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P98161 (PKD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycystin-1
Alternative name(s):
Autosomal dominant polycystic kidney disease 1 protein
Gene names
Name:PKD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in renal tubulogenesis. Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Acts as a regulator of cilium length, together with PKD2. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling By similarity. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Ref.6

Subunit structure

Interacts with PKD2 and PKD2L1. Interacts with PRKX; involved in differentiation and controlled morphogenesis of the kidney. Interacts with NPHP1 (via SH3 domain). Ref.8 Ref.10

Subcellular location

Membrane; Multi-pass membrane protein. Cell projectioncilium By similarity. Note: PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autoproteolytic cleavage at the GPS domain. Ref.9

Domain

The LDL-receptor class A domain is atypical; the potential calcium-binding site is missing. Ref.6

Post-translational modification

After synthesis, undergoes cleavage between Leu-3048 and Thr-3049 in the GPS domain. Cleavage at the GPS domain occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement. This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain. There is evidence that cleavage at GPS domain is incomplete. Uncleaved and cleaved products may have different functions in vivo. Ref.6 Ref.7

Involvement in disease

Polycystic kidney disease 1 (PKD1) [MIM:173900]: A disorder characterized by renal cysts, liver cysts and intracranial aneurysm. Clinical variability is due to differences in the rate of loss of glomerular filtration, the age of reaching end-stage renal disease and the occurrence of hypertension, symptomatic extrarenal cysts, and subarachnoid hemorrhage from intracranial 'berry' aneurysm.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46

Sequence similarities

Belongs to the polycystin family.

Contains 1 C-type lectin domain.

Contains 1 GPS domain.

Contains 1 LDL-receptor class A domain.

Contains 2 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Contains 17 PKD domains.

Contains 1 PLAT domain.

Contains 1 REJ domain.

Contains 1 WSC domain.

Caution

Variant Cys-2379 has been originally described as a benign polymorphism (Ref.25). However, it is a likely pathogenic mutation (PubMed:Ref.46).

Ontologies

Keywords
   Cellular componentCell projection
Cilium
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCiliopathy
Disease mutation
   DomainCoiled coil
Leucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

anatomical structure morphogenesis

Traceable author statement PubMed 9326937. Source: ProtInc

branching morphogenesis of an epithelial tube

Inferred from direct assay Ref.6. Source: UniProtKB

calcium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

calcium-independent cell-matrix adhesion

Traceable author statement PubMed 10861291. Source: ProtInc

cartilage condensation

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

cell cycle arrest

Inferred from sequence or structural similarity. Source: BHF-UCL

cell-matrix adhesion

Traceable author statement Ref.2. Source: ProtInc

cytoplasmic sequestering of transcription factor

Inferred from sequence or structural similarity. Source: BHF-UCL

detection of mechanical stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

digestive tract development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

embryonic placenta development

Inferred from sequence or structural similarity. Source: BHF-UCL

genitalia development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

heart development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

homophilic cell adhesion

Traceable author statement PubMed 10861291. Source: ProtInc

in utero embryonic development

Inferred from sequence or structural similarity. Source: BHF-UCL

kidney development

Inferred from sequence or structural similarity. Source: BHF-UCL

liver development

Inferred from electronic annotation. Source: Ensembl

lung epithelium development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

mesonephric duct development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

mesonephric tubule development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric ascending thin limb development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric collecting duct development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric distal tubule morphogenesis

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric proximal tubule development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

neural tube development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

nitrogen compound metabolic process

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

placenta blood vessel development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 16311606. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16311606. Source: BHF-UCL

protein export from nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of mitotic spindle organization

Inferred from electronic annotation. Source: Ensembl

regulation of proteasomal protein catabolic process

Inferred from direct assay PubMed 23001567. Source: MGI

skin development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

spinal cord development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867. Source: UniProt

integral component of membrane

Non-traceable author statement PubMed 10097141. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

motile primary cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 23001567. Source: MGI

polycystin complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functioncalcium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

cation channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 9192675. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 9171830. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P98161-1)

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: P98161-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2497-2507: GWHDAEDAGAP → A
     3390-3390: Missing.
Isoform 3 (identifier: P98161-3)

The sequence of this isoform differs from the canonical sequence as follows:
     3390-3390: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 43034280Polycystin-1
PRO_0000024298

Regions

Topological domain24 – 30743051Extracellular Potential
Transmembrane3075 – 309521Helical; Potential
Topological domain3096 – 3282187Cytoplasmic Potential
Transmembrane3283 – 330321Helical; Potential
Topological domain3304 – 332320Extracellular Potential
Transmembrane3324 – 334421Helical; Potential
Topological domain3345 – 3559215Cytoplasmic Potential
Transmembrane3560 – 358021Helical; Potential
Topological domain3581 – 35822Extracellular Potential
Transmembrane3583 – 360321Helical; Potential
Topological domain3604 – 367370Cytoplasmic Potential
Transmembrane3674 – 369421Helical; Potential
Topological domain3695 – 3896202Extracellular Potential
Transmembrane3897 – 391721Helical; Potential
Topological domain3918 – 393821Cytoplasmic Potential
Transmembrane3939 – 395921Helical; Potential
Topological domain3960 – 397920Extracellular Potential
Transmembrane3980 – 400021Helical; Potential
Topological domain4001 – 402727Cytoplasmic Potential
Transmembrane4028 – 404821Helical; Potential
Topological domain4049 – 408537Extracellular Potential
Transmembrane4086 – 410621Helical; Potential
Topological domain4107 – 4303197Cytoplasmic Potential
Domain24 – 6744LRRNT
Repeat68 – 9124LRR 1
Repeat92 – 11322LRR 2
Domain125 – 17854LRRCT
Domain177 – 27195WSC
Domain272 – 35988PKD 1
Domain415 – 531117C-type lectin
Domain638 – 67134LDL-receptor class A; atypical
Domain743 – 81775PKD 2
Domain855 – 92874PKD 3
Domain935 – 102086PKD 4
Domain1023 – 1129107PKD 5
Domain1127 – 121589PKD 6
Domain1213 – 129886PKD 7
Domain1294 – 138390PKD 8
Domain1382 – 146988PKD 9
Domain1468 – 155184PKD 10
Domain1550 – 163586PKD 11
Domain1634 – 172188PKD 12
Domain1719 – 180587PKD 13
Domain1807 – 189084PKD 14
Domain1889 – 197486PKD 15
Domain1977 – 205781PKD 16
Domain2060 – 214889PKD 17
Domain2146 – 2833688REJ
Domain3012 – 306150GPS
Domain3118 – 3233116PLAT
Coiled coil4220 – 425132 Potential
Motif3744 – 375613Polycystin motif

