DCNL2_HUMAN - dbPTM
DCNL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCNL2_HUMAN
UniProt AC Q6PH85
Protein Name DCN1-like protein 2
Gene Name DCUN1D2
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization
Protein Description Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8-conjugating E2 enzyme UBC12. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity..
Protein Sequence MHKLKSSQKDKVRQFMACTQAGERTAIYCLTQNEWRLDEATDSFFQNPDSLHRESMRNAVDKKKLERLYGRYKDPQDENKIGVDGIQQFCDDLSLDPASISVLVIAWKFRAATQCEFSRKEFLDGMTELGCDSMEKLKALLPRLEQELKDTAKFKDFYQFTFTFAKNPGQKGLDLEMAVAYWKLVLSGRFKFLDLWNTFLMEHHKRSIPRDTWNLLLDFGNMIADDMSNYDEEGAWPVLIDDFVEYARPVVTGGKRSLF
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--MHKLKSSQKDKVR
--CCCCCCCHHHHHH
48.7327174698
7Phosphorylation-MHKLKSSQKDKVRQ
-CCCCCCCHHHHHHH
39.4027174698
18S-nitrosylationKVRQFMACTQAGERT
HHHHHHHHCCCCCCE
1.6224105792
19PhosphorylationVRQFMACTQAGERTA
HHHHHHHCCCCCCEE
16.3523663014
25PhosphorylationCTQAGERTAIYCLTQ
HCCCCCCEEEEEEEC
17.0723663014
28PhosphorylationAGERTAIYCLTQNEW
CCCCEEEEEEECCEE
4.4823663014
31PhosphorylationRTAIYCLTQNEWRLD
CEEEEEEECCEEECC
26.2823663014
41PhosphorylationEWRLDEATDSFFQNP
EEECCCCCHHHHCCH
30.0826471730
43PhosphorylationRLDEATDSFFQNPDS
ECCCCCHHHHCCHHH
24.4926471730
50PhosphorylationSFFQNPDSLHRESMR
HHHCCHHHHCHHHHH
27.6026471730
55PhosphorylationPDSLHRESMRNAVDK
HHHHCHHHHHHHHCH
24.01-
69PhosphorylationKKKLERLYGRYKDPQ
HHHHHHHHCCCCCCC
13.0420562096
138UbiquitinationCDSMEKLKALLPRLE
CCHHHHHHHHHHHHH
48.3229967540
187PhosphorylationAYWKLVLSGRFKFLD
HHHHHHHCCCCHHHH
22.0524719451

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 DCNL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCNL2_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 DCNL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CUL1_HUMANCUL1physical
23201271
CUL2_HUMANCUL2physical
23201271
CUL3_HUMANCUL3physical
23201271
CUL4A_HUMANCUL4Aphysical
23201271
CUL4B_HUMANCUL4Bphysical
23201271
CUL5_HUMANCUL5physical
23201271
CUL1_HUMANCUL1physical
19617556
CUL2_HUMANCUL2physical
19617556
CUL3_HUMANCUL3physical
19617556
CUL4A_HUMANCUL4Aphysical
19617556
CUL4B_HUMANCUL4Bphysical
19617556
CUL5_HUMANCUL5physical
19617556
UBC12_HUMANUBE2Mphysical
19617556
CUL1_HUMANCUL1physical
26906416
CUL2_HUMANCUL2physical
26906416
CUL3_HUMANCUL3physical
26906416
CUL4A_HUMANCUL4Aphysical
26906416
CUL4B_HUMANCUL4Bphysical
26906416
CUL5_HUMANCUL5physical
26906416
CAND1_HUMANCAND1physical
26906416
RBX1_HUMANRBX1physical
26906416
RBX2_HUMANRNF7physical
26906416
ELOB_HUMANTCEB2physical
26906416
UBC12_HUMANUBE2Mphysical
26906416

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 DCNL2_HUMAN

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Related Literatures of Post-Translational Modification

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