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P07911 (UROM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uromodulin
Alternative name(s):
Tamm-Horsfall urinary glycoprotein
Short name=THP

Cleaved into the following chain:

  1. Uromodulin, secreted form
Gene names
Name:UMOD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

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. Ref.10

Subcellular location

Apical cell membrane; Lipid-anchorGPI-anchor. Basolateral cell membrane; Lipid-anchorGPI-anchor. Cell projectioncilium membrane. Note: Only a small fraction is sort to the basolateral pole of tubular epithelial cells compared to apical localization. Secreted into urine after cleavage. Colocalized with NPHP1 and KIF3A. Ref.8 Ref.9 Ref.10 Ref.11

Uromodulin, secreted form: Secreted Ref.8 Ref.10 Ref.11.

Tissue specificity

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. Ref.8

Domain

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

Post-translational modification

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). Ref.12

Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found into urine. Ref.7

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.13 Ref.15

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.14 Ref.16

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Miscellaneous

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

Sequence similarities

Contains 3 EGF-like domains.

Contains 1 ZP domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cilium
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCiliopathy
Disease mutation
Nephronophthisis
   DomainEGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular defense response

Traceable author statement PubMed 2409603. Source: ProtInc

chemical homeostasis

Inferred from electronic annotation. Source: Ensembl

excretion

Inferred from electronic annotation. Source: Ensembl

metanephric ascending thin limb development

Inferred from electronic annotation. Source: Ensembl

metanephric distal convoluted tubule development

Inferred from electronic annotation. Source: Ensembl

metanephric thick ascending limb development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement PubMed 2409603. Source: ProtInc

regulation of ion homeostasis

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

anchored component of membrane

Inferred from direct assay PubMed 91065873. Source: UniProtKB

apical plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of membrane

Traceable author statement PubMed 7873609. Source: ProtInc

membrane raft

Inferred from electronic annotation. Source: Ensembl

primary cilium

Inferred from direct assay Ref.11. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07911-1)

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.
Isoform 2 (identifier: P07911-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P07911-3)

The sequence of this isoform differs from the canonical sequence as follows:
     205-234: FVGQGGARMAETCVPVLRCNTAAPMWLNGT → P
Note: No experimental confirmation available.
Isoform 4 (identifier: P07911-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 614590Uromodulin
PRO_0000041671
Chain25 – 587563Uromodulin, secreted form
PRO_0000407909
Propeptide615 – 64026Removed in mature form Potential
PRO_0000041672

Regions

Domain28 – 6437EGF-like 1
Domain65 – 10743EGF-like 2; calcium-binding Potential
Domain108 – 14942EGF-like 3; calcium-binding Potential
Domain334 – 589256ZP

Sites

Site587 – 5882Cleavage

Amino acid modifications

Lipidation6141GPI-anchor amidated serine Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) (complex) Ref.12
Glycosylation2751N-linked (GlcNAc...)
CAR_000178
Glycosylation3221N-linked (GlcNAc...) (complex) Ref.12
Glycosylation3961N-linked (GlcNAc...) (complex) Ref.12
Disulfide bond32 ↔ 41 By similarity
Disulfide bond35 ↔ 50 By similarity
Disulfide bond52 ↔ 63 By similarity
Disulfide bond69 ↔ 83 By similarity
Disulfide bond77 ↔ 92 By similarity
Disulfide bond94 ↔ 106 By similarity
Disulfide bond112 ↔ 126 By similarity
Disulfide bond120 ↔ 135 By similarity
Disulfide bond137 ↔ 148 By similarity
Disulfide bond506 ↔ 566 By similarity

Natural variations

Alternative sequence67 – 199133Missing in isoform 2.
VSP_017565
Alternative sequence133 – 15422Missing in isoform 4.
VSP_040973
Alternative sequence205 – 23430FVGQG…WLNGT → P in isoform 3.
VSP_017566
Natural variant771C → Y in HNFJ1. Ref.15
VAR_025950
Natural variant93 – 975VCPEG → AASC in MCKD2.
VAR_025951
Natural variant1031G → C in MCKD2. Ref.3
Corresponds to variant rs28934584 [ dbSNP | Ensembl ].
VAR_017666
Natural variant1261C → R in HNFJ1. Ref.15
VAR_025952
Natural variant1281N → S in HNFJ1. Ref.15
VAR_025953
Natural variant1481C → W in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14
VAR_025954
Natural variant1481C → Y in HNFJ1. Ref.3
Corresponds to variant rs28934582 [ dbSNP | Ensembl ].
VAR_017667
Natural variant1501C → S in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14
VAR_025955
Natural variant2171C → R in HNFJ1. Ref.3
Corresponds to variant rs28934583 [ dbSNP | Ensembl ].
VAR_017668
Natural variant2231C → Y in HNFJ1. Ref.13
VAR_025956
Natural variant2251T → K in MCKD2. Ref.16
VAR_025957
Natural variant2481C → W in MCKD2. Ref.16
VAR_025958
Natural variant2551C → Y in HNFJ1. Ref.15
VAR_025959
Natural variant3001C → G in HNFJ1. Ref.15
VAR_025960
Natural variant3151C → R in GCKDHI; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14
VAR_025961
Natural variant3171C → Y in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14
VAR_025962
Natural variant4581V → L.
Corresponds to variant rs55772253 [ dbSNP | Ensembl ].
VAR_061993

