UniProt ID | ZMAT2_HUMAN | |
---|---|---|
UniProt AC | Q96NC0 | |
Protein Name | Zinc finger matrin-type protein 2 | |
Gene Name | ZMAT2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 199 | |
Subcellular Localization | Nucleus . | |
Protein Description | ||
Protein Sequence | MASGSGTKNLDFRRKWDKDEYEKLAEKRLTEEREKKDGKPVQPVKRELLRHRDYKVDLESKLGKTIVITKTTPQSEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSTLDQVKKRFEVNKKKMEEKQKDYDFEERMKELREEEEKAKAYKKEKQKEKKRRAEEDLTFEEDDEMAAVMGFSGFGSTKKSY | |
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 | ------MASGSGTKN ------CCCCCCCCC | 23.69 | 22814378 | |
3 | Phosphorylation | -----MASGSGTKNL -----CCCCCCCCCC | 31.99 | 24719451 | |
5 | Phosphorylation | ---MASGSGTKNLDF ---CCCCCCCCCCCH | 40.57 | 22617229 | |
8 | Sumoylation | MASGSGTKNLDFRRK CCCCCCCCCCCHHHH | 60.07 | - | |
8 | Ubiquitination | MASGSGTKNLDFRRK CCCCCCCCCCCHHHH | 60.07 | 24816145 | |
8 | Sumoylation | MASGSGTKNLDFRRK CCCCCCCCCCCHHHH | 60.07 | 28112733 | |
18 | Acetylation | DFRRKWDKDEYEKLA CHHHHCCHHHHHHHH | 51.88 | 26051181 | |
21 | Phosphorylation | RKWDKDEYEKLAEKR HHCCHHHHHHHHHHH | 28.62 | 28796482 | |
23 | Ubiquitination | WDKDEYEKLAEKRLT CCHHHHHHHHHHHHH | 52.69 | 33845483 | |
36 | Ubiquitination | LTEEREKKDGKPVQP HHHHHHHHCCCCCCH | 67.94 | 24816145 | |
36 | Sumoylation | LTEEREKKDGKPVQP HHHHHHHHCCCCCCH | 67.94 | 28112733 | |
39 | Sumoylation | EREKKDGKPVQPVKR HHHHHCCCCCCHHHH | 52.75 | 28112733 | |
39 | Ubiquitination | EREKKDGKPVQPVKR HHHHHCCCCCCHHHH | 52.75 | 33845483 | |
39 | Acetylation | EREKKDGKPVQPVKR HHHHHCCCCCCHHHH | 52.75 | 23749302 | |
45 | Sumoylation | GKPVQPVKRELLRHR CCCCCHHHHHHHHCC | 47.00 | - | |
45 | Sumoylation | GKPVQPVKRELLRHR CCCCCHHHHHHHHCC | 47.00 | 28112733 | |
45 | Ubiquitination | GKPVQPVKRELLRHR CCCCCHHHHHHHHCC | 47.00 | 33845483 | |
54 | Phosphorylation | ELLRHRDYKVDLESK HHHHCCCCEEEHHHH | 16.93 | - | |
55 | Sumoylation | LLRHRDYKVDLESKL HHHCCCCEEEHHHHC | 33.30 | - | |
55 | Sumoylation | LLRHRDYKVDLESKL HHHCCCCEEEHHHHC | 33.30 | 28112733 | |
60 | Phosphorylation | DYKVDLESKLGKTIV CCEEEHHHHCCCEEE | 40.24 | - | |
61 | Acetylation | YKVDLESKLGKTIVI CEEEHHHHCCCEEEE | 52.46 | 25953088 | |
61 | Ubiquitination | YKVDLESKLGKTIVI CEEEHHHHCCCEEEE | 52.46 | 33845483 | |
61 | Sumoylation | YKVDLESKLGKTIVI CEEEHHHHCCCEEEE | 52.46 | - | |
61 | Sumoylation | YKVDLESKLGKTIVI CEEEHHHHCCCEEEE | 52.46 | 28112733 | |
64 | Sumoylation | DLESKLGKTIVITKT EHHHHCCCEEEEECC | 45.58 | 28112733 | |
64 | Acetylation | DLESKLGKTIVITKT EHHHHCCCEEEEECC | 45.58 | 25953088 | |
64 | Sumoylation | DLESKLGKTIVITKT EHHHHCCCEEEEECC | 45.58 | - | |
