Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Coiled-coil and C2 domain-containing protein 2A

 C2D2A_HUMAN             Reviewed;        1620 AA.
Q9P2K1; A6ND97; B3FW08; D6RB72; E7EP21; E9PEV5; Q3SYP3; Q9H8A7;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
28-FEB-2018, entry version 119.
RecName: Full=Coiled-coil and C2 domain-containing protein 2A;
Name=CC2D2A; Synonyms=KIAA1345;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INVOLVEMENT IN
MKS6.
PubMed=18513680; DOI=10.1016/j.ajhg.2008.05.004;
Tallila J., Jakkula E., Peltonen L., Salonen R., Kestilae M.;
"Identification of CC2D2A as a Meckel syndrome gene adds an important
piece to the ciliopathy puzzle.";
Am. J. Hum. Genet. 82:1361-1367(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-527 (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-1620 (ISOFORMS 1/2).
TISSUE=Thyroid;
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).
[7]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN JBTS9.
PubMed=18387594; DOI=10.1016/j.ajhg.2008.01.021;
Noor A., Windpassinger C., Patel M., Stachowiak B., Mikhailov A.,
Azam M., Irfan M., Siddiqui Z.K., Naeem F., Paterson A.D.,
Lutfullah M., Vincent J.B., Ayub M.;
"CC2D2A, encoding a coiled-coil and C2 domain protein, causes
autosomal-recessive mental retardation with retinitis pigmentosa.";
Am. J. Hum. Genet. 82:1011-1018(2008).
[8]
ERRATUM.
PubMed=19068953; DOI=10.1016/j.ajhg.2008.10.005;
Noor A., Windpassinger C., Patel M., Stachowiak B., Mikhailov A.,
Azam M., Irfan M., Paterson A.D., Lutufullah M., Doherty D.,
Vincent J.B., Ayub M.;
Am. J. Hum. Genet. 83:656-656(2008).
[9]
DEVELOPMENTAL STAGE, VARIANTS JBTS9 SER-721; MET-1114 AND VAL-1556,
AND VARIANT GLU-800.
PubMed=19777577; DOI=10.1002/humu.21116;
Mougou-Zerelli S., Thomas S., Szenker E., Audollent S.,
Elkhartoufi N., Babarit C., Romano S., Salomon R., Amiel J.,
Esculpavit C., Gonzales M., Escudier E., Leheup B., Loget P.,
Odent S., Roume J., Gerard M., Delezoide A.-L., Khung S., Patrier S.,
Cordier M.-P., Bouvier R., Martinovic J., Gubler M.-C., Boddaert N.,
Munnich A., Encha-Razavi F., Valente E.M., Saad A., Saunier S.,
Vekemans M., Attie-Bitach T.;
"CC2D2A mutations in Meckel and Joubert syndromes indicate a genotype-
phenotype correlation.";
Hum. Mutat. 30:1574-1582(2009).
[10]
VARIANTS JBTS9 HIS-1096; SER-1122; CYS-1528 AND PRO-1551, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP290.
PubMed=18950740; DOI=10.1016/j.ajhg.2008.10.002;
Gorden N.T., Arts H.H., Parisi M.A., Coene K.L.M., Letteboer S.J.F.,
van Beersum S.E.C., Mans D.A., Hikida A., Eckert M., Knutzen D.,
Alswaid A.F., Oezyurek H., Dibooglu S., Otto E.A., Liu Y., Davis E.E.,
Hutter C.M., Bammler T.K., Farin F.M., Dorschner M., Topcu M.,
Zackai E.H., Rosenthal P., Owens K.N., Katsanis N., Vincent J.B.,
Hildebrandt F., Rubel E.W., Raible D.W., Knoers N.V.A.M., Chance P.F.,
Roepman R., Moens C.B., Glass I.A., Doherty D.;
"CC2D2A is mutated in Joubert syndrome and interacts with the
ciliopathy-associated basal body protein CEP290.";
Am. J. Hum. Genet. 83:559-571(2008).
[11]
VARIANT MKS6 MET-1114.
PubMed=19466712; DOI=10.1002/humu.21057;
Tallila J., Salonen R., Kohlschmidt N., Peltonen L., Kestilae M.;
"Mutation spectrum of Meckel syndrome genes: one group of syndromes or
several distinct groups?";
Hum. Mutat. 30:E813-E830(2009).
[12]
VARIANTS COACHS MET-1116 AND CYS-1528.
