NUB1_HUMAN - dbPTM
NUB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUB1_HUMAN
UniProt AC Q9Y5A7
Protein Name NEDD8 ultimate buster 1
Gene Name NUB1
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization Nucleus . Predominantly nuclear.
Protein Description Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation. Isoform 1 promotes the degradation of NEDD8 more efficiently than isoform 2..
Protein Sequence MAQKKYLQAKLTQFLREDRIQLWKPPYTDENKKVGLALKDLAKQYSDRLECCENEVEKVIEEIRCKAIERGTGNDNYRTTGIATIEVFLPPRLKKDRKNLLETRLHITGRELRSKIAETFGLQENYIKIVINKKQLQLGKTLEEQGVAHNVKAMVLELKQSEEDARKNFQLEEEEQNEAKLKEKQIQRTKRGLEILAKRAAETVVDPEMTPYLDIANQTGRSIRIPPSERKALMLAMGYHEKGRAFLKRKEYGIALPCLLDADKYFCECCRELLDTVDNYAVLQLDIVWCYFRLEQLECLDDAEKKLNLAQKCFKNCYGENHQRLVHIKGNCGKEKVLFLRLYLLQGIRNYHSGNDVEAYEYLNKARQLFKELYIDPSKVDNLLQLGFTAQEARLGLRACDGNVDHAATHITNRREELAQIRKEEKEKKRRRLENIRFLKGMGYSTHAAQQVLHAASGNLDEALKILLSNPQMWWLNDSNPETDNRQESPSQENIDRLVYMGFDALVAEAALRVFRGNVQLAAQTLAHNGGSLPPELPLSPEDSLSPPATSPSDSAGTSSASTDEDMETEAVNEILEDIPEHEEDYLDSTLEDEEIIIAEYLSYVENRKSATKKN
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
6Phosphorylation--MAQKKYLQAKLTQ
--CCCHHHHHHHHHH		15.8718083107
10UbiquitinationQKKYLQAKLTQFLRE
CHHHHHHHHHHHHHH		38.8221890473
10 (in isoform 2)Ubiquitination-38.8221890473
10 (in isoform 1)Ubiquitination-38.8221890473
24AcetylationEDRIQLWKPPYTDEN
HHHHHHCCCCCCCCC		44.7125953088
34UbiquitinationYTDENKKVGLALKDL
CCCCCHHHHHHHHHH		8.96-
34 (in isoform 2)Ubiquitination-8.9621890473
63UbiquitinationVEKVIEEIRCKAIER
HHHHHHHHHHHHHHC		3.98-
67UbiquitinationIEEIRCKAIERGTGN
HHHHHHHHHHCCCCC		16.70-
70PhosphorylationIRCKAIERGTGNDNY
HHHHHHHCCCCCCCC		41.69-
82UbiquitinationDNYRTTGIATIEVFL
CCCCCEEEEEEEEEC		2.61-
103PhosphorylationDRKNLLETRLHITGR
HHHHHHHHHHHHHHH		38.20-
126PhosphorylationTFGLQENYIKIVINK
HHCCCCCEEEEEEEH		11.6628152594
127PhosphorylationFGLQENYIKIVINKK
HCCCCCEEEEEEEHH		3.56-
139UbiquitinationNKKQLQLGKTLEEQG
EHHHHHHCCCHHHHC		14.13-
141PhosphorylationKQLQLGKTLEEQGVA
HHHHHCCCHHHHCHH		37.2928674151
158UbiquitinationVKAMVLELKQSEEDA
HHHHEEEHHHCHHHH		5.52-
159 (in isoform 2)Ubiquitination-42.26-
159UbiquitinationKAMVLELKQSEEDAR
HHHEEEHHHCHHHHH		42.26-
164UbiquitinationELKQSEEDARKNFQL
EHHHCHHHHHHHCCC		47.85-
167UbiquitinationQSEEDARKNFQLEEE
HCHHHHHHHCCCCHH		64.9321906983
167 (in isoform 2)Ubiquitination-64.93-
167 (in isoform 1)Ubiquitination-64.9321890473
176UbiquitinationFQLEEEEQNEAKLKE
CCCCHHHHHHHHHHH		57.24-
183UbiquitinationQNEAKLKEKQIQRTK
HHHHHHHHHHHHHHH		61.71-
191UbiquitinationKQIQRTKRGLEILAK
HHHHHHHHHHHHHHH		55.08-
191 (in isoform 2)Ubiquitination-55.0821890473
198UbiquitinationRGLEILAKRAAETVV
HHHHHHHHHHHHHCC		38.84-
198AcetylationRGLEILAKRAAETVV
HHHHHHHHHHHHHCC		38.8430590985
204UbiquitinationAKRAAETVVDPEMTP
HHHHHHHCCCCCCCC		3.28-
208UbiquitinationAETVVDPEMTPYLDI
HHHCCCCCCCCCCCC		51.75-
209SulfoxidationETVVDPEMTPYLDIA
HHCCCCCCCCCCCCC		5.7930846556
210PhosphorylationTVVDPEMTPYLDIAN
HCCCCCCCCCCCCCC		13.7128555341
212PhosphorylationVDPEMTPYLDIANQT
CCCCCCCCCCCCCCC		14.0828796482
219PhosphorylationYLDIANQTGRSIRIP
CCCCCCCCCCCEECC		34.0821406692
222UbiquitinationIANQTGRSIRIPPSE
CCCCCCCCEECCHHH		19.98-
222PhosphorylationIANQTGRSIRIPPSE
CCCCCCCCEECCHHH		19.9821406692
234SulfoxidationPSERKALMLAMGYHE
HHHHHHHHHHHCCHH		2.4030846556
237SulfoxidationRKALMLAMGYHEKGR
HHHHHHHHCCHHHHH		4.8830846556
239PhosphorylationALMLAMGYHEKGRAF
HHHHHHCCHHHHHHH		8.1720068231
243PhosphorylationAMGYHEKGRAFLKRK
HHCCHHHHHHHHHHH		24.14-
