Q9Y283 (INVS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inversin

Alternative name(s):
Inversion of embryo turning homolog
Nephrocystin-2

Gene names

Name:	INVS
Synonyms:	INV, NPHP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1065 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8
Subunit structure	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 NPHP3. Interacts with IQCB1; the interaction likely requires additional interactors. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Cell projection › cilium. 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. Ref.6
Tissue specificity	Widely expressed. Strongly expressed in the primary cilia of renal tubular cells. Ref.1 Ref.6
Domain	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.
Post-translational modification	May be ubiquitinated via its interaction with APC2 By similarity.
Involvement in disease	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. Ref.6
Sequence similarities	Contains 16 ANK repeats. Contains 2 IQ domains.
Sequence caution	The sequence AAD02131.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH41665.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Membrane Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Disease	Ciliopathy Disease mutation Nephronophthisis
Domain	ANK repeat Repeat
Ligand	Calmodulin-binding
Molecular function	Developmental protein
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW embryonic heart tube left/right pattern formation Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara negative regulation of canonical Wnt receptor signaling pathway Inferred from direct assay Ref.8. Source: UniProtKB pancreas development Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara
Cellular_component	cilium Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y283-1)

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: Q9Y283-2)

Also known as: S2;

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

Isoform 3 (identifier: Q9Y283-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1065	1065	Inversin		PRO_0000067016
Regions
	Repeat	13 – 42	30	ANK 1
	Repeat	47 – 76	30	ANK 2
	Repeat	80 – 110	31	ANK 3
	Repeat	113 – 144	32	ANK 4
	Repeat	148 – 177	30	ANK 5
	Repeat	181 – 213	33	ANK 6
	Repeat	220 – 250	31	ANK 7
	Repeat	254 – 283	30	ANK 8
	Repeat	288 – 317	30	ANK 9
	Repeat	321 – 350	30	ANK 10
	Repeat	356 – 385	30	ANK 11
	Repeat	389 – 418	30	ANK 12
	Repeat	422 – 451	30	ANK 13
	Repeat	455 – 484	30	ANK 14
	Repeat	488 – 517	30	ANK 15
	Repeat	523 – 553	31	ANK 16
	Domain	555 – 584	30	IQ 1
	Domain	916 – 945	30	IQ 2
	Motif	490 – 498	9	D-box 1
	Motif	909 – 917	9	D-box 2
Natural variations
	Alternative sequence	92 – 101	10	GNYRFMKLLL → ALRTISTGRI in isoform 3.		VSP_014495
	Alternative sequence	102 – 1065	964	Missing in isoform 3.		VSP_014496
	Alternative sequence	727 – 896	170	Missing in isoform 2.		VSP_014497
	Natural variant	242	1	S → L. Corresponds to variant rs2491097 [ dbSNP | Ensembl ].		VAR_044119
	Natural variant	482	1	P → R in NPHP2. Ref.6		VAR_022822
	Natural variant	493	1	L → S in NPHP2; impairs ability to target DVL1 for degradation. Ref.6		VAR_022823
	Natural variant	888	1	S → R. Corresponds to variant rs1052867 [ dbSNP | Ensembl ].		VAR_044120
Experimental info
