UBR7_HUMAN - dbPTM
UBR7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBR7_HUMAN
UniProt AC Q8N806
Protein Name Putative E3 ubiquitin-protein ligase UBR7
Gene Name UBR7
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation..
Protein Sequence MAGAEGAAGRQSELEPVVSLVDVLEEDEELENEACAVLGGSDSEKCSYSQGSVKRQALYACSTCTPEGEEPAGICLACSYECHGSHKLFELYTKRNFRCDCGNSKFKNLECKLLPDKAKVNSGNKYNDNFFGLYCICKRPYPDPEDEIPDEMIQCVVCEDWFHGRHLGAIPPESGDFQEMVCQACMKRCSFLWAYAAQLAVTKISTEDDGLVRNIDGIGDQEVIKPENGEHQDSTLKEDVPEQGKDDVREVKVEQNSEPCAGSSSESDLQTVFKNESLNAESKSGCKLQELKAKQLIKKDTATYWPLNWRSKLCTCQDCMKMYGDLDVLFLTDEYDTVLAYENKGKIAQATDRSDPLMDTLSSMNRVQQVELICEYNDLKTELKDYLKRFADEGTVVKREDIQQFFEEFQSKKRRRVDGMQYYCS
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
41PhosphorylationACAVLGGSDSEKCSY
CEEECCCCCCCCCCC		35.8430278072
43PhosphorylationAVLGGSDSEKCSYSQ
EECCCCCCCCCCCCC		40.4230278072
49PhosphorylationDSEKCSYSQGSVKRQ
CCCCCCCCCCCHHHH		16.2727282143
52PhosphorylationKCSYSQGSVKRQALY
CCCCCCCCHHHHHHH		19.4827251275
54AcetylationSYSQGSVKRQALYAC
CCCCCCHHHHHHHEE		40.2525953088
54UbiquitinationSYSQGSVKRQALYAC
CCCCCCHHHHHHHEE		40.2529967540
92PhosphorylationSHKLFELYTKRNFRC
CHHHHHHHHCCCCCC		11.7419658100
94UbiquitinationKLFELYTKRNFRCDC
HHHHHHHCCCCCCCC		31.61-
105UbiquitinationRCDCGNSKFKNLECK
CCCCCCCCCCCCEEE		65.4429967540
105AcetylationRCDCGNSKFKNLECK
CCCCCCCCCCCCEEE		65.4425953088
107UbiquitinationDCGNSKFKNLECKLL
CCCCCCCCCCEEEEC		65.4429967540
112SumoylationKFKNLECKLLPDKAK
CCCCCEEEECCCHHC		43.62-
112UbiquitinationKFKNLECKLLPDKAK
CCCCCEEEECCCHHC		43.6229967540
112SumoylationKFKNLECKLLPDKAK
CCCCCEEEECCCHHC		43.62-
122PhosphorylationPDKAKVNSGNKYNDN
CCHHCCCCCCCCCCC		46.8933259812
190PhosphorylationQACMKRCSFLWAYAA
HHHHHHHHHHHHHHH		27.6628464451
195PhosphorylationRCSFLWAYAAQLAVT
HHHHHHHHHHHHHHH		7.2925907765
225SumoylationIGDQEVIKPENGEHQ
CCCCEEECCCCCCCC		52.0028112733
225SumoylationIGDQEVIKPENGEHQ
CCCCEEECCCCCCCC		52.00-
225UbiquitinationIGDQEVIKPENGEHQ
CCCCEEECCCCCCCC		52.0024816145
234PhosphorylationENGEHQDSTLKEDVP
CCCCCCCCCCCCCCC		29.1228555341
235PhosphorylationNGEHQDSTLKEDVPE
CCCCCCCCCCCCCCC		50.5725627689
252SumoylationKDDVREVKVEQNSEP
CCCCCEEEEEECCCC		34.9928112733
252SumoylationKDDVREVKVEQNSEP
CCCCCEEEEEECCCC		34.99-
257PhosphorylationEVKVEQNSEPCAGSS
EEEEEECCCCCCCCC		42.4826074081
263PhosphorylationNSEPCAGSSSESDLQ
CCCCCCCCCCHHHHH		16.5025159151
264PhosphorylationSEPCAGSSSESDLQT
CCCCCCCCCHHHHHH		36.8925159151
265PhosphorylationEPCAGSSSESDLQTV
CCCCCCCCHHHHHHH		42.7025159151
267PhosphorylationCAGSSSESDLQTVFK
CCCCCCHHHHHHHHC		45.6430278072
271PhosphorylationSSESDLQTVFKNESL
CCHHHHHHHHCCCCC		34.9028450419
274UbiquitinationSDLQTVFKNESLNAE
HHHHHHHCCCCCCCC		56.3132015554
