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McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin (Bardet-Biedl syndrome 6 protein)

 MKKS_HUMAN              Reviewed;         570 AA.
Q9NPJ1; A8K7B0; D3DW18;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 165.
RecName: Full=McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin;
AltName: Full=Bardet-Biedl syndrome 6 protein;
Name=MKKS {ECO:0000312|HGNC:HGNC:7108};
Synonyms=BBS6 {ECO:0000303|PubMed:28753627};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MKKS CYS-37; TYR-84 AND SER-242,
AND VARIANTS VAL-49 AND CYS-517.
PubMed=10802661; DOI=10.1038/75637;
Stone D.L., Slavotinek A.M., Bouffard G.G., Banerjee-Basu S.,
Baxevanis A.D., Barr M., Biesecker L.G.;
"Mutation of a gene encoding a putative chaperonin causes McKusick-
Kaufman syndrome.";
Nat. Genet. 25:79-82(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS BBS6 ASP-52;
LEU-155; ALA-286; GLU-345 AND SER-499, AND CHARACTERIZATION OF VARIANT
PRO-325.
PubMed=15731008; DOI=10.1242/jcs.01676;
Kim J.C., Ou Y.Y., Badano J.L., Esmail M.A., Leitch C.C., Fiedrich E.,
Beales P.L., Archibald J.M., Katsanis N., Rattner J.B., Leroux M.R.;
"MKKS/BBS6, a divergent chaperonin-like protein linked to the obesity
disorder Bardet-Biedl syndrome, is a novel centrosomal component
required for cytokinesis.";
J. Cell Sci. 118:1007-1020(2005).
[7]
INTERACTION WITH CCDC28B.
PubMed=16327777; DOI=10.1038/nature04370;
Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S.,
Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.;
"Dissection of epistasis in oligogenic Bardet-Biedl syndrome.";
Nature 439:326-330(2006).
[8]
SUBCELLULAR LOCATION, INTERACTION WITH STUB1, AND CHARACTERIZATION OF
VARIANTS BBS6 CYS-37; ALA-57; SER-242; GLU-345 AND SER-499.
PubMed=18094050; DOI=10.1091/mbc.E07-07-0631;
Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K.,
Kimura H., Cyr D.M., Kubota H., Nagata K.;
"MKKS is a centrosome-shuttling protein degraded by disease-causing
mutations via CHIP-mediated ubiquitination.";
Mol. Biol. Cell 19:899-911(2008).
[9]
FUNCTION, IDENTIFICATION IN BBS/CCT COMPLEX, INTERACTION WITH BBS2,
AND CHARACTERIZATION OF VARIANTS BBS6 CYS-37; ASP-52; ALA-57; TYR-84;
PRO-236 AND PRO-277.
PubMed=20080638; DOI=10.1073/pnas.0910268107;
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
Sheffield V.C.;
"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
chaperonins and mediate BBSome assembly.";
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
[10]
INTERACTION WITH BBS12, VARIANT BBS6 ARG-395, AND CHARACTERIZATION OF
VARIANT BBS6 ARG-395.
PubMed=26900326;
Hulleman J.D., Nguyen A., Ramprasad V.L., Murugan S., Gupta R.,
Mahindrakar A., Angara R., Sankurathri C., Mootha V.V.;
"A novel H395R mutation in MKKS/BBS6 causes retinitis pigmentosa and
polydactyly without other findings of Bardet-Biedl or McKusick-Kaufman
syndrome.";
Mol. Vis. 22:73-81(2016).
[11]
VARIANT BBS6 ASP-52.
PubMed=10973238; DOI=10.1038/79116;
Slavotinek A.M., Stone E.M., Mykytyn K., Heckenlively J.R.,
Green J.S., Heon E., Musarella M.A., Parfrey P.S., Sheffield V.C.,
Biesecker L.G.;
"Mutations in MKKS cause Bardet-Biedl syndrome.";
Nat. Genet. 26:15-16(2000).
[12]
VARIANTS BBS6 CYS-37; ALA-57 AND PRO-277.