246PhosphorylationYHEKGRAFLKRKEYG
CHHHHHHHHHHHCCC		8.77-
255UbiquitinationKRKEYGIALPCLLDA
HHHCCCCCHHHHHCC		10.90-
263PhosphorylationLPCLLDADKYFCECC
HHHHHCCHHHHHHHH		45.9420068231
266UbiquitinationLLDADKYFCECCREL
HHCCHHHHHHHHHHH		3.31-
272UbiquitinationYFCECCRELLDTVDN
HHHHHHHHHHHHCCC		39.51-
274UbiquitinationCECCRELLDTVDNYA
HHHHHHHHHHCCCCH		4.43-
315UbiquitinationNLAQKCFKNCYGENH
HHHHHHHHHCCCCCC		56.42-
329UbiquitinationHQRLVHIKGNCGKEK
CCEEEEEECCCCHHH		29.23-
330UbiquitinationQRLVHIKGNCGKEKV
CEEEEEECCCCHHHH		33.77-
336AcetylationKGNCGKEKVLFLRLY
ECCCCHHHHHHHHHH		47.9625953088
336UbiquitinationKGNCGKEKVLFLRLY
ECCCCHHHHHHHHHH		47.96-
336MalonylationKGNCGKEKVLFLRLY
ECCCCHHHHHHHHHH		47.9626320211
339UbiquitinationCGKEKVLFLRLYLLQ
CCHHHHHHHHHHHHH		4.12-
353UbiquitinationQGIRNYHSGNDVEAY
HHHHHCCCCCCHHHH		29.00-
360PhosphorylationSGNDVEAYEYLNKAR
CCCCHHHHHHHHHHH		7.50-
365UbiquitinationEAYEYLNKARQLFKE
HHHHHHHHHHHHHHH		42.21-
371UbiquitinationNKARQLFKELYIDPS
HHHHHHHHHHCCCHH		56.2421890473
371 (in isoform 1)Ubiquitination-56.2421890473
371 (in isoform 2)Ubiquitination-56.2421890473
379 (in isoform 2)Ubiquitination-60.02-
389UbiquitinationNLLQLGFTAQEARLG
HHHHHCCCHHHHHHC		26.15-
395 (in isoform 2)Ubiquitination-11.0521890473
395UbiquitinationFTAQEARLGLRACDG
CCHHHHHHCCCCCCC		11.05-
403UbiquitinationGLRACDGNVDHAATH
CCCCCCCCCCHHHHH		23.85-
440 (in isoform 2)Ubiquitination-44.11-
465 (in isoform 2)Phosphorylation-38.0528348404
469 (in isoform 2)Phosphorylation-42.9128348404
475 (in isoform 2)Phosphorylation-4.6728348404
479PhosphorylationQMWWLNDSNPETDNR
CCEECCCCCCCCCCC		53.8926074081
483PhosphorylationLNDSNPETDNRQESP
CCCCCCCCCCCCCCC		39.5726074081
489PhosphorylationETDNRQESPSQENID
CCCCCCCCCCHHHHH		22.8525849741
491PhosphorylationDNRQESPSQENIDRL
CCCCCCCCHHHHHHH		60.4521815630
500PhosphorylationENIDRLVYMGFDALV
HHHHHHHHCHHHHHH		8.9826074081
513PhosphorylationLVAEAALRVFRGNVQ
HHHHHHHHHHHCCHH		22.32-
569PhosphorylationSTDEDMETEAVNEIL
CCCHHHHHHHHHHHH		23.7024275569
593PhosphorylationYLDSTLEDEEIIIAE
HHCCCCCCHHHHHHH		63.04-
601PhosphorylationEEIIIAEYLSYVENR
HHHHHHHHHHHHHHH		7.6029759185
603PhosphorylationIIIAEYLSYVENRKS
HHHHHHHHHHHHHHH		26.6529759185
604PhosphorylationIIAEYLSYVENRKSA
HHHHHHHHHHHHHHH		14.8029759185
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 NUB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUB1_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 NUB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBD_HUMANUBDphysical
14757770
PSMD4_HUMANPSMD4physical
11585840
NEDD8_HUMANNEDD8physical
20101219
P53_HUMANTP53physical
20101219
PSMD4_HUMANPSMD4physical
22434192
RPN10_YEASTRPN10physical
22434192
PSMD2_HUMANPSMD2physical
22434192
UBD_HUMANUBDphysical
22434192
PSMD4_HUMANPSMD4physical
16171779
UBD_HUMANUBDphysical
16707496
SNCAP_HUMANSNCAIPphysical
16877356
NEDD8_HUMANNEDD8physical
16877356
UBE2K_HUMANUBE2Kphysical
16877356
AIPL1_HUMANAIPL1physical
15081406
NEDD8_HUMANNEDD8physical
17549501
SNCAP_HUMANSNCAIPphysical
17549501
TAU_HUMANMAPTphysical
22965877
GSK3B_HUMANGSK3Bphysical
22965877
TERA_HUMANVCPphysical
24019527
TERA_HUMANVCPphysical
24100225
UBC_HUMANUBCphysical
23649778
TERF1_HUMANTERF1physical
27214791
PSMD4_HUMANPSMD4physical
27214791
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 NUB1_HUMAN

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Related Literatures of Post-Translational Modification

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