UBP27_HUMAN - dbPTM
UBP27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP27_HUMAN
UniProt AC A6NNY8
Protein Name Ubiquitin carboxyl-terminal hydrolase 27
Gene Name USP27X
Organism Homo sapiens (Human).
Sequence Length 438
Subcellular Localization Cytoplasm, cytosol . Nucleus .
Protein Description Deubiquitinase that can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal. By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity..
Protein Sequence MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEHESEKVKEMNTQAY
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
54UbiquitinationFPTWETTKPELELLG
CCCCCCCCHHHHHCC
43.8721890473
54AcetylationFPTWETTKPELELLG
CCCCCCCCHHHHHCC
43.8723236377
70PhosphorylationNPRRRRITSSFTIGL
CCCCCCCCCCEEEEH
19.2624719451
71PhosphorylationPRRRRITSSFTIGLR
CCCCCCCCCEEEEHH
22.5329978859
72PhosphorylationRRRRITSSFTIGLRG
CCCCCCCCEEEEHHH
20.1229978859
110MethylationRDFFLSDRHRCEMPS
HHHHCCCCCCCCCCC
18.77-
128PhosphorylationCLVCEMSSLFRELYS
HHHHHHHHHHHHHHC
30.1624719451
278PhosphorylationTRPEHLGSSAKIKCG
CCHHHHCCCCEEECC
33.2229214152
279PhosphorylationRPEHLGSSAKIKCGS
CHHHHCCCCEEECCC
31.6129214152
281UbiquitinationEHLGSSAKIKCGSCQ
HHHCCCCEEECCCCH
44.6532015554
298PhosphorylationQESTKQLTMNKLPVV
HHHHHCCCCCCCCEE
19.0629759185
325PhosphorylationKQRRKITTYISFPLE
HHHHCCEEEEECEEE
23.4929759185
326PhosphorylationQRRKITTYISFPLEL
HHHCCEEEEECEEEC
5.9729759185
328PhosphorylationRKITTYISFPLELDM
HCCEEEEECEEECCC
15.4829759185
355PhosphorylationNGQLQLPTNSGNNEN
CCEEECCCCCCCCCC
51.0825072903
357PhosphorylationQLQLPTNSGNNENKY
EEECCCCCCCCCCCE
45.4325072903
386MethylationGHYTSFIRHHKDQWF
CCCHHHHCCCCCCCE
24.69-
406UbiquitinationVITKASIKDVLDSEG
EEEECHHHHHHCCCC
39.0121890473

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 UBP27_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP27_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 UBP27_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
27013495
B2L11_HUMANBCL2L11physical
27013495

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 UBP27_HUMAN

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Related Literatures of Post-Translational Modification

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