Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y283 (INVS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

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

Names and origin

Protein namesRecommended name:
Inversin
Alternative name(s):
Inversion of embryo turning homolog
Nephrocystin-2
Gene names
Name:INVS
Synonyms:INV, NPHP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1065 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

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. 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.

Hydroxylated at Asn-75, most probably by HIF1AN.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

B9D2Q9BPU94EBI-751472,EBI-6958971

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10651065Inversin
PRO_0000067016

Regions

Repeat13 – 4230ANK 1
Repeat47 – 7630ANK 2
Repeat80 – 11031ANK 3
Repeat113 – 14432ANK 4
Repeat148 – 17730ANK 5
Repeat181 – 21333ANK 6
Repeat220 – 25031ANK 7
Repeat254 – 28330ANK 8
Repeat288 – 31730ANK 9
Repeat321 – 35030ANK 10
Repeat356 – 38530ANK 11
Repeat389 – 41830ANK 12
Repeat422 – 45130ANK 13
Repeat455 – 48430ANK 14
Repeat488 – 51730ANK 15
Repeat523 – 55331ANK 16
Domain555 – 58430IQ 1
Domain916 – 94530IQ 2
Motif490 – 4989D-box 1
Motif909 – 9179D-box 2

Amino acid modifications

Modified residue7513-hydroxyasparagine Ref.10

Natural variations

Alternative sequence92 – 10110GNYRFMKLLL → ALRTISTGRI in isoform 3.
VSP_014495
Alternative sequence102 – 1065964Missing in isoform 3.
VSP_014496
Alternative sequence727 – 896170Missing in isoform 2.
VSP_014497
Natural variant2421S → L.
Corresponds to variant rs2491097 [ dbSNP | Ensembl ].
VAR_044119
Natural variant4821P → R in NPHP2. Ref.6
VAR_022822
Natural variant4931L → S in NPHP2; impairs ability to target DVL1 for degradation. Ref.6
VAR_022823
Natural variant8881S → R.
Corresponds to variant rs1052867 [ dbSNP | Ensembl ].
VAR_044120

Experimental info

Sequence conflict4871K → Q in AAI11762. Ref.5
Sequence conflict7641A → G in AAC79436. Ref.2
Sequence conflict7641A → G in AAC79456. Ref.2

Sequences

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

Last modified July 5, 2005. Version 2.
Checksum: DACDF33C1B8573AC

FASTA1,065117,826
        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 

« Hide

Isoform 2 (S2) [UniParc].

Checksum: 4604C8A1C03E40C6
Show »

FASTA89599,564
Isoform 3 [UniParc].

Checksum: C98F2838A19DFD5D
Show »

FASTA10110,748

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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] (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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
[10]"ANKS6 is a central component of a nephronophthisis module linking NEK8 to INVS and NPHP3."
Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M., van Reeuwijk J., Boehlke C., Schell C., Yasunaga T., Helmstadter M., Mergen M., Filhol E., Boldt K., Horn N., Ueffing M., Otto E.A., Eisenberger T., Elting M.W. expand/collapse author list , van Wijk J.A., Bockenhauer D., Sebire N.J., Rittig S., Vyberg M., Ring T., Pohl M., Pape L., Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C., Grahammer F., Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J., Roepman R., Saunier S., Walz G., Hildebrandt F., Bergmann C., Lienkamp S.S.
Nat. Genet. 45:951-956(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKS6; NEK8 AND NPHP3, HYDROXYLATION AT ASN-75.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039217 mRNA. Translation: AAD02131.2. Different initiation.
AF084367 mRNA. Translation: AAC79436.1.
AF084382 expand/collapse EMBL AC list , AF084373, AF084374, AF084375, AF084377, AF084379, AF084381, AF084371, AF084369, AF084368, AF084370, AF084372, AF084380, AF084378, AF084376 Genomic DNA. Translation: AAC79456.1.
AF084382 expand/collapse EMBL AC list , 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.
RefSeqNP_055240.2. NM_014425.3.
NP_899068.1. NM_183245.2.
UniGeneHs.558477.

3D structure databases

ProteinModelPortalQ9Y283.
SMRQ9Y283. Positions 12-573.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118021. 7 interactions.
IntActQ9Y283. 6 interactions.
MINTMINT-1196568.
STRING9606.ENSP00000262457.

PTM databases

PhosphoSiteQ9Y283.

Polymorphism databases

DMDM68565551.

Proteomic databases

PaxDbQ9Y283.
PRIDEQ9Y283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262456; ENSP00000262456; ENSG00000119509. [Q9Y283-2]
ENST00000262457; ENSP00000262457; ENSG00000119509. [Q9Y283-1]
ENST00000374921; ENSP00000364056; ENSG00000119509. [Q9Y283-3]
GeneID27130.
KEGGhsa:27130.
UCSCuc004bao.2. human. [Q9Y283-2]
uc004bap.2. human. [Q9Y283-1]

Organism-specific databases

CTD27130.
GeneCardsGC09P102861.
HGNCHGNC:17870. INVS.
HPAHPA049994.
MIM243305. gene.
602088. phenotype.
neXtProtNX_Q9Y283.
Orphanet93591. Infantile autosomal recessive medullary cystic kidney disease.
3156. Senior-Loken syndrome.
PharmGKBPA38472.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG083788.
InParanoidQ9Y283.
OMANLQCIHL.
OrthoDBEOG7P02H2.
PhylomeDBQ9Y283.
TreeFamTF312824.

Enzyme and pathway databases

SignaLinkQ9Y283.

Gene expression databases

ArrayExpressQ9Y283.
BgeeQ9Y283.
CleanExHS_INVS.
GenevestigatorQ9Y283.

Family and domain databases

Gene3D1.25.40.20. 5 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 6 hits.
PF00612. IQ. 2 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 15 hits.
SM00015. IQ. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 11 hits.
PS50096. IQ. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINVS. human.
GeneWikiINVS.
GenomeRNAi27130.
NextBio49848.
PROQ9Y283.
SOURCESearch...

Entry information

Entry nameINVS_HUMAN
AccessionPrimary (citable) accession number: Q9Y283
Secondary accession number(s): A2A2Y2 expand/collapse secondary AC list , Q2NKL0, Q5W0T6, Q8IVX8, Q9BRB9, Q9Y488, Q9Y498
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM