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Q9Y283

- INVS_HUMAN

UniProt

Q9Y283 - INVS_HUMAN

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Protein
Inversin
Gene
INVS, INV, NPHP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling. Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8 By similarity. Does not seem to be strictly required for ciliogenesis By similarity.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. embryonic heart tube left/right pattern formation Source: Ensembl
  3. kidney development Source: Ensembl
  4. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  5. pancreas development Source: Ensembl
  6. post-embryonic development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

SignaLinkiQ9Y283.

Names & Taxonomyi

Protein namesi
Recommended name:
Inversin
Alternative name(s):
Inversion of embryo turning homolog
Nephrocystin-2
Gene namesi
Name:INVS
Synonyms:INV, NPHP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17870. INVS.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonspindle By similarity. Membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Cell projectioncilium
Note: Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle. Frequently membrane-associated, membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium.1 Publication

GO - Cellular componenti

  1. cilium Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. membrane Source: UniProtKB-SubCell
  4. microtubule Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-SubCell
  6. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nephronophthisis 2 (NPHP2) [MIM:602088]: An autosomal recessive disorder resulting in end-stage renal disease. It is characterized by early onset and rapid progression. Phenotypic manifestations include enlarged kidneys, chronic tubulo-interstitial nephritis, anemia, hyperkalemic metabolic acidosis. Some patients also display situs inversus. Pathologically, it differs from later-onset nephronophthisis by the absence of medullary cysts and thickened tubular basement membranes, and by the presence of cortical microcysts.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti482 – 4821P → R in NPHP2. 1 Publication
VAR_022822
Natural varianti493 – 4931L → S in NPHP2; impairs ability to target DVL1 for degradation. 1 Publication
VAR_022823

Keywords - Diseasei

Ciliopathy, Disease mutation, Nephronophthisis

Organism-specific databases

MIMi602088. phenotype.
Orphaneti93591. Infantile autosomal recessive medullary cystic kidney disease.
3156. Senior-Loken syndrome.
PharmGKBiPA38472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10651065Inversin
PRO_0000067016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 7513-hydroxyasparagine1 Publication

Post-translational modificationi

May be ubiquitinated via its interaction with APC2 By similarity.
Hydroxylated at Asn-75, most probably by HIF1AN.

Keywords - PTMi

Hydroxylation, Ubl conjugation

Proteomic databases

MaxQBiQ9Y283.
PaxDbiQ9Y283.
PRIDEiQ9Y283.

PTM databases

PhosphoSiteiQ9Y283.

Expressioni

Tissue specificityi

Widely expressed. Strongly expressed in the primary cilia of renal tubular cells.2 Publications

Gene expression databases

ArrayExpressiQ9Y283.
BgeeiQ9Y283.
CleanExiHS_INVS.
GenevestigatoriQ9Y283.

Organism-specific databases

HPAiHPA049994.

Interactioni

Subunit structurei

Binds calmodulin via its IQ domains. Interacts with APC2. Interacts with alpha-, beta-, and gamma-catenin. Interacts with N-cadherin (CDH2). Interacts with microtubules By similarity. Interacts with NPHP1. Interacts with DVL1, PRICKLE (PRICKLE1 or PRICKLE2) and Strabismus (VANGL1 or VANGL2). Interacts with IQCB1; the interaction likely requires additional interactors. Component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B9D2Q9BPU94EBI-751472,EBI-6958971

Protein-protein interaction databases

BioGridi118021. 7 interactions.
IntActiQ9Y283. 6 interactions.
MINTiMINT-1196568.
STRINGi9606.ENSP00000262457.

Structurei

3D structure databases

ProteinModelPortaliQ9Y283.
SMRiQ9Y283. Positions 12-573.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 4230ANK 1
Add
BLAST
Repeati47 – 7630ANK 2
Add
BLAST
Repeati80 – 11031ANK 3
Add
BLAST
Repeati113 – 14432ANK 4
Add
BLAST
Repeati148 – 17730ANK 5
Add
BLAST
Repeati181 – 21333ANK 6
Add
BLAST
Repeati220 – 25031ANK 7
Add
BLAST
Repeati254 – 28330ANK 8
Add
BLAST
Repeati288 – 31730ANK 9
Add
BLAST
Repeati321 – 35030ANK 10
Add
BLAST
Repeati356 – 38530ANK 11
Add
BLAST
Repeati389 – 41830ANK 12
Add
BLAST
Repeati422 – 45130ANK 13
Add
BLAST
Repeati455 – 48430ANK 14
Add
BLAST
Repeati488 – 51730ANK 15
Add
BLAST
Repeati523 – 55331ANK 16
Add
BLAST
Domaini555 – 58430IQ 1
Add
BLAST
Domaini916 – 94530IQ 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 4989D-box 1
Motifi909 – 9179D-box 2

Domaini

The D-box 1 (destruction box 1) mediates the interaction with APC2, and may act as a recognition signal for degradation via the ubiquitin-proteasome pathway By similarity.

