UniProt ID | MND1_HUMAN | |
---|---|---|
UniProt AC | Q9BWT6 | |
Protein Name | Meiotic nuclear division protein 1 homolog | |
Gene Name | MND1 {ECO:0000312|EMBL:EAX04964.1} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 205 | |
Subcellular Localization | Nucleus . | |
Protein Description | Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis (By similarity). Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.. | |
Protein Sequence | MSKKKGLSAEEKRTRMMEIFSETKDVFQLKDLEKIAPKEKGITAMSVKEVLQSLVDDGMVDCERIGTSNYYWAFPSKALHARKHKLEVLESQLSEGSQKHASLQKSIEKAKIGRCETEERTRLAKELSSLRDQREQLKAEVEKYKDCDPQVVEEIRQANKVAKEAANRWTDNIFAIKSWAKRKFGFEENKIDRTFGIPEDFDYID | |
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 | Acetylation | ------MSKKKGLSA ------CCCCCCCCH | 53.86 | 22814378 | |
14 | Phosphorylation | LSAEEKRTRMMEIFS CCHHHHHHHHHHHHH | 33.70 | 29759185 | |
30 | Ubiquitination | TKDVFQLKDLEKIAP CCCCHHHCCHHHHCC | 49.86 | 21890473 | |
46 | Phosphorylation | EKGITAMSVKEVLQS CCCCCCCCHHHHHHH | 27.81 | 24719451 | |
67 | Phosphorylation | VDCERIGTSNYYWAF EEHHHCCCCCCEEEC | 16.07 | 28796482 | |
68 | Phosphorylation | DCERIGTSNYYWAFP EHHHCCCCCCEEECC | 20.02 | 28796482 | |
70 | Phosphorylation | ERIGTSNYYWAFPSK HHCCCCCCEEECCHH | 10.51 | 28796482 | |
71 | Phosphorylation | RIGTSNYYWAFPSKA HCCCCCCEEECCHHH | 8.43 | 28796482 | |
77 | Ubiquitination | YYWAFPSKALHARKH CEEECCHHHHHHHHH | 56.03 | - | |
77 | Acetylation | YYWAFPSKALHARKH CEEECCHHHHHHHHH | 56.03 | 26051181 | |
102 | Phosphorylation | EGSQKHASLQKSIEK HHHHHHHHHHHHHHH | 30.93 | 26270265 | |
105 | Ubiquitination | QKHASLQKSIEKAKI HHHHHHHHHHHHHHC | 59.71 | - | |
106 | Phosphorylation | KHASLQKSIEKAKIG HHHHHHHHHHHHHCC | 24.02 | 26270265 | |
121 | O-linked_Glycosylation | RCETEERTRLAKELS CCCHHHHHHHHHHHH | 33.06 | 30379171 | |
125 | Ubiquitination | EERTRLAKELSSLRD HHHHHHHHHHHHHHH | 64.87 | - | |
128 | Phosphorylation | TRLAKELSSLRDQRE HHHHHHHHHHHHHHH | 28.55 | 30301811 | |
129 | Phosphorylation | RLAKELSSLRDQREQ HHHHHHHHHHHHHHH | 39.80 | 25954137 | |
138 | Ubiquitination | RDQREQLKAEVEKYK HHHHHHHHHHHHHHC | 42.04 | - | |
145 | Acetylation | KAEVEKYKDCDPQVV HHHHHHHCCCCHHHH | 64.05 | 26051181 | |
177 | Ubiquitination | TDNIFAIKSWAKRKF HHCCHHHHHHHHHHH | 36.19 | - | |
190 | Ubiquitination | KFGFEENKIDRTFGI HHCCCCCCCCCCCCC | 49.62 | - | |
203 | Phosphorylation | GIPEDFDYID----- CCCCCCCCCC----- | 13.64 | - |
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 MND1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MND1_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 MND1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
A4_HUMAN | APP | physical | 21832049 | |
HOP2_HUMAN | PSMC3IP | physical | 26344197 | |
RED_HUMAN | IK | physical | 26496610 | |
HOP2_HUMAN | PSMC3IP | physical | 26496610 | |
HOP2_HUMAN | PSMC3IP | physical | 28514442 | |
MTEF4_HUMAN | MTERF4 | physical | 28514442 | |
NSUN4_HUMAN | NSUN4 | physical | 28514442 | |
JIP4_HUMAN | SPAG9 | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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