| UniProt ID | ALG1_HUMAN | |
|---|---|---|
| UniProt AC | Q9BT22 | |
| Protein Name | Chitobiosyldiphosphodolichol beta-mannosyltransferase | |
| Gene Name | ALG1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 464 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type II membrane protein . |
|
| Protein Description | Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.. | |
| Protein Sequence | MAASCLVLLALCLLLPLLLLGGWKRWRRGRAARHVVAVVLGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLGSMHSPFRARSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFPDPAGKLNQFRKNLRESQQLRWDESWVQTVLPLVMDT | |
| 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 |
|---|---|---|---|---|---|
| 46 | Phosphorylation | VLGDVGRSPRMQYHA EECCCCCCHHHHHHH | 15.78 | 21712546 | |
| 68 | Ubiquitination | FSVTLLGFCNSKPHD CEEEEEHHCCCCCCH | 3.44 | 22817900 | |
| 72 | Ubiquitination | LLGFCNSKPHDELLQ EEHHCCCCCCHHHHH | 32.17 | 21890473 | |
| 72 | Ubiquitination | LLGFCNSKPHDELLQ EEHHCCCCCCHHHHH | 32.17 | 21890473 | |
| 106 | Ubiquitination | RVFQYGVKVVLQAMY HHHHHHHHHHHHHHH | 23.43 | 21890473 | |
| 106 | Ubiquitination | RVFQYGVKVVLQAMY HHHHHHHHHHHHHHH | 23.43 | 21890473 | |
| 112 | Ubiquitination | VKVVLQAMYLLWKLM HHHHHHHHHHHHHHH | 1.24 | 21890473 | |
| 112 | Ubiquitination | VKVVLQAMYLLWKLM HHHHHHHHHHHHHHH | 1.24 | 21890473 | |
| 113 | Phosphorylation | KVVLQAMYLLWKLMW HHHHHHHHHHHHHHC | 11.14 | 28634298 | |
| 125 | Ubiquitination | LMWREPGAYIFLQNP HHCCCCCEEEEECCC | 12.64 | - | |
| 125 | Ubiquitination | LMWREPGAYIFLQNP HHCCCCCEEEEECCC | 12.64 | 21987572 | |
| 179 | Ubiquitination | HPLVLLAKWYEKFFG CHHHHHHHHHHHHHH | 50.72 | 22817900 | |
| 183 | Ubiquitination | LLAKWYEKFFGRLSH HHHHHHHHHHHHHHH | 30.23 | 21890473 | |
| 217 | Ubiquitination | RAVTVYDKPASFFKE EEEEEECCCHHHHCC | 25.46 | 21890473 | |
| 223 | Ubiquitination | DKPASFFKETPLDLQ CCCHHHHCCCCCCHH | 59.68 | 22817900 | |
| 236 | Ubiquitination | LQHRLFMKLGSMHSP HHHHHHHHHCCCCCC | 42.22 | 21987572 | |
| 239 | Phosphorylation | RLFMKLGSMHSPFRA HHHHHHCCCCCCCCC | 24.61 | 18691976 | |
| 242 | Phosphorylation | MKLGSMHSPFRARSE HHHCCCCCCCCCCCC | 19.66 | 26931382 | |
| 284 | Ubiquitination | PALLVSSTSWTEDED CEEEEECCCCCCCCC | 22.30 | 21963094 | |
| 284 | Ubiquitination | PALLVSSTSWTEDED CEEEEECCCCCCCCC | 22.30 | - | |
| 322 | Ubiquitination | LVCVITGKGPLREYY EEEEEECCCHHHHHH | 49.02 | - | |
| 382 | Ubiquitination | LPMKVVDMFGCCLPV CCHHHHHHHCCCHHH | 1.78 | 21963094 | |
| 395 | Ubiquitination | PVCAVNFKCLHELVK HHHHHCHHHHHHHHH | 30.59 | 21963094 |
| 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 ALG1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ALG1_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 ALG1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ALG1_HUMAN !! | ||||
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| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASSSPECTROMETRY. | |