	Sequence conflict	764	1	A → G in AAC79436. Ref.2
	Sequence conflict	764	1	A → G in AAC79456. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: DACDF33C1B8573AC	FASTA	1,065	117,826
	10 20 30 40 50 60 MNKSENLLFA GSSLASQVHA AAVNGDKGAL QRLIVGNSAL KDKEDQFGRT PLMYCVLADR 70 80 90 100 110 120 LDCADALLKA GADVNKTDHS QRTALHLAAQ KGNYRFMKLL LTRRANWMQK DLEEMTPLHL 130 140 150 160 170 180 TTRHRSPKCL ALLLKFMAPG EVDTQDKNKQ TALHWSAYYN NPEHVKLLIK HDSNIGIPDV 190 200 210 220 230 240 EGKIPLHWAA NHKDPSAVHT VRCILDAAPT ESLLNWQDYE GRTPLHFAVA DGNVTVVDVL 250 260 270 280 290 300 TSYESCNITS YDNLFRTPLH WAALLGHAQI VHLLLERNKS GTIPSDSQGA TPLHYAAQSN 310 320 330 340 350 360 FAETVKVFLK HPSVKDDSDL EGRTSFMWAA GKGSDDVLRT MLSLKSDIDI NMADKYGGTA 370 380 390 400 410 420 LHAAALSGHV STVKLLLENN AQVDATDVMK HTPLFRACEM GHKDVIQTLI KGGARVDLVD 430 440 450 460 470 480 QDGHSLLHWA ALGGNADVCQ ILIENKINPN VQDYAGRTPL QCAAYGGYIN CMAVLMENNA 490 500 510 520 530 540 DPNIQDKEGR TALHWSCNNG YLDAIKLLLD FAAFPNQMEN NEERYTPLDY ALLGERHEVI 550 560 570 580 590 600 QFMLEHGALS IAAIQDIAAF KIQAVYKGYK VRKAFRDRKN LLMKHEQLRK DAAAKKREEE 610 620 630 640 650 660 NKRKEAEQQK GRRSPDSCRP QALPCLPSTQ DVPSRQSRAP SKQPPAGNVA QGPEPRDSRG 670 680 690 700 710 720 SPGGSLGGAL QKEQHVSSDL QGTNSRRPNE TAREHSKGQS ACVHFRPNEG SDGSRHPGVP 730 740 750 760 770 780 SVEKSRGETA GDERCAKGKG FVKQPSCIRV AGPDEKGEDS RRAAASLPPH DSHWKPSRRH 790 800 810 820 830 840 DTEPKAKCAP QKRRTQELRG GRCSPAGSSR PGSARGEAVH AGQNPPHHRT PRNKVTQAKL 850 860 870 880 890 900 TGGLYSHLPQ STEELRSGAR RLETSTLSED FQVSKETDPA PGPLSGQSVN IDLLPVELRL 910 920 930 940 950 960 QIIQRERRRK ELFRKKNKAA AVIQRAWRSY QLRKHLSHLR HMKQLGAGDV DRWRQESTAL 970 980 990 1000 1010 1020 LLQVWRKELE LKFPQTTAVS KAPKSPSKGT SGTKSTKHSV LKQIYGCSHE GKIHHPTRSV 1030 1040 1050 1060 KASSVLRLNS VSNLQCIHLL ENSGRSKNFS YNLQSATQPK NKTKP
	Isoform 2 (S2) [UniParc]. Checksum: 4604C8A1C03E40C6	FASTA	895	99,564
	10 20 30 40 50 60 MNKSENLLFA GSSLASQVHA AAVNGDKGAL QRLIVGNSAL KDKEDQFGRT PLMYCVLADR 70 80 90 100 110 120 LDCADALLKA GADVNKTDHS QRTALHLAAQ KGNYRFMKLL LTRRANWMQK DLEEMTPLHL 130 140 150 160 170 180 TTRHRSPKCL ALLLKFMAPG EVDTQDKNKQ TALHWSAYYN NPEHVKLLIK HDSNIGIPDV 190 200 210 220 230 240 EGKIPLHWAA NHKDPSAVHT VRCILDAAPT ESLLNWQDYE GRTPLHFAVA DGNVTVVDVL 250 260 270 280 290 300 TSYESCNITS YDNLFRTPLH WAALLGHAQI VHLLLERNKS GTIPSDSQGA TPLHYAAQSN 310 320 330 340 350 360 FAETVKVFLK HPSVKDDSDL EGRTSFMWAA GKGSDDVLRT MLSLKSDIDI NMADKYGGTA 370 380 390 400 410 420 LHAAALSGHV STVKLLLENN AQVDATDVMK HTPLFRACEM GHKDVIQTLI KGGARVDLVD 430 440 450 460 470 480 QDGHSLLHWA ALGGNADVCQ ILIENKINPN VQDYAGRTPL QCAAYGGYIN CMAVLMENNA 490 500 510 520 530 540 DPNIQDKEGR TALHWSCNNG YLDAIKLLLD FAAFPNQMEN NEERYTPLDY ALLGERHEVI 550 560 570 580 590 600 QFMLEHGALS IAAIQDIAAF KIQAVYKGYK VRKAFRDRKN LLMKHEQLRK DAAAKKREEE 610 620 630 640 650 660 NKRKEAEQQK GRRSPDSCRP QALPCLPSTQ DVPSRQSRAP SKQPPAGNVA QGPEPRDSRG 670 680 690 700 710 720 SPGGSLGGAL QKEQHVSSDL QGTNSRRPNE TAREHSKGQS ACVHFRPNEG SDGSRHPGVP 730 740 750 760 770 780 SVEKSRELRL QIIQRERRRK ELFRKKNKAA AVIQRAWRSY QLRKHLSHLR HMKQLGAGDV 790 800 810 820 830 840 DRWRQESTAL LLQVWRKELE LKFPQTTAVS KAPKSPSKGT SGTKSTKHSV LKQIYGCSHE 850 860 870 880 890 GKIHHPTRSV KASSVLRLNS VSNLQCIHLL ENSGRSKNFS YNLQSATQPK NKTKP
	Isoform 3 [UniParc]. Checksum: C98F2838A19DFD5D	FASTA	101	10,748
