ZN451_MOUSE - dbPTM
ZN451_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN451_MOUSE
UniProt AC Q8C0P7
Protein Name E3 SUMO-protein ligase ZNF451 {ECO:0000305|PubMed:26524493}
Gene Name Znf451
Organism Mus musculus (Mouse).
Sequence Length 1056
Subcellular Localization Nucleus . Nucleus, PML body . Nucleus, nucleoplasm . Colocalizes with UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules
this probably requires sumoylation. Desumoylation leads to diffuse nucleoplasmic location.
Protein Description E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins. Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation. Has no activity with SUMO1. [PubMed: 26524493 Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11'. Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9'. Plays a role in regulating the transcription of AR targets (By similarity]
Protein Sequence MGDPGPEIIESVPPAGPEASESTTDENEDDIQFVSEGPLRPVLEYIDLVSSDDEEPSTSHSDENFKCKDYIDHQKDKVALTLARLARHVEVEKQQKEEKNRAFREKIDFQHAHGLQELEFIQGHSETEAARQCVDQWLKMPGLRTNAANSGTKRSFQRGGRMWRSEKPILCPIMHCNKEFDNGHLLLGHLKRFDHSPCDPTITLHGPLANSFACAVCYEHFVTQQQYKDHLLSRTAAADGHSNSLLPQIIQCYACPQCFLLFSTKDECLKHMSTKNHFHQSFKLSDNKGTARPISFPSFAKKRLVSLCKDVPFQVKCVACHQTLRSHMELTAHFRVRCQNAGPVAIAEKSITQVAKEFIVRGYCSDCNQVFMDVASTQSHKNSGHKITLANSVEESVLLYCHISEGSRPPCDLHLFSQPKISSLKRILSVKESSAEDCIVPTKKVNLGVESLGGATRVQRQSPAVTAWFCECRRQFPSEEAVEKHVFSANTMCYKCVVCGKVCEDSGVMRLHMSRFHGGAHLNNFLFWCRTCKKELVKKDAIMAHITEFHSGHRYFYEMDEVEEEEEEAMPSSSVESHLNTDKPPSPIAVVDHCPANSPPRGRWQCRICEDMFESQECVKQHCMSLTSHRFHRYSCAHCRKTFHKVETLYRHCQDEHDSEIMMKYFCGLCDLIFNKEEEFLSHYKEHHSIDYVFVSEKTKTSIKTEGDFKIVETSSLLSCGCHESYMCKINRKEDYDRCLPVLLEKGRLWFRCSSCSATAQNVTDINTHVCQVHRKEKSEEEQQYVIKCGICTKAFQNTESAQQHFHRKHAALQKPTATPGGANRSSTCQLAASASHAEKNLKQPSSQKHSDVEKGAEHDVRCQNIEEEVELPDVDYLRTMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAGRLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAHILNPHHLEGDMMCALLNSISDTTKECDSDDSSGMKGSPAEELRATEDVELEEAIRRSLEEM
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
45PhosphorylationPLRPVLEYIDLVSSD
CCCCCCHHEEECCCC
8.7921149613
50PhosphorylationLEYIDLVSSDDEEPS
CHHEEECCCCCCCCC
35.0321149613
51PhosphorylationEYIDLVSSDDEEPST
HHEEECCCCCCCCCC
41.4221149613
59PhosphorylationDDEEPSTSHSDENFK
CCCCCCCCCCCCCCC
25.9021149613
155PhosphorylationANSGTKRSFQRGGRM
CCCCCCCCHHHCCCC
27.56-
158MethylationGTKRSFQRGGRMWRS
CCCCCHHHCCCCCCC
47.74-
302UbiquitinationSFPSFAKKRLVSLCK
CCHHHHHHHHHHHHC
47.75-
309UbiquitinationKRLVSLCKDVPFQVK
HHHHHHHCCCCCEEE
68.03-
422PhosphorylationLFSQPKISSLKRILS
ECCCCCHHHHHHHHC
35.4324719451
429PhosphorylationSSLKRILSVKESSAE
HHHHHHHCCCCCCCC
28.8622942356
586PhosphorylationLNTDKPPSPIAVVDH
CCCCCCCCCEEEEEC
37.1522006019
598PhosphorylationVDHCPANSPPRGRWQ
EECCCCCCCCCCCCC
38.0922006019
704UbiquitinationEKTKTSIKTEGDFKI
CCCCCCCCCCCCEEE
40.05-
725PhosphorylationLSCGCHESYMCKINR
CCCCCCHHHEECCCC
8.42-
726PhosphorylationSCGCHESYMCKINRK
CCCCCHHHEECCCCH
11.98-
817PhosphorylationHAALQKPTATPGGAN
HHHHCCCCCCCCCCC
50.6426239621
819PhosphorylationALQKPTATPGGANRS
HHCCCCCCCCCCCCC
25.5825338131
1023PhosphorylationDTTKECDSDDSSGMK
CCCCCCCCCCCCCCC
55.7821149613
1026PhosphorylationKECDSDDSSGMKGSP
CCCCCCCCCCCCCCH
33.5121149613
1027PhosphorylationECDSDDSSGMKGSPA
CCCCCCCCCCCCCHH
50.3121149613
1032PhosphorylationDSSGMKGSPAEELRA
CCCCCCCCHHHHHHC
18.5421149613

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 ZN451_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN451_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 ZN451_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN451_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN451_MOUSE

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Related Literatures of Post-Translational Modification

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