ZN131_HUMAN - dbPTM
ZN131_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN131_HUMAN
UniProt AC P52739
Protein Name Zinc finger protein 131
Gene Name ZNF131
Organism Homo sapiens (Human).
Sequence Length 623
Subcellular Localization Nucleus . Sumoylation does not affect nuclear localization.
Protein Description Plays a role during development and organogenesis as well as in the function of the adult central nervous system (By similarity). May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling..
Protein Sequence MEAEETMECLQEFPEHHKMILDRLNEQREQDRFTDITLIVDGHHFKAHKAVLAACSKFFYKFFQEFTQEPLVEIEGVSKMAFRHLIEFTYTAKLMIQGEEEANDVWKAAEFLQMLEAIKALEVRNKENSAPLEENTTGKNEAKKRKIAETSNVITESLPSAESEPVEIEVEIAEGTIEVEDEGIETLEEVASAKQSVKYIQSTGSSDDSALALLADITSKYRQGDRKGQIKEDGCPSDPTSKQVEGIEIVELQLSHVKDLFHCEKCNRSFKLFYHFKEHMKSHSTESFKCEICNKRYLRESAWKQHLNCYHLEEGGVSKKQRTGKKIHVCQYCEKQFDHFGHFKEHLRKHTGEKPFECPNCHERFARNSTLKCHLTACQTGVGAKKGRKKLYECQVCNSVFNSWDQFKDHLVIHTGDKPNHCTLCDLWFMQGNELRRHLSDAHNISERLVTEEVLSVETRVQTEPVTSMTIIEQVGKVHVLPLLQVQVDSAQVTVEQVHPDLLQDSQVHDSHMSELPEQVQVSYLEVGRIQTEEGTEVHVEELHVERVNQMPVEVQTELLEADLDHVTPEIMNQEERESSQADAAEAAREDHEDAEDLETKPTVDSEAEKAENEDRTALPVLE
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
18UbiquitinationQEFPEHHKMILDRLN
HHCHHHHHHHHHHHH		29.55-
49UbiquitinationGHHFKAHKAVLAACS
CCHHHHHHHHHHHHH		45.08-
57AcetylationAVLAACSKFFYKFFQ
HHHHHHHHHHHHHHH		39.1026051181
93AcetylationIEFTYTAKLMIQGEE
HHHEEEEEEEECCHH		30.6830593573
126UbiquitinationKALEVRNKENSAPLE
HHHHHCCCCCCCCCC		47.94-
139AcetylationLEENTTGKNEAKKRK
CCCCCCCCHHHHHHH		49.9026051181
198UbiquitinationASAKQSVKYIQSTGS
HHHHHHHHHHHCCCC		41.71-
203PhosphorylationSVKYIQSTGSSDDSA
HHHHHHCCCCCCHHH		25.3828348404
205PhosphorylationKYIQSTGSSDDSALA
HHHHCCCCCCHHHHH		30.5928348404
206PhosphorylationYIQSTGSSDDSALAL
HHHCCCCCCHHHHHH		46.9426657352
209PhosphorylationSTGSSDDSALALLAD
CCCCCCHHHHHHHHH		30.1228348404
218PhosphorylationLALLADITSKYRQGD
HHHHHHHHHHHCCCC		21.51-
219PhosphorylationALLADITSKYRQGDR
HHHHHHHHHHCCCCC		28.20-
220UbiquitinationLLADITSKYRQGDRK
HHHHHHHHHCCCCCC		35.48-
231UbiquitinationGDRKGQIKEDGCPSD
CCCCCCCCCCCCCCC		41.69-
237PhosphorylationIKEDGCPSDPTSKQV
CCCCCCCCCCCCCCC		61.3728985074
265UbiquitinationKDLFHCEKCNRSFKL
HHHHCCHHCCCHHHE		42.05-
282PhosphorylationHFKEHMKSHSTESFK
HHHHHHHHCCCCCCE		18.3325278378
284PhosphorylationKEHMKSHSTESFKCE
HHHHHHCCCCCCEEE		40.7525278378
285PhosphorylationEHMKSHSTESFKCEI
HHHHHCCCCCCEEEE		30.1725278378
287PhosphorylationMKSHSTESFKCEICN
HHHCCCCCCEEEECC		30.0525278378
289SumoylationSHSTESFKCEICNKR
HCCCCCCEEEECCHH		39.99-
289SumoylationSHSTESFKCEICNKR
HCCCCCCEEEECCHH		39.9928112733
289UbiquitinationSHSTESFKCEICNKR
HCCCCCCEEEECCHH		39.99-
295SumoylationFKCEICNKRYLRESA
CEEEECCHHHHCHHH		37.7028112733
319UbiquitinationLEEGGVSKKQRTGKK
HHHCCCCCCCCCCCE		50.98-
320UbiquitinationEEGGVSKKQRTGKKI
HHCCCCCCCCCCCEE		37.19-
325AcetylationSKKQRTGKKIHVCQY
CCCCCCCCEEEEHHH		48.1920167786
326UbiquitinationKKQRTGKKIHVCQYC
CCCCCCCEEEEHHHH		39.11-
344UbiquitinationFDHFGHFKEHLRKHT
CCCCHHHHHHHHHHC		38.25-
351PhosphorylationKEHLRKHTGEKPFEC
HHHHHHHCCCCCCCC		50.5028985074
354UbiquitinationLRKHTGEKPFECPNC
HHHHCCCCCCCCCCH		57.25-
372MethylationFARNSTLKCHLTACQ
HHHCCCCCEEEEHHH		21.5083047019
372UbiquitinationFARNSTLKCHLTACQ
HHHCCCCCEEEEHHH		21.50-
385UbiquitinationCQTGVGAKKGRKKLY
HHCCCCCCCCCCCCC		50.24-
385AcetylationCQTGVGAKKGRKKLY
HHCCCCCCCCCCCCC		50.2423749302
386UbiquitinationQTGVGAKKGRKKLYE
HCCCCCCCCCCCCCC		64.51-
440PhosphorylationNELRRHLSDAHNISE
HHHHHHHHHHCCHHH		26.9927732954
467PhosphorylationRVQTEPVTSMTIIEQ
EEECCCCCEEEEEEE		24.4028555341
468PhosphorylationVQTEPVTSMTIIEQV
EECCCCCEEEEEEEC		17.7328555341
470PhosphorylationTEPVTSMTIIEQVGK
CCCCCEEEEEEECCC		20.6928555341
568PhosphorylationEADLDHVTPEIMNQE
HCCCCCCCHHHHCHH		16.2828348404
579PhosphorylationMNQEERESSQADAAE
HCHHHHHHHHHHHHH		33.6923663014
580PhosphorylationNQEERESSQADAAEA
CHHHHHHHHHHHHHH		25.3223663014
600PhosphorylationEDAEDLETKPTVDSE
CCHHHHCCCCCCCHH		50.0123186163
601SumoylationDAEDLETKPTVDSEA
CHHHHCCCCCCCHHH		29.34-
603PhosphorylationEDLETKPTVDSEAEK
HHHCCCCCCCHHHHH		38.2023186163
606PhosphorylationETKPTVDSEAEKAEN
CCCCCCCHHHHHHHC		34.0823186163
617PhosphorylationKAENEDRTALPVLE-
HHHCCCCCCCCCCC-		44.8820860994
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