Sites

Site3048 – 30492Cleavage; by autolysis

Amino acid modifications

Modified residue41661Phosphoserine; by PRKX; in vitro Ref.8
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation6211N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Glycosylation7461N-linked (GlcNAc...) Potential
Glycosylation8101N-linked (GlcNAc...) Potential
Glycosylation8411N-linked (GlcNAc...) Potential
Glycosylation8541N-linked (GlcNAc...) Potential
Glycosylation8901N-linked (GlcNAc...) Potential
Glycosylation9211N-linked (GlcNAc...) Potential
Glycosylation10041N-linked (GlcNAc...) Potential
Glycosylation10101N-linked (GlcNAc...) Potential
Glycosylation10341N-linked (GlcNAc...) Potential
Glycosylation10721N-linked (GlcNAc...) Potential
Glycosylation11131N-linked (GlcNAc...) Potential
Glycosylation11781N-linked (GlcNAc...) Potential
Glycosylation11941N-linked (GlcNAc...) Potential
Glycosylation12401N-linked (GlcNAc...) Potential
Glycosylation12691N-linked (GlcNAc...) Potential
Glycosylation13361N-linked (GlcNAc...) Potential
Glycosylation13481N-linked (GlcNAc...) Potential
Glycosylation13821N-linked (GlcNAc...) Potential
Glycosylation14501N-linked (GlcNAc...) Potential
Glycosylation14551N-linked (GlcNAc...) Potential
Glycosylation14741N-linked (GlcNAc...) Potential
Glycosylation15181N-linked (GlcNAc...) Potential
Glycosylation15411N-linked (GlcNAc...) Potential
Glycosylation15541N-linked (GlcNAc...) Potential
Glycosylation15631N-linked (GlcNAc...) Potential
Glycosylation16471N-linked (GlcNAc...) Potential
Glycosylation16611N-linked (GlcNAc...) Potential
Glycosylation17331N-linked (GlcNAc...) Potential
Glycosylation17911N-linked (GlcNAc...) Potential
Glycosylation18341N-linked (GlcNAc...) Potential
Glycosylation18671N-linked (GlcNAc...) Potential
Glycosylation18801N-linked (GlcNAc...) Potential
Glycosylation19911N-linked (GlcNAc...) Potential
Glycosylation20501N-linked (GlcNAc...) Potential
Glycosylation20741N-linked (GlcNAc...) Potential
Glycosylation21251N-linked (GlcNAc...) Potential
Glycosylation22481N-linked (GlcNAc...) Potential
Glycosylation23531N-linked (GlcNAc...) Potential
Glycosylation23951N-linked (GlcNAc...) Potential
Glycosylation24121N-linked (GlcNAc...) Potential
Glycosylation25671N-linked (GlcNAc...) Potential
Glycosylation25781N-linked (GlcNAc...) Potential
Glycosylation26451N-linked (GlcNAc...) Potential
Glycosylation27181N-linked (GlcNAc...) Potential
Glycosylation27541N-linked (GlcNAc...) Potential
Glycosylation28411N-linked (GlcNAc...) Potential
Glycosylation28781N-linked (GlcNAc...) Potential
Glycosylation29251N-linked (GlcNAc...) Potential
Glycosylation29561N-linked (GlcNAc...) Potential
Glycosylation29941N-linked (GlcNAc...) Potential
Glycosylation37381N-linked (GlcNAc...) Potential
Glycosylation37901N-linked (GlcNAc...) Potential
Glycosylation38451N-linked (GlcNAc...) Potential
Disulfide bond436 ↔ 530 By similarity
Disulfide bond508 ↔ 522 By similarity
Disulfide bond640 ↔ 653 By similarity
Disulfide bond647 ↔ 665 By similarity
Disulfide bond660 ↔ 669 By similarity