TISSUE=Peripheral blood lymphocyte;
PubMed=10973251; DOI=10.1038/79201;
Katsanis N., Beales P.L., Woods M.O., Lewis R.A., Green J.S.,
Parfrey P.S., Ansley S.J., Davidson W.S., Lupski J.R.;
"Mutations in MKKS cause obesity, retinal dystrophy and renal
malformations associated with Bardet-Biedl syndrome.";
Nat. Genet. 26:67-70(2000).
[13]
VARIANTS BBS6 MET-32; ALA-57; PRO-236; ALA-286; SER-499; ALA-511 AND
HIS-518, AND VARIANT SER-242.
PubMed=11179009; DOI=10.1086/318794;
Beales P.L., Katsanis N., Lewis R.A., Ansley S.J., Elcioglu N.,
Raza J., Woods M.O., Green J.S., Parfrey P.S., Davidson W.S.,
Lupski J.R.;
"Genetic and mutational analyses of a large multiethnic Bardet-Biedl
cohort reveal a minor involvement of BBS6 and delineate the critical
intervals of other loci.";
Am. J. Hum. Genet. 68:606-616(2001).
[14]
VARIANTS BBS6 CYS-37; SER-242 AND SER-499.
PubMed=11567139; DOI=10.1126/science.1063525;
Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A.,
Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.;
"Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian
recessive disorder.";
Science 293:2256-2259(2001).
[15]
VARIANTS BBS6 LEU-155; SER-242 AND GLU-345, AND VARIANT VAL-339.
PubMed=12107442; DOI=10.1007/s00439-002-0733-3;
Slavotinek A.M., Searby C., Al-Gazali L., Hennekam R.C.M.,
Schrander-Stumpel C., Orcana-Losa M., Pardo-Reoyo S., Cantani A.,
Kumar D., Capellini Q., Neri G., Zackai E., Biesecker L.G.;
"Mutation analysis of the MKKS gene in McKusick-Kaufman syndrome and
selected Bardet-Biedl syndrome patients.";
Hum. Genet. 110:561-567(2002).
[16]
VARIANT BBS6 PRO-236, AND VARIANT PRO-325.
PubMed=12677556; DOI=10.1086/375178;
Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E.,
Kirsten B., Mein C.A., Froguel P., Scambler P.J., Lewis R.A.,
Lupski J.R., Katsanis N.;
"Genetic interaction of BBS1 mutations with alleles at other BBS loci
can result in non-Mendelian Bardet-Biedl syndrome.";
Am. J. Hum. Genet. 72:1187-1199(2003).
[17]
VARIANT PRO-325, AND CHARACTERIZATION OF VARIANT PRO-325.
PubMed=12837689; DOI=10.1093/hmg/ddg188;
Badano J.L., Kim J.C., Hoskins B.E., Lewis R.A., Ansley S.J.,
Cutler D.J., Castellan C., Beales P.L., Leroux M.R., Katsanis N.;
"Heterozygous mutations in BBS1, BBS2 and BBS6 have a potential
epistatic effect on Bardet-Biedl patients with two mutations at a
second BBS locus.";
Hum. Mol. Genet. 12:1651-1659(2003).
[18]
VARIANTS BBS6 PRO-181 AND ASN-492.
PubMed=12920096; DOI=10.1136/jmg.40.8.e104;
Fauser S., Munz M., Besch D.;
"Further support for digenic inheritance in Bardet-Biedl syndrome.";
J. Med. Genet. 40:E104-E104(2003).
[19]
VARIANTS BBS6 PRO-237 AND PRO-460, AND VARIANTS VAL-339; CYS-517 AND
VAL-532.
PubMed=15666242; DOI=10.1086/428679;
Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L.,
Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E.,
Esculpavit C., Audollent S., Goudefroye G., Gonzales M., Tantau J.,
Loget P., Joubert M., Gaillard D., Jeanne-Pasquier C.,
Delezoide A.-L., Peter M.-O., Plessis G., Simon-Bouy B., Dollfus H.,
Le Merrer M., Munnich A., Encha-Razavi F., Vekemans M.,
Attie-Bitach T.;
"Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel
syndrome.";
Am. J. Hum. Genet. 76:493-504(2005).
[20]
VARIANTS BBS6 ALA-237 AND PRO-237, AND VARIANTS VAL-339; CYS-517 AND
VAL-532.