Oops, there are no upstream regulatory protein records of ZN131_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
601KSumoylation

22467880
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 ZN131_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX4_HUMANCBX4physical
22467880
UHRF2_HUMANUHRF2physical
23404503
ESR1_HUMANESR1physical
23159625
RM28_HUMANMRPL28physical
26841866
ZN281_HUMANZNF281physical
26841866
EXOS3_HUMANEXOSC3physical
26841866
RARA_HUMANRARAphysical
26841866
CBX6_HUMANCBX6physical
26841866
NSUN4_HUMANNSUN4physical
26841866
SMD3_HUMANSNRPD3physical
26841866
SENP5_HUMANSENP5physical
26841866
INP4B_HUMANINPP4Bphysical
26841866
PRPF3_HUMANPRPF3physical
26841866
KMT2A_HUMANKMT2Aphysical
26841866
K1109_HUMANKIAA1109physical
26841866
CBX4_HUMANCBX4physical
26841866
TRAD1_HUMANTRAFD1physical
26841866
DNJA2_HUMANDNAJA2physical
26841866
KDM4A_HUMANKDM4Aphysical
26841866
SIN3B_HUMANSIN3Bphysical
26841866
AGR2_HUMANAGR2physical
26841866
KITH_HUMANTK1physical
26841866
LEG1_HUMANLGALS1physical
26841866
RPB1_HUMANPOLR2Aphysical
26841866
KDM5A_HUMANKDM5Aphysical
26841866
TXLNA_HUMANTXLNAphysical
26841866
RS27_HUMANRPS27physical
26841866
ZN131_HUMANZNF131physical
26841866
MTPN_HUMANMTPNphysical
26841866
SC61B_HUMANSEC61Bphysical
26841866
TPM4_HUMANTPM4physical
26841866
RUNX1_HUMANRUNX1physical
26841866
AHNK_HUMANAHNAKphysical
26841866
LTBP1_HUMANLTBP1physical
26841866
RB39A_HUMANRAB39Aphysical
26841866
RAB6A_HUMANRAB6Aphysical
26841866
RAB6B_HUMANRAB6Bphysical
26841866
EMSY_HUMANC11orf30physical
26841866
ZMYM1_HUMANZMYM1physical
26841866
FBX31_HUMANFBXO31physical
26841866
PWP2B_HUMANPWWP2Bphysical
26841866
RIR2B_HUMANRRM2Bphysical
26841866
XRN1_HUMANXRN1physical
26841866
PHC3_HUMANPHC3physical
26841866
GATD1_HUMANGATAD1physical
26841866
NEUG_HUMANNRGNphysical
26841866
ZBT45_HUMANZBTB45physical
26841866
TIGD1_HUMANTIGD1physical
26841866
PHF12_HUMANPHF12physical
26841866
RING2_HUMANRNF2physical
26841866
NTM1A_HUMANNTMT1physical
26841866
DPY30_HUMANDPY30physical
26841866
ZBTB3_HUMANZBTB3physical
26841866
XPO5_HUMANXPO5physical
26841866
MRM3_HUMANRNMTL1physical
26841866
RBM22_HUMANRBM22physical
26841866
NHP2_HUMANNHP2physical
26841866
MRM2_HUMANFTSJ2physical
26841866
KMT2B_HUMANKMT2Bphysical
26841866
HCFC2_HUMANHCFC2physical
26841866
GBB3_HUMANGNB3physical
28514442
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 ZN131_HUMAN

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Related Literatures of Post-Translational Modification

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