Natural variations

Alternative sequence2497 – 250711GWHDAEDAGAP → A in isoform 2.
VSP_009677
Alternative sequence33901Missing in isoform 2 and isoform 3.
VSP_009678
Natural variant131L → Q in PKD1. Ref.31
VAR_011030
Natural variant361P → H. Ref.43 Ref.44
VAR_058759
Natural variant611P → L in PKD1; unknown pathological significance. Ref.40 Ref.44
VAR_058760
Natural variant751S → F in PKD1. Ref.31
VAR_011031
Natural variant871L → M. Ref.38
VAR_058761
Natural variant881A → V. Ref.33
VAR_012452
Natural variant971D → G in PKD1. Ref.45
VAR_064380
Natural variant991S → I in PKD1; unknown pathological significance. Ref.44
VAR_058762
Natural variant1391W → C in PKD1. Ref.31
VAR_011032
Natural variant1641Q → R in PKD1. Ref.42
VAR_058763
Natural variant2101C → G in PKD1. Ref.42
VAR_058764
Natural variant3241R → L in PKD1. Ref.20
VAR_010085
Natural variant3251Y → C in PKD1. Ref.46
VAR_068024
Natural variant3811G → C in PKD1. Ref.37
VAR_058765
Natural variant4361C → R in PKD1. Ref.45
VAR_064381
Natural variant4421A → P in PKD1. Ref.45
VAR_064382
Natural variant5081C → R in PKD1. Ref.42
Corresponds to variant rs58598099 [ dbSNP | Ensembl ].
VAR_058766
Natural variant5721P → S. Ref.40
Corresponds to variant rs149022148 [ dbSNP | Ensembl ].
VAR_058767
Natural variant5941F → Y in PKD1. Ref.44
VAR_058768
Natural variant6111R → W in PKD1. Ref.46
VAR_068025
Natural variant6901V → D in PKD1. Ref.42
VAR_058769
Natural variant6981Y → D in PKD1. Ref.46
VAR_068026
Natural variant7271L → P in PKD1. Ref.45 Ref.46
VAR_064383
Natural variant7271L → R in PKD1. Ref.45
VAR_064384
Natural variant7381P → R.
VAR_058770
Natural variant7391R → Q. Ref.2 Ref.37 Ref.44
Corresponds to variant rs40433 [ dbSNP | Ensembl ].
VAR_058771
Natural variant8451L → S in PKD1. Ref.20 Ref.43
VAR_010086
Natural variant9501L → P.
Corresponds to variant rs2369063 [ dbSNP | Ensembl ].
VAR_056696
Natural variant9671W → R in PKD1. Ref.33
VAR_012453
Natural variant9871Q → H in PKD1. Ref.39
VAR_058772
Natural variant10921M → T in PKD1. Ref.1 Ref.37 Ref.40 Ref.44
Corresponds to variant rs2549677 [ dbSNP | Ensembl ].
VAR_056697
Natural variant11141L → R.
Corresponds to variant rs241573 [ dbSNP | Ensembl ].
VAR_056698
Natural variant11661G → S in PKD1. Ref.29
VAR_011033
Natural variant11681P → S. Ref.40
Corresponds to variant rs146887330 [ dbSNP | Ensembl ].
VAR_058773
Natural variant12061V → G in PKD1. Ref.46
VAR_068027
Natural variant12401Missing in PKD1. Ref.42
VAR_058774
Natural variant12421T → M in PKD1; unknown pathological significance. Ref.44
VAR_058775
Natural variant13401R → W in PKD1. Ref.40
Corresponds to variant rs143690392 [ dbSNP | Ensembl ].
VAR_058776
Natural variant13991W → R. Ref.20 Ref.21 Ref.37 Ref.39 Ref.40 Ref.44
Corresponds to variant rs116092985 [ dbSNP | Ensembl ].
VAR_010087
Natural variant15161A → T. Ref.44
Corresponds to variant rs148164067 [ dbSNP | Ensembl ].
VAR_058777
Natural variant15571R → P.
Corresponds to variant rs241572 [ dbSNP | Ensembl ].
VAR_056699
Natural variant16491T → M. Ref.37
VAR_058778
Natural variant16671T → P in PKD1. Ref.42
VAR_058779
Natural variant16841S → L. Ref.40
Corresponds to variant rs139520275 [ dbSNP | Ensembl ].
VAR_058780
Natural variant17341T → K.
Corresponds to variant rs241571 [ dbSNP | Ensembl ].
VAR_056700
Natural variant17861P → L Rare polymorphism. Ref.20
VAR_010088
Natural variant18111E → K in PKD1. Ref.40 Ref.42
VAR_058781
Natural variant18711A → T. Ref.44
VAR_058782
Natural variant19261A → V. Ref.44
VAR_058783
Natural variant19431V → I. Ref.40
Corresponds to variant rs137978188 [ dbSNP | Ensembl ].
VAR_058784
Natural variant19521G → D. Ref.44
VAR_058785
Natural variant19561V → E in PKD1. Ref.29
VAR_011034
Natural variant1992 – 19932FT → L in PKD1.
VAR_011035
Natural variant19951R → H. Ref.29
VAR_011036
Natural variant20831T → I in PKD1. Ref.38
VAR_058786
Natural variant20921Y → C in PKD1. Ref.40 Ref.42
VAR_058787
Natural variant21851Y → D in PKD1. Ref.37
VAR_058788
Natural variant22001R → C in PKD1. Ref.42 Ref.44
Corresponds to variant rs140869992 [ dbSNP | Ensembl ].
VAR_058789
Natural variant2220 – 22245Missing in PKD1.
VAR_011037
Natural variant22501T → M in PKD1; unknown pathological significance. Ref.25
VAR_011038
Natural variant22601Missing in PKD1. Ref.40 Ref.42
VAR_058790
Natural variant23291R → W in PKD1; unknown pathological significance. Ref.25
VAR_011039
Natural variant23361Y → D in PKD1. Ref.31
VAR_011040
Natural variant23701C → R in PKD1. Ref.42
VAR_058791
Natural variant23731C → Y in PKD1. Ref.42
VAR_058792
Natural variant23791Y → C in PKD1. Ref.25 Ref.46
VAR_011041
Natural variant23911G → D in PKD1. Ref.45
VAR_064385
Natural variant23921R → P in PKD1. Ref.21
VAR_012454
Natural variant24081R → C in PKD1. Ref.29
VAR_011042
Natural variant24211Missing in PKD1. Ref.37
VAR_058793
Natural variant24221T → K in PKD1. Ref.44
VAR_058794
Natural variant24231S → F in PKD1. Ref.21
VAR_012455
Natural variant24341R → W in PKD1. Ref.45
VAR_064386
Natural variant24431G → GG in PKD1.
VAR_011043
Natural variant24711P → L in PKD1. Ref.32
VAR_012456
Natural variant25151R → Q.
Corresponds to variant rs2432404 [ dbSNP | Ensembl ].
VAR_056701
Natural variant25191Q → L in PKD1; unknown pathological significance. Ref.32
VAR_012457
Natural variant25341S → G.
Corresponds to variant rs3874655 [ dbSNP | Ensembl ].
VAR_056702
Natural variant25461H → Y in PKD1. Ref.45
VAR_064387
Natural variant25481E → Q. Ref.21
Corresponds to variant rs28369051 [ dbSNP | Ensembl ].
VAR_012458
Natural variant25691S → C in PKD1. Ref.45
VAR_064388
Natural variant25791Missing in PKD1; unknown pathological significance. Ref.32
VAR_012459
Natural variant25821T → M. Ref.32
Corresponds to variant rs2432405 [ dbSNP | Ensembl ].
VAR_012460
Natural variant26041D → N. Ref.29
VAR_011044
Natural variant26131Missing in PKD1; unknown pathological significance. Ref.32
VAR_012461
Natural variant26381H → R in PKD1. Ref.21 Ref.32 Ref.37 Ref.40 Ref.43 Ref.44
Corresponds to variant rs9936785 [ dbSNP | Ensembl ].
VAR_012462
Natural variant26461I → T in PKD1. Ref.45
VAR_064389
Natural variant26491T → I in PKD1; unknown pathological significance. Ref.32
VAR_012463
Natural variant26741P → S. Ref.31 Ref.40
VAR_011045
Natural variant26961L → R in PKD1. Ref.33
VAR_012464
Natural variant27081T → M. Ref.31 Ref.40 Ref.44
VAR_011046
Natural variant27341P → T. Ref.31
Corresponds to variant rs150568356 [ dbSNP | Ensembl ].
VAR_011047
Natural variant27351Q → L. Ref.31
Corresponds to variant rs141717814 [ dbSNP | Ensembl ].
VAR_011048
Natural variant27461R → P.
Corresponds to variant rs1800569 [ dbSNP | Ensembl ].
VAR_014918
Natural variant27521A → D in PKD1. Ref.31
VAR_011049
Natural variant27601M → T Associated with PKD1. Ref.16
Corresponds to variant rs1800568 [ dbSNP | Ensembl ].
VAR_005533
Natural variant27611R → P Associated with PKD1. Ref.16
VAR_058795
Natural variant27631L → V in PKD1. Ref.16
VAR_005535
Natural variant27641M → T Associated with PKD1. Ref.16
Corresponds to variant rs1800570 [ dbSNP | Ensembl ].
VAR_005536
Natural variant27651R → C. Ref.31 Ref.37
Corresponds to variant rs144979397 [ dbSNP | Ensembl ].
VAR_011051
Natural variant27651R → RILMR in PKD1.
VAR_011050
Natural variant27671R → C in PKD1. Ref.46
VAR_068028
Natural variant27681V → M in PKD1; associated with S-2858. Ref.31
VAR_011052
Natural variant27711E → K in PKD1; does not undergo autoproteolytic cleavage. Ref.6 Ref.31 Ref.42 Ref.46
VAR_011053
Natural variant27821V → M. Ref.31
VAR_011054
Natural variant27851G → D in PKD1. Ref.37
VAR_058796
Natural variant27911R → Q in a patient with polycystic kidney disease; does not affect autoproteolytic cleavage at the GPS domain. Ref.6 Ref.16
VAR_005537
Natural variant28021P → L in PKD1. Ref.42
VAR_058797
Natural variant28141G → R in PKD1; unknown pathological significance. Ref.31 Ref.38 Ref.40 Ref.44
Corresponds to variant rs149151043 [ dbSNP | Ensembl ].
VAR_011055
Natural variant28161L → P in PKD1. Ref.31 Ref.38
VAR_011056
Natural variant28261I → T in PKD1. Ref.16
VAR_005538
Natural variant28581G → S in PKD1; associated with M-2768. Ref.31
VAR_011057
Natural variant28881R → G. Ref.31
VAR_011058
Natural variant28891S → R in PKD1. Ref.45
VAR_064390
Natural variant29051V → I. Ref.31
Corresponds to variant rs147788838 [ dbSNP | Ensembl ].
VAR_011059
Natural variant29211H → P in PKD1; does not undergo autoproteolytic cleavage. Ref.6 Ref.27
VAR_011060
Natural variant29581S → L. Ref.40
VAR_058798
Natural variant29661E → D. Ref.31
Corresponds to variant rs13337123 [ dbSNP | Ensembl ].
VAR_011061
Natural variant29721D → N. Ref.32
VAR_012465
Natural variant29771T → N. Ref.40
VAR_058799
Natural variant29781Missing in PKD1; unknown pathological significance. Ref.32
VAR_012466
Natural variant29851R → G in PKD1. Ref.33
VAR_012467
Natural variant29931L → P in PKD1; does not undergo autoproteolytic cleavage. Ref.6 Ref.14
VAR_010089
Natural variant29951L → R in PKD1. Ref.46
VAR_068029
Natural variant30051Q → E.
Corresponds to variant rs1063401 [ dbSNP | Ensembl ].
VAR_056703
Natural variant30081V → L in PKD1. Ref.16
VAR_005539
Natural variant30081V → M. Ref.34
Corresponds to variant rs117896488 [ dbSNP | Ensembl ].
VAR_058800
Natural variant3012 – 30176Missing in PKD1.
VAR_011062
Natural variant30161Q → R in PKD1; does not undergo autoproteolytic cleavage. Ref.6 Ref.14
VAR_010090
Natural variant30231M → V.
Corresponds to variant rs17135779 [ dbSNP | Ensembl ].
VAR_056704
Natural variant3027 – 303913Missing in PKD1.
VAR_058801
Natural variant30391R → C in PKD1. Ref.33
VAR_012468
Natural variant30571V → M. Ref.40
VAR_058802
Natural variant30661F → L in PKD1. Ref.16 Ref.25 Ref.27 Ref.31 Ref.32 Ref.37 Ref.43 Ref.44
Corresponds to variant rs77028972 [ dbSNP | Ensembl ].
VAR_011063
Natural variant31381V → M in PKD1; unknown pathological significance. Ref.43
VAR_058803
Natural variant31391G → V. Ref.25
VAR_011064
Natural variant31541L → P in PKD1. Ref.45
VAR_064391
Natural variant31671I → F in PKD1. Ref.40
VAR_058804
Natural variant31881Missing in PKD1. Ref.42
VAR_058805
Natural variant31931P → L. Ref.25
VAR_011065
Natural variant32471R → H in PKD1. Ref.26
VAR_013838
Natural variant32851V → I in PKD1. Ref.33
VAR_012469
Natural variant33111H → R. Ref.33
VAR_012470
Natural variant33551P → L in PKD1. Ref.42
VAR_058806
Natural variant33751V → M in PKD1. Ref.19 Ref.27
VAR_005541
Natural variant33821T → M in PKD1. Ref.26
VAR_013839
Natural variant34351R → Q. Ref.40
Corresponds to variant rs140189010 [ dbSNP | Ensembl ].
VAR_058807
Natural variant35101T → M in PKD1. Ref.14 Ref.34 Ref.35 Ref.38 Ref.43
Corresponds to variant rs45478794 [ dbSNP | Ensembl ].
VAR_010091
Natural variant35111L → V in PKD1; unknown pathological significance. Ref.14
VAR_010092
Natural variant35121A → V. Ref.40 Ref.43 Ref.44
Corresponds to variant rs34197769 [ dbSNP | Ensembl ].
VAR_011066
Natural variant35601G → R in PKD1. Ref.35
Corresponds to variant rs79000340 [ dbSNP | Ensembl ].
VAR_012471
Natural variant35621S → N.
VAR_010093
Natural variant36021G → S in PKD1. Ref.36
VAR_058808
Natural variant36031W → R in PKD1. Ref.45
VAR_064392
Natural variant36321E → D in PKD1. Ref.13 Ref.41
VAR_005542
Natural variant36491P → L in PKD1. Ref.41
VAR_058809
Natural variant36511G → S in PKD1. Ref.46
VAR_068030
Natural variant36781M → T in PKD1. Ref.17 Ref.41
VAR_005543
Natural variant36821L → P in PKD1. Ref.42
VAR_058810
Natural variant37191R → Q in PKD1. Ref.28 Ref.35
VAR_011067
Natural variant37261W → S in PKD1; unknown pathological significance. Ref.44
VAR_058811
Natural variant3748 – 37525Missing in PKD1.
VAR_005544
Natural variant37501R → Q in PKD1. Ref.45 Ref.46
VAR_064393
Natural variant37511Q → R in PKD1. Ref.42
VAR_058812
Natural variant37531R → W in PKD1. Ref.30 Ref.35 Ref.46
VAR_011068
Natural variant38151D → N in PKD1. Ref.30
VAR_011069
Natural variant38521L → P in PKD1. Ref.28 Ref.40
VAR_011070
Natural variant39541A → P in PKD1; unknown pathological significance. Ref.43
VAR_058813
Natural variant39961F → FLLF in PKD1.
VAR_010094
Natural variant40321G → D in PKD1. Ref.18
VAR_005545
Natural variant40451I → V. Ref.18 Ref.23 Ref.28 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44
Corresponds to variant rs10960 [ dbSNP | Ensembl ].
VAR_005546
Natural variant40581V → A. Ref.15
VAR_005547
Natural variant40591A → V. Ref.40 Ref.41 Ref.43 Ref.44
Corresponds to variant rs3209986 [ dbSNP | Ensembl ].
VAR_010095
Natural variant41021G → E. Ref.41
VAR_058814
Natural variant41061L → P. Ref.41
VAR_058815
Natural variant41241P → S. Ref.40
VAR_058816
Natural variant41321Missing in PKD1. Ref.23
VAR_011071
Natural variant41361R → G in PKD1. Ref.22
VAR_010096
Natural variant41461V → I. Ref.40 Ref.41
Corresponds to variant rs148478410 [ dbSNP | Ensembl ].
VAR_058817
Natural variant41501R → C in PKD1. Ref.46
VAR_068031
Natural variant41541R → C in PKD1. Ref.22
Corresponds to variant rs115538130 [ dbSNP | Ensembl ].
VAR_010097
Natural variant41551F → V in PKD1. Ref.44
VAR_058818
Natural variant41901S → F. Ref.14 Ref.40
VAR_010098
Natural variant42251Q → P in PKD1. Ref.24
VAR_010099
Natural variant42551P → S in PKD1. Ref.36
VAR_058819
Natural variant42761R → W in PKD1. Ref.24 Ref.46
Corresponds to variant rs114251396 [ dbSNP | Ensembl ].
VAR_010100

