UniProt ID | ASND1_HUMAN | |
---|---|---|
UniProt AC | Q9NWL6 | |
Protein Name | Asparagine synthetase domain-containing protein 1 | |
Gene Name | ASNSD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 643 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MCGICCSVNFSAEHFSQDLKEDLLYNLKQRGPNSSKQLLKSDVNYQCLFSAHVLHLRGVLTTQPVEDERGNVFLWNGEIFSGIKVEAEENDTQILFNYLSSCKNESEILSLFSEVQGPWSFIYYQASSHYLWFGRDFFGRRSLLWHFSNLGKSFCLSSVGTQTSGLANQWQEVPASGLFRIDLKSTVISGCIILQLYPWKYISRENIIEENVNSLSQISADLPAFVSVVANEAKLYLEKPVVPLNMMLPQAALETHCSNISNVPPTREILQVFLTDVHMKEVIQQFIDVLSVAVKKRVLCLPRDENLTANEVLKTCDRKANVAILFSGGIDSMVIATLADRHIPLDEPIDLLNVAFIAEEKTMPTTFNREGNKQKNKCEIPSEEFSKDVAAAAADSPNKHVSVPDRITGRAGLKELQAVSPSRIWNFVEINVSMEELQKLRRTRICHLIRPLDTVLDDSIGCAVWFASRGIGWLVAQEGVKSYQSNAKVVLTGIGADEQLAGYSRHRVRFQSHGLEGLNKEIMMELGRISSRNLGRDDRVIGDHGKEARFPFLDENVVSFLNSLPIWEKANLTLPRGIGEKLLLRLAAVELGLTASALLPKRAMQFGSRIAKMEKINEKASDKCGRLQIMSLENLSIEKETKL | |
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 |
---|---|---|---|---|---|
28 | Ubiquitination | EDLLYNLKQRGPNSS HHHHHHHHHHCCCCH | 34.02 | 29967540 | |
36 | Ubiquitination | QRGPNSSKQLLKSDV HHCCCCHHHHHHCCC | 44.80 | 29967540 | |
186 | Phosphorylation | FRIDLKSTVISGCII CCCCCCCCEEEECCH | 21.92 | 28555341 | |
197 | Phosphorylation | GCIILQLYPWKYISR ECCHHHHCCCCCCCH | 8.29 | 25690035 | |
314 | Ubiquitination | LTANEVLKTCDRKAN CCHHHHHHHCCCCCC | 52.89 | 29967540 | |
377 | Ubiquitination | EGNKQKNKCEIPSEE CCCCCCCCCCCCHHH | 40.04 | 29967540 | |
387 | Ubiquitination | IPSEEFSKDVAAAAA CCHHHHHHHHHHHHC | 62.64 | 29967540 | |
396 | Phosphorylation | VAAAAADSPNKHVSV HHHHHCCCCCCCCCC | 26.16 | 29255136 | |
399 | Ubiquitination | AAADSPNKHVSVPDR HHCCCCCCCCCCCCH | 49.09 | 22817900 | |
402 | Phosphorylation | DSPNKHVSVPDRITG CCCCCCCCCCCHHCC | 27.87 | 29978859 | |
414 | Ubiquitination | ITGRAGLKELQAVSP HCCCCCHHHHHCCCH | 56.30 | - | |
512 | Phosphorylation | RHRVRFQSHGLEGLN CCCHHHHHCCCCCCC | 19.46 | 20068231 | |
530 | Phosphorylation | MMELGRISSRNLGRD HHHHHHHHCCCCCCC | 23.14 | 27282143 | |
531 | Phosphorylation | MELGRISSRNLGRDD HHHHHHHCCCCCCCC | 23.87 | 27499020 | |
573 | Phosphorylation | IWEKANLTLPRGIGE HHHHCCCCCCCCHHH | 34.23 | 24719451 | |
594 | Phosphorylation | AAVELGLTASALLPK HHHHHCCCHHHHCHH | 19.44 | - | |
596 | Phosphorylation | VELGLTASALLPKRA HHHCCCHHHHCHHHH | 17.76 | 24425749 | |
608 | Phosphorylation | KRAMQFGSRIAKMEK HHHHHHHHHHHHHHH | 23.08 | - | |
621 | Phosphorylation | EKINEKASDKCGRLQ HHHCHHHHCCCCCEE | 48.98 | 20068231 | |
631 | Phosphorylation | CGRLQIMSLENLSIE CCCEEEEEEECCCCC | 33.87 | 28348404 | |
636 | Phosphorylation | IMSLENLSIEKETKL EEEEECCCCCCCCCC | 40.04 | 28348404 | |
641 | Phosphorylation | NLSIEKETKL----- CCCCCCCCCC----- | 49.03 | 20068231 |
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 ASND1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASND1_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 ASND1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ASND1_HUMAN !! |
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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