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Protein

Uromodulin

Gene

UMOD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PubMed:20798515).Curated2 Publications
Uromodulin, secreted form: In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.By similarityCurated

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • IgG binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Uromodulin
Alternative name(s):
Tamm-Horsfall urinary glycoprotein
Short name:
THP
Cleaved into the following chain:
Gene namesi
Name:UMOD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:12559. UMOD.

Subcellular locationi

Uromodulin, secreted form :

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • ciliary membrane Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: Ensembl
  • extrinsic component of membrane Source: ProtInc
  • Golgi apparatus Source: Ensembl
  • membrane raft Source: Ensembl
  • primary cilium Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Familial juvenile hyperuricemic nephropathy 1 (HNFJ1)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal disease characterized by juvenile onset of hyperuricemia, polyuria, progressive renal failure, and gout. The disease is associated with interstitial pathological changes resulting in fibrosis.
See also OMIM:162000
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521C → W in HNFJ1. 1 Publication
VAR_073052
Natural varianti59 – 591D → A in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_073053
Natural varianti77 – 771C → Y in HNFJ1. 1 Publication
Corresponds to variant rs121917768 [ dbSNP | Ensembl ].
VAR_025950
Natural varianti109 – 1091V → E in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
Corresponds to variant rs780462125 [ dbSNP | Ensembl ].
VAR_071398
Natural varianti112 – 1121C → R in HNFJ1. 1 Publication
VAR_073054
Natural varianti126 – 1261C → R in HNFJ1. 2 Publications
Corresponds to variant rs121917769 [ dbSNP | Ensembl ].
VAR_025952
Natural varianti128 – 1281N → S in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
Corresponds to variant rs121917770 [ dbSNP | Ensembl ].
VAR_025953
Natural varianti135 – 1351C → S in HNFJ1. 1 Publication
VAR_073055
Natural varianti148 – 1481C → W in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
VAR_025954
Natural varianti148 – 1481C → Y in HNFJ1. 1 Publication
Corresponds to variant rs28934582 [ dbSNP | Ensembl ].
VAR_017667
Natural varianti150 – 1501C → S in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER; results is abnormal intracellular polymerization of the mutant protein. 3 Publications
VAR_025955
Natural varianti170 – 1701C → Y in HNFJ1. 1 Publication
VAR_073057
Natural varianti185 – 1851R → S in HNFJ1. 1 Publication
VAR_073058
Natural varianti195 – 1951C → F in HNFJ1. 1 Publication
VAR_073059
Natural varianti202 – 2021W → S in HNFJ1. 1 Publication
VAR_073060
Natural varianti204 – 2041R → G in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_073061
Natural varianti217 – 2171C → G in HNFJ1. 1 Publication
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_073062
Natural varianti217 – 2171C → R in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_017668
Natural varianti222 – 2221R → P in HNFJ1. 1 Publication
VAR_073063
Natural varianti223 – 2231C → Y in HNFJ1. 1 Publication
VAR_025956
Natural varianti225 – 2251T → M in HNFJ1. 1 Publication
VAR_073064
Natural varianti230 – 2301W → R in HNFJ1. 1 Publication
VAR_071399
Natural varianti236 – 2361P → L in HNFJ1. 1 Publication
VAR_073065
Natural varianti236 – 2361P → Q in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_071400
Natural varianti236 – 2361P → R in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 1 Publication
VAR_073066
Natural varianti248 – 2481C → W in MCKD2 and HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
VAR_025958
Natural varianti255 – 2551C → Y in HNFJ1. 1 Publication
Corresponds to variant rs121917771 [ dbSNP | Ensembl ].
VAR_025959
Natural varianti282 – 2821C → R in HNFJ1. 1 Publication
VAR_073067
Natural varianti300 – 3001C → G in HNFJ1. 1 Publication
Corresponds to variant rs121917772 [ dbSNP | Ensembl ].
VAR_025960
Natural varianti316 – 3161Q → P in HNFJ1. 1 Publication
VAR_073068
Natural varianti317 – 3171C → Y in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025962
Natural varianti347 – 3471C → G in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_073069
Natural varianti461 – 4611A → E in HNFJ1. 1 Publication
VAR_071401
Medullary cystic kidney disease 2 (MCKD2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of tubulointerstitial nephropathy characterized by formation of renal cysts at the corticomedullary junction. It is characterized by adult onset of impaired renal function and salt wasting resulting in end-stage renal failure by the sixth decade.
See also OMIM:603860
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 975VCPEG → AASC in MCKD2; results in mutant retention in the ER; results is abnormal intracellular polymerization of the mutant protein. 2 Publications
VAR_025951
Natural varianti103 – 1031G → C in MCKD2. 1 Publication
Corresponds to variant rs28934584 [ dbSNP | Ensembl ].
VAR_017666
Natural varianti225 – 2251T → K in MCKD2; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_025957
Natural varianti248 – 2481C → W in MCKD2 and HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
VAR_025958
Glomerulocystic kidney disease with hyperuricemia and isosthenuria (GCKDHI)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal disorder characterized by a cystic dilation of Bowman space, a collapse of glomerular tuft, and hyperuricemia due to low fractional excretion of uric acid and severe impairment of urine concentrating ability.
See also OMIM:609886
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti315 – 3151C → R in GCKDHI; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
Corresponds to variant rs121917773 [ dbSNP | Ensembl ].
VAR_025961