Experimental info

Mutagenesis30491T → C or S: Does not affect auto-cleavage. Ref.7
Mutagenesis30491T → G, R or V: Does not undergo auto-cleavage. Ref.7
Sequence conflict711A → E in AAC50128. Ref.1
Sequence conflict1381R → Q in AAC50128. Ref.1
Sequence conflict2531P → A in AAC50128. Ref.1
Sequence conflict3021A → D in AAC50128. Ref.1
Sequence conflict6911P → A in AAC37576. Ref.2
Sequence conflict6911P → A in AAC41765. Ref.2
Sequence conflict7631A → G in AAC50128. Ref.1
Sequence conflict774 – 7752AT → QR in AAC50128. Ref.1
Sequence conflict7921L → M in AAC37576. Ref.2
Sequence conflict7921L → M in AAC41765. Ref.2
Sequence conflict8661V → L in AAC50128. Ref.1
Sequence conflict8841G → A in AAC50128. Ref.1
Sequence conflict10561T → N in AAC37576. Ref.2
Sequence conflict10561T → N in AAC41765. Ref.2
Sequence conflict12771A → G in AAC50128. Ref.1
Sequence conflict17241A → T in AAC37576. Ref.2
Sequence conflict17241A → T in AAC41765. Ref.2
Sequence conflict19761V → M in AAC37576. Ref.2
Sequence conflict19761V → M in AAC41765. Ref.2
Sequence conflict3982 – 39832QL → HV in AAC50128. Ref.1
Sequence conflict4005 – 40062QL → HV in AAC50128. Ref.1

Secondary structure

............... 4303
Helix Strand Turn

Details...

Sequences

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

Last modified March 23, 2010. Version 3.
Checksum: AEDAC48F3F0A853C

FASTA4,303462,529
        10         20         30         40         50         60 
MPPAAPARLA LALGLGLWLG ALAGGPGRGC GPCEPPCLCG PAPGAACRVN CSGRGLRTLG 

        70         80         90        100        110        120 
PALRIPADAT ALDVSHNLLR ALDVGLLANL SALAELDISN NKISTLEEGI FANLFNLSEI 

       130        140        150        160        170        180 
NLSGNPFECD CGLAWLPRWA EEQQVRVVQP EAATCAGPGS LAGQPLLGIP LLDSGCGEEY 

       190        200        210        220        230        240 
VACLPDNSSG TVAAVSFSAA HEGLLQPEAC SAFCFSTGQG LAALSEQGWC LCGAAQPSSA 

       250        260        270        280        290        300 
SFACLSLCSG PPPPPAPTCR GPTLLQHVFP ASPGATLVGP HGPLASGQLA AFHIAAPLPV 

       310        320        330        340        350        360 
TATRWDFGDG SAEVDAAGPA ASHRYVLPGR YHVTAVLALG AGSALLGTDV QVEAAPAALE 

       370        380        390        400        410        420 
LVCPSSVQSD ESLDLSIQNR GGSGLEAAYS IVALGEEPAR AVHPLCPSDT EIFPGNGHCY 

       430        440        450        460        470        480 
RLVVEKAAWL QAQEQCQAWA GAALAMVDSP AVQRFLVSRV TRSLDVWIGF STVQGVEVGP 

       490        500        510        520        530        540 
APQGEAFSLE SCQNWLPGEP HPATAEHCVR LGPTGWCNTD LCSAPHSYVC ELQPGGPVQD 

       550        560        570        580        590        600 
AENLLVGAPS GDLQGPLTPL AQQDGLSAPH EPVEVMVFPG LRLSREAFLT TAEFGTQELR 

       610        620        630        640        650        660 
RPAQLRLQVY RLLSTAGTPE NGSEPESRSP DNRTQLAPAC MPGGRWCPGA NICLPLDASC 

       670        680        690        700        710        720 
HPQACANGCT SGPGLPGAPY ALWREFLFSV PAGPPAQYSV TLHGQDVLML PGDLVGLQHD 

       730        740        750        760        770        780 
AGPGALLHCS PAPGHPGPRA PYLSANASSW LPHLPAQLEG TWACPACALR LLAATEQLTV 

       790        800        810        820        830        840 
LLGLRPNPGL RLPGRYEVRA EVGNGVSRHN LSCSFDVVSP VAGLRVIYPA PRDGRLYVPT 

       850        860        870        880        890        900 
NGSALVLQVD SGANATATAR WPGGSVSARF ENVCPALVAT FVPGCPWETN DTLFSVVALP 

       910        920        930        940        950        960 
WLSEGEHVVD VVVENSASRA NLSLRVTAEE PICGLRATPS PEARVLQGVL VRYSPVVEAG 

       970        980        990       1000       1010       1020 
SDMVFRWTIN DKQSLTFQNV VFNVIYQSAA VFKLSLTASN HVSNVTVNYN VTVERMNRMQ 

      1030       1040       1050       1060       1070       1080 
GLQVSTVPAV LSPNATLALT AGVLVDSAVE VAFLWTFGDG EQALHQFQPP YNESFPVPDP 

      1090       1100       1110       1120       1130       1140 
SVAQVLVEHN VMHTYAAPGE YLLTVLASNA FENLTQQVPV SVRASLPSVA VGVSDGVLVA 

      1150       1160       1170       1180       1190       1200 
GRPVTFYPHP LPSPGGVLYT WDFGDGSPVL TQSQPAANHT YASRGTYHVR LEVNNTVSGA 

      1210       1220       1230       1240       1250       1260 
AAQADVRVFE ELRGLSVDMS LAVEQGAPVV VSAAVQTGDN ITWTFDMGDG TVLSGPEATV 

      1270       1280       1290       1300       1310       1320 
EHVYLRAQNC TVTVGAASPA GHLARSLHVL VFVLEVLRVE PAACIPTQPD ARLTAYVTGN 

      1330       1340       1350       1360       1370       1380 
PAHYLFDWTF GDGSSNTTVR GCPTVTHNFT RSGTFPLALV LSSRVNRAHY FTSICVEPEV 

