBC9_HUMANUBE2Iphysical
21988832
EVI1_HUMANMECOMphysical
23770046
PDE4A_HUMANPDE4Aphysical
20196770
PDE4D_HUMANPDE4Dphysical
20196770
VHL_HUMANVHLphysical
24002598
HIC1_HUMANHIC1physical
23704280
HNF4A_HUMANHNF4Aphysical
12727872
UBC9_HUMANUBE2Iphysical
12727872
VHL_HUMANVHLphysical
20844582
UBC9_HUMANUBE2Iphysical
22661230
TOP2A_HUMANTOP2Aphysical
20696768
PARP1_HUMANPARP1physical
20696768
UBC9_HUMANUBE2Iphysical
20696768
IF2P_HUMANEIF5Bphysical
26344197
AREL1_HUMANAREL1physical
27162139
KPCZ_HUMANPRKCZphysical
27162139
FANCA_HUMANFANCAphysical
28215707
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 PIAS4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-125, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4.";
Ihara M., Yamamoto H., Kikuchi A.;
Mol. Cell. Biol. 25:3506-3518(2005).
Cited for: SUMOYLATION AT LYS-35 AND LYS-128, FUNCTION IN TCF4 SUMOYLATION,SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-35 AND LYS-128.

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