UBCP1_HUMAN - dbPTM
UBCP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBCP1_HUMAN
UniProt AC Q8WVY7
Protein Name Ubiquitin-like domain-containing CTD phosphatase 1
Gene Name UBLCP1
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Nucleus . Colocalizes with nuclear proteasomes.
Protein Description Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome..
Protein Sequence MALPIIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGTREESLEDVLGPPPDNDDVVNDFDIEDEVVEVENREENLLKISRRVKEYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKELGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHLNRDKDKELLKLTQYLKEIAKLDDFLDLNHKYWERYLSKKQGQ
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
2Acetylation------MALPIIVKW
------CCCCEEEEE		23.2622223895
29UbiquitinationDDTVLDLKQFLKTLT
CCCEEEHHHHHHHHH		38.3829967540
49AcetylationRQKLLGLKVKGKPAE
HHHHHCCEECCCCCC		39.8525953088
65AcetylationDVKLGALKLKPNTKI
CCEECEEECCCCCEE		54.6625953088
65UbiquitinationDVKLGALKLKPNTKI
CCEECEEECCCCCEE		54.66-
67UbiquitinationKLGALKLKPNTKIMM
EECEEECCCCCEEEE		34.3329967540
71AcetylationLKLKPNTKIMMMGTR
EECCCCCEEEECCCC		34.9325953088
71UbiquitinationLKLKPNTKIMMMGTR
EECCCCCEEEECCCC		34.9329967540
81PhosphorylationMMGTREESLEDVLGP
ECCCCHHHHHHHHCC		32.1026657352
117AcetylationNREENLLKISRRVKE
CHHHHHHHHHHHHHC		41.6319608861
117MalonylationNREENLLKISRRVKE
CHHHHHHHHHHHHHC		41.6326320211
117UbiquitinationNREENLLKISRRVKE
CHHHHHHHHHHHHHC		41.6332015554
138UbiquitinationNPPREGKKLLVLDVD
CCCCCCCEEEEEECE		58.8933845483
193AcetylationNMKWIEAKMKELGVS
CCHHHHHHHHHHCCC		37.4025953088
193UbiquitinationNMKWIEAKMKELGVS
CCHHHHHHHHHHCCC		37.4023000965
195UbiquitinationKWIEAKMKELGVSTN
HHHHHHHHHHCCCCC		49.4323000965
200PhosphorylationKMKELGVSTNANYKI
HHHHHCCCCCCCCEE		17.7220068231
201PhosphorylationMKELGVSTNANYKIT
HHHHCCCCCCCCEEE		35.6221406692
205PhosphorylationGVSTNANYKITFMLD
CCCCCCCCEEEEEEC		11.0121406692
213PhosphorylationKITFMLDSAAMITVH
EEEEEECCCEEEEEE		17.6124114839
230UbiquitinationRRGLIDVKPLGVIWG
CCCCCCCEECEEEEE		30.6721906983
240PhosphorylationGVIWGKFSEFYSKKN
EEEEEEHHHHHHCCC		30.2222817900
243PhosphorylationWGKFSEFYSKKNTIM
EEEHHHHHHCCCEEE		18.6122817900
244PhosphorylationGKFSEFYSKKNTIMF
EEHHHHHHCCCEEEE		42.3422817900
245UbiquitinationKFSEFYSKKNTIMFD
EHHHHHHCCCEEEEC		38.3732015554
245SuccinylationKFSEFYSKKNTIMFD
EHHHHHHCCCEEEEC		38.3723954790
245AcetylationKFSEFYSKKNTIMFD
EHHHHHHCCCEEEEC		38.3723749302
246UbiquitinationFSEFYSKKNTIMFDD
HHHHHHCCCEEEECC		54.0730230243
2462-HydroxyisobutyrylationFSEFYSKKNTIMFDD
HHHHHHCCCEEEECC		54.07-
248PhosphorylationEFYSKKNTIMFDDIG
HHHHCCCEEEECCCC		23.77-
267UbiquitinationMNPQNGLKIRPFMKA
CCCCCCCCCHHHHHH		37.7623000965
273UbiquitinationLKIRPFMKAHLNRDK
CCCHHHHHHHHCCCC		32.7923000965
280UbiquitinationKAHLNRDKDKELLKL
HHHHCCCCCHHHHHH		68.4223000965
280AcetylationKAHLNRDKDKELLKL
HHHHCCCCCHHHHHH		68.4223749302
282UbiquitinationHLNRDKDKELLKLTQ
HHCCCCCHHHHHHHH		56.8723000965
282AcetylationHLNRDKDKELLKLTQ
HHCCCCCHHHHHHHH		56.8725953088
286UbiquitinationDKDKELLKLTQYLKE
CCCHHHHHHHHHHHH		63.2123000965
288PhosphorylationDKELLKLTQYLKEIA
CHHHHHHHHHHHHHH		17.3620068231
292UbiquitinationLKLTQYLKEIAKLDD
HHHHHHHHHHHCCHH		41.9823000965
296UbiquitinationQYLKEIAKLDDFLDL
HHHHHHHCCHHHHCC		59.1021906983
306UbiquitinationDFLDLNHKYWERYLS
HHHCCCHHHHHHHHH		51.4932015554
306AcetylationDFLDLNHKYWERYLS
HHHCCCHHHHHHHHH		51.4923954790
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 UBCP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBCP1_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 UBCP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZFAN5_HUMANZFAND5physical
22939629
GT251_HUMANCOLGALT1physical
27880917
PAAF1_HUMANPAAF1physical
27880917
PSB2_HUMANPSMB2physical
27880917
PRS4_HUMANPSMC1physical
27880917
PRS7_HUMANPSMC2physical
27880917
PRS6A_HUMANPSMC3physical
27880917
PRS6B_HUMANPSMC4physical
27880917
PRS8_HUMANPSMC5physical
27880917
PRS10_HUMANPSMC6physical
27880917
PSMD1_HUMANPSMD1physical
27880917
PSD11_HUMANPSMD11physical
27880917
PSD12_HUMANPSMD12physical
27880917
PSD13_HUMANPSMD13physical
27880917
PSDE_HUMANPSMD14physical
27880917
PSMD2_HUMANPSMD2physical
27880917
PSMD3_HUMANPSMD3physical
27880917
PSMD4_HUMANPSMD4physical
27880917
PSMD6_HUMANPSMD6physical
27880917
PSMD7_HUMANPSMD7physical
27880917
PSMD8_HUMANPSMD8physical
27880917
UCHL5_HUMANUCHL5physical
27880917
PRS4_HUMANPSMC1physical
28539385
PSMD2_HUMANPSMD2physical
28539385
PSMD6_HUMANPSMD6physical
28539385
PRS7_HUMANPSMC2physical
28539385
PSD13_HUMANPSMD13physical
28539385
PRS8_HUMANPSMC5physical
28539385
PSMD7_HUMANPSMD7physical
28539385
PRS10_HUMANPSMC6physical
28539385
PRS6B_HUMANPSMC4physical
28539385
PSMD1_HUMANPSMD1physical
28539385
PSD11_HUMANPSMD11physical
28539385
PSDE_HUMANPSMD14physical
28539385
PSMD8_HUMANPSMD8physical
28539385
PSD12_HUMANPSMD12physical
28539385
PSMD3_HUMANPSMD3physical
28539385
PSD10_HUMANPSMD10physical
28539385
PAAF1_HUMANPAAF1physical
28539385
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 UBCP1_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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-306, AND MASSSPECTROMETRY.

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