Sequence similaritiesi

Contains 16 ANK repeats.
Contains 2 IQ domains.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOVERGENiHBG083788.
InParanoidiQ9Y283.
OMAiNLQCIHL.
OrthoDBiEOG7P02H2.
PhylomeDBiQ9Y283.
TreeFamiTF312824.

Family and domain databases

Gene3Di1.25.40.20. 5 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 6 hits.
PF00612. IQ. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 15 hits.
SM00015. IQ. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 11 hits.
PS50096. IQ. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y283-1) [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

MNKSENLLFA GSSLASQVHA AAVNGDKGAL QRLIVGNSAL KDKEDQFGRT     50
PLMYCVLADR LDCADALLKA GADVNKTDHS QRTALHLAAQ KGNYRFMKLL 100
LTRRANWMQK DLEEMTPLHL TTRHRSPKCL ALLLKFMAPG EVDTQDKNKQ 150
TALHWSAYYN NPEHVKLLIK HDSNIGIPDV EGKIPLHWAA NHKDPSAVHT 200
VRCILDAAPT ESLLNWQDYE GRTPLHFAVA DGNVTVVDVL TSYESCNITS 250
YDNLFRTPLH WAALLGHAQI VHLLLERNKS GTIPSDSQGA TPLHYAAQSN 300
FAETVKVFLK HPSVKDDSDL EGRTSFMWAA GKGSDDVLRT MLSLKSDIDI 350
NMADKYGGTA LHAAALSGHV STVKLLLENN AQVDATDVMK HTPLFRACEM 400
GHKDVIQTLI KGGARVDLVD QDGHSLLHWA ALGGNADVCQ ILIENKINPN 450
VQDYAGRTPL QCAAYGGYIN CMAVLMENNA DPNIQDKEGR TALHWSCNNG 500
YLDAIKLLLD FAAFPNQMEN NEERYTPLDY ALLGERHEVI QFMLEHGALS 550
IAAIQDIAAF KIQAVYKGYK VRKAFRDRKN LLMKHEQLRK DAAAKKREEE 600
NKRKEAEQQK GRRSPDSCRP QALPCLPSTQ DVPSRQSRAP SKQPPAGNVA 650
QGPEPRDSRG SPGGSLGGAL QKEQHVSSDL QGTNSRRPNE TAREHSKGQS 700
ACVHFRPNEG SDGSRHPGVP SVEKSRGETA GDERCAKGKG FVKQPSCIRV 750
AGPDEKGEDS RRAAASLPPH DSHWKPSRRH DTEPKAKCAP QKRRTQELRG 800
GRCSPAGSSR PGSARGEAVH AGQNPPHHRT PRNKVTQAKL TGGLYSHLPQ 850
STEELRSGAR RLETSTLSED FQVSKETDPA PGPLSGQSVN IDLLPVELRL 900
QIIQRERRRK ELFRKKNKAA AVIQRAWRSY QLRKHLSHLR HMKQLGAGDV 950
DRWRQESTAL LLQVWRKELE LKFPQTTAVS KAPKSPSKGT SGTKSTKHSV 1000
LKQIYGCSHE GKIHHPTRSV KASSVLRLNS VSNLQCIHLL ENSGRSKNFS 1050
YNLQSATQPK NKTKP 1065
Length:1,065
Mass (Da):117,826
Last modified:July 5, 2005 - v2
Checksum:iDACDF33C1B8573AC
GO
Isoform 2 (identifier: Q9Y283-2) [UniParc]FASTAAdd to Basket

Also known as: S2

The sequence of this isoform differs from the canonical sequence as follows:
     727-896: Missing.

Show »
Length:895
Mass (Da):99,564
Checksum:i4604C8A1C03E40C6
GO
Isoform 3 (identifier: Q9Y283-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     92-101: GNYRFMKLLL → ALRTISTGRI
     102-1065: Missing.

Note: No experimental confirmation available.