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi333 – 3331L → K: Abolishes polymerization and filament formation of the secreted form. 1 Publication
Mutagenesisi421 – 4211I → K: Abolishes polymerization and filament formation of the secreted form. 1 Publication
Mutagenesisi430 – 4301D → L: Impairs polymerization and filament formation of the secreted form. 1 Publication
Mutagenesisi435 – 4351L → S: Impairs polymerization and filament formation of the secreted form. 1 Publication
Mutagenesisi458 – 4581V → R: Leads to retention in the endoplasmic reticulum, probably due to misfolding. 1 Publication
Mutagenesisi586 – 5894RFRS → AAAA: Abolishes cleavage by HPN. 3 Publications
Mutagenesisi598 – 6003VLN → AAA: Decreased export from the endoplasmic reticulum, leading to decreased secretion. Impairs polymerization. 1 Publication
Mutagenesisi602 – 6032GP → AA: Decreased export from the endoplasmic reticulum, leading to decreased secretion. Impairs polymerization. 1 Publication
Mutagenesisi605 – 6073TRK → AAA: No effect on secretion. Does not impair polymerization. 1 Publication

Keywords - Diseasei

Ciliopathy, Disease mutation, Nephronophthisis

Organism-specific databases

MalaCardsiUMOD.
MIMi162000. phenotype.
603860. phenotype.
609886. phenotype.
Orphaneti34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
209886. Familial juvenile hyperuricemic nephropathy type 1.
PharmGKBiPA37199.

Polymorphism and mutation databases

BioMutaiUMOD.
DMDMi137116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 614590UromodulinPRO_0000041671Add
BLAST
Chaini25 – 587563Uromodulin, secreted formPRO_0000407909Add
BLAST
Propeptidei615 – 64026Removed in mature formSequence analysisPRO_0000041672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 50PROSITE-ProRule annotation
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi52 ↔ 63PROSITE-ProRule annotation
Disulfide bondi69 ↔ 83PROSITE-ProRule annotation
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi77 ↔ 92PROSITE-ProRule annotation
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence analysis
Disulfide bondi94 ↔ 106PROSITE-ProRule annotation
Disulfide bondi112 ↔ 126PROSITE-ProRule annotation
Disulfide bondi120 ↔ 135PROSITE-ProRule annotation
Disulfide bondi137 ↔ 148PROSITE-ProRule annotation
Glycosylationi232 – 2321N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi275 – 2751N-linked (GlcNAc...)CAR_000178
Disulfide bondi297 ↔ 3061 Publication
Disulfide bondi300 ↔ 3151 Publication
Disulfide bondi317 ↔ 3471 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi335 ↔ 4251 Publication
Disulfide bondi366 ↔ 3891 Publication
Glycosylationi396 – 3961N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi506 ↔ 566PROSITE-ProRule annotation1 Publication
Disulfide bondi527 ↔ 5821 Publication
Disulfide bondi571 ↔ 5781 Publication
Lipidationi614 – 6141GPI-anchor amidated serineSequence analysis

