| UniProt ID | MA1C1_HUMAN | |
|---|---|---|
| UniProt AC | Q9NR34 | |
| Protein Name | Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC | |
| Gene Name | MAN1C1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 630 | |
| Subcellular Localization |
Golgi apparatus membrane Single-pass type II membrane protein. |
|
| Protein Description | Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc.. | |
| Protein Sequence | MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQPGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREEATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKEMMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAKAWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTGIPKGVVSFKSGNWGWATAGSSSILAEFGSLHLEFLHLTELSGNQVFAEKVRNIRKVLRKIEKPFGLYPNFLSPVSGNWVQHHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNVSPGGLTYIAEWRGGILDHKMGHLACFSGGMIALGAEDAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDWVFNTEAHPLPVNHSDSSGRAWGRH | |
| 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 |
|---|---|---|---|---|---|
| 58 | O-linked_Glycosylation | RLFLAPRTQQPGLEV HHHCCCCCCCCCCHH | 30.42 | OGP | |
| 98 | O-linked_Glycosylation | PGEDDPSSWASPRRR CCCCCCCCCCCCCCC | 31.86 | OGP | |
| 115 | Phosphorylation | GLRRTRPTGPREEAT CCCCCCCCCCHHHHH | 57.43 | 28258704 | |
| 122 | Phosphorylation | TGPREEATAARGNSI CCCHHHHHHHCCCCC | 24.91 | 28258704 | |
| 128 | Phosphorylation | ATAARGNSIPASRPG HHHHCCCCCCCCCCC | 32.54 | - | |
| 128 | O-linked_Glycosylation | ATAARGNSIPASRPG HHHHCCCCCCCCCCC | 32.54 | 55834205 | |
| 132 | O-linked_Glycosylation | RGNSIPASRPGDEGV CCCCCCCCCCCCCCC | 33.38 | 16964243 | |
| 132 | Phosphorylation | RGNSIPASRPGDEGV CCCCCCCCCCCCCCC | 33.38 | 16964243 | |
| 159 | Phosphorylation | LRHPVLGTRADESQE HCCCCCCCCCCCCCC | 20.65 | - | |
| 164 | Phosphorylation | LGTRADESQEPQSQV CCCCCCCCCCCHHHH | 40.15 | 23911959 | |
| 169 | Phosphorylation | DESQEPQSQVRAQRE CCCCCCHHHHHHHHH | 41.16 | 25954137 | |
| 207 | Phosphorylation | RPLTKDGYEGNMFGG CCCCCCCCCCCCCCC | 30.69 | 22210691 | |
| 223 | Phosphorylation | SGATVIDSLDTLYLM CCCCHHHCHHHHHHH | 19.61 | 22210691 | |
| 226 | Phosphorylation | TVIDSLDTLYLMELK CHHHCHHHHHHHHHH | 23.69 | 22210691 | |
| 250 | N-linked_Glycosylation | VGESFHLNVSGEASL CCCCEEEEECCCCEE | 19.83 | UniProtKB CARBOHYD | |
| 264 | Phosphorylation | LFEVNIRYIGGLLSA EEEEEHHHHHHHHHH | 10.50 | 22817900 | |
| 297 | Phosphorylation | KLLPAFNTPTGIPKG CCHHHCCCCCCCCCC | 18.77 | 28258704 | |
| 403 | Phosphorylation | LIKSWLMSGKTDMEA HHHHHHHCCCCCHHH | 34.66 | 24719451 | |
| 447 | Acetylation | RGGILDHKMGHLACF CCCCCCCCCCEEEHH | 46.36 | 7663145 | |
| 492 | Phosphorylation | CHESYARSDTKLGPE HHHHHCCCCCCCCCC | 41.27 | 24719451 | |
| 505 | Phosphorylation | PEAFWFNSGREAVAT CCEEEECCCHHHHHH | 29.74 | 28857561 | |
| 528 | Phosphorylation | LRPEVVESYMYLWRQ ECHHHHHHHHHHHHH | 12.00 | 23898821 | |
| 529 | Phosphorylation | RPEVVESYMYLWRQT CHHHHHHHHHHHHHC | 4.01 | 23898821 | |
| 531 | Phosphorylation | EVVESYMYLWRQTHN HHHHHHHHHHHHCCC | 8.55 | 23898821 | |
| 536 | Phosphorylation | YMYLWRQTHNPIYRE HHHHHHHCCCHHHHH | 18.29 | 23898821 | |
| 541 | Phosphorylation | RQTHNPIYREWGWEV HHCCCHHHHHHCHHH | 12.07 | 23898821 | |
| 554 | Acetylation | EVVLALEKYCRTEAG HHHHHHHHHHCCCCC | 50.96 | 20167786 | |
| 618 | N-linked_Glycosylation | EAHPLPVNHSDSSGR CCCCCCCCCCCCCCC | 27.31 | UniProtKB CARBOHYD |
| 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 MA1C1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MA1C1_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 MA1C1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MA1C1_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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| Phosphorylation | |
| Reference | PubMed |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY. | |