Show »
Length:101
Mass (Da):10,748
Checksum:iC98F2838A19DFD5D
GO

Sequence cautioni

The sequence AAH41665.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAD02131.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti242 – 2421S → L.
Corresponds to variant rs2491097 [ dbSNP | Ensembl ].
VAR_044119
Natural varianti482 – 4821P → R in NPHP2. 1 Publication
VAR_022822
Natural varianti493 – 4931L → S in NPHP2; impairs ability to target DVL1 for degradation. 1 Publication
VAR_022823
Natural varianti888 – 8881S → R.
Corresponds to variant rs1052867 [ dbSNP | Ensembl ].
VAR_044120

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei92 – 10110GNYRFMKLLL → ALRTISTGRI in isoform 3.
VSP_014495
Alternative sequencei102 – 1065964Missing in isoform 3.
VSP_014496Add
BLAST
Alternative sequencei727 – 896170Missing in isoform 2.
VSP_014497Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti487 – 4871K → Q in AAI11762. 1 Publication
Sequence conflicti764 – 7641A → G in AAC79436. 1 Publication
Sequence conflicti764 – 7641A → G in AAC79456. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039217 mRNA. Translation: AAD02131.2. Different initiation.
AF084367 mRNA. Translation: AAC79436.1.
AF084382
, AF084373, AF084374, AF084375, AF084377, AF084379, AF084381, AF084371, AF084369, AF084368, AF084370, AF084372, AF084380, AF084378, AF084376 Genomic DNA. Translation: AAC79456.1.
AF084382
, AF084368, AF084369, AF084370, AF084371, AF084372, AF084373, AF084374, AF084375, AF084376, AF084377, AF084378, AF084379, AF084380, AF084381 Genomic DNA. Translation: AAC79457.1.
AL137072, AL356798, AL445214 Genomic DNA. Translation: CAH72173.1.
AL137072 Genomic DNA. Translation: CAH72174.1.
AL445214, AL137072, AL356798 Genomic DNA. Translation: CAI39744.1.
AL445214, AL137072, AL356798 Genomic DNA. Translation: CAI39745.2.
AL356798, AL137072, AL445214 Genomic DNA. Translation: CAI40807.1.
AL356798, AL137072, AL445214 Genomic DNA. Translation: CAI40808.2.
AL137072, AL356798, AL445214 Genomic DNA. Translation: CAM16212.1.
CH471105 Genomic DNA. Translation: EAW58926.1.
BC006370 mRNA. Translation: AAH06370.1.
BC041665 mRNA. Translation: AAH41665.1. Sequence problems.
BC111761 mRNA. Translation: AAI11762.1.
CCDSiCCDS6746.1. [Q9Y283-1]
CCDS6747.1. [Q9Y283-2]
RefSeqiNP_055240.2. NM_014425.3. [Q9Y283-1]
NP_899068.1. NM_183245.2. [Q9Y283-2]
UniGeneiHs.558477.

Genome annotation databases

EnsembliENST00000262456; ENSP00000262456; ENSG00000119509. [Q9Y283-2]
ENST00000262457; ENSP00000262457; ENSG00000119509. [Q9Y283-1]
ENST00000374921; ENSP00000364056; ENSG00000119509. [Q9Y283-3]
GeneIDi27130.
KEGGihsa:27130.
UCSCiuc004bao.2. human. [Q9Y283-2]
uc004bap.2. human. [Q9Y283-1]

Polymorphism databases

DMDMi68565551.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039217 mRNA. Translation: AAD02131.2 . Different initiation.
AF084367 mRNA. Translation: AAC79436.1 .
AF084382
, AF084373 , AF084374 , AF084375 , AF084377 , AF084379 , AF084381 , AF084371 , AF084369 , AF084368 , AF084370 , AF084372 , AF084380 , AF084378 , AF084376 Genomic DNA. Translation: AAC79456.1 .
AF084382
, AF084368 , AF084369 , AF084370 , AF084371 , AF084372 , AF084373 , AF084374 , AF084375 , AF084376 , AF084377 , AF084378 , AF084379 , AF084380 , AF084381 Genomic DNA. Translation: AAC79457.1 .
AL137072 , AL356798 , AL445214 Genomic DNA. Translation: CAH72173.1 .
AL137072 Genomic DNA. Translation: CAH72174.1 .
AL445214 , AL137072 , AL356798 Genomic DNA. Translation: CAI39744.1 .
AL445214 , AL137072 , AL356798 Genomic DNA. Translation: CAI39745.2 .
AL356798 , AL137072 , AL445214 Genomic DNA. Translation: CAI40807.1 .
AL356798 , AL137072 , AL445214 Genomic DNA. Translation: CAI40808.2 .
AL137072 , AL356798 , AL445214 Genomic DNA. Translation: CAM16212.1 .
CH471105 Genomic DNA. Translation: EAW58926.1 .
BC006370 mRNA. Translation: AAH06370.1 .
BC041665 mRNA. Translation: AAH41665.1 . Sequence problems.
BC111761 mRNA. Translation: AAI11762.1 .
CCDSi CCDS6746.1. [Q9Y283-1 ]
CCDS6747.1. [Q9Y283-2 ]
RefSeqi NP_055240.2. NM_014425.3. [Q9Y283-1 ]
NP_899068.1. NM_183245.2. [Q9Y283-2 ]
UniGenei Hs.558477.

