DCOR_HUMAN - dbPTM
DCOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCOR_HUMAN
UniProt AC P11926
Protein Name Ornithine decarboxylase
Gene Name ODC1
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization
Protein Description Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis..
Protein Sequence MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
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
27UbiquitinationAKDILDQKINEVSSS
HHHHHHHHHHCCCCC
47.3621906983
37UbiquitinationEVSSSDDKDAFYVAD
CCCCCCCCCCEEECC
56.82-
50UbiquitinationADLGDILKKHLRWLK
CCHHHHHHHHHHHHH
38.1821906983
51UbiquitinationDLGDILKKHLRWLKA
CHHHHHHHHHHHHHH
44.41-
57UbiquitinationKKHLRWLKALPRVTP
HHHHHHHHHCCCCCC
40.70-
66PhosphorylationLPRVTPFYAVKCNDS
CCCCCCEEEEECCCC
16.2230631047
69OtherVTPFYAVKCNDSKAI
CCCEEEEECCCCHHH
21.1017407445
69UbiquitinationVTPFYAVKCNDSKAI
CCCEEEEECCCCHHH
21.10-
69N6-(pyridoxal phosphate)lysineVTPFYAVKCNDSKAI
CCCEEEEECCCCHHH
21.10-
73PhosphorylationYAVKCNDSKAIVKTL
EEEECCCCHHHHHHH
15.2530631047
74UbiquitinationAVKCNDSKAIVKTLA
EEECCCCHHHHHHHH
45.02-
78UbiquitinationNDSKAIVKTLAATGT
CCCHHHHHHHHHCCC
31.54-
115UbiquitinationIIYANPCKQVSQIKY
EEEEECCCCHHHHHH
55.80-
122PhosphorylationKQVSQIKYAANNGVQ
CCHHHHHHHHHCCCE
16.7528165663
132PhosphorylationNNGVQMMTFDSEVEL
HCCCEEEEECCHHHH
20.9628165663
135PhosphorylationVQMMTFDSEVELMKV
CEEEEECCHHHHHHH
39.0728165663
141UbiquitinationDSEVELMKVARAHPK
CCHHHHHHHHHHCCC
45.42-
150UbiquitinationARAHPKAKLVLRIAT
HHHCCCCEEEEEEEC
45.30-
161UbiquitinationRIATDDSKAVCRLSV
EEECCCCCCCHHHHH
52.40-
247UbiquitinationGSEDVKLKFEEITGV
CCHHCEEEHEEHHCC
45.0421906983
261UbiquitinationVINPALDKYFPSDSG
CCCHHHHHHCCCCCC
50.032190698
303PhosphorylationVLKEQTGSDDEDESS
HHEECCCCCCCCCCC
45.32-
345UbiquitinationPLLQKRPKPDEKYYS
HHHHCCCCCCCCCCC
69.96-
360S-nitrosocysteineSSIWGPTCDGLDRIV
CCCCCCCCCCHHHHH
4.38-
360S-nitrosylationSSIWGPTCDGLDRIV
CCCCCCCCCCHHHHH
4.3811461922

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
303SPhosphorylationKinaseCK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCOR_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 DCOR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCOR_HUMANODC1physical
10623504
SSRA_HUMANSSR1physical
21988832
KAT5_HUMANKAT5physical
25416956
GORS2_HUMANGORASP2physical
25416956
OAZ3_HUMANOAZ3physical
25416956
OAZ1_HUMANOAZ1physical
12359729
OAZ2_HUMANOAZ2physical
12359729
RSCA1_HUMANRSC1A1physical
27555600

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
DB00127Spermine
Regulatory Network of DCOR_HUMAN

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Related Literatures of Post-Translational Modification

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