PubMed=15770229; DOI=10.1038/sj.ejhg.5201372;
Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P.,
Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M.,
Kaplan J., Bitoun P., Lacombe D., Verloes A., Bonneau D.,
Perrin-Schmitt F., Brandt C., Besancon A.-F., Mandel J.-L., Cossee M.,
Dollfus H.;
"Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl
syndrome family cohort.";
Eur. J. Hum. Genet. 13:607-616(2005).
[21]
VARIANTS SER-242; CYS-517 AND VAL-532.
PubMed=15483080; DOI=10.1210/jc.2004-0465;
Andersen K.L., Echwald S.M., Larsen L.H., Hamid Y.H., Glumer C.,
Jorgensen T., Borch-Johnsen K., Andersen T., Sorensen T.I., Hansen T.,
Pedersen O.;
"Variation of the McKusick-Kaufman gene and studies of relationships
with common forms of obesity.";
J. Clin. Endocrinol. Metab. 90:225-230(2005).
[22]
VARIANT SER-242, AND DISCUSSION OF THE PATHOLOGICAL ROLE OF VARIANT
SER-242.
PubMed=20120035; DOI=10.1002/humu.21204;
Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R.,
Sheffield V.C., Rosenberg T., Brondum-Nielsen K.;
"Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence
variations in six genes.";
Hum. Mutat. 31:429-436(2010).
[23]
VARIANTS BBS6 ARG-41; ARG-99 AND LEU-299, AND VARIANT THR-488.
PubMed=21344540; DOI=10.1002/humu.21480;
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R.,
Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I.,
Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L.,
Kennedy D., Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K.,
Heon E.;
"BBS genotype-phenotype assessment of a multiethnic patient cohort
calls for a revision of the disease definition.";
Hum. Mutat. 32:610-619(2011).
[24]
VARIANT BBS6 ALA-57.
PubMed=22152675; DOI=10.1016/j.ajhg.2011.11.005;
Huang L., Szymanska K., Jensen V.L., Janecke A.R., Innes A.M.,
Davis E.E., Frosk P., Li C., Willer J.R., Chodirker B.N.,
Greenberg C.R., McLeod D.R., Bernier F.P., Chudley A.E., Muller T.,
Shboul M., Logan C.V., Loucks C.M., Beaulieu C.L., Bowie R.V.,
Bell S.M., Adkins J., Zuniga F.I., Ross K.D., Wang J., Ban M.R.,
Becker C., Nurnberg P., Douglas S., Craft C.M., Akimenko M.A.,
Hegele R.A., Ober C., Utermann G., Bolz H.J., Bulman D.E.,
Katsanis N., Blacque O.E., Doherty D., Parboosingh J.S., Leroux M.R.,
Johnson C.A., Boycott K.M.;
"TMEM237 is mutated in individuals with a Joubert syndrome related
disorder and expands the role of the TMEM family at the ciliary
transition zone.";
Am. J. Hum. Genet. 89:713-730(2011).
[25]
VARIANT BBS6 40-SER--ASN-570 DEL.
PubMed=28761321;
Ullah A., Umair M., Yousaf M., Khan S.A., Nazim-Ud-Din M., Shah K.,
Ahmad F., Azeem Z., Ali G., Alhaddad B., Rafique A., Jan A.,
Haack T.B., Strom T.M., Meitinger T., Ghous T., Ahmad W.;
"Sequence variants in four genes underlying Bardet-Biedl syndrome in
consanguineous families.";
Mol. Vis. 23:482-494(2017).
[26]
CHARACTERIZATION OF VARIANTS MKKS CYS-37; TYR-84 AND SER-242,
SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LEU-454,
CHARACTERIZATION OF VARIANT BBS6 CYS-37, AND INTERACTION WITH SMARCC1.
PubMed=28753627; DOI=10.1371/journal.pgen.1006936;
Scott C.A., Marsden A.N., Rebagliati M.R., Zhang Q., Chamling X.,
Searby C.C., Baye L.M., Sheffield V.C., Slusarski D.C.;
"Nuclear/cytoplasmic transport defects in BBS6 underlie congenital
heart disease through perturbation of a chromatin remodeling
protein.";
PLoS Genet. 13:E1006936-E1006936(2017).