3D structure databases

ProteinModelPortali Q9Y283.
SMRi Q9Y283. Positions 12-573.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118021. 7 interactions.
IntActi Q9Y283. 6 interactions.
MINTi MINT-1196568.
STRINGi 9606.ENSP00000262457.

PTM databases

PhosphoSitei Q9Y283.

Polymorphism databases

DMDMi 68565551.

Proteomic databases

MaxQBi Q9Y283.
PaxDbi Q9Y283.
PRIDEi Q9Y283.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262456 ; ENSP00000262456 ; ENSG00000119509 . [Q9Y283-2 ]
ENST00000262457 ; ENSP00000262457 ; ENSG00000119509 . [Q9Y283-1 ]
ENST00000374921 ; ENSP00000364056 ; ENSG00000119509 . [Q9Y283-3 ]
GeneIDi 27130.
KEGGi hsa:27130.
UCSCi uc004bao.2. human. [Q9Y283-2 ]
uc004bap.2. human. [Q9Y283-1 ]

Organism-specific databases

CTDi 27130.
GeneCardsi GC09P102861.
HGNCi HGNC:17870. INVS.
HPAi HPA049994.
MIMi 243305. gene.
602088. phenotype.
neXtProti NX_Q9Y283.
Orphaneti 93591. Infantile autosomal recessive medullary cystic kidney disease.
3156. Senior-Loken syndrome.
PharmGKBi PA38472.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOVERGENi HBG083788.
InParanoidi Q9Y283.
OMAi NLQCIHL.
OrthoDBi EOG7P02H2.
PhylomeDBi Q9Y283.
TreeFami TF312824.

Enzyme and pathway databases

SignaLinki Q9Y283.

Miscellaneous databases

ChiTaRSi INVS. human.
GeneWikii INVS.
GenomeRNAii 27130.
NextBioi 49848.
PROi Q9Y283.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y283.
Bgeei Q9Y283.
CleanExi HS_INVS.
Genevestigatori Q9Y283.

Family and domain databases

Gene3Di 1.25.40.20. 5 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000048. IQ_motif_EF-hand-BS.
[Graphical view ]
Pfami PF00023. Ank. 1 hit.
PF12796. Ank_2. 6 hits.
PF00612. IQ. 2 hits.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 15 hits.
SM00015. IQ. 2 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 2 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 11 hits.
PS50096. IQ. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, genomic organization, chromosomal mapping and mutation analysis of the human INV gene, the ortholog of a murine gene implicated in left-right axis development and biliary atresia."
    Schoen P., Tsuchiya K., Lenoir D., Mochizuki T., Guichard C., Takai S., Maiti A.K., Nihei H., Weil J., Yokoyama T., Bouvagnet P.
    Hum. Genet. 110:157-165(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "The left-right determinant inversin has highly conserved ankyrin repeat and IQ domains and interacts with calmodulin."
    Morgan D., Goodship J., Essner J.J., Vogan K.J., Turnpenny L., Yost H.J., Tabin C.J., Strachan T.
    Hum. Genet. 110:377-384(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 3).
    Tissue: Lymph and Muscle.
  6. "Mutations in INVS encoding inversin cause nephronophthisis type 2, linking renal cystic disease to the function of primary cilia and left-right axis determination."
    Otto E.A., Schermer B., Obara T., O'Toole J.F., Hiller K.S., Mueller A.M., Ruf R.G., Hoefele J., Beekmann F., Landau D., Foreman J.W., Goodship J.A., Strachan T., Kispert A., Wolf M.T., Gagnadoux M.F., Nivet H., Antignac C.
    , Walz G., Drummond I.A., Benzing T., Hildebrandt F.
    Nat. Genet. 34:413-420(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NPHP1, VARIANTS NPHP2 ARG-482 AND SER-493.
  7. "Inversin, the gene product mutated in nephronophthisis type II, functions as a molecular switch between Wnt signaling pathways."
    Simons M., Gloy J., Ganner A., Bullerkotte A., Bashkurov M., Kroenig C., Schermer B., Benzing T., Cabello O.A., Jenny A., Mlodzik M., Polok B., Driever W., Obara T., Walz G.
    Nat. Genet. 37:537-543(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DVL1; PRICKLE AND VANGL.
  8. Cited for: FUNCTION, INTERACTION WITH NPHP3.
  9. Cited for: INTERACTION WITH NPHP1 AND IQCB1.
  10. Cited for: INTERACTION WITH ANKS6; NEK8 AND NPHP3, HYDROXYLATION AT ASN-75.

Entry informationi

Entry nameiINVS_HUMAN
AccessioniPrimary (citable) accession number: Q9Y283
Secondary accession number(s): A2A2Y2
, Q2NKL0, Q5W0T6, Q8IVX8, Q9BRB9, Q9Y488, Q9Y498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

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