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P07911

- UROM_HUMAN

UniProt

P07911 - UROM_HUMAN

Protein

Uromodulin

Gene

UMOD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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

    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; 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.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB
    3. basolateral plasma membrane Source: UniProtKB
    4. ciliary membrane Source: UniProtKB-SubCell
    5. cytoplasmic vesicle Source: Ensembl
    6. extracellular space Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. extrinsic component of membrane Source: ProtInc
    9. Golgi apparatus Source: Ensembl
    10. membrane raft Source: Ensembl
    11. primary cilium Source: UniProtKB
    12. spindle pole Source: UniProtKB

    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.4 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 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 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
    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.
    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. 1 Publication
    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

    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.1 Publication

    Gene expression databases

    ArrayExpressiP07911.
    BgeeiP07911.
    CleanExiHS_UMOD.
    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 29-137.
    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.
    HOGENOMiHOG000293303.
    HOVERGENiHBG004349.
    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

    MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC    50
    TCQEGFTGDG LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL 100
    SPGLGCTDVD ECAEPGLSHC HALATCVNVV GSYLCVCPAG YRGDGWHCEC 150
    SPGSCGPGLD CVPEGDALVC ADPCQAHRTL DEYWRSTEYG EGYACDTDLR 200
    GWYRFVGQGG ARMAETCVPV LRCNTAAPMW LNGTHPSSDE GIVSRKACAH 250
    WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC 300
    SIDEDCKSNN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK 350
    SLGFDKVFMY LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA 400
    TYSNTLYLAD EIIIRDLNIK INFACSYPLD MKVSLKTALQ PMVSALNIRV 450
    GGTGMFTVRM ALFQTPSYTQ PYQGSSVTLS TEAFLYVGTM LDGGDLSRFA 500
    LLMTNCYATP SSNATDPLKY FIIQDRCPHT RDSTIQVVEN GESSQGRFSV 550
    QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN 600
    LGPITRKGVQ ATVSRAFSSL GLLKVWLPLL LSATLTLTFQ 640
    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.
    VAR_025951
    Natural varianti103 – 1031G → C in MCKD2. 1 Publication
    Corresponds to variant rs28934584 [ dbSNP | Ensembl ].
    VAR_017666
    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 varianti248 – 2481C → W in MCKD2. 1 Publication
    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

    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 29-137.
    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.
    HOGENOMi HOG000293303.
    HOVERGENi HBG004349.
    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

    ArrayExpressi P07911.
    Bgeei P07911.
    CleanExi HS_UMOD.
    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

    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. "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. 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. 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.

    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 1, 2014
    This is version 150 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