	10 20 30 40 50 60 MNKSENLLFA GSSLASQVHA AAVNGDKGAL QRLIVGNSAL KDKEDQFGRT PLMYCVLADR 70 80 90 100 LDCADALLKA GADVNKTDHS QRTALHLAAQ KALRTISTGR I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-600 (ISOFORM 1). 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]	"Loss of nephrocystin-3 function can cause embryonic lethality, Meckel-Gruber-like syndrome, situs inversus, and renal-hepatic-pancreatic dysplasia." Bergmann C., Fliegauf M., Bruechle N.O., Frank V., Olbrich H., Kirschner J., Schermer B., Schmedding I., Kispert A., Kraenzlin B., Nuernberg G., Becker C., Grimm T., Girschick G., Lynch S.A., Kelehan P., Senderek J., Neuhaus T.J. , Stallmach T., Zentgraf H., Nuernberg P., Gretz N., Lo C., Lienkamp S., Schaefer T., Walz G., Benzing T., Zerres K., Omran H. Am. J. Hum. Genet. 82:959-970(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NPHP3.
[9]	"Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways." Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., O'Toole J.F. , Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K. Cell 145:513-528(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NPHP1 AND IQCB1.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00017764. IPI00034309. IPI00478910.
RefSeq	NP_055240.2. NM_014425.3. NP_899068.1. NM_183245.2.
UniGene	Hs.558477.
3D structure databases
ProteinModelPortal	Q9Y283.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y283. 2 interactions.
MINT	MINT-1196568.
STRING	9606.ENSP00000262457.
PTM databases
PhosphoSite	Q9Y283.
Polymorphism databases
DMDM	68565551.
Proteomic databases
PaxDb	Q9Y283.
PRIDE	Q9Y283.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262456; ENSP00000262456; ENSG00000119509. ENST00000262457; ENSP00000262457; ENSG00000119509. ENST00000374921; ENSP00000364056; ENSG00000119509.
GeneID	27130.
KEGG	hsa:27130.
UCSC	uc004bao.1. human. uc004bap.1. human.
Organism-specific databases
CTD	27130.
GeneCards	GC09P102861.
HGNC	HGNC:17870. INVS.
MIM	243305. gene. 602088. phenotype.
neXtProt	NX_Q9Y283.
Orphanet	93591. Infantile autosomal recessive medullary cystic kidney disease. 3156. Senior-Loken syndrome.
PharmGKB	PA38472.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0666.
HOVERGEN	HBG083788.
InParanoid	Q9Y283.
OMA	NLQCIHL.
OrthoDB	EOG4R5028.
PhylomeDB	Q9Y283.
Enzyme and pathway databases
SignaLink	Q9Y283.
Gene expression databases
ArrayExpress	Q9Y283.
Bgee	Q9Y283.
CleanEx	HS_INVS.
Genevestigator	Q9Y283.
GermOnline	ENSG00000119509. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 5 hits.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000048. IQ_motif_EF-hand-BS. [Graphical view]
Pfam	PF12796. Ank_2. 6 hits. PF00612. IQ. 2 hits. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 15 hits. SM00015. IQ. 2 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 2 hits.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 11 hits. PS50096. IQ. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	INVS. human.
GenomeRNAi	27130.
NextBio	49848.
SOURCE	Search...

Entry information

Entry name

INVS_HUMAN

Accession

Primary (citable) accession number: Q9Y283
Secondary accession number(s): A2A2Y2 , Q5W0T6, Q8IVX8, Q9BRB9, Q9Y488, Q9Y498

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.