Post-translational modificationi

N-glycosylated (PubMed:19005207, PubMed:26673890, PubMed:26811476). N-glycan heterogeneity at Asn-232: Hex7HexNAc6 (major) and dHex1Hex7HexNAc6 (minor); at Asn-322: dHex1Hex6HexNAc5 (minor), dHex1Hex7HexNAc6 (major) and dHex1Hex8HexNAc7 (minor); at Asn-396: Hex6HexNAc5 (major), dHex1Hex6HexNAc5 (minor) and Hex7HexNAc6 (minor) (PubMed:22171320).4 Publications
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine (PubMed:18375198, PubMed:19005207). This cleavage is catalyzed by HPN (PubMed:26673890).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei587 – 5882Cleavage1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP07911.
PeptideAtlasiP07911.
PRIDEiP07911.

PTM databases

UniCarbKBiP07911.

Expressioni

Tissue specificityi

Expressed in the tubular cells of the kidney. Most abundant protein in normal urine (at protein level). Synthesized exclusively in the kidney. Expressed exclusively by epithelial cells of the thick ascending limb of Henle's loop (TALH) and of distal convoluted tubule lumen.5 Publications

Gene expression databases

BgeeiP07911.
CleanExiHS_UMOD.
ExpressionAtlasiP07911. baseline and differential.
GenevisibleiP07911. HS.

Organism-specific databases

HPAiCAB009446.
HPA043420.
HPA054721.

Interactioni

Subunit structurei

Uromodulin, secreted form: homodimer that then polymerizes into long filaments.3 Publications

GO - Molecular functioni

  • IgG binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113216. 1 interaction.
IntActiP07911. 2 interactions.
STRINGi9606.ENSP00000306279.

Structurei

Secondary structure

1
640
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi296 – 2994Combined sources
Beta strandi304 – 3085Combined sources
Beta strandi313 – 3175Combined sources
Helixi327 – 3293Combined sources
Beta strandi332 – 3354Combined sources
Beta strandi337 – 3459Combined sources
Helixi346 – 3505Combined sources
Turni351 – 3533Combined sources
Beta strandi377 – 38711Combined sources
Helixi388 – 3903Combined sources
Beta strandi392 – 3954Combined sources
Beta strandi397 – 40812Combined sources
Turni411 – 4144Combined sources
Beta strandi419 – 42810Combined sources
Helixi431 – 4377Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi443 – 4508Combined sources
Turni451 – 4533Combined sources
Beta strandi454 – 46512Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi485 – 49410Combined sources
Turni496 – 4983Combined sources
Beta strandi499 – 51214Combined sources
Beta strandi520 – 5245Combined sources
Beta strandi527 – 5293Combined sources
Beta strandi535 – 55016Combined sources
Helixi552 – 5554Combined sources
Beta strandi560 – 57213Combined sources
Turni573 – 5753Combined sources
Helixi595 – 5973Combined sources
Beta strandi598 – 6069Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WRNX-ray3.20A/B295-610[»]
ProteinModelPortaliP07911.
SMRiP07911. Positions 29-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6437EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini65 – 10743EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini108 – 14942EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini334 – 589256ZPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni430 – 45324Important for secretion and polymerization into filaments1 PublicationAdd
BLAST
Regioni586 – 5894Essential for cleavage by HPN3 Publications
Regioni598 – 60710Regulates polymerization into filaments1 Publication

Domaini

The ZP domain mediates polymerization, leading to the formation of long filaments.1 Publication

