UniProt ID | ANM2_HUMAN | |
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UniProt AC | P55345 | |
Protein Name | Protein arginine N-methyltransferase 2 | |
Gene Name | PRMT2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 433 | |
Subcellular Localization |
Isoform 1: Cytoplasm. Nucleus. Translocates from the cytoplasm to the nucleus, after hormone exposure. Excluded from nucleolus. Isoform PRMT2Alpha: Nucleus. Excluded from nucleolus. Isoform PRMT2Beta: Cytoplasm. Nucleus. Nucleus, nucleolus. I |
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Protein Description | Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation.. | |
Protein Sequence | MATSGDCPRSESQGEEPAECSEAGLLQEGVQPEEFVAIADYAATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHVGKHVDEYDPEDTWQDEEYFGSYGTLKLHLEMLADQPRTTKYHSVILQNKESLTDKVILDVGCGTGIISLFCAHYARPRAVYAVEASEMAQHTGQLVLQNGFADIITVYQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCLSEPCTILQLDMRTVQISDLETLRGELRFDIRKAGTLHGFTAWFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVPVHTGDVVTGSVVLQRNPVWRRHMSVALSWAVTSRQDPTSQKVGEKVFPIWR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
41 | Phosphorylation | EFVAIADYAATDETQ HHEEEEEEECCCHHH | 6.79 | 22817900 | |
53 | Methylation | ETQLSFLRGEKILIL HHHHHHHCCCEEEEE | 49.57 | 58854897 | |
56 | Ubiquitination | LSFLRGEKILILRQT HHHHCCCEEEEEEEC | 45.71 | - | |
61 | Asymmetric dimethylarginine | GEKILILRQTTADWW CCEEEEEEECCCCCC | 25.46 | - | |
61 | Methylation | GEKILILRQTTADWW CCEEEEEEECCCCCC | 25.46 | 24129315 | |
72 | Asymmetric dimethylarginine | ADWWWGERAGCCGYI CCCCCCCCCCCCCEE | 32.13 | - | |
72 | Methylation | ADWWWGERAGCCGYI CCCCCCCCCCCCCEE | 32.13 | 24129315 | |
86 | Ubiquitination | IPANHVGKHVDEYDP EEHHHCCCCCCCCCC | 39.09 | - | |
124 | Ubiquitination | ADQPRTTKYHSVILQ CCCCCCCCEEEEEEC | 40.11 | - | |
125 | Phosphorylation | DQPRTTKYHSVILQN CCCCCCCEEEEEECC | 9.38 | 17322306 | |
127 | Phosphorylation | PRTTKYHSVILQNKE CCCCCEEEEEECCCC | 14.04 | 28857561 | |
133 | Ubiquitination | HSVILQNKESLTDKV EEEEECCCCCCCCCE | 35.40 | - | |
222 | Ubiquitination | TCLLFEFMIESILYA HHHHHHHHHHHHHHH | 2.33 | - | |
277 | Ubiquitination | EFNLSALKSLAVKEF HCCHHHHHHHHHHHH | 43.04 | - | |
286 | Phosphorylation | LAVKEFFSKPKYNHI HHHHHHHCCCCCCCC | 54.06 | 24719451 | |
406 | Phosphorylation | PVWRRHMSVALSWAV CCHHHHHHHHHHHHH | 9.71 | 24043423 | |
410 | Phosphorylation | RHMSVALSWAVTSRQ HHHHHHHHHHHHCCC | 11.85 | 24043423 | |
414 | Phosphorylation | VALSWAVTSRQDPTS HHHHHHHHCCCCCCC | 15.50 | 24043423 | |
415 | Phosphorylation | ALSWAVTSRQDPTSQ HHHHHHHCCCCCCCC | 22.73 | 24043423 | |
427 | Ubiquitination | TSQKVGEKVFPIWR- CCCCCCCEEECCCC- | 43.16 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ANM2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ANM2_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of ANM2_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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