-!- FUNCTION: Probable molecular chaperone. Assists the folding of
proteins upon ATP hydrolysis. As part of the BBS/CCT complex plays
a role in the assembly of BBSome, a complex involved in
ciliogenesis regulating transports vesicles to the cilia. May play
a role in protein processing in limb, cardiac and reproductive
system development. May play a role in cytokinesis.
{ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:28753627}.
-!- SUBUNIT: Component of the BBS/CCT complex composed at least of
MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
Interacts with STUB1. Interacts with BBS2 (via coiled coil
domain). Interacts with CCDC28B. Interacts with BBS12
(PubMed:26900326). Interacts with SMARCC1, a component of the
SWI/SNF complexes; the interaction takes place predominantly in
the cytoplasm and may modulate SMARCC1 location (PubMed:28753627).
{ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:18094050,
ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:26900326,
ECO:0000269|PubMed:28753627}.
-!- INTERACTION:
Q6ZW61:BBS12; NbExp=11; IntAct=EBI-721319, EBI-6128352;
Q9BXC9:BBS2; NbExp=3; IntAct=EBI-721319, EBI-748297;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Cytoplasm, cytosol
{ECO:0000269|PubMed:28753627}. Nucleus
{ECO:0000269|PubMed:28753627}. Note=The majority of the protein
resides within the pericentriolar material (PCM), a proteinaceous
tube surrounding centrioles. During interphase, the protein is
confined to the lateral surfaces of the PCM but during mitosis it
relocalizes throughout the PCM and is found at the intercellular
bridge. The MKSS protein is highly mobile and rapidly shuttles
between the cytosol and centrosome.
-!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues.
-!- DOMAIN: The substrate-binding apical domain region is sufficient
for centrosomal association.
-!- DISEASE: McKusick-Kaufman syndrome (MKKS) [MIM:236700]: Autosomal
recessive developmental disorder. It is characterized by
hydrometrocolpos, postaxial polydactyly and congenital heart
defects. {ECO:0000269|PubMed:10802661,
ECO:0000269|PubMed:28753627}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Bardet-Biedl syndrome 6 (BBS6) [MIM:605231]: A syndrome
characterized by usually severe pigmentary retinopathy, early-
onset obesity, polydactyly, hypogenitalism, renal malformation and
mental retardation. Secondary features include diabetes mellitus,
hypertension and congenital heart disease. Bardet-Biedl syndrome
inheritance is autosomal recessive, but three mutated alleles (two
at one locus, and a third at a second locus) may be required for
clinical manifestation of some forms of the disease.
{ECO:0000269|PubMed:10973238, ECO:0000269|PubMed:10973251,
ECO:0000269|PubMed:11179009, ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:12107442, ECO:0000269|PubMed:12677556,
ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15731008, ECO:0000269|PubMed:15770229,
ECO:0000269|PubMed:18094050, ECO:0000269|PubMed:20080638,
ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:22152675,
ECO:0000269|PubMed:26900326, ECO:0000269|PubMed:28753627,
ECO:0000269|PubMed:28761321}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Mutations of the MKKS gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/mkksmut.htm";
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EMBL; AF221992; AAF73872.1; -; mRNA.
EMBL; AF221993; AAF73873.1; -; mRNA.
EMBL; AK291925; BAF84614.1; -; mRNA.
EMBL; AL157427; CAB75652.1; -; mRNA.
EMBL; AL034430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10344.1; -; Genomic_DNA.
EMBL; CH471133; EAX10345.1; -; Genomic_DNA.
CCDS; CCDS13111.1; -.
PIR; T46911; T46911.
RefSeq; NP_061336.1; NM_018848.3.
RefSeq; NP_740754.1; NM_170784.2.
UniGene; Hs.472119; -.
UniGene; Hs.741430; -.
ProteinModelPortal; Q9NPJ1; -.
BioGrid; 113837; 11.
CORUM; Q9NPJ1; -.
DIP; DIP-60349N; -.
IntAct; Q9NPJ1; 14.
STRING; 9606.ENSP00000246062; -.
iPTMnet; Q9NPJ1; -.
PhosphoSitePlus; Q9NPJ1; -.
BioMuta; MKKS; -.
DMDM; 11133565; -.
EPD; Q9NPJ1; -.
PaxDb; Q9NPJ1; -.
PeptideAtlas; Q9NPJ1; -.
PRIDE; Q9NPJ1; -.