Sequence similaritiesi

Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IVSV. Eukaryota.
ENOG410YDU6. LUCA.
GeneTreeiENSGT00530000063244.
HOGENOMiHOG000293303.
HOVERGENiHBG004349.
InParanoidiP07911.
KOiK18274.
OrthoDBiEOG7SFHWJ.
PhylomeDBiP07911.
TreeFamiTF330284.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR023413. GFP-like.
IPR009030. Growth_fac_rcpt_.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 2 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07911-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC
60 70 80 90 100
TCQEGFTGDG LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL
110 120 130 140 150
SPGLGCTDVD ECAEPGLSHC HALATCVNVV GSYLCVCPAG YRGDGWHCEC
160 170 180 190 200
SPGSCGPGLD CVPEGDALVC ADPCQAHRTL DEYWRSTEYG EGYACDTDLR
210 220 230 240 250
GWYRFVGQGG ARMAETCVPV LRCNTAAPMW LNGTHPSSDE GIVSRKACAH
260 270 280 290 300
WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC
310 320 330 340 350
SIDEDCKSNN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK
360 370 380 390 400
SLGFDKVFMY LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA
410 420 430 440 450
TYSNTLYLAD EIIIRDLNIK INFACSYPLD MKVSLKTALQ PMVSALNIRV
460 470 480 490 500
GGTGMFTVRM ALFQTPSYTQ PYQGSSVTLS TEAFLYVGTM LDGGDLSRFA
510 520 530 540 550
LLMTNCYATP SSNATDPLKY FIIQDRCPHT RDSTIQVVEN GESSQGRFSV
560 570 580 590 600
QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN
610 620 630 640
LGPITRKGVQ ATVSRAFSSL GLLKVWLPLL LSATLTLTFQ
Length:640
Mass (Da):69,761
Last modified:August 1, 1988 - v1
Checksum:iD26A07A76353AE48
GO
Isoform 2 (identifier: P07911-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.

Note: No experimental confirmation available.
Show »
Length:507
Mass (Da):55,960
Checksum:iFBFC739EA15E3D22
GO
Isoform 3 (identifier: P07911-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-234: FVGQGGARMAETCVPVLRCNTAAPMWLNGT → P

Note: No experimental confirmation available.
Show »
Length:611
Mass (Da):66,724
Checksum:i459663CEADC74EA3
GO
Isoform 4 (identifier: P07911-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-154: Missing.

Show »
Length:618
Mass (Da):67,418
Checksum:iAF3732AED73ADEF2
GO
Isoform 5 (identifier: P07911-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-29: A → ARTKYNCPARWSWRTPQRGGDTEQGPDEDFTSQG

Show »
Length:673
Mass (Da):73,571
Checksum:i55D7B9D0F81974C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881T → A in BAG51560 (PubMed:14702039).Curated
Sequence conflicti503 – 5031M → I in BAG51560 (PubMed:14702039).Curated
Sequence conflicti565 – 5651H → D in AAA36799 (PubMed:3498215).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521C → W in HNFJ1. 1 Publication
VAR_073052
Natural varianti59 – 591D → A in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_073053
Natural varianti77 – 771C → Y in HNFJ1. 1 Publication
Corresponds to variant rs121917768 [ dbSNP | Ensembl ].
VAR_025950
Natural varianti93 – 975VCPEG → AASC in MCKD2; results in mutant retention in the ER; results is abnormal intracellular polymerization of the mutant protein. 2 Publications
VAR_025951
Natural varianti103 – 1031G → C in MCKD2. 1 Publication
Corresponds to variant rs28934584 [ dbSNP | Ensembl ].
VAR_017666
Natural varianti109 – 1091V → E in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
Corresponds to variant rs780462125 [ dbSNP | Ensembl ].
VAR_071398
Natural varianti112 – 1121C → R in HNFJ1. 1 Publication
VAR_073054
Natural varianti126 – 1261C → R in HNFJ1. 2 Publications
Corresponds to variant rs121917769 [ dbSNP | Ensembl ].
VAR_025952
Natural varianti128 – 1281N → S in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
Corresponds to variant rs121917770 [ dbSNP | Ensembl ].
VAR_025953
Natural varianti135 – 1351C → S in HNFJ1. 1 Publication
VAR_073055
Natural varianti148 – 1481C → W in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
VAR_025954
Natural varianti148 – 1481C → Y in HNFJ1. 1 Publication
Corresponds to variant rs28934582 [ dbSNP | Ensembl ].
VAR_017667
Natural varianti150 – 1501C → S in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER; results is abnormal intracellular polymerization of the mutant protein. 3 Publications
VAR_025955
Natural varianti155 – 1551C → R Probable-disease association mutation found in a patient with cystic kidney disease; results in mutant retention in the ER; results is abnormal intracellular polymerization of the mutant protein. 1 Publication
VAR_073056
Natural varianti170 – 1701C → Y in HNFJ1. 1 Publication
VAR_073057
Natural varianti185 – 1851R → S in HNFJ1. 1 Publication
VAR_073058
Natural varianti195 – 1951C → F in HNFJ1. 1 Publication
VAR_073059
Natural varianti202 – 2021W → S in HNFJ1. 1 Publication
VAR_073060
Natural varianti204 – 2041R → G in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_073061
Natural varianti217 – 2171C → G in HNFJ1. 1 Publication
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_073062
Natural varianti217 – 2171C → R in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_017668
Natural varianti222 – 2221R → P in HNFJ1. 1 Publication
VAR_073063
Natural varianti223 – 2231C → Y in HNFJ1. 1 Publication
VAR_025956
Natural varianti225 – 2251T → K in MCKD2; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 2 Publications
VAR_025957
Natural varianti225 – 2251T → M in HNFJ1. 1 Publication
VAR_073064
Natural varianti230 – 2301W → R in HNFJ1. 1 Publication
VAR_071399
Natural varianti236 – 2361P → L in HNFJ1. 1 Publication
VAR_073065
Natural varianti236 – 2361P → Q in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_071400
Natural varianti236 – 2361P → R in HNFJ1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER. 1 Publication
VAR_073066
Natural varianti248 – 2481C → W in MCKD2 and HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
VAR_025958
Natural varianti255 – 2551C → Y in HNFJ1. 1 Publication
Corresponds to variant rs121917771 [ dbSNP | Ensembl ].
VAR_025959
Natural varianti282 – 2821C → R in HNFJ1. 1 Publication
VAR_073067
Natural varianti300 – 3001C → G in HNFJ1. 1 Publication
Corresponds to variant rs121917772 [ dbSNP | Ensembl ].
VAR_025960
Natural varianti315 – 3151C → R in GCKDHI; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 2 Publications
Corresponds to variant rs121917773 [ dbSNP | Ensembl ].
VAR_025961
Natural varianti316 – 3161Q → P in HNFJ1. 1 Publication
VAR_073068
Natural varianti317 – 3171C → Y in HNFJ1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025962
Natural varianti347 – 3471C → G in HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_073069
Natural varianti458 – 4581V → L.
Corresponds to variant rs55772253 [ dbSNP | Ensembl ].
VAR_061993
Natural varianti461 – 4611A → E in HNFJ1. 1 Publication
VAR_071401

