UROM_HUMAN - dbPTM
UROM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
38N-linked_GlycosylationWCSECHSNATCTEDE
CCHHHCCCCEECCCC
18.66UniProtKB CARBOHYD
76N-linked_GlycosylationCAIPGAHNCSANSSC
CCCCCCCCCCCCCCC
22.399884403
76N-linked_GlycosylationCAIPGAHNCSANSSC
CCCCCCCCCCCCCCC
22.399884403
80N-linked_GlycosylationGAHNCSANSSCVNTP
CCCCCCCCCCCCCCC
20.409884403
80N-linked_GlycosylationGAHNCSANSSCVNTP
CCCCCCCCCCCCCCC
20.409884403
232N-linked_GlycosylationTAAPMWLNGTHPSSD
CCCCEECCCCCCCCC
37.4922171320
232N-linked_GlycosylationTAAPMWLNGTHPSSD
CCCCEECCCCCCCCC
37.4922171320
275N-linked_GlycosylationAGGYYVYNLTAPPEC
CCCEEEEECCCCCCE
22.379884403
275N-linked_GlycosylationAGGYYVYNLTAPPEC
CCCEEEEECCCCCCE
22.379884403
292PhosphorylationAYCTDPSSVEGTCEE
EEECCHHHCCCCEEE
29.5829759185
322N-linked_GlycosylationCQCKQDFNITDISLL
EEECCCCCCCCHHHH
44.5322171320
322N-linked_GlycosylationCQCKQDFNITDISLL
EEECCCCCCCCHHHH
44.5322171320
351PhosphorylationLGKCQLKSLGFDKVF
ECCHHHHHCCCCEEE
42.1724719451
362PhosphorylationDKVFMYLSDSRCSGF
CEEEEEEECCCCCCC
18.9524719451
391PhosphorylationARDGPCGTVLTRNET
CCCCCCCCEEECCCC
21.0429759185
394PhosphorylationGPCGTVLTRNETHAT
CCCCCEEECCCCCCE
27.4129759185
396N-linked_GlycosylationCGTVLTRNETHATYS
CCCEEECCCCCCEEC
53.9722171320
396N-linked_GlycosylationCGTVLTRNETHATYS
CCCEEECCCCCCEEC
53.9722171320
513N-linked_GlycosylationCYATPSSNATDPLKY
CCCCCCCCCCCCCEE
51.7232815518
513N-linked_GlycosylationCYATPSSNATDPLKY
CCCCCCCCCCCCCEE
51.729884403
543PhosphorylationQVVENGESSQGRFSV
EEEECCCCCCCEEEE
29.3829759185
612PhosphorylationTRKGVQATVSRAFSS
CCHHHHHHHHHHHHH
11.2624732914
614PhosphorylationKGVQATVSRAFSSLG
HHHHHHHHHHHHHHC
17.3424732914
614GPI-anchorKGVQATVSRAFSSLG
HHHHHHHHHHHHHHC
17.34-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UROM_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UROM_HUMAN !!

Drug and Disease Associations
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
162000Familial juvenile hyperuricemic nephropathy 1 (HNFJ1)
603860Medullary cystic kidney disease 2 (MCKD2)
609886Glomerulocystic 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.
Regulatory Network of UROM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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