Experimental info

Sequence conflict2881T → A in BAG51560. Ref.4
Sequence conflict5031M → I in BAG51560. Ref.4
Sequence conflict5651H → D in AAA36799. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: D26A07A76353AE48

FASTA64069,761
        10         20         30         40         50         60 
MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG 

        70         80         90        100        110        120 
LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC 

       130        140        150        160        170        180 
HALATCVNVV GSYLCVCPAG YRGDGWHCEC SPGSCGPGLD CVPEGDALVC ADPCQAHRTL 

       190        200        210        220        230        240 
DEYWRSTEYG EGYACDTDLR GWYRFVGQGG ARMAETCVPV LRCNTAAPMW LNGTHPSSDE 

       250        260        270        280        290        300 
GIVSRKACAH WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC 

       310        320        330        340        350        360 
SIDEDCKSNN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK SLGFDKVFMY 

       370        380        390        400        410        420 
LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA TYSNTLYLAD EIIIRDLNIK 

       430        440        450        460        470        480 
INFACSYPLD MKVSLKTALQ PMVSALNIRV GGTGMFTVRM ALFQTPSYTQ PYQGSSVTLS 

       490        500        510        520        530        540 
TEAFLYVGTM LDGGDLSRFA LLMTNCYATP SSNATDPLKY FIIQDRCPHT RDSTIQVVEN 

       550        560        570        580        590        600 
GESSQGRFSV QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN 

       610        620        630        640 
LGPITRKGVQ ATVSRAFSSL GLLKVWLPLL LSATLTLTFQ 

« Hide

Isoform 2 [UniParc].

Checksum: FBFC739EA15E3D22
Show »

FASTA50755,960
Isoform 3 [UniParc].

Checksum: 459663CEADC74EA3
Show »

FASTA61166,724
Isoform 4 [UniParc].

Checksum: AF3732AED73ADEF2
Show »

FASTA61867,418

References

« Hide 'large scale' references
[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]"Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines."
Hession C., Decker J.M., Sherblom A.P., Kumar S., Yue C.C., Mattaliano R.J., Tizard R., Kawashima E., Schmeissner U., Heletky S., Chow E.P., Burne C.A., Shaw A., Muchmore A.V.
Science 237:1479-1484(1987) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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 AND 4).
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. expand/collapse author list , 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]"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.
[14]"Allelism of MCKD, FJHN and GCKD caused by impairment of uromodulin export dynamics."
Rampoldi L., Caridi G., Santon D., Boaretto F., Bernascone I., Lamorte G., Tardanico R., Dagnino M., Colussi G., Scolari F., Ghiggeri G.M., Amoroso A., Casari G.
Hum. Mol. Genet. 12:3369-3384(2003) [PubMed] [Europe PMC] [Abstract]
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.
[15]"UROMODULIN mutations cause familial juvenile hyperuricemic nephropathy."
Turner J.J.O., Stacey J.M., Harding B., Kotanko P., Lhotta K., Puig J.G., Roberts I., Torres R.J., Thakker R.V.
J. Clin. Endocrinol. Metab. 88:1398-1401(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNFJ1 TYR-77; ARG-126; SER-128; TYR-255 AND GLY-300.
[16]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15881 mRNA. Translation: AAA36798.1.
M17778 mRNA. Translation: AAA36799.1.
AY162970 expand/collapse EMBL AC list , 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.
PIRA30452.
RefSeqNP_001008390.1. NM_001008389.2.
NP_001265543.1. NM_001278614.1.
NP_003352.2. NM_003361.3.
UniGeneHs.654425.

3D structure databases

ProteinModelPortalP07911.
SMRP07911. Positions 29-188, 264-325, 457-590.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113216. 1 interaction.
IntActP07911. 2 interactions.
STRING9606.ENSP00000306279.

PTM databases

UniCarbKBP07911.

Polymorphism databases

DMDM137116.

Proteomic databases

PaxDbP07911.
PRIDEP07911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302509; ENSP00000306279; ENSG00000169344. [P07911-1]
ENST00000396142; ENSP00000379446; ENSG00000169344. [P07911-1]
ENST00000570689; ENSP00000460548; ENSG00000169344. [P07911-1]
GeneID7369.
KEGGhsa:7369.
UCSCuc002dgz.3. human. [P07911-1]

Organism-specific databases

CTD7369.
GeneCardsGC16M020344.
H-InvDBHIX0012858.
HGNCHGNC:12559. UMOD.
HPACAB009446.
HPA043420.
HPA054721.
MIM162000. phenotype.
191845. gene.
603860. phenotype.
609886. phenotype.
neXtProtNX_P07911.
Orphanet34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
209886. Familial juvenile hyperuricemic nephropathy type 1.
PharmGKBPA37199.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44010.
HOGENOMHOG000293303.
HOVERGENHBG004349.
OrthoDBEOG7SFHWJ.
PhylomeDBP07911.
TreeFamTF330284.

Gene expression databases

ArrayExpressP07911.
BgeeP07911.
CleanExHS_UMOD.
GenevestigatorP07911.

Family and domain databases

Gene3D2.40.155.10. 1 hit.
InterProIPR000742. 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]
PfamPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

GeneWikiTamm%E2%80%93Horsfall_protein.
GenomeRNAi7369.
NextBio28856.
PROP07911.
SOURCESearch...

Entry information

Entry nameUROM_HUMAN
AccessionPrimary (citable) accession number: P07911
Secondary accession number(s): B3KP48 expand/collapse secondary AC list , B3KRN9, Q540J6, Q6ZS84, Q8IYG0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM