UniProt ID | UBC9_HUMAN | |
---|---|---|
UniProt AC | P63279 | |
Protein Name | SUMO-conjugating enzyme UBC9 | |
Gene Name | UBE2I | |
Organism | Homo sapiens (Human). | |
Sequence Length | 158 | |
Subcellular Localization | Nucleus. Cytoplasm. Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body (By similarity).. | |
Protein Description | Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'.. | |
Protein Sequence | MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSGIALSRL ------CCCHHHHHH | 38.62 | 23403867 | |
2 | Acetylation | ------MSGIALSRL ------CCCHHHHHH | 38.62 | 20058876 | |
7 | Phosphorylation | -MSGIALSRLAQERK -CCCHHHHHHHHHHH | 19.07 | 24719451 | |
14 | Sumoylation | SRLAQERKAWRKDHP HHHHHHHHHHHCCCC | 52.10 | - | |
14 | Sumoylation | SRLAQERKAWRKDHP HHHHHHHHHHHCCCC | 52.10 | - | |
18 | Ubiquitination | QERKAWRKDHPFGFV HHHHHHHCCCCCEEE | 50.08 | 18781797 | |
18 | 2-Hydroxyisobutyrylation | QERKAWRKDHPFGFV HHHHHHHCCCCCEEE | 50.08 | - | |
18 | Sumoylation | QERKAWRKDHPFGFV HHHHHHHCCCCCEEE | 50.08 | 28112733 | |
30 | Acetylation | GFVAVPTKNPDGTMN EEEEEECCCCCCCEE | 61.48 | 25953088 | |
35 | Phosphorylation | PTKNPDGTMNLMNWE ECCCCCCCEEEEEEE | 15.40 | 21406692 | |
43 | Glutathionylation | MNLMNWECAIPGKKG EEEEEEEEECCCCCC | 2.92 | 22555962 | |
48 | Sumoylation | WECAIPGKKGTPWEG EEEECCCCCCCCCCC | 42.55 | - | |
48 | Acetylation | WECAIPGKKGTPWEG EEEECCCCCCCCCCC | 42.55 | 25953088 | |
48 | Sumoylation | WECAIPGKKGTPWEG EEEECCCCCCCCCCC | 42.55 | - | |
49 | Sumoylation | ECAIPGKKGTPWEGG EEECCCCCCCCCCCC | 74.14 | 25114211 | |
49 | Ubiquitination | ECAIPGKKGTPWEGG EEECCCCCCCCCCCC | 74.14 | 21906983 | |
49 | Sumoylation | ECAIPGKKGTPWEGG EEECCCCCCCCCCCC | 74.14 | - | |
59 | Ubiquitination | PWEGGLFKLRMLFKD CCCCCEEEEEECCCC | 39.98 | 21890473 | |
59 | 2-Hydroxyisobutyrylation | PWEGGLFKLRMLFKD CCCCCEEEEEECCCC | 39.98 | - | |
59 | Acetylation | PWEGGLFKLRMLFKD CCCCCEEEEEECCCC | 39.98 | 25953088 | |
65 | Sumoylation | FKLRMLFKDDYPSSP EEEEECCCCCCCCCC | 45.81 | 19608861 | |
65 | Acetylation | FKLRMLFKDDYPSSP EEEEECCCCCCCCCC | 45.81 | 19608861 | |
65 | Ubiquitination | FKLRMLFKDDYPSSP EEEEECCCCCCCCCC | 45.81 | 21890473 | |
68 | Phosphorylation | RMLFKDDYPSSPPKC EECCCCCCCCCCCCC | 18.36 | 29978859 | |
70 | Phosphorylation | LFKDDYPSSPPKCKF CCCCCCCCCCCCCCC | 49.61 | 21712546 | |
71 | Phosphorylation | FKDDYPSSPPKCKFE CCCCCCCCCCCCCCC | 40.49 | 23401153 | |
74 | Ubiquitination | DYPSSPPKCKFEPPL CCCCCCCCCCCCCCC | 54.14 | - | |
101 | Sumoylation | LSILEEDKDWRPAIT EHHHHCCCCCCCCHH | 63.57 | 28112733 | |
146 | Acetylation | QNRVEYEKRVRAQAK CCCHHHHHHHHHHHH | 56.12 | 26051181 | |
146 | Sumoylation | QNRVEYEKRVRAQAK CCCHHHHHHHHHHHH | 56.12 | - | |
146 | Sumoylation | QNRVEYEKRVRAQAK CCCHHHHHHHHHHHH | 56.12 | - | |
153 | Sumoylation | KRVRAQAKKFAPS-- HHHHHHHHHHCCC-- | 36.02 | - | |
153 | Sumoylation | KRVRAQAKKFAPS-- HHHHHHHHHHCCC-- | 36.02 | - | |
154 | Sumoylation | RVRAQAKKFAPS--- HHHHHHHHHCCC--- | 50.18 | - | |
158 | Phosphorylation | QAKKFAPS------- HHHHHCCC------- | 49.80 | 24719451 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
71 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
* 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 UBC9_HUMAN !! |
Kegg Disease | ||||||
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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. |
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Acetylation | |
Reference | PubMed |
"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-65, AND MASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-18, AND MASSSPECTROMETRY. |