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P07911

- UROM_HUMAN

UniProt

P07911 - UROM_HUMAN

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Protein

Uromodulin

Gene

UMOD

Organism
Homo sapiens (Human)
Status
Reviewed - 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 providing the water barrier permeability. May serve as a receptor for binding and endocytosis for cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelial.1 Publication
Uromodulin, secreted form: Secreted into urine after proteolytically cleaveage. Into the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and modulates formation of supersaturated salts and their crystals.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei587 – 5882Cleavage

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. IgG binding Source: BHF-UCL

GO - Biological processi

  1. cellular defense response Source: ProtInc
  2. chemical homeostasis Source: Ensembl
  3. excretion Source: Ensembl
  4. heterophilic cell-cell adhesion Source: BHF-UCL
  5. leukocyte cell-cell adhesion Source: BHF-UCL
  6. metanephric ascending thin limb development Source: Ensembl
  7. metanephric distal convoluted tubule development Source: Ensembl
  8. metanephric thick ascending limb development Source: Ensembl
  9. negative regulation of cell proliferation Source: ProtInc
  10. neutrophil migration Source: BHF-UCL
  11. regulation of ion homeostasis Source: Ensembl
  12. response to organic substance Source: Ensembl
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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:12559. UMOD.

Subcellular locationi

Apical cell membrane 2 Publications; Lipid-anchorGPI-anchor. Basolateral cell membrane; Lipid-anchorGPI-anchor. Cell projectioncilium membrane
Note: Only a small fraction sorts to the basolateral pole of tubular epithelial cells compared to apical localization. Secreted into urine after cleavage. Colocalized with NPHP1 and KIF3A.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB
  2. apical plasma membrane Source: UniProtKB
  3. basolateral plasma membrane Source: UniProtKB
  4. cytoplasmic vesicle Source: Ensembl
  5. extracellular space Source: Ensembl
  6. extracellular vesicular exosome Source: UniProtKB
  7. extrinsic component of membrane Source: ProtInc
  8. Golgi apparatus Source: Ensembl
  9. membrane raft Source: Ensembl
  10. primary cilium Source: UniProtKB
  11. 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) [MIM:162000]: A 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.8 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771C → Y in HNFJ1. 1 Publication
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
VAR_071398
Natural varianti126 – 1261C → R in HNFJ1. 1 Publication
VAR_025952
Natural varianti128 – 1281N → S in HNFJ1. 1 Publication
VAR_025953
Natural varianti148 – 1481C → W in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025954
Natural varianti148 – 1481C → Y in HNFJ1. 1 Publication
Corresponds to variant rs28934582 [ dbSNP | Ensembl ].
VAR_017667
Natural varianti150 – 1501C → S in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025955
Natural varianti217 – 2171C → R in HNFJ1. 1 Publication
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_017668
Natural varianti223 – 2231C → Y in HNFJ1. 1 Publication
VAR_025956
Natural varianti230 – 2301W → R in HNFJ1. 1 Publication
VAR_071399
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 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
VAR_025959
Natural varianti300 – 3001C → G in HNFJ1. 1 Publication
VAR_025960
Natural varianti317 – 3171C → Y in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025962
Natural varianti461 – 4611A → E in HNFJ1. 1 Publication
VAR_071401
Medullary cystic kidney disease 2 (MCKD2) [MIM:603860]: A 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 975VCPEG → AASC in MCKD2. 1 Publication
VAR_025951
Natural varianti103 – 1031G → C in MCKD2. 1 Publication
Corresponds to variant rs28934584 [ dbSNP | Ensembl ].
VAR_017666
Natural varianti148 – 1481C → W in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025954
Natural varianti150 – 1501C → S in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025955
Natural varianti225 – 2251T → K in MCKD2. 1 Publication
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
Natural varianti317 – 3171C → Y in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025962
Glomerulocystic kidney disease with hyperuricemia and isosthenuria (GCKDHI) [MIM:609886]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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. 1 Publication
VAR_025961

Keywords - Diseasei

Ciliopathy, Disease mutation, Nephronophthisis

Organism-specific databases

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.

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)1 Publication
Glycosylationi275 – 2751N-linked (GlcNAc...)CAR_000178
Glycosylationi322 – 3221N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi396 – 3961N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi506 ↔ 566PROSITE-ProRule annotation
Lipidationi614 – 6141GPI-anchor amidated serineSequence Analysis

Post-translational modificationi

N-glycosylated. 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).1 Publication
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found into urine.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP07911.
PRIDEiP07911.

PTM databases

UniCarbKBiP07911.

Expressioni

Tissue specificityi

Expressed in the tubular cells of the kidney (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. Most abundant protein in normal urine.3 Publications

Gene expression databases

BgeeiP07911.
CleanExiHS_UMOD.
ExpressionAtlasiP07911. baseline.
GenevestigatoriP07911.

Organism-specific databases

HPAiCAB009446.
HPA043420.
HPA054721.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP07911.
SMRiP07911. Positions 29-146, 299-324.
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

Domaini

The ZP domain is involved in the polymerization of the protein to promote the formation of complex gel-like structure.

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

eggNOGiNOG44010.
GeneTreeiENSGT00530000063244.
HOGENOMiHOG000293303.
HOVERGENiHBG004349.
InParanoidiP07911.
KOiK18274.
OrthoDBiEOG7SFHWJ.
PhylomeDBiP07911.
TreeFamiTF330284.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR023413. GFP_like.
IPR009030. Growth_fac_rcpt_N_dom.
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. 1 hit.
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. Align

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 varianti77 – 771C → Y in HNFJ1. 1 Publication
VAR_025950
Natural varianti93 – 975VCPEG → AASC in MCKD2. 1 Publication
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
VAR_071398
Natural varianti126 – 1261C → R in HNFJ1. 1 Publication
VAR_025952
Natural varianti128 – 1281N → S in HNFJ1. 1 Publication
VAR_025953
Natural varianti148 – 1481C → W in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025954
Natural varianti148 – 1481C → Y in HNFJ1. 1 Publication
Corresponds to variant rs28934582 [ dbSNP | Ensembl ].
VAR_017667
Natural varianti150 – 1501C → S in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025955
Natural varianti217 – 2171C → R in HNFJ1. 1 Publication
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_017668
Natural varianti223 – 2231C → Y in HNFJ1. 1 Publication
VAR_025956
Natural varianti225 – 2251T → K in MCKD2. 1 Publication
VAR_025957
Natural varianti230 – 2301W → R in HNFJ1. 1 Publication
VAR_071399
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 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
VAR_025959
Natural varianti300 – 3001C → G in HNFJ1. 1 Publication
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. 1 Publication
VAR_025961
Natural varianti317 – 3171C → Y in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. 1 Publication
VAR_025962
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:
EMBL
GenBank
DDBJ
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]
XP_006721149.1. XM_006721086.1. [P07911-1]
XP_006721150.1. XM_006721087.1. [P07911-1]
XP_006721151.1. XM_006721088.1. [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.3. human. [P07911-1]

Polymorphism databases

DMDMi137116.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10583.1. [P07911-1 ]
CCDS61876.1. [P07911-5 ]
PIRi A30452.
RefSeqi NP_001008390.1. NM_001008389.2. [P07911-1 ]
NP_001265543.1. NM_001278614.1. [P07911-5 ]
NP_003352.2. NM_003361.3. [P07911-1 ]
XP_006721149.1. XM_006721086.1. [P07911-1 ]
XP_006721150.1. XM_006721087.1. [P07911-1 ]
XP_006721151.1. XM_006721088.1. [P07911-1 ]
UniGenei Hs.654425.

3D structure databases

ProteinModelPortali P07911.
SMRi P07911. Positions 29-146, 299-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113216. 1 interaction.
IntActi P07911. 2 interactions.
STRINGi 9606.ENSP00000306279.

PTM databases

UniCarbKBi P07911.

Polymorphism databases

DMDMi 137116.

Proteomic databases

PaxDbi P07911.
PRIDEi P07911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302509 ; ENSP00000306279 ; ENSG00000169344 . [P07911-1 ]
ENST00000396134 ; ENSP00000379438 ; ENSG00000169344 . [P07911-5 ]
ENST00000570689 ; ENSP00000460548 ; ENSG00000169344 . [P07911-1 ]
GeneIDi 7369.
KEGGi hsa:7369.
UCSCi uc002dgz.3. human. [P07911-1 ]

Organism-specific databases

CTDi 7369.
GeneCardsi GC16M020344.
GeneReviewsi UMOD.
H-InvDB HIX0012858.
HGNCi HGNC:12559. UMOD.
HPAi CAB009446.
HPA043420.
HPA054721.
MIMi 162000. phenotype.
191845. gene.
603860. phenotype.
609886. phenotype.
neXtProti NX_P07911.
Orphaneti 34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
209886. Familial juvenile hyperuricemic nephropathy type 1.
PharmGKBi PA37199.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44010.
GeneTreei ENSGT00530000063244.
HOGENOMi HOG000293303.
HOVERGENi HBG004349.
InParanoidi P07911.
KOi K18274.
OrthoDBi EOG7SFHWJ.
PhylomeDBi P07911.
TreeFami TF330284.

Miscellaneous databases

GeneWikii Tamm%E2%80%93Horsfall_protein.
GenomeRNAii 7369.
NextBioi 28856.
PROi P07911.
SOURCEi Search...

Gene expression databases

Bgeei P07911.
CleanExi HS_UMOD.
ExpressionAtlasi P07911. baseline.
Genevestigatori P07911.

Family and domain databases

Gene3Di 2.40.155.10. 1 hit.
InterProi IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR023413. GFP_like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view ]
Pfami PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view ]
PRINTSi PR00023. ZPELLUCIDA.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

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).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  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.
  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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. Cited for: VARIANTS MCKD2/HNFJ1 TRP-148; SER-150 AND TYR-317, VARIANT GCKDHI ARG-315, CHARACTERIZATION OF VARIANTS MCKD2/HNFJ1 TRP-148; SER-150 AND TYR-317, CHARACTERIZATION OF VARIANT GCKDHI ARG-315.
  16. Cited for: VARIANTS HNFJ1 TYR-77; ARG-126; SER-128; TYR-255 AND GLY-300.
  17. "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.
  18. "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.
  19. "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.
  20. "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.

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: October 29, 2014
This is version 151 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

Miscellaneous

A specific, but as yet unidentified, protease(s) cleaves off and releases UMOD into urine.

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3