64 | Ubiquitination | DLESKLGKTIVITKT EHHHHCCCEEEEECC | 45.58 | 33845483 | |
70 | Ubiquitination | GKTIVITKTTPQSEM CCEEEEECCCCHHHH | 39.00 | 33845483 | |
70 | Sumoylation | GKTIVITKTTPQSEM CCEEEEECCCCHHHH | 39.00 | 28112733 | |
70 | Acetylation | GKTIVITKTTPQSEM CCEEEEECCCCHHHH | 39.00 | 25953088 | |
71 | Phosphorylation | KTIVITKTTPQSEMG CEEEEECCCCHHHHC | 34.75 | 25159151 | |
72 | Phosphorylation | TIVITKTTPQSEMGG EEEEECCCCHHHHCC | 22.38 | 25159151 | |
75 | Phosphorylation | ITKTTPQSEMGGYYC EECCCCHHHHCCEEE | 30.65 | 28555341 | |
102 | Sumoylation | FLDHINGKKHQRNLG HHHHCCCHHHHHHCC | 42.46 | 28112733 | |
102 | Acetylation | FLDHINGKKHQRNLG HHHHCCCHHHHHHCC | 42.46 | 25953088 | |
102 | Ubiquitination | FLDHINGKKHQRNLG HHHHCCCHHHHHHCC | 42.46 | 33845483 | |
102 | Sumoylation | FLDHINGKKHQRNLG HHHHCCCHHHHHHCC | 42.46 | - | |
103 | Ubiquitination | LDHINGKKHQRNLGM HHHCCCHHHHHHCCC | 46.50 | - | |
111 | Phosphorylation | HQRNLGMSMRVERST HHHHCCCCCEECHHH | 11.13 | 28555341 | |
123 | Sumoylation | RSTLDQVKKRFEVNK HHHHHHHHHHHHHCH | 32.38 | 28112733 | |
123 | 2-Hydroxyisobutyrylation | RSTLDQVKKRFEVNK HHHHHHHHHHHHHCH | 32.38 | - | |
123 | Ubiquitination | RSTLDQVKKRFEVNK HHHHHHHHHHHHHCH | 32.38 | 33845483 | |
138 | Ubiquitination | KKMEEKQKDYDFEER HHHHHHHHCCCHHHH | 70.13 | 29967540 | |
140 | Phosphorylation | MEEKQKDYDFEERMK HHHHHHCCCHHHHHH | 29.57 | 22817900 | |
190 | Phosphorylation | MAAVMGFSGFGSTKK HHHHHCCCCCCCCCC | 27.73 | 26074081 | |
194 | Phosphorylation | MGFSGFGSTKKSY-- HCCCCCCCCCCCC-- | 34.49 | 26074081 | |
195 | Phosphorylation | GFSGFGSTKKSY--- CCCCCCCCCCCC--- | 42.76 | 26074081 | |
198 | Phosphorylation | GFGSTKKSY------ CCCCCCCCC------ | 37.32 | 26074081 | |
199 | Phosphorylation | FGSTKKSY------- CCCCCCCC------- | 31.30 | 26074081 |
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 ZMAT2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZMAT2_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 ZMAT2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HD_HUMAN | HTT | physical | 23275563 | |
KAD8_HUMAN | AK8 | physical | 25416956 | |
SPERT_HUMAN | SPERT | physical | 25416956 | |
CCD57_HUMAN | CCDC57 | physical | 25416956 | |
ZBT8A_HUMAN | ZBTB8A | physical | 25416956 | |
LSM2_HUMAN | LSM2 | physical | 26344197 | |
LSM3_HUMAN | LSM3 | physical | 26344197 | |
LSM6_HUMAN | LSM6 | physical | 26344197 | |
MAP11_HUMAN | METAP1 | physical | 26344197 | |
NF2IP_HUMAN | NFATC2IP | physical | 26344197 |
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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