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei29 – 291A → ARTKYNCPARWSWRTPQRGG DTEQGPDEDFTSQG in isoform 5. 1 PublicationVSP_054828
Alternative sequencei67 – 199133Missing in isoform 2. 1 PublicationVSP_017565Add
BLAST
Alternative sequencei133 – 15422Missing in isoform 4. 1 PublicationVSP_040973Add
BLAST
Alternative sequencei205 – 23430FVGQG…WLNGT → P in isoform 3. 1 PublicationVSP_017566Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15881 mRNA. Translation: AAA36798.1.
M17778 mRNA. Translation: AAA36799.1.
AY162970
, AY162963, AY162964, AY162965, AY162967, AY162968, AY162969 Genomic DNA. Translation: AAO64446.1.
AK127643 mRNA. Translation: BAC87070.1.
AK055722 mRNA. Translation: BAG51560.1.
AK091961 mRNA. Translation: BAG52451.1.
AC106796 Genomic DNA. No translation available.
BC035975 mRNA. Translation: AAH35975.1.
CCDSiCCDS10583.1. [P07911-1]
CCDS61876.1. [P07911-5]
PIRiA30452.
RefSeqiNP_001008390.1. NM_001008389.2. [P07911-1]
NP_001265543.1. NM_001278614.1. [P07911-5]
NP_003352.2. NM_003361.3. [P07911-1]
UniGeneiHs.654425.

