UniProt ID | UROM_HUMAN | |
---|---|---|
UniProt AC | P07911 | |
Protein Name | Uromodulin | |
Gene Name | UMOD | |
Organism | Homo sapiens (Human). | |
Sequence Length | 640 | |
Subcellular Localization |
Apical cell membrane Lipid-anchor, GPI-anchor . Basolateral cell membrane Lipid-anchor, GPI-anchor . Cell projection, cilium membrane . Only a small fraction sorts to the basolateral pole of tubular epithelial cells compared to apical localizatio |
|
Protein Description | Uromodulin: Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability (Probable). May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. [PubMed: 3498215 Facilitates neutrophil migration across renal epithelia] | |
Protein Sequence | MGQPSLTWMLMVVVASWFITTAATDTSEARWCSECHSNATCTEDEAVTTCTCQEGFTGDGLTCVDLDECAIPGAHNCSANSSCVNTPGSFSCVCPEGFRLSPGLGCTDVDECAEPGLSHCHALATCVNVVGSYLCVCPAGYRGDGWHCECSPGSCGPGLDCVPEGDALVCADPCQAHRTLDEYWRSTEYGEGYACDTDLRGWYRFVGQGGARMAETCVPVLRCNTAAPMWLNGTHPSSDEGIVSRKACAHWSGHCCLWDASVQVKACAGGYYVYNLTAPPECHLAYCTDPSSVEGTCEECSIDEDCKSNNGRWHCQCKQDFNITDISLLEHRLECGANDMKVSLGKCQLKSLGFDKVFMYLSDSRCSGFNDRDNRDWVSVVTPARDGPCGTVLTRNETHATYSNTLYLADEIIIRDLNIKINFACSYPLDMKVSLKTALQPMVSALNIRVGGTGMFTVRMALFQTPSYTQPYQGSSVTLSTEAFLYVGTMLDGGDLSRFALLMTNCYATPSSNATDPLKYFIIQDRCPHTRDSTIQVVENGESSQGRFSVQMFRFAGNYDLVYLHCEVYLCDTMNEKCKPTCSGTRFRSGSVIDQSRVLNLGPITRKGVQATVSRAFSSLGLLKVWLPLLLSATLTLTFQ | |
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 |
---|---|---|---|---|---|
38 | N-linked_Glycosylation | WCSECHSNATCTEDE CCHHHCCCCEECCCC | 18.66 | UniProtKB CARBOHYD | |
76 | N-linked_Glycosylation | CAIPGAHNCSANSSC CCCCCCCCCCCCCCC | 22.39 | 9884403 | |
76 | N-linked_Glycosylation | CAIPGAHNCSANSSC CCCCCCCCCCCCCCC | 22.39 | 9884403 | |
80 | N-linked_Glycosylation | GAHNCSANSSCVNTP CCCCCCCCCCCCCCC | 20.40 | 9884403 | |
80 | N-linked_Glycosylation | GAHNCSANSSCVNTP CCCCCCCCCCCCCCC | 20.40 | 9884403 | |
232 | N-linked_Glycosylation | TAAPMWLNGTHPSSD CCCCEECCCCCCCCC | 37.49 | 22171320 | |
232 | N-linked_Glycosylation | TAAPMWLNGTHPSSD CCCCEECCCCCCCCC | 37.49 | 22171320 | |
275 | N-linked_Glycosylation | AGGYYVYNLTAPPEC CCCEEEEECCCCCCE | 22.37 | 9884403 | |
275 | N-linked_Glycosylation | AGGYYVYNLTAPPEC CCCEEEEECCCCCCE | 22.37 | 9884403 | |
292 | Phosphorylation | AYCTDPSSVEGTCEE EEECCHHHCCCCEEE | 29.58 | 29759185 | |
322 | N-linked_Glycosylation | CQCKQDFNITDISLL EEECCCCCCCCHHHH | 44.53 | 22171320 | |
322 | N-linked_Glycosylation | CQCKQDFNITDISLL EEECCCCCCCCHHHH | 44.53 | 22171320 | |
351 | Phosphorylation | LGKCQLKSLGFDKVF ECCHHHHHCCCCEEE | 42.17 | 24719451 | |
362 | Phosphorylation | DKVFMYLSDSRCSGF CEEEEEEECCCCCCC | 18.95 | 24719451 | |
391 | Phosphorylation | ARDGPCGTVLTRNET CCCCCCCCEEECCCC | 21.04 | 29759185 | |
394 | Phosphorylation | GPCGTVLTRNETHAT CCCCCEEECCCCCCE | 27.41 | 29759185 | |
396 | N-linked_Glycosylation | CGTVLTRNETHATYS CCCEEECCCCCCEEC | 53.97 | 22171320 | |
396 | N-linked_Glycosylation | CGTVLTRNETHATYS CCCEEECCCCCCEEC | 53.97 | 22171320 | |
513 | N-linked_Glycosylation | CYATPSSNATDPLKY CCCCCCCCCCCCCEE | 51.72 | 32815518 | |
513 | N-linked_Glycosylation | CYATPSSNATDPLKY CCCCCCCCCCCCCEE | 51.72 | 9884403 | |
543 | Phosphorylation | QVVENGESSQGRFSV EEEECCCCCCCEEEE | 29.38 | 29759185 | |
612 | Phosphorylation | TRKGVQATVSRAFSS CCHHHHHHHHHHHHH | 11.26 | 24732914 | |
614 | Phosphorylation | KGVQATVSRAFSSLG HHHHHHHHHHHHHHC | 17.34 | 24732914 | |
614 | GPI-anchor | KGVQATVSRAFSSLG HHHHHHHHHHHHHHC | 17.34 | - |
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 UROM_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UROM_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 UROM_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of UROM_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00537 | Nephronophthisis-medullary cystic kidney disease, including; Nephronophthisis (NPH) ; Nephronophthis | |||||
H00541 | Uromodulin-associated kidney diseases, including: Medullary cystic kidney disease 2; Familial juveni | |||||
OMIM Disease | ||||||
162000 | Familial juvenile hyperuricemic nephropathy 1 (HNFJ1) | |||||
603860 | Medullary cystic kidney disease 2 (MCKD2) | |||||
609886 | Glomerulocystic kidney disease with hyperuricemia and isosthenuria (GCKDHI) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-232; ASN-322 AND ASN-396, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY. |