      1390       1400       1410       1420       1430       1440 
GNVTLQPERQ FVQLGDEAWL VACAWPPFPY RYTWDFGTEE AAPTRARGPE VTFIYRDPGS 

      1450       1460       1470       1480       1490       1500 
YLVTVTASNN ISAANDSALV EVQEPVLVTS IKVNGSLGLE LQQPYLFSAV GRGRPASYLW 

      1510       1520       1530       1540       1550       1560 
DLGDGGWLEG PEVTHAYNST GDFTVRVAGW NEVSRSEAWL NVTVKRRVRG LVVNASRTVV 

      1570       1580       1590       1600       1610       1620 
PLNGSVSFST SLEAGSDVRY SWVLCDRCTP IPGGPTISYT FRSVGTFNII VTAENEVGSA 

      1630       1640       1650       1660       1670       1680 
QDSIFVYVLQ LIEGLQVVGG GRYFPTNHTV QLQAVVRDGT NVSYSWTAWR DRGPALAGSG 

      1690       1700       1710       1720       1730       1740 
KGFSLTVLEA GTYHVQLRAT NMLGSAWADC TMDFVEPVGW LMVAASPNPA AVNTSVTLSA 

      1750       1760       1770       1780       1790       1800 
ELAGGSGVVY TWSLEEGLSW ETSEPFTTHS FPTPGLHLVT MTAGNPLGSA NATVEVDVQV 

      1810       1820       1830       1840       1850       1860 
PVSGLSIRAS EPGGSFVAAG SSVPFWGQLA TGTNVSWCWA VPGGSSKRGP HVTMVFPDAG 

      1870       1880       1890       1900       1910       1920 
TFSIRLNASN AVSWVSATYN LTAEEPIVGL VLWASSKVVA PGQLVHFQIL LAAGSAVTFR 

      1930       1940       1950       1960       1970       1980 
LQVGGANPEV LPGPRFSHSF PRVGDHVVSV RGKNHVSWAQ AQVRIVVLEA VSGLQVPNCC 

      1990       2000       2010       2020       2030       2040 
EPGIATGTER NFTARVQRGS RVAYAWYFSL QKVQGDSLVI LSGRDVTYTP VAAGLLEIQV 

      2050       2060       2070       2080       2090       2100 
RAFNALGSEN RTLVLEVQDA VQYVALQSGP CFTNRSAQFE AATSPSPRRV AYHWDFGDGS 

      2110       2120       2130       2140       2150       2160 
PGQDTDEPRA EHSYLRPGDY RVQVNASNLV SFFVAQATVT VQVLACREPE VDVVLPLQVL 

      2170       2180       2190       2200       2210       2220 
MRRSQRNYLE AHVDLRDCVT YQTEYRWEVY RTASCQRPGR PARVALPGVD VSRPRLVLPR 

      2230       2240       2250       2260       2270       2280 
LALPVGHYCF VFVVSFGDTP LTQSIQANVT VAPERLVPII EGGSYRVWSD TRDLVLDGSE 

      2290       2300       2310       2320       2330       2340 
SYDPNLEDGD QTPLSFHWAC VASTQREAGG CALNFGPRGS STVTIPRERL AAGVEYTFSL 

      2350       2360       2370       2380       2390       2400 
TVWKAGRKEE ATNQTVLIRS GRVPIVSLEC VSCKAQAVYE VSRSSYVYLE GRCLNCSSGS 

      2410       2420       2430       2440       2450       2460 
KRGRWAARTF SNKTLVLDET TTSTGSAGMR LVLRRGVLRD GEGYTFTLTV LGRSGEEEGC 

      2470       2480       2490       2500       2510       2520 
ASIRLSPNRP PLGGSCRLFP LGAVHALTTK VHFECTGWHD AEDAGAPLVY ALLLRRCRQG 

      2530       2540       2550       2560       2570       2580 
HCEEFCVYKG SLSSYGAVLP PGFRPHFEVG LAVVVQDQLG AAVVALNRSL AITLPEPNGS 

      2590       2600       2610       2620       2630       2640 
ATGLTVWLHG LTASVLPGLL RQADPQHVIE YSLALVTVLN EYERALDVAA EPKHERQHRA 

      2650       2660       2670       2680       2690       2700 
QIRKNITETL VSLRVHTVDD IQQIAAALAQ CMGPSRELVC RSCLKQTLHK LEAMMLILQA 

      2710       2720       2730       2740       2750       2760 
ETTAGTVTPT AIGDSILNIT GDLIHLASSD VRAPQPSELG AESPSRMVAS QAYNLTSALM 

      2770       2780       2790       2800       2810       2820 
RILMRSRVLN EEPLTLAGEE IVAQGKRSDP RSLLCYGGAP GPGCHFSIPE AFSGALANLS 

      2830       2840       2850       2860       2870       2880 
DVVQLIFLVD SNPFPFGYIS NYTVSTKVAS MAFQTQAGAQ IPIERLASER AITVKVPNNS 

      2890       2900       2910       2920       2930       2940 
DWAARGHRSS ANSANSVVVQ PQASVGAVVT LDSSNPAAGL HLQLNYTLLD GHYLSEEPEP 

      2950       2960       2970       2980       2990       3000 
YLAVYLHSEP RPNEHNCSAS RRIRPESLQG ADHRPYTFFI SPGSRDPAGS YHLNLSSHFR 

      3010       3020       3030       3040       3050       3060 
WSALQVSVGL YTSLCQYFSE EDMVWRTEGL LPLEETSPRQ AVCLTRHLTA FGASLFVPPS 

      3070       3080       3090       3100       3110       3120 
HVRFVFPEPT ADVNYIVMLT CAVCLVTYMV MAAILHKLDQ LDASRGRAIP FCGQRGRFKY 

      3130       3140       3150       3160       3170       3180 
EILVKTGWGR GSGTTAHVGI MLYGVDSRSG HRHLDGDRAF HRNSLDIFRI ATPHSLGSVW 

      3190       3200       3210       3220       3230       3240 
KIRVWHDNKG LSPAWFLQHV IVRDLQTARS AFFLVNDWLS VETEANGGLV EKEVLAASDA 

      3250       3260       3270       3280       3290       3300 
ALLRFRRLLV AELQRGFFDK HIWLSIWDRP PRSRFTRIQR ATCCVLLICL FLGANAVWYG 

      3310       3320       3330       3340       3350       3360 
AVGDSAYSTG HVSRLSPLSV DTVAVGLVSS VVVYPVYLAI LFLFRMSRSK VAGSPSPTPA 

      3370       3380       3390       3400       3410       3420 
GQQVLDIDSC LDSSVLDSSF LTFSGLHAEQ AFVGQMKSDL FLDDSKSLVC WPSGEGTLSW 

      3430       3440       3450       3460       3470       3480 
PDLLSDPSIV GSNLRQLARG QAGHGLGPEE DGFSLASPYS PAKSFSASDE DLIQQVLAEG 

      3490       3500       3510       3520       3530       3540 
VSSPAPTQDT HMETDLLSSL SSTPGEKTET LALQRLGELG PPSPGLNWEQ PQAARLSRTG 

      3550       3560       3570       3580       3590       3600 
LVEGLRKRLL PAWCASLAHG LSLLLVAVAV AVSGWVGASF PPGVSVAWLL SSSASFLASF 

      3610       3620       3630       3640       3650       3660 
LGWEPLKVLL EALYFSLVAK RLHPDEDDTL VESPAVTPVS ARVPRVRPPH GFALFLAKEE 

      3670       3680       3690       3700       3710       3720 
ARKVKRLHGM LRSLLVYMLF LLVTLLASYG DASCHGHAYR LQSAIKQELH SRAFLAITRS 

      3730       3740       3750       3760       3770       3780 
EELWPWMAHV LLPYVHGNQS SPELGPPRLR QVRLQEALYP DPPGPRVHTC SAAGGFSTSD 

      3790       3800       3810       3820       3830       3840 
YDVGWESPHN GSGTWAYSAP DLLGAWSWGS CAVYDSGGYV QELGLSLEES RDRLRFLQLH 

      3850       3860       3870       3880       3890       3900 
NWLDNRSRAV FLELTRYSPA VGLHAAVTLR LEFPAAGRAL AALSVRPFAL RRLSAGLSLP 

      3910       3920       3930       3940       3950       3960 
LLTSVCLLLF AVHFAVAEAR TWHREGRWRV LRLGAWARWL LVALTAATAL VRLAQLGAAD 

      3970       3980       3990       4000       4010       4020 
RQWTRFVRGR PRRFTSFDQV AQLSSAARGL AASLLFLLLV KAAQQLRFVR QWSVFGKTLC 

      4030       4040       4050       4060       4070       4080 
RALPELLGVT LGLVVLGVAY AQLAILLVSS CVDSLWSVAQ ALLVLCPGTG LSTLCPAESW 

      4090       4100       4110       4120       4130       4140 
HLSPLLCVGL WALRLWGALR LGAVILRWRY HALRGELYRP AWEPQDYEMV ELFLRRLRLW 

      4150       4160       4170       4180       4190       4200 
MGLSKVKEFR HKVRFEGMEP LPSRSSRGSK VSPDVPPPSA GSDASHPSTS SSQLDGLSVS 

      4210       4220       4230       4240       4250       4260 
LGRLGTRCEP EPSRLQAVFE ALLTQFDRLN QATEDVYQLE QQLHSLQGRR SSRAPAGSSR 

      4270       4280       4290       4300 
GPSPGLRPAL PSRLARASRG VDLATGPSRT PLRAKNKVHP SST 

« Hide

Isoform 2 [UniParc].