Genome annotation databases

EnsembliENST00000302509; ENSP00000306279; ENSG00000169344. [P07911-1]
ENST00000396134; ENSP00000379438; ENSG00000169344. [P07911-5]
ENST00000570689; ENSP00000460548; ENSG00000169344. [P07911-1]
GeneIDi7369.
KEGGihsa:7369.
UCSCiuc002dgz.5. human. [P07911-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15881 mRNA. Translation: AAA36798.1.
M17778 mRNA. Translation: AAA36799.1.
AY162970
, AY162963, AY162964, AY162965, AY162967, AY162968, AY162969 Genomic DNA. Translation: AAO64446.1.
AK127643 mRNA. Translation: BAC87070.1.
AK055722 mRNA. Translation: BAG51560.1.
AK091961 mRNA. Translation: BAG52451.1.
AC106796 Genomic DNA. No translation available.
BC035975 mRNA. Translation: AAH35975.1.
CCDSiCCDS10583.1. [P07911-1]
CCDS61876.1. [P07911-5]
PIRiA30452.
RefSeqiNP_001008390.1. NM_001008389.2. [P07911-1]
NP_001265543.1. NM_001278614.1. [P07911-5]
NP_003352.2. NM_003361.3. [P07911-1]
UniGeneiHs.654425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WRNX-ray3.20A/B295-610[»]
ProteinModelPortaliP07911.
SMRiP07911. Positions 29-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113216. 1 interaction.
IntActiP07911. 2 interactions.
STRINGi9606.ENSP00000306279.

PTM databases

UniCarbKBiP07911.

Polymorphism and mutation databases

BioMutaiUMOD.
DMDMi137116.

Proteomic databases

PaxDbiP07911.
PeptideAtlasiP07911.
PRIDEiP07911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302509; ENSP00000306279; ENSG00000169344. [P07911-1]
ENST00000396134; ENSP00000379438; ENSG00000169344. [P07911-5]
ENST00000570689; ENSP00000460548; ENSG00000169344. [P07911-1]
GeneIDi7369.
KEGGihsa:7369.
UCSCiuc002dgz.5. human. [P07911-1]

Organism-specific databases

CTDi7369.
GeneCardsiUMOD.
GeneReviewsiUMOD.
H-InvDBHIX0012858.
HGNCiHGNC:12559. UMOD.
HPAiCAB009446.
HPA043420.
HPA054721.
MalaCardsiUMOD.
MIMi162000. phenotype.
191845. gene.
603860. phenotype.
609886. phenotype.
neXtProtiNX_P07911.
Orphaneti34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
209886. Familial juvenile hyperuricemic nephropathy type 1.
PharmGKBiPA37199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IVSV. Eukaryota.
ENOG410YDU6. LUCA.
GeneTreeiENSGT00530000063244.
HOGENOMiHOG000293303.
HOVERGENiHBG004349.
InParanoidiP07911.
KOiK18274.
OrthoDBiEOG7SFHWJ.
PhylomeDBiP07911.
TreeFamiTF330284.

Miscellaneous databases

GeneWikiiTamm%E2%80%93Horsfall_protein.
GenomeRNAii7369.
PROiP07911.
SOURCEiSearch...

