UniProt ID | TRI27_HUMAN | |
---|---|---|
UniProt AC | P14373 | |
Protein Name | Zinc finger protein RFP | |
Gene Name | TRIM27 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 513 | |
Subcellular Localization | Nucleus . Cytoplasm . Nucleus, PML body. Early endosome . Nuclear or cytoplasmic depending on the cell type (By similarity). Colocalized with PML and EIF3S6 in nuclear bodies. Recruited to retromer-containing endosomes via interaction with MAGEL2 (Pu | |
Protein Description | E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly. [PubMed: 23452853 Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA.] | |
Protein Sequence | MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP | |
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 |
---|---|---|---|---|---|
79 | Acetylation | ANVTQLVKQLRTERP HHHHHHHHHHHCCCC | 52.81 | 26051181 | |
79 | Ubiquitination | ANVTQLVKQLRTERP HHHHHHHHHHHCCCC | 52.81 | 21890473 | |
79 (in isoform 2) | Ubiquitination | - | 52.81 | 21890473 | |
79 (in isoform 1) | Ubiquitination | - | 52.81 | 21890473 | |
79 | Ubiquitination | ANVTQLVKQLRTERP HHHHHHHHHHHCCCC | 52.81 | 21890473 | |
79 | Ubiquitination | ANVTQLVKQLRTERP HHHHHHHHHHHCCCC | 52.81 | 21890473 | |
98 | Ubiquitination | GEMGVCEKHREPLKL CCCCCCHHCCCCCEE | 42.72 | - | |
128 | Phosphorylation | SREHRGHSVLPLEEA CCCCCCCCCCCHHHH | 28.33 | 27050516 | |
140 | Ubiquitination | EEAVEGFKEQIQNQL HHHHHHHHHHHHHHH | 60.61 | - | |
151 | Acetylation | QNQLDHLKRVKDLKK HHHHHHHHHHHHHHH | 52.29 | 26051181 | |
151 | Ubiquitination | QNQLDHLKRVKDLKK HHHHHHHHHHHHHHH | 52.29 | - | |
173 | Phosphorylation | QARAELLSLTQMERE HHHHHHHHHHHHHHH | 41.83 | 28555341 | |
175 | Phosphorylation | RAELLSLTQMEREKI HHHHHHHHHHHHHHH | 23.61 | 29083192 | |
177 | Sulfoxidation | ELLSLTQMEREKIVW HHHHHHHHHHHHHHH | 4.40 | 21406390 | |
181 | Ubiquitination | LTQMEREKIVWEFEQ HHHHHHHHHHHHHHH | 49.10 | - | |
190 | Phosphorylation | VWEFEQLYHSLKEHE HHHHHHHHHHHHHHH | 6.78 | 22210691 | |
192 | Phosphorylation | EFEQLYHSLKEHEYR HHHHHHHHHHHHHHH | 27.81 | 22210691 | |
194 | Ubiquitination | EQLYHSLKEHEYRLL HHHHHHHHHHHHHHH | 61.10 | - | |
269 | Phosphorylation | RIPEPWITPPDLQEK CCCCCCCCCCCHHHH | 25.54 | - | |
276 | Ubiquitination | TPPDLQEKIHIFAQK CCCCHHHHHHHHHHH | 26.99 | - | |
283 | Ubiquitination | KIHIFAQKCLFLTES HHHHHHHHHHHHHHH | 29.49 | - | |
292 | Ubiquitination | LFLTESLKQFTEKMQ HHHHHHHHHHHHHHH | 53.28 | - | |
297 | Ubiquitination | SLKQFTEKMQSDMEK HHHHHHHHHHHHHHH | 38.90 | - | |
304 | Ubiquitination | KMQSDMEKIQELREA HHHHHHHHHHHHHHH | 42.95 | - | |
341 | Phosphorylation | NLRQVRYSYLQQDLP CHHHHHHHHHHHCCC | 14.59 | 19691289 | |
342 | Phosphorylation | LRQVRYSYLQQDLPD HHHHHHHHHHHCCCC | 10.29 | 29496907 | |
380 | Ubiquitination | WEVEVGDKAKWTIGV EEEEECCEEEEEEEE | 46.03 | 22053931 | |
380 (in isoform 1) | Ubiquitination | - | 46.03 | 21890473 | |
382 | Ubiquitination | VEVGDKAKWTIGVCE EEECCEEEEEEEEEC | 51.08 | - | |
479 | Phosphorylation | PYFSLSYSGGKSAAP CCEEEEECCCCCCCC | 37.38 | 30576142 | |
483 | Phosphorylation | LSYSGGKSAAPLIIC EEECCCCCCCCEEEE | 32.70 | 20068231 | |
493 | Phosphorylation | PLIICPMSGIDGFSG CEEEEECCCCCCCCC | 20.10 | 20068231 | |
499 | Phosphorylation | MSGIDGFSGHVGNHG CCCCCCCCCCCCCCC | 33.25 | 25159151 | |
508 | Phosphorylation | HVGNHGHSMETSP-- CCCCCCCCCCCCC-- | 23.94 | 30576142 | |
511 | Phosphorylation | NHGHSMETSP----- CCCCCCCCCC----- | 37.34 | 30576142 | |
512 | Phosphorylation | HGHSMETSP------ CCCCCCCCC------ | 18.46 | 25159151 |
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 TRI27_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI27_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 TRI27_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
188550 | Thyroid papillary carcinoma (TPC) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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