Checksum: A5E38810302239F2
Show »

FASTA4,292461,365
Isoform 3 [UniParc].

Checksum: 23CADEBB778AC22D
Show »

FASTA4,302462,401

References

« Hide 'large scale' references
[1]"Polycystic kidney disease: the complete structure of the PKD1 gene and its protein."
Gluecksmann-Kuis M.A., Tayber O., Woolf E.A., Bougueleret L., Deng N., Alperin G.D., Iris F., Hawkins F., Munro C., Lakey N., Duyk G., Schneider M.C., Geng L., Zhang F., Zhao Z., Torosian S., Reeders S.T., Bork P. expand/collapse author list , Pohlschmidt M., Loehning C., Kraus B., Nowicka U., Leung A.L.S., Frischauf A.-M.
Cell 81:289-298(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1092.
[2]"The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains."
Hughes J., Ward C.J., Peral B., Aspinwall R., Clark K., San Millan J.L., Gamble V., Harris P.C.
Nat. Genet. 10:151-160(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), VARIANT GLN-739.
[3]"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].
[4]"The polycystic kidney disease 1 gene encodes a 14 kb transcript and lies within a duplicated region on chromosome 16."
Ward C.J., Peral B., Hughes J., Thomas S., Gamble V., Maccarthy A.B., Sloane-Stanley J., Buckle V.J., Kearney L., Higgs D.R., Ratcliffe P.J., Harris P.C., Roelfsema J.H., Spruit L.L., Saris J.J., Dauwerse H.G., Peters D.J.M., Breuning M.H. expand/collapse author list , Nellist M., Brook-Carter P.T., Maheshwar M.M., Cordeiro I., Santos H., Cabral P., Sampson J.R., Janssen B., Hesseling-Janssen A.L.W., van den Ouweland A.M.W., Eussen B., Verhoef S., Lindhout D., Halley D.J.J.
Cell 77:881-894(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2769-4303.
[5]Erratum
Ward C.J., Peral B., Hughes J., Thomas S., Gamble V., Maccarthy A.B., Sloane-Stanley J., Buckle V.J., Kearney L., Higgs D.R., Ratcliffe P.J., Harris P.C., Roelfsema J.H., Spruit L.L., Saris J.J., Dauwerse H.G., Peters D.J.M., Breuning M.H. expand/collapse author list , Nellist M., Brook-Carter P.T., Maheshwar M.M., Cordeiro I., Santos H., Cabral P., Sampson J.R., Janssen B., Hesseling-Janssen A.L.W., van den Ouweland A.M.W., Eussen B., Verhoef S., Lindhout D., Halley D.J.J.
Cell 78:725-725(1994) [PubMed] [Europe PMC] [Abstract]
[6]"Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations."
Qian F., Boletta A., Bhunia A.K., Xu H., Liu L., Ahrabi A.K., Watnick T.J., Zhou F., Germino G.G.
Proc. Natl. Acad. Sci. U.S.A. 99:16981-16986(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RENAL TUBULOGENESIS, CLEAVAGE AT GPS DOMAIN, CHARACTERIZATION OF VARIANTS PKD1 LYS-2771; PRO-2921; PRO-2993 AND ARG-3016, CHARACTERIZATION OF VARIANT GLN-2791.
[7]"Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene."
Wei W., Hackmann K., Xu H., Germino G., Qian F.
J. Biol. Chem. 282:21729-21737(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPROTEOLYTIC CLEAVAGE, DETERMINATION OF AUTOPROTEOLYTIC CLEAVAGE SITE, MUTAGENESIS OF THR-3049.
[8]"Protein kinase X (PRKX) can rescue the effects of polycystic kidney disease-1 gene (PKD1) deficiency."
Li X., Burrow C.R., Polgar K., Hyink D.P., Gusella G.L., Wilson P.D.
Biochim. Biophys. Acta 1782:1-9(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-4166, INTERACTION WITH PRKX.
[9]"Polycystin-1 surface localization is stimulated by polycystin-2 and cleavage at the G protein-coupled receptor proteolytic site."
Chapin H.C., Rajendran V., Caplan M.J.
Mol. Biol. Cell 21:4338-4348(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/SH3 domain interaction and regulates the apoptotic response in mammals."
Wodarczyk C., Distefano G., Rowe I., Gaetani M., Bricoli B., Muorah M., Spitaleri A., Mannella V., Ricchiuto P., Pema M., Castelli M., Casanova A.E., Mollica L., Banzi M., Boca M., Antignac C., Saunier S., Musco G., Boletta A.
PLoS ONE 5:E12719-E12719(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPHP1.
[11]"The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease."
Bycroft M., Bateman A., Clarke J., Hamill S.J., Sandford R., Thomas R.L., Chothia C.
EMBO J. 18:297-305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 275-354.
[12]"Polycystin channels and kidney disease."
Stayner C., Zhou J.
Trends Pharmacol. Sci. 22:543-546(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Screening the 3' region of the polycystic kidney disease 1 (PKD1) gene reveals six novel mutations."
Peral B., San Millan J.L., Ong A.C.M., Gamble V., Ward C.J., Strong C., Harris P.C.
Am. J. Hum. Genet. 58:86-96(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 3748-ARG--VAL-3752 DEL, VARIANT ASP-3632.
[14]"Identification of mutations in the duplicated region of the polycystic kidney disease 1 gene (PKD1) by a novel approach."
Peral B., Gamble V., Strong C., Ong A.C.M., Sloane-Stanley J., Zerres K., Winearls C.G., Harris P.C.
Am. J. Hum. Genet. 60:1399-1410(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 PRO-2993; ARG-3016 AND VAL-3511, VARIANTS MET-3510 AND PHE-4190.
[15]"New amino acid polymorphism, Ala/Val4058, in exon 45 of the polycystic kidney disease 1 gene: evolution of alleles."
Constantinides R., Xenophontos S.L., Neophytou P., Nomura S., Pierides A., Constantinou-Deltas C.D.
Hum. Genet. 99:644-647(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-4058.
[16]"An unusual pattern of mutation in the duplicated portion of PKD1 is revealed by use of a novel strategy for mutation detection."
Watnick T.J., Piontek K.B., Cordal T.M., Weber H., Gandolph M.A., Qian F., Lens X.M., Neumann H.P.H., Germino G.G.
Hum. Mol. Genet. 6:1473-1481(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 VAL-2763; THR-2826 AND LEU-3008, VARIANTS THR-2760; PRO-2761; THR-2764; GLN-2791 AND LEU-3066.
[17]"Three novel mutations of the PKD1 gene in Italian families with autosomal dominant polycystic kidney disease."
Turco A.E., Rossetti S., Bresin E., Englisch S., Corra S., Pignatti P.F.
Hum. Mutat. 10:164-167(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 THR-3678.
[18]"Novel and recurrent mutations in the PKD1 (polycystic kidney disease) gene."
Daniells C., Maheshwar M.M., Lazarou L., Davies F., Coles G., Ravine D.
Hum. Genet. 102:216-220(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 ASP-4032, VARIANT VAL-4045.
[19]"Loss of heterozygosity in polycystic kidney disease with a missense mutation in the repeated region of PKD1."
Koptides M., Constantinides R., Kyriakides G., Hadjigavriel M., Patsalis P.C., Pierides A., Deltas C.C.
Hum. Genet. 103:709-717(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 MET-3375.
[20]"Identification of mutations in the repeated part of the autosomal dominant polycystic kidney disease type 1 gene, PKD1, by long-range PCR."
Thomas R.L., McConnell R., Whittacker J., Kirkpatrick P., Bradley J., Sandford R.
Am. J. Hum. Genet. 65:39-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 LEU-324 AND SER-845, VARIANTS ARG-1399 AND LEU-1786.
[21]"Mutation detection of PKD1 identifies a novel mutation common to three families with aneurysms and/or very-early-onset disease."
Watnick T., Phakdeekitcharoen B., Johnson A., Gandolph M.A., Wang M., Briefel G., Klinger K.W., Kimberling W., Gabow P., Germino G.G.
Am. J. Hum. Genet. 65:1561-1571(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 PRO-2392 AND PHE-2423, VARIANTS ARG-1399; GLN-2548 AND ARG-2638.
[22]"DGGE screening of PKD1 gene reveals novel mutations in a large cohort of 146 unrelated patients."
Perrichot R.A., Mercier B., Simon P.M., Whebe B., Cledes J., Ferec C.
Hum. Genet. 105:231-239(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 LEU-LEU-PHE-3996 INS; GLY-4136 AND CYS-4154, VARIANTS.
[23]"Novel mutations in the 3 region of the polycystic kidney disease 1 (PKD1) gene."
Afzal A.R., Hand M., Ternes-Pereira E., Saggar-Malik A., Taylor R., Jeffery S.
Hum. Genet. 105:648-653(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 3748-ARG--VAL-3752 DEL AND LEU-4132 DEL, VARIANT VAL-4045.
[24]"Mutational analysis within the 3' region of the PKD1 gene."
Badenas C., Torra R., San Millan J.L., Lucero L., Mila M., Estivill X., Darnell A.
Kidney Int. 55:1225-1233(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 PRO-4225 AND TRP-4276.
[25]"Novel mutations in the duplicated region of PKD1 gene."
Perrichot R., Mercier B., Quere I., Carre A., Simon P., Whebe B., Cledes J., Ferec C.
Eur. J. Hum. Genet. 8:353-359(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 MET-2250; TRP-2329 AND CYS-2379, VARIANTS LEU-3066; VAL-3139 AND LEU-3193.
[26]"Novel mutations in the duplicated region of the polycystic kidney disease 1 (PKD1) gene provides supporting evidence for gene conversion."
Afzal A.R., Florencio R.N., Taylor R., Patton M.A., Saggar-Malik A., Jeffery S.
Genet. Test. 4:365-370(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 HIS-3247 AND MET-3382.