DNASU; 8195; -.
Ensembl; ENST00000347364; ENSP00000246062; ENSG00000125863.
Ensembl; ENST00000399054; ENSP00000382008; ENSG00000125863.
GeneID; 8195; -.
KEGG; hsa:8195; -.
UCSC; uc002wnt.3; human.
CTD; 8195; -.
DisGeNET; 8195; -.
EuPathDB; HostDB:ENSG00000125863.17; -.
GeneCards; MKKS; -.
GeneReviews; MKKS; -.
HGNC; HGNC:7108; MKKS.
HPA; HPA041071; -.
HPA; HPA044233; -.
MalaCards; MKKS; -.
MIM; 236700; phenotype.
MIM; 604896; gene.
MIM; 605231; phenotype.
neXtProt; NX_Q9NPJ1; -.
OpenTargets; ENSG00000125863; -.
Orphanet; 110; Bardet-Biedl syndrome.
Orphanet; 2473; McKusick-Kaufman syndrome.
PharmGKB; PA30826; -.
eggNOG; KOG0360; Eukaryota.
eggNOG; COG0459; LUCA.
GeneTree; ENSGT00390000007214; -.
HOGENOM; HOG000013131; -.
HOVERGEN; HBG005055; -.
InParanoid; Q9NPJ1; -.
KO; K09492; -.
OMA; TSKPACM; -.
OrthoDB; EOG091G0VW9; -.
PhylomeDB; Q9NPJ1; -.
TreeFam; TF329106; -.
Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
ChiTaRS; MKKS; human.
GeneWiki; MKKS; -.
GenomeRNAi; 8195; -.
PRO; PR:Q9NPJ1; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125863; -.
CleanEx; HS_MKKS; -.
ExpressionAtlas; Q9NPJ1; baseline and differential.
Genevisible; Q9NPJ1; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:1902636; C:kinociliary basal body; IEA:Ensembl.
GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:MGI.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0060027; P:convergent extension involved in gastrulation; ISS:BHF-UCL.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
GO; GO:0008406; P:gonad development; TAS:ProtInc.
GO; GO:0007507; P:heart development; TAS:ProtInc.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL.
GO; GO:0046907; P:intracellular transport; ISS:BHF-UCL.
GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL.
GO; GO:0051877; P:pigment granule aggregation in cell center; ISS:BHF-UCL.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL.
GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0007608; P:sensory perception of smell; ISS:BHF-UCL.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
GO; GO:0021756; P:striatum development; ISS:BHF-UCL.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.30.260.10; -; 2.
Gene3D; 3.50.7.10; -; 1.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
InterPro; IPR028790; MKKS.
InterPro; IPR027410; TCP-1-like_intermed_sf.
PANTHER; PTHR11353:SF77; PTHR11353:SF77; 1.
Pfam; PF00118; Cpn60_TCP1; 1.
SUPFAM; SSF48592; SSF48592; 2.
SUPFAM; SSF52029; SSF52029; 1.
1: Evidence at protein level;
ATP-binding; Bardet-Biedl syndrome; Chaperone; Ciliopathy;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
Mental retardation; Nucleotide-binding; Nucleus; Obesity;
Polymorphism; Reference proteome; Sensory transduction; Vision.
CHAIN 1 570 McKusick-Kaufman/Bardet-Biedl syndromes
putative chaperonin.
/FTId=PRO_0000128415.
NP_BIND 192 199 ATP. {ECO:0000255}.
REGION 198 370 Substrate-binding apical domain.
VARIANT 32 32 I -> M (in BBS6).
{ECO:0000269|PubMed:11179009}.
/FTId=VAR_017035.
VARIANT 37 37 Y -> C (in MKKS and BBS6; causes both
increased MKKS protein degradation and
reduced solubility relative to wild-type
and Tyr-84 mutant; the mutant is
immobilized at the centrosome even in the
absence of proteasome inhibition; the
mutant is also highly polyubiquitinated;
no effect on import to the nucleus;
dbSNP:rs74315396).
{ECO:0000269|PubMed:10802661,
ECO:0000269|PubMed:10973251,
ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:18094050,
ECO:0000269|PubMed:20080638,
ECO:0000269|PubMed:28753627}.
/FTId=VAR_009864.