274SumoylationSDLQTVFKNESLNAE
HHHHHHHCCCCCCCC		56.3128112733
277PhosphorylationQTVFKNESLNAESKS
HHHHCCCCCCCCCCC		36.0021815630
282PhosphorylationNESLNAESKSGCKLQ
CCCCCCCCCCCCCHH		29.7029396449
283UbiquitinationESLNAESKSGCKLQE
CCCCCCCCCCCCHHH		42.2332015554
283SumoylationESLNAESKSGCKLQE
CCCCCCCCCCCCHHH		42.23-
283SumoylationESLNAESKSGCKLQE
CCCCCCCCCCCCHHH		42.23-
287AcetylationAESKSGCKLQELKAK
CCCCCCCCHHHHHHH		57.6525953088
292UbiquitinationGCKLQELKAKQLIKK
CCCHHHHHHHHHHHC		53.43-
312UbiquitinationWPLNWRSKLCTCQDC
CCCCHHHCEEEHHHH		38.72-
312AcetylationWPLNWRSKLCTCQDC
CCCCHHHCEEEHHHH		38.7225953088
346UbiquitinationLAYENKGKIAQATDR
EEECCCCCCCCCCCC		36.1629967540
351PhosphorylationKGKIAQATDRSDPLM
CCCCCCCCCCCCHHH		21.6228464451
354PhosphorylationIAQATDRSDPLMDTL
CCCCCCCCCHHHHHH		46.5228112733
360PhosphorylationRSDPLMDTLSSMNRV
CCCHHHHHHHHCCHH		17.9925850435
362PhosphorylationDPLMDTLSSMNRVQQ
CHHHHHHHHCCHHHH		29.6323186163
363PhosphorylationPLMDTLSSMNRVQQV
HHHHHHHHCCHHHHH		24.1623186163
376PhosphorylationQVELICEYNDLKTEL
HHHHHHHHCCHHHHH		15.0128796482
380UbiquitinationICEYNDLKTELKDYL
HHHHCCHHHHHHHHH		42.7023000965
380NeddylationICEYNDLKTELKDYL
HHHHCCHHHHHHHHH		42.7032015554
384UbiquitinationNDLKTELKDYLKRFA
CCHHHHHHHHHHHHC		37.7923000965
388UbiquitinationTELKDYLKRFADEGT
HHHHHHHHHHCCCCC		38.9623000965
398UbiquitinationADEGTVVKREDIQQF
CCCCCEEEHHHHHHH		45.8133845483
3982-HydroxyisobutyrylationADEGTVVKREDIQQF
CCCCCEEEHHHHHHH		45.81-
398SumoylationADEGTVVKREDIQQF
CCCCCEEEHHHHHHH		45.81-
398SumoylationADEGTVVKREDIQQF
CCCCCEEEHHHHHHH		45.8128112733
412UbiquitinationFFEEFQSKKRRRVDG
HHHHHHHHHHHCCCC		39.2432015554
413UbiquitinationFEEFQSKKRRRVDGM
HHHHHHHHHHCCCCC		57.28-
422PhosphorylationRRVDGMQYYCS----
HCCCCCCCCCC----		9.5027642862
423PhosphorylationRVDGMQYYCS-----
CCCCCCCCCC-----		3.0027642862
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 UBR7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBR7_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 UBR7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VP33A_HUMANVPS33Aphysical
22939629
AL1B1_HUMANALDH1B1physical
22863883
FUMH_HUMANFHphysical
22863883
FKBP9_HUMANFKBP9physical
22863883
HDGF_HUMANHDGFphysical
22863883
HEXB_HUMANHEXBphysical
22863883
LIMD1_HUMANLIMD1physical
22863883
NUBP2_HUMANNUBP2physical
22863883
OGFD1_HUMANOGFOD1physical
22863883
PDC10_HUMANPDCD10physical
22863883
PLCG1_HUMANPLCG1physical
22863883
ANM6_HUMANPRMT6physical
22863883
PYGB_HUMANPYGBphysical
22863883
PDIA6_HUMANPDIA6physical
26344197
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 UBR7_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.

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