[27]"Screening of the PKD1 duplicated region reveals multiple single nucleotide polymorphisms and a de novo mutation in Hellenic polycystic kidney disease families."
Koptides M., Mean R., Demetriou K., Constantinides R., Pierides A., Harris P.C., Deltas C.C.
Hum. Mutat. 16:176-176(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 PRO-2921 AND MET-3375, VARIANT LEU-3066.
[28]"Novel splicing and missense mutations in autosomal dominant polycystic kidney disease 1 (PKD1) gene: expression of mutated genes."
Aguiari G., Savelli S., Garbo M., Bozza A., Augello G., Penolazzi L., De Paoli Vitali E., La Torre C., Cappelli G., Piva R., del Senno L.
Hum. Mutat. 16:444-445(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 GLN-3719 AND PRO-3852, VARIANT VAL-4045.
[29]"Thirteen novel mutations of the replicated region of PKD1 in an Asian population."
Phakdeekitcharoen B., Watnick T.J., Ahn C., Whang D.-Y., Burkhart B., Germino G.G.
Kidney Int. 58:1400-1412(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 SER-1166; GLU-1956; CYS-2408 AND GLY-2442--2443 INS, VARIANTS HIS-1995 AND ASN-2604.
[30]"Novel mutations of the PKD1 gene in Korean patients with autosomal dominant polycystic kidney disease."
Kim U.K., Jin D.K., Ahn C., Shin J.H., Lee K.B., Kim S.H., Chae J.J., Hwang D.Y., Lee J.G., Namkoong Y., Lee C.C.
Mutat. Res. 432:39-45(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 TRP-3753 AND ASN-3815.
[31]"Mutation analysis of the entire PKD1 gene: genetic and diagnostic implications."
Rossetti S., Strmecki L., Gamble V., Burton S., Sneddon V., Peral B., Roy S., Bakkaloglu A., Komel R., Winearls C.G., Harris P.C.
Am. J. Hum. Genet. 68:46-63(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 GLN-13; PHE-75; CYS-139; 1992-PHE-THR-1993 DELINS LEU; 2220-ARG--PRO-2224 DEL; ASP-2336; ASP-2752; ILE-LEU-MET-ARG-2765 INS; MET-2768; LYS-2771; PRO-2816; SER-2858; 3012-THR--TYR-3017 DEL AND 3748-LEU--ARG-3752 DEL, VARIANTS SER-2674; MET-2708; THR-2734; LEU-2735; CYS-2765; MET-2782; ARG-2814; GLY-2888; ILE-2905; ASP-2966 AND LEU-3066.
[32]"Novel PKD1 deletions and missense variants in a cohort of Hellenic polycystic kidney disease families."
Bouba I., Koptides M., Mean R., Costi C.-E., Demetriou K., Georgiou I., Pierides A., Siamopoulos K., Deltas C.C.
Eur. J. Hum. Genet. 9:677-684(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 LEU-2471; LEU-2519; GLY-2579 DEL; LEU-2613 DEL; ILE-2649 AND PHE-2978 DEL, VARIANTS MET-2582; ARG-2638; ASN-2972 AND LEU-3066.
[33]"Mutation analysis of the entire replicated portion of PKD1 using genomic DNA samples."
Phakdeekitcharoen B., Watnick T.J., Germino G.G.
J. Am. Soc. Nephrol. 12:955-963(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 ARG-967; ARG-2696; GLY-2985; CYS-3039 AND ILE-3285, VARIANTS VAL-88 AND ARG-3311.
[34]"Mutations of the PKD1 gene among Japanese autosomal dominant polycystic kidney disease patients, including one heterozygous mutation identified in members of the same family."
Mizoguchi M., Tamura T., Yamaki A., Higashihara E., Shimizu Y.
J. Hum. Genet. 46:511-517(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 MET-3510, VARIANT MET-3008.
[35]"Mutational analysis within the 3' region of the PKD1 gene in Japanese families."
Tsuchiya K., Komeda M., Takahashi M., Yamashita N., Cigira M., Suzuki T., Suzuki K., Nihei H., Mochizuki T.
Mutat. Res. 458:77-84(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 ARG-3560; GLN-3719 AND TRP-3753, VARIANT MET-3510.
[36]"Three novel mutations of the PKD1 gene in Korean patients with autosomal dominant polycystic kidney disease."
Eo H.-S., Lee J.G., Ahn C., Cho J.T., Hwang D.Y., Hwang Y.H., Lee E.J., Kim Y.S., Han J.S., Kim S., Lee J.S., Jeoung D.I., Lee S.E., Kim U.K.
Clin. Genet. 62:169-174(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 SER-3602 AND SER-4255.
[37]"Mutation detection in the duplicated region of the polycystic kidney disease 1 (PKD1) gene in PKD1-linked Australian families."
McCluskey M., Schiavello T., Hunter M., Hantke J., Angelicheva D., Bogdanova N., Markoff A., Thomas M., Dworniczak B., Horst J., Kalaydjieva L.
Hum. Mutat. 19:240-250(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 CYS-381; ASP-2185; THR-2421 DEL; ASP-2785 AND 3027-THR--ARG-3039 DEL, VARIANTS GLN-739; THR-1092; ARG-1399; MET-1649; ARG-2638; CYS-2765 AND LEU-3066.
[38]"Mutation analysis in PKD1 of Japanese autosomal dominant polycystic kidney disease patients."
Inoue S., Inoue K., Utsunomiya M., Nozaki J., Yamada Y., Iwasa T., Mori E., Yoshinaga T., Koizumi A.
Hum. Mutat. 19:622-628(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 ILE-2083; ARG-2814 AND PRO-2816, VARIANTS MET-87 AND MET-3510.
[39]"Mutation screening of the PKD1 transcript by RT-PCR."
Burtey S., Lossi A.M., Bayle J., Berland Y., Fontes M.
J. Med. Genet. 39:422-429(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PKD1 HIS-987, VARIANTS ARG-1399 AND VAL-4045.
[40]"A complete mutation screen of the ADPKD genes by DHPLC."
Rossetti S., Chauveau D., Walker D., Saggar-Malik A., Winearls C.G., Torres V.E., Harris P.C.
Kidney Int. 61:1588-1599(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 TRP-1340; LYS-1811; CYS-2092; ILE-2260 DEL; PHE-3167 AND PRO-3852, VARIANTS LEU-61; SER-572; THR-1092; SER-1168; ARG-1399; LEU-1684; ILE-1943; ARG-2638; SER-2674; MET-2708; ARG-2814; LEU-2958; ASN-2977; MET-3057; GLN-3435; VAL-3512; VAL-4045; VAL-4059; SER-4124; ILE-4146 AND PHE-4190.
[41]"Novel mutations of PKD1 gene in Chinese patients with autosomal dominant polycystic kidney disease."
Ding L., Zhang S., Qiu W., Xiao C., Wu S., Zhang G., Cheng L., Zhang S.
Nephrol. Dial. Transplant. 17:75-80(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 ASP-3632; LEU-3649 AND THR-3678, VARIANTS VAL-4045; VAL-4059; GLU-4102; PRO-4106 AND ILE-4146.
[42]"Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype."
Rossetti S., Chauveau D., Kubly V., Slezak J.M., Saggar-Malik A.K., Pei Y., Ong A.C.M., Stewart F., Watson M.L., Bergstralh E.J., Winearls C.G., Torres V.E., Harris P.C.
Lancet 361:2196-2201(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 ARG-164; GLY-210; ARG-508; ASP-690; ASN-1240 DEL; PRO-1667; LYS-1811; CYS-2092; CYS-2200; ILE-2260 DEL; ARG-2370; TYR-2373; LYS-2771; LEU-2802; ASN-3188 DEL; LEU-3355; PRO-3682 AND ARG-3751.
[43]"Genetics and phenotypic characteristics of autosomal dominant polycystic kidney disease in Finns."
Peltola P., Lumiaho A., Miettinen R., Pihlajamaeki J., Sandford R., Laakso M.
J. Mol. Med. 83:638-646(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 SER-845; MET-3138 AND PRO-3954, VARIANTS HIS-36; ARG-2638; LEU-3066; MET-3510; VAL-3512; VAL-4045 AND VAL-4059.
[44]"Novel method for genomic analysis of PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease."
Tan Y.-C., Blumenfeld J.D., Anghel R., Donahue S., Belenkaya R., Balina M., Parker T., Levine D., Leonard D.G.B., Rennert H.
Hum. Mutat. 30:264-273(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 LEU-61; ILE-99; TYR-594; THR-1092; MET-1242; CYS-2200; LYS-2422; ARG-2638; LEU-3066; SER-3726 AND VAL-4155, VARIANTS HIS-36; GLN-739; ARG-1399; THR-1516; THR-1871; VAL-1926; ASP-1952; MET-2708; ARG-2814; VAL-3512; VAL-4045 AND VAL-4059.
[45]"Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease (ADPKD)."
Hoefele J., Mayer K., Scholz M., Klein H.G.
Nephrol. Dial. Transplant. 26:2181-2188(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 GLY-97; ARG-436; PRO-442; ARG-727; PRO-727; ASP-2391; TRP-2434; TYR-2546; CYS-2569; THR-2646; ARG-2889; PRO-3154; ARG-3603 AND GLN-3750.
[46]"Autosomal dominant polycystic kidney disease: Comprehensive mutation analysis of PKD1 and PKD2 in 700 unrelated patients."
Audrezet M.P., Gall E.C., Chen J.M., Redon S., Quere I., Creff J., Benech C., Maestri S., Meur Y.L., Ferec C.
Hum. Mutat. 33:1239-1250(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PKD1 CYS-325; TRP-611; ASP-698; PRO-727; GLY-1206; CYS-2379; CYS-2767; LYS-2771; ARG-2995; SER-3651; GLN-3750; TRP-3753; CYS-4150 AND TRP-4276.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24497 mRNA. Translation: AAC50128.1.
L33243 mRNA. Translation: AAC37576.1.
L43619 expand/collapse EMBL AC list , L43601, L43602, L43604, L43605, L43610, L43617, L43618 Genomic DNA. Translation: AAC41765.1.
AC093513 Genomic DNA. No translation available.
AC009065 Genomic DNA. No translation available.
PIRA38971.
RefSeqNP_000287.3. NM_000296.3.
NP_001009944.2. NM_001009944.2.
UniGeneHs.75813.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4RNMR-A275-354[»]
ProteinModelPortalP98161.
SMRP98161. Positions 275-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111327. 18 interactions.
DIPDIP-52317N.
IntActP98161. 7 interactions.
MINTMINT-1199187.
STRING9606.ENSP00000262304.

Chemistry

BindingDBP98161.
ChEMBLCHEMBL5772.

Protein family/group databases

MEROPST06.001.
TCDB1.A.5.1.1. the polycystin cation channel (pcc) family.

PTM databases

PhosphoSiteP98161.

Polymorphism databases

DMDM292495072.

Proteomic databases

PaxDbP98161.
PRIDEP98161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262304; ENSP00000262304; ENSG00000008710. [P98161-1]
ENST00000423118; ENSP00000399501; ENSG00000008710. [P98161-3]
GeneID5310.
KEGGhsa:5310.
UCSCuc002cos.1. human. [P98161-1]
uc002cot.1. human. [P98161-3]

Organism-specific databases

CTD5310.
GeneCardsGC16M002138.
H-InvDBHIX0173395.
HIX0202314.
HGNCHGNC:9008. PKD1.
HPACAB046448.
MIM173900. phenotype.
601313. gene+phenotype.
neXtProtNX_P98161.
Orphanet730. Autosomal dominant polycystic kidney disease.
88924. Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis.
PharmGKBPA35521.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3291.
HOGENOMHOG000168445.
HOVERGENHBG049412.
InParanoidP98161.
KOK04985.
OMAGQCNTDL.
OrthoDBEOG76X5Z6.
PhylomeDBP98161.
TreeFamTF316484.

Enzyme and pathway databases

SignaLinkP98161.

Gene expression databases

ArrayExpressP98161.
BgeeP98161.
CleanExHS_PKD1.
GenevestigatorP98161.

Family and domain databases

Gene3D2.60.40.670. 14 hits.
2.60.60.20. 1 hit.
3.10.100.10. 2 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR000483. Cys-rich_flank_reg_C.
IPR000203. GPS.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR008976. Lipase_LipOase.
IPR000372. LRR-contain_N.
IPR022409. PKD/Chitinase_dom.
IPR002859. PKD/REJ-like.
IPR013122. PKD1_2_channel.
IPR000434. PKD_1.
IPR000601. PKD_dom.
IPR001024. PLAT/LH2_dom.
IPR006228. Polycystin_cat.
IPR014010. REJ-like.
IPR002889. WSC_carb-bd.
IPR013994. WSC_carb-bd_subgr.
[Graphical view]
PfamPF01825. GPS. 1 hit.
PF00059. Lectin_C. 1 hit.
PF01462. LRRNT. 1 hit.
PF00801. PKD. 15 hits.
PF08016. PKD_channel. 1 hit.
PF01477. PLAT. 1 hit.
PF02010. REJ. 1 hit.
PF01822. WSC. 1 hit.
[Graphical view]
PRINTSPR00500. POLYCYSTIN1.
SMARTSM00034. CLECT. 1 hit.
SM00303. GPS. 1 hit.
SM00308. LH2. 1 hit.
SM00369. LRR_TYP. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00089. PKD. 15 hits.
SM00321. WSC. 1 hit.
[Graphical view]
SUPFAMSSF49299. SSF49299. 13 hits.
SSF49723. SSF49723. 1 hit.
SSF56436. SSF56436. 1 hit.
TIGRFAMsTIGR00864. PCC. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
PS50221. GPS. 1 hit.
PS51450. LRR. 2 hits.
PS50093. PKD. 12 hits.
PS50095. PLAT. 1 hit.
PS51111. REJ. 1 hit.
PS51212. WSC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP98161.
GeneWikiPKD1.
GenomeRNAi5310.
NextBio20530.
PROP98161.
SOURCESearch...

Entry information

Entry namePKD1_HUMAN
AccessionPrimary (citable) accession number: P98161
Secondary accession number(s): Q15140, Q15141
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 178 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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