VARIANT 40 570 Missing (in BBS6).
{ECO:0000269|PubMed:28761321}.
/FTId=VAR_080223.
VARIANT 41 41 G -> R (in BBS6; dbSNP:rs766132697).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066262.
VARIANT 49 49 G -> V (in dbSNP:rs528833454).
{ECO:0000269|PubMed:10802661}.
/FTId=VAR_009865.
VARIANT 52 52 G -> D (in BBS6; fails to associate with
centrosome; dbSNP:rs28937875).
{ECO:0000269|PubMed:10973238,
ECO:0000269|PubMed:15731008,
ECO:0000269|PubMed:20080638}.
/FTId=VAR_009882.
VARIANT 57 57 T -> A (in BBS6; found in a patient also
carrying A-155 in TMEM237; causes both
increased MKKS protein degradation and
reduced solubility relative to wild-type
and Y-84 mutant; greatly reduces the
ability to interact with BBS12;
dbSNP:rs74315399).
{ECO:0000269|PubMed:10973251,
ECO:0000269|PubMed:11179009,
ECO:0000269|PubMed:18094050,
ECO:0000269|PubMed:20080638,
ECO:0000269|PubMed:22152675}.
/FTId=VAR_009883.
VARIANT 84 84 H -> Y (in MKKS; associated with S-242;
decreased interaction with BBS12; no
effect on ciliogenesis; disrupts import
to the nucleus; no effect on interaction
with SMARCC1; may affect modulation of
SMARCC1 subcellular location;
dbSNP:rs281797258).
{ECO:0000269|PubMed:10802661,
ECO:0000269|PubMed:20080638,
ECO:0000269|PubMed:28753627}.
/FTId=VAR_009866.
VARIANT 99 99 C -> R (in BBS6).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066263.
VARIANT 155 155 R -> L (in BBS6; increases MKKS protein
degradation; localizes properly to the
centrosome; dbSNP:rs138111422).
{ECO:0000269|PubMed:12107442,
ECO:0000269|PubMed:15731008}.
/FTId=VAR_017040.
VARIANT 181 181 A -> P (in BBS6).
{ECO:0000269|PubMed:12920096}.
/FTId=VAR_038898.
VARIANT 236 236 S -> P (in BBS6).
{ECO:0000269|PubMed:11179009,
ECO:0000269|PubMed:12677556,
ECO:0000269|PubMed:20080638}.
/FTId=VAR_017036.
VARIANT 237 237 T -> A (in BBS6; dbSNP:rs760185677).
{ECO:0000269|PubMed:15770229}.
/FTId=VAR_038899.
VARIANT 237 237 T -> P (in BBS6).
{ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15770229}.
/FTId=VAR_038900.
VARIANT 242 242 A -> S (in MKKS and BBS6; associated with
Y-84 in MKKS; unknown pathological
significance; increases MKKS protein
degradation; no effect on ciliogenesis;
disrupts import to the nucleus; no effect
on interaction with SMARCC1; may affect
modulation of SMARCC1 subcellular
location; dbSNP:rs74315394).
{ECO:0000269|PubMed:10802661,
ECO:0000269|PubMed:11179009,
ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:12107442,
ECO:0000269|PubMed:15483080,
ECO:0000269|PubMed:18094050,
ECO:0000269|PubMed:20120035,
ECO:0000269|PubMed:28753627}.
/FTId=VAR_009867.
VARIANT 277 277 L -> P (in BBS6; moderately affects
interaction with BBS2; greatly reduces
the ability to interact with BBS12;
dbSNP:rs74315398).
{ECO:0000269|PubMed:10973251,
ECO:0000269|PubMed:20080638}.
/FTId=VAR_009884.
VARIANT 286 286 D -> A (in BBS6; fails to associate with
centrosome).
{ECO:0000269|PubMed:11179009,
ECO:0000269|PubMed:15731008}.
/FTId=VAR_017037.
VARIANT 299 299 P -> L (in BBS6; dbSNP:rs756083063).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066264.
VARIANT 325 325 T -> P (has a modifier effect on BBS;
causes a mislocalization of the protein;
fails to associate with centrosome;
dbSNP:rs137853156).
{ECO:0000269|PubMed:12677556,
ECO:0000269|PubMed:12837689,
ECO:0000269|PubMed:15731008}.
