MIDN_HUMAN - dbPTM
MIDN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIDN_HUMAN
UniProt AC Q504T8
Protein Name Midnolin
Gene Name MIDN
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Nucleus, nucleolus . Nucleus . Cytoplasm, cytosol . Detected in the nucleus and nucleolus with no expression in the cytoplasm (By similarity). However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus (P
Protein Description Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion..
Protein Sequence MEPQPGGARSCRRGAPGGACELGPAAEAAPMSLAIHSTTGTRYDLAVPPDETVEGLRKRLSQRLKVPKERLALLHKDTRLSSGKLQEFGVGDGSKLTLVPTVEAGLMSQASRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAAQHAPLQHRHVLAAAAAAAAARGDPSIASPVSSPCRPVSSAARVPPVPTSPSPASPSPITAGSFRSHAASTTCPEQMDCSPTASSSASPGASTTSTPGASPAPRSRKPGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMPPSLAQLRCHAQCSPASPAPDLAPRTTSCEKLTAAPSASLLQGQSQIRMCKPPGDRLRQTENRATRCKVERLQLLLQQKRLRRKARRDARGPYHWSPSRKAGRSDSSSSGGGGSPSEASGLGLDFEDSVWKPEVNPDIKSEFVVA
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
76UbiquitinationERLALLHKDTRLSSG
HHHHHHCCCCCCCCC
61.8429967540
84UbiquitinationDTRLSSGKLQEFGVG
CCCCCCCCCEEECCC
49.2822817900
134PhosphorylationTQVSDFLSGRSPLTL
HHHHHHHCCCCCCEE
31.9624719451
183PhosphorylationAAARGDPSIASPVSS
HHHCCCCCCCCCCCC
35.2123312004
186PhosphorylationRGDPSIASPVSSPCR
CCCCCCCCCCCCCCC
24.9421712546
189PhosphorylationPSIASPVSSPCRPVS
CCCCCCCCCCCCCCC
31.7623312004
190PhosphorylationSIASPVSSPCRPVSS
CCCCCCCCCCCCCCC
28.4021712546
196PhosphorylationSSPCRPVSSAARVPP
CCCCCCCCCCCCCCC
19.5522817900
197PhosphorylationSPCRPVSSAARVPPV
CCCCCCCCCCCCCCC
26.6123312004
206PhosphorylationARVPPVPTSPSPASP
CCCCCCCCCCCCCCC
54.2029978859
207PhosphorylationRVPPVPTSPSPASPS
CCCCCCCCCCCCCCC
19.8127050516
209PhosphorylationPPVPTSPSPASPSPI
CCCCCCCCCCCCCCC
32.6328464451
212PhosphorylationPTSPSPASPSPITAG
CCCCCCCCCCCCCCC
29.3329978859
214PhosphorylationSPSPASPSPITAGSF
CCCCCCCCCCCCCCH
26.8329978859
217PhosphorylationPASPSPITAGSFRSH
CCCCCCCCCCCHHCC
28.4922817900
241PhosphorylationMDCSPTASSSASPGA
CCCCCCCCCCCCCCC
27.5722210691
305PhosphorylationRPRRDIGTILQILND
CCCCHHHHHHHHHHH
20.88-
337PhosphorylationLRCHAQCSPASPAPD
HHHHCCCCCCCCCCC
16.0627251275
340PhosphorylationHAQCSPASPAPDLAP
HCCCCCCCCCCCCCC
25.6127251275
354UbiquitinationPRTTSCEKLTAAPSA
CCCCCHHHCCCCCCH
56.3021963094
360PhosphorylationEKLTAAPSASLLQGQ
HHCCCCCCHHHHCCC
26.26-
396UbiquitinationRCKVERLQLLLQQKR
HHHHHHHHHHHHHHH
35.9621963094
397UbiquitinationCKVERLQLLLQQKRL
HHHHHHHHHHHHHHH
6.4521963094
402UbiquitinationLQLLLQQKRLRRKAR
HHHHHHHHHHHHHHH
40.2029967540
419PhosphorylationARGPYHWSPSRKAGR
HCCCCCCCCCCCCCC
10.3323898821
462SumoylationPEVNPDIKSEFVVA-
CCCCCCCCCCCCCC-
51.84-

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 MIDN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIDN_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 MIDN_HUMAN !!

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

Oops, there are no PPI records of MIDN_HUMAN !!

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 MIDN_HUMAN

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Related Literatures of Post-Translational Modification

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