UniProt ID | FUND2_HUMAN | |
---|---|---|
UniProt AC | Q9BWH2 | |
Protein Name | FUN14 domain-containing protein 2 | |
Gene Name | FUNDC2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 189 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | METSAPRAGSQVVATTARHSAAYRADPLRVSSRDKLTEMAASSQGNFEGNFESLDLAEFAKKQPWWRKLFGQESGPSAEKYSVATQLFIGGVTGWCTGFIFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKSNQIPTEVRSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS | |
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 |
---|---|---|---|---|---|
10 | Phosphorylation | TSAPRAGSQVVATTA CCCCCCCCCEEEEEC | 20.86 | 25159151 | |
15 | Phosphorylation | AGSQVVATTARHSAA CCCCEEEEECCCCHH | 14.91 | 23312004 | |
16 | Phosphorylation | GSQVVATTARHSAAY CCCEEEEECCCCHHH | 16.38 | 29214152 | |
20 | Phosphorylation | VATTARHSAAYRADP EEEECCCCHHHHCCC | 14.72 | 29214152 | |
23 | Phosphorylation | TARHSAAYRADPLRV ECCCCHHHHCCCCCC | 13.17 | 30177828 | |
31 | Phosphorylation | RADPLRVSSRDKLTE HCCCCCCCCHHHHHH | 17.14 | 30266825 | |
32 | Phosphorylation | ADPLRVSSRDKLTEM CCCCCCCCHHHHHHH | 41.46 | 30266825 | |
37 | Phosphorylation | VSSRDKLTEMAASSQ CCCHHHHHHHHHHCC | 29.47 | 28857561 | |
42 | Phosphorylation | KLTEMAASSQGNFEG HHHHHHHHCCCCCCC | 17.41 | 28857561 | |
43 | Phosphorylation | LTEMAASSQGNFEGN HHHHHHHCCCCCCCC | 37.06 | 28857561 | |
53 | Phosphorylation | NFEGNFESLDLAEFA CCCCCCCCCCHHHHH | 24.05 | 25693802 | |
61 | Ubiquitination | LDLAEFAKKQPWWRK CCHHHHHHHCHHHHH | 58.21 | 21963094 | |
62 | Ubiquitination | DLAEFAKKQPWWRKL CHHHHHHHCHHHHHH | 59.15 | - | |
68 | Ubiquitination | KKQPWWRKLFGQESG HHCHHHHHHHCCCCC | 34.15 | 21906983 | |
147 | Ubiquitination | KKAKEQLKIRKSNQI HHHHHHHHHHHHCCC | 39.91 | 23000965 | |
150 | Ubiquitination | KEQLKIRKSNQIPTE HHHHHHHHHCCCCHH | 58.18 | 23000965 | |
151 | Phosphorylation | EQLKIRKSNQIPTEV HHHHHHHHCCCCHHH | 24.90 | 29255136 | |
156 | Phosphorylation | RKSNQIPTEVRSKAE HHHCCCCHHHHHHHH | 49.06 | 24702127 | |
161 | Ubiquitination | IPTEVRSKAEEVVSF CCHHHHHHHHHHHHH | 49.61 | 21906983 | |
167 | Phosphorylation | SKAEEVVSFVKKNVL HHHHHHHHHHHCCEE | 29.51 | 20833797 | |
170 | Ubiquitination | EEVVSFVKKNVLVTG HHHHHHHHCCEEEEC | 36.30 | 33845483 | |
176 | Phosphorylation | VKKNVLVTGGFFGGF HHCCEEEECCCCHHH | 27.68 | - | |
189 | Phosphorylation | GFLLGMAS------- HHHHCCCC------- | 31.68 | - |
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 FUND2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FUND2_HUMAN !! |
* 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 FUND2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
FUND2_HUMAN | FUNDC2 | physical | 25416956 | |
SEC62_HUMAN | SEC62 | physical | 26186194 | |
FAF2_HUMAN | FAF2 | physical | 26186194 | |
FUND1_HUMAN | FUNDC1 | physical | 26186194 | |
FAF2_HUMAN | FAF2 | physical | 28514442 | |
FUND1_HUMAN | FUNDC1 | physical | 28514442 |
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. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY. |