/FTId=VAR_038901.
VARIANT 339 339 I -> V (in dbSNP:rs137853909).
{ECO:0000269|PubMed:12107442,
ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15770229}.
/FTId=VAR_017041.
VARIANT 345 345 G -> E (in BBS6; increases MKKS protein
degradation; fails to associate with
centrosome; the mutant is highly
polyubiquitinated and rapidly degraded by
the ubiquitin-proteasome protein
degradation pathway; dbSNP:rs779116830).
{ECO:0000269|PubMed:12107442,
ECO:0000269|PubMed:15731008,
ECO:0000269|PubMed:18094050}.
/FTId=VAR_017042.
VARIANT 395 395 H -> R (in BBS6; atypical mild phenotype
consisting of retinitis pigmentosa and
polydactyly without other signs of
Bardet-Biedl syndrome; results in
decreased interaction with BBS12;
dbSNP:rs912923677).
{ECO:0000269|PubMed:26900326}.
/FTId=VAR_077208.
VARIANT 460 460 S -> P (in BBS6).
{ECO:0000269|PubMed:15666242}.
/FTId=VAR_038902.
VARIANT 488 488 A -> T (in a patient with Bardet-Biedl
syndrome compound heterozygote for
mutations in BBS12; uncertain
pathological role; dbSNP:rs61734546).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066265.
VARIANT 492 492 D -> N (in BBS6; dbSNP:rs142327258).
{ECO:0000269|PubMed:12920096}.
/FTId=VAR_038903.
VARIANT 499 499 C -> S (in BBS6; causes both increased
MKKS protein degradation and reduced
solubility relative to wild-type and Tyr-
84 mutant; localizes properly to the
centrosome; dbSNP:rs281797259 and
dbSNP:rs137853155).
{ECO:0000269|PubMed:11179009,
ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:15731008,
ECO:0000269|PubMed:18094050}.
/FTId=VAR_013161.
VARIANT 511 511 S -> A (in BBS6).
{ECO:0000269|PubMed:11179009}.
/FTId=VAR_017038.
VARIANT 517 517 R -> C (in dbSNP:rs1547).
{ECO:0000269|PubMed:10802661,
ECO:0000269|PubMed:15483080,
ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15770229}.
/FTId=VAR_009868.
VARIANT 518 518 R -> H (in BBS6; dbSNP:rs149051148).
{ECO:0000269|PubMed:11179009}.
/FTId=VAR_017039.
VARIANT 532 532 G -> V (in dbSNP:rs1545).
{ECO:0000269|PubMed:15483080,
ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15770229}.
/FTId=VAR_009869.
MUTAGEN 454 454 L->P: No effect on import to the nucleus.
{ECO:0000269|PubMed:28753627}.
SEQUENCE 570 AA; 62342 MW; 14BA57FF8AEA0AF7 CRC64;
MSRLEAKKPS LCKSEPLTTE RVRTTLSVLK RIVTSCYGPS GRLKQLHNGF GGYVCTTSQS
SALLSHLLVT HPILKILTAS IQNHVSSFSD CGLFTAILCC NLIENVQRLG LTPTTVIRLN
KHLLSLCISY LKSETCGCRI PVDFSSTQIL LCLVRSILTS KPACMLTRKE TEHVSALILR
AFLLTIPENA EGHIILGKSL IVPLKGQRVI DSTVLPGILI EMSEVQLMRL LPIKKSTALK
VALFCTTLSG DTSDTGEGTV VVSYGVSLEN AVLDQLLNLG RQLISDHVDL VLCQKVIHPS
LKQFLNMHRI IAIDRIGVTL MEPLTKMTGT QPIGSLGSIC PNSYGSVKDV CTAKFGSKHF
FHLIPNEATI CSLLLCNRND TAWDELKLTC QTALHVLQLT LKEPWALLGG GCTETHLAAY
IRHKTHNDPE SILKDDECTQ TELQLIAEAF CSALESVVGS LEHDGGEILT DMKYGHLWSV
QADSPCVANW PDLLSQCGCG LYNSQEELNW SFLRSTRRPF VPQSCLPHEA VGSASNLTLD
CLTAKLSGLQ VAVETANLIL DLSYVIEDKN


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