UniProt ID | SAC1_HUMAN | |
---|---|---|
UniProt AC | Q9NTJ5 | |
Protein Name | Phosphatidylinositide phosphatase SAC1 | |
Gene Name | SACM1L | |
Organism | Homo sapiens (Human). | |
Sequence Length | 587 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | Phosphoinositide phosphatase that hydrolyzes phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). [PubMed: 24209621 Has low activity towards PtdIns(3,5)P2 (By similarity] | |
Protein Sequence | MATAAYEQLKLHITPEKFYVEACDDGADDVLTIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLIVITKKIKVGEFFSHVVWKATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLNVDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYNGSKASFVQTRGSIPVFWSQRPNLKYKPLPQISKVANHMDGFQRHFDSQVIIYGKQVIINLINQKGSEKPLEQTFATMVSSLGSGMMRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGQVVANQEGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKIYKNAWADNANACAKQYAGTGALKTDFTRTGKRTHLGLIMDGWNSMIRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MATAAYEQLKLHI --CCCHHHHHHHHCC | 11.18 | 27642862 | |
10 | Acetylation | TAAYEQLKLHITPEK CHHHHHHHHCCCCHH | 37.40 | 25953088 | |
45 | Acetylation | TEVTLAVKKDVPPSA CEEEEEEECCCCHHH | 37.33 | 25953088 | |
101 | Ubiquitination | DFDVLSYKKTMLHLT CCHHHHHEEEEEEEE | 38.09 | - | |
157 | Phosphorylation | SPEFQEMSLLERADQ CHHHHHHHHHHHHHH | 29.11 | 28857561 | |
189 | Ubiquitination | VHRFALPVLHGFITM HHHHHHHHHHCCEEE | 6.83 | - | |
205 | Phosphorylation | SCSINGKYFDWILIS EEEECCEEEEEEEEE | 14.25 | 20068231 | |
212 | Ubiquitination | YFDWILISRRSCFRA EEEEEEEECHHHHHC | 20.42 | - | |
212 | Phosphorylation | YFDWILISRRSCFRA EEEEEEEECHHHHHC | 20.42 | 20068231 | |
230 | Phosphorylation | YYVRGIDSEGHAANF EEEECCCCCCCCCCE | 43.49 | 28270605 | |
240 | Phosphorylation | HAANFVETEQIVHYN CCCCEEEEEEEEEEC | 28.08 | 28270605 | |
250 | Ubiquitination | IVHYNGSKASFVQTR EEEECCCCEEEEEEC | 49.82 | - | |
265 | Phosphorylation | GSIPVFWSQRPNLKY CCCCEEECCCCCCCC | 12.59 | 28857561 | |
273 | Ubiquitination | QRPNLKYKPLPQISK CCCCCCCCCCCHHHH | 38.19 | - | |
294 | Phosphorylation | GFQRHFDSQVIIYGK HHHHHCCCEEEEEEE | 25.96 | 23312004 | |
342 | Malonylation | YIAFDFHKECKNMRW HHEEEHHHHHHCCCH | 65.87 | 26320211 | |
362 | Ubiquitination | LLDQVAEMQDELSYF HHHHHHHCHHHHHEE | 4.36 | - | |
386 | Ubiquitination | ANQEGVFRSNCMDCL ECCCCCCCCCCHHHH | 25.26 | - | |
387 | Phosphorylation | NQEGVFRSNCMDCLD CCCCCCCCCCHHHHC | 23.94 | 20068231 | |
395 | Ubiquitination | NCMDCLDRTNVIQSL CCHHHHCHHHHHHHH | 18.43 | - | |
396 | Phosphorylation | CMDCLDRTNVIQSLL CHHHHCHHHHHHHHH | 33.24 | 20068231 | |
401 | Phosphorylation | DRTNVIQSLLARRSL CHHHHHHHHHHHHHH | 17.77 | 24076635 | |
407 | Phosphorylation | QSLLARRSLQAQLQR HHHHHHHHHHHHHHH | 21.19 | 27174698 | |
422 | Ubiquitination | LGVLHVGQKLEEQDE HCCCCCCCHHHCHHH | 46.18 | - | |
423 | Ubiquitination | GVLHVGQKLEEQDEF CCCCCCCHHHCHHHH | 52.52 | - | |
432 | Ubiquitination | EEQDEFEKIYKNAWA HCHHHHHHHHHHHHH | 57.57 | - | |
432 | Methylation | EEQDEFEKIYKNAWA HCHHHHHHHHHHHHH | 57.57 | 66692039 | |
435 | Ubiquitination | DEFEKIYKNAWADNA HHHHHHHHHHHHHHH | 43.60 | - | |
447 | Ubiquitination | DNANACAKQYAGTGA HHHHHHHHHHCCCCC | 43.66 | - | |
456 | Ubiquitination | YAGTGALKTDFTRTG HCCCCCCCCCCCCCC | 45.58 | 19608861 | |
456 | Malonylation | YAGTGALKTDFTRTG HCCCCCCCCCCCCCC | 45.58 | 26320211 | |
456 | Acetylation | YAGTGALKTDFTRTG HCCCCCCCCCCCCCC | 45.58 | 19608861 | |
483 | Ubiquitination | NSMIRYYKNNFSDGF HHHHHHHHHCCCCCC | 36.16 | 21890473 | |
483 | Ubiquitination | NSMIRYYKNNFSDGF HHHHHHHHHCCCCCC | 36.16 | 21890473 | |
511 | Phosphorylation | VDELESHSPLSVPRD HHHHHHCCCCCCCCC | 36.49 | 29802988 | |
514 | Phosphorylation | LESHSPLSVPRDWKF HHHCCCCCCCCCHHH | 33.20 | 24719451 |
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 SAC1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAC1_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 SAC1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SAC1_HUMAN | SACM1L | physical | 14527956 | |
COPA_HUMAN | COPA | physical | 14527956 | |
COPB_HUMAN | COPB1 | physical | 14527956 | |
COPE_HUMAN | COPE | physical | 14527956 | |
COPG1_HUMAN | COPG1 | physical | 14527956 |
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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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, AND MASS SPECTROMETRY. |