Gene expression databases

BgeeiP07911.
CleanExiHS_UMOD.
ExpressionAtlasiP07911. baseline and differential.
GenevisibleiP07911. HS.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR023413. GFP-like.
IPR009030. Growth_fac_rcpt_.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 2 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein."
    Pennica D., Kohr W.J., Kuang W.-J., Glaister D., Aggarwal B.B., Chen E.Y., Goeddel D.V.
    Science 236:83-88(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION.
  3. "Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy."
    Hart T.C., Gorry M.C., Hart P.S., Woodard A.S., Shihabi Z., Sandhu J., Shirts B., Xu L., Zhu H., Barmada M.M., Bleyer A.J.
    J. Med. Genet. 39:882-892(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HNFJ1 TYR-148 AND ARG-217, VARIANT MCKD2 CYS-103.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
    Tissue: Kidney.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Kidney.
  7. "Urinary uromodulin carries an intact ZP domain generated by a conserved C-terminal proteolytic cleavage."
    Santambrogio S., Cattaneo A., Bernascone I., Schwend T., Jovine L., Bachi A., Rampoldi L.
    Biochem. Biophys. Res. Commun. 370:410-413(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 578-587, PROTEOLYTIC CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Localization of Tamm-Horsfall glycoprotein in the human kidney using immuno-fluorescence and immuno-electron microscopical techniques."
    Sikri K.L., Foster C.L., MacHugh N., Marshall R.D.
    J. Anat. 132:597-605(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a phosphatidylinositol-linked membrane protein."
    Rindler M.J., Naik S.S., Li N., Hoops T.C., Peraldi M.-N.
    J. Biol. Chem. 265:20784-20789(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR, SUBCELLULAR LOCATION.
  10. "Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly."
    Schaeffer C., Santambrogio S., Perucca S., Casari G., Rampoldi L.
    Mol. Biol. Cell 20:589-599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ASP-430; LEU-435; VAL-458; 586-ARG--SER-589; 598-VAL--ASN-600; 602-GLY-PRO-603 AND 605-THR--LYS-607, REGION, GLYCOSYLATION.
  11. "Uromodulin facilitates neutrophil migration across renal epithelial monolayers."
    Schmid M., Prajczer S., Gruber L.N., Bertocchi C., Gandini R., Pfaller W., Jennings P., Joannidis M.
    Cell. Physiol. Biochem. 26:311-318(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Uromodulin is expressed in renal primary cilia and UMOD mutations result in decreased ciliary uromodulin expression."
    Zaucke F., Boehnlein J.M., Steffens S., Polishchuk R.S., Rampoldi L., Fischer A., Pasch A., Boehm C.W., Baasner A., Attanasio M., Hoppe B., Hopfer H., Beck B.B., Sayer J.A., Hildebrandt F., Wolf M.T.
    Hum. Mol. Genet. 19:1985-1997(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Human urinary glycoproteomics; attachment site specific analysis of N-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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-232; ASN-322 AND ASN-396, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Novel uromodulin mutation in familial juvenile hyperuricemic nephropathy."
    Wei X., Xu R., Yang Z., Li Z., Liao Y., Johnson R.J., Yu X., Chen W.
    Am. J. Nephrol. 36:114-120(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN HNFJ1.
  15. "The serine protease hepsin mediates urinary secretion and polymerisation of Zona Pellucida domain protein uromodulin."
    Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A., Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S., Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L., Rampoldi L.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, ELECTRON MICROSCOPY, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF 586-ARG--SER-589, PROTEOLYTIC CLEAVAGE BY HPN, IDENTIFICATION BY MASS SPECTROMETRY.
  16. "A structured interdomain linker directs self-polymerization of human uromodulin."
    Bokhove M., Nishimura K., Brunati M., Han L., de Sanctis D., Rampoldi L., Jovine L.
    Proc. Natl. Acad. Sci. U.S.A. 113:1552-1557(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 295-610, ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, DISULFIDE BOND, DOMAIN, GLYCOSYLATION AT ASN-396, MUTAGENESIS OF LEU-333; ILE-421 AND 586-ARG--SER-589, REGION.
  17. "Renal manifestations of a mutation in the uromodulin (Tamm Horsfall protein) gene."
    Bleyer A.J., Trachtman H., Sandhu J., Gorry M.C., Hart T.C.
    Am. J. Kidney Dis. 42:E20-E26(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNFJ1 TYR-223.
  18. Cited for: INVOLVEMENT IN MCKD2, VARIANTS HNFJ1 TRP-148; SER-150 AND TYR-317, VARIANT GCKDHI ARG-315, CHARACTERIZATION OF VARIANTS HNFJ1 TRP-148; SER-150 AND TYR-317, CHARACTERIZATION OF VARIANT GCKDHI ARG-315.
  19. "A cluster of mutations in the UMOD gene causes familial juvenile hyperuricemic nephropathy with abnormal expression of uromodulin."
    Dahan K., Devuyst O., Smaers M., Vertommen D., Loute G., Poux J.M., Viron B., Jacquot C., Gagnadoux M.F., Chauveau D., Buchler M., Cochat P., Cosyns J.P., Mougenot B., Rider M.H., Antignac C., Verellen-Dumoulin C., Pirson Y.
    J. Am. Soc. Nephrol. 14:2883-2893(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HNFJ1, VARIANTS HNFJ1 ALA-59; ARG-112; ARG-126; TYR-170; SER-185; GLY-204; GLY-217; PRO-222; MET-225 AND ARG-282.
  20. Cited for: VARIANTS HNFJ1 TYR-77; ARG-126; SER-128; TYR-255 AND GLY-300.
  21. "Mutations of the Uromodulin gene in MCKD type 2 patients cluster in exon 4, which encodes three EGF-like domains."
    Wolf M.T.F., Mucha B.E., Attanasio M., Zalewski I., Karle S.M., Neumann H.P.H., Rahman N., Bader B., Baldamus C.A., Otto E., Witzgall R., Fuchshuber A., Hildebrandt F.
    Kidney Int. 64:1580-1587(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCKD2 93-VAL--GLY-97 DELINS ALA-ALA-SER-CYS; LYS-225 AND TRP-248.
  22. "Familial juvenile hyperuricemic nephropathy: detection of mutations in the uromodulin gene in five Japanese families."
    Kudo E., Kamatani N., Tezuka O., Taniguchi A., Yamanaka H., Yabe S., Osabe D., Shinohara S., Nomura K., Segawa M., Miyamoto T., Moritani M., Kunika K., Itakura M.
    Kidney Int. 65:1589-1597(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HNFJ1, VARIANTS HNFJ1 TRP-52; SER-135; PHE-195; SER-202 AND LEU-236.
  23. "Functional consequences of a novel uromodulin mutation in a family with familial juvenile hyperuricaemic nephropathy."
    Tinschert S., Ruf N., Bernascone I., Sacherer K., Lamorte G., Neumayer H.H., Nurnberg P., Luft F.C., Rampoldi L.
    Nephrol. Dial. Transplant. 19:3150-3154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNFJ1 GLY-347, CHARACTERIZATION OF VARIANT HNFJ1 GLY-347.
  24. "A novel pattern of mutation in uromodulin disorders: autosomal dominant medullary cystic kidney disease type 2, familial juvenile hyperuricemic nephropathy, and autosomal dominant glomerulocystic kidney disease."
    Lens X.M., Banet J.F., Outeda P., Barrio-Lucia V.
    Am. J. Kidney Dis. 46:52-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNFJ1 PRO-316.
  25. Cited for: VARIANT HNFJ1 ARG-236, CHARACTERIZATION OF VARIANTS HNFJ1 ALA-59; SER-128; TRP-148; SER-150; GLY-204; ARG-217 AND ARG-236, CHARACTERIZATION OF VARIANT MCKD2 LYS-225, CHARACTERIZATION OF VARIANT GCKDHI ARG-315.
  26. "A case of familial juvenile hyperuricemic nephropathy with novel uromodulin gene mutation, a novel heterozygous missense mutation in Korea."
    Lee D.H., Kim J.K., Oh S.E., Noh J.W., Lee Y.K.
    J. Korean Med. Sci. 25:1680-1682(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNFJ1 GLU-461.
  27. "A Japanese family suffering from familial juvenile hyperuricemic nephropathy due to a rare mutation of the uromodulin gene."
    Nakayama M., Mori Y., Ota N., Ishida M., Shiotsu Y., Matsuoka E., Kado H., Ishida R., Nakata M., Kitani T., Tamagaki K., Sekita C., Taniguchi A.
    Case Rep. Nephrol. Urol. 2:15-19(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNFJ1 ARG-230.
  28. "Novel UMOD mutations in familial juvenile hyperuricemic nephropathy lead to abnormal uromodulin intracellular trafficking."
    Liu M., Chen Y., Liang Y., Liu Y., Wang S., Hou P., Zhang H., Zhao M.
    Gene 531:363-369(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HNFJ1 GLU-109; GLN-236 AND TRP-248, CHARACTERIZATION OF VARIANTS HNFJ1 GLU-109; GLN-236 AND TRP-248, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  29. "Pathogenic uromodulin mutations result in premature intracellular polymerization."
    Stewart A.P., Sandford R.N., Karet Frankl F.E., Edwardson J.M.
    FEBS Lett. 589:89-93(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-155, CHARACTERIZATION OF VARIANT MCKD2 93-VAL--GLY-97 DELINS ALA-ALA-SER-CYS, CHARACTERIZATION OF VARIANTS HNFJ1 SER-150, CHARACTERIZATION OF VARIANT ARG-155.

Entry informationi

Entry nameiUROM_HUMAN
AccessioniPrimary (citable) accession number: P07911
Secondary accession number(s): B3KP48
, B3KRN9, E9PEA4, Q540J6, Q6ZS84, Q8IYG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 6, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.