PubMed=19574260; DOI=10.1136/jmg.2009.067249;
Doherty D., Parisi M.A., Finn L.S., Gunay-Aygun M., Al-Mateen M.,
Bates D., Clericuzio C., Demir H., Dorschner M., van Essen A.J.,
Gahl W.A., Gentile M., Gorden N.T., Hikida A., Knutzen D., Ozyurek H.,
Phelps I., Rosenthal P., Verloes A., Weigand H., Chance P.F.,
Dobyns W.B., Glass I.A.;
"Mutations in 3 genes (MKS3, CC2D2A and RPGRIP1L) cause COACH syndrome
(Joubert syndrome with congenital hepatic fibrosis).";
J. Med. Genet. 47:8-21(2010).
[13]
VARIANTS JBTS9 LYS-1126 AND VAL-1556.
PubMed=22425360; DOI=10.1016/j.ajhg.2012.02.011;
Srour M., Schwartzentruber J., Hamdan F.F., Ospina L.H., Patry L.,
Labuda D., Massicotte C., Dobrzeniecka S., Capo-Chichi J.M.,
Papillon-Cavanagh S., Samuels M.E., Boycott K.M., Shevell M.I.,
Laframboise R., Desilets V., Maranda B., Rouleau G.A., Majewski J.,
Michaud J.L.;
"Mutations in C5ORF42 cause Joubert syndrome in the French Canadian
population.";
Am. J. Hum. Genet. 90:693-700(2012).
[14]
VARIANTS JBTS9 ARG-117; GLU-507; PRO-559; ALA-1045; HIS-1096;
MET-1116; SER-1122; ALA-1151; CYS-1284; HIS-1284; GLN-1330; ALA-1430;
CYS-1528 AND VAL-1556, AND VARIANTS ILE-660; ILE-684 AND VAL-701.
PubMed=22241855; DOI=10.1136/jmedgenet-2011-100552;
Bachmann-Gagescu R., Ishak G.E., Dempsey J.C., Adkins J., O'Day D.,
Phelps I.G., Gunay-Aygun M., Kline A.D., Szczaluba K., Martorell L.,
Alswaid A., Alrasheed S., Pai S., Izatt L., Ronan A., Parisi M.A.,
Mefford H., Glass I., Doherty D.;
"Genotype-phenotype correlation in CC2D2A-related Joubert syndrome
reveals an association with ventriculomegaly and seizures.";
J. Med. Genet. 49:126-137(2012).
[15]
VARIANTS JBTS9 LYS-1126; SER-1520; VAL-1556 AND HIS-1568.
PubMed=23012439; DOI=10.1136/jmedgenet-2012-101132;
Srour M., Hamdan F.F., Schwartzentruber J.A., Patry L., Ospina L.H.,
Shevell M.I., Desilets V., Dobrzeniecka S., Mathonnet G., Lemyre E.,
Massicotte C., Labuda D., Amrom D., Andermann E., Sebire G.,
Maranda B., Consortium F.C., Rouleau G.A., Majewski J., Michaud J.L.;
"Mutations in TMEM231 cause Joubert syndrome in French Canadians.";
J. Med. Genet. 49:636-641(2012).
[16]
VARIANT JBTS9 ALA-1447.
PubMed=22246503; DOI=10.1038/ng.1078;
Lee J.E., Silhavy J.L., Zaki M.S., Schroth J., Bielas S.L.,
Marsh S.E., Olvera J., Brancati F., Iannicelli M., Ikegami K.,
Schlossman A.M., Merriman B., Attie-Bitach T., Logan C.V., Glass I.A.,
Cluckey A., Louie C.M., Lee J.H., Raynes H.R., Rapin I.,
Castroviejo I.P., Setou M., Barbot C., Boltshauser E., Nelson S.F.,
Hildebrandt F., Johnson C.A., Doherty D.A., Valente E.M.,
Gleeson J.G.;
"CEP41 is mutated in Joubert syndrome and is required for tubulin
glutamylation at the cilium.";
Nat. Genet. 44:193-199(2012).
[17]
VARIANT MKS6 SER-1517.
PubMed=24706459; DOI=10.1002/uog.13381;
Jones D., Fiozzo F., Waters B., McKnight D., Brown S.;
"First-trimester diagnosis of Meckel-Gruber syndrome by fetal
ultrasound with molecular identification of CC2D2A mutations by next-
generation sequencing.";
Ultrasound Obstet. Gynecol. 44:719-721(2014).
[18]
VARIANTS JBTS9 LYS-1126; SER-1520; VAL-1556 AND HIS-1568.
PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
Care4Rare Canada Consortium;
Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
Schwartzentruber J., Martin B., Patry L., Nassif C.,
Dionne-Laporte A., Ospina L.H., Lemyre E., Massicotte C.,
Laframboise R., Maranda B., Labuda D., Decarie J.C., Rypens F.,
Goldsher D., Fallet-Bianco C., Soucy J.F., Laberge A.M., Maftei C.,
Boycott K., Brais B., Boucher R.M., Rouleau G.A., Katsanis N.,
Majewski J., Elpeleg O., Kukolich M.K., Shalev S., Michaud J.L.;
"Joubert Syndrome in French Canadians and Identification of Mutations
in CEP104.";
Am. J. Hum. Genet. 97:744-753(2015).
-!- FUNCTION: Component of the tectonic-like complex, a complex
localized at the transition zone of primary cilia and acting as a
barrier that prevents diffusion of transmembrane proteins between
the cilia and plasma membranes. Required for ciliogenesis and
sonic hedgehog/SHH signaling (By similarity). {ECO:0000250,
ECO:0000269|PubMed:18513680}.
-!- SUBUNIT: Part of the tectonic-like complex (also named B9
complex). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium
basal body. Note=Localizes at the transition zone, a region
between the basal body and the ciliary axoneme. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9P2K1-4; Sequence=Displayed;
Name=2;
IsoId=Q9P2K1-2; Sequence=VSP_030923, VSP_037223;
Name=3;
IsoId=Q9P2K1-5; Sequence=VSP_045255, VSP_045256;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9P2K1-6; Sequence=VSP_045453, VSP_045454;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in prostate, pancreas,
kidney, lung, liver, retina, kidney, fetal brain and fetal kidney.
Lower expression in spleen, small intestine, colon, skeletal
muscle, ovary, thymus and heart. {ECO:0000269|PubMed:18387594,
ECO:0000269|PubMed:18950740}.
-!- DEVELOPMENTAL STAGE: At Carnagie stage 13 (CS13, after 4 weeks of
development) and CS14 CC2D2A is ubiquitously expressed, with a
distinct signal in the spinal cord and limb buds. At CS17 CC2D2A
continue to be widely expressedin particular throughout the
central nervous system (CNS), lung, and digestive tract epithelia.
At CS22 expression continues to be intense within the CNS, where
strong and specific expression is observed in the eye and in
external granular layer of cerebellum. CC2D2A expression is also
observed in the costal perichondrium.
{ECO:0000269|PubMed:19777577}.
-!- DISEASE: Meckel syndrome 6 (MKS6) [MIM:612284]: A disorder
characterized by a combination of renal cysts and variably
associated features including developmental anomalies of the
central nervous system (typically encephalocele), hepatic ductal
dysplasia and cysts, and polydactyly.
{ECO:0000269|PubMed:18513680, ECO:0000269|PubMed:19466712,
ECO:0000269|PubMed:24706459}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Joubert syndrome 9 (JBTS9) [MIM:612285]: A disorder
presenting with cerebellar ataxia, oculomotor apraxia, hypotonia,
neonatal breathing abnormalities and psychomotor delay.
Neuroradiologically, it is characterized by cerebellar vermian
hypoplasia/aplasia, thickened and reoriented superior cerebellar
peduncles, and an abnormally large interpeduncular fossa, giving
the appearance of a molar tooth on transaxial slices (molar tooth
sign). Additional variable features include retinal dystrophy and
renal disease. {ECO:0000269|PubMed:18387594,
ECO:0000269|PubMed:18950740, ECO:0000269|PubMed:19777577,
ECO:0000269|PubMed:22241855, ECO:0000269|PubMed:22246503,
ECO:0000269|PubMed:22425360, ECO:0000269|PubMed:23012439,
ECO:0000269|PubMed:26477546}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: COACH syndrome (COACHS) [MIM:216360]: A disorder
characterized by mental retardation, ataxia due to cerebellar
hypoplasia, and hepatic fibrosis. Patients present the molar tooth
sign, a midbrain-hindbrain malformation pathognomonic for Joubert
syndrome and related disorders. Other features, such as coloboma
and renal cysts, may be variable. {ECO:0000269|PubMed:19574260}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAI03711.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA92583.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14710.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; EU450799; ACC96081.1; -; mRNA.
EMBL; AB037766; BAA92583.1; ALT_INIT; mRNA.
EMBL; AC007016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC116651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471069; EAW92734.1; -; Genomic_DNA.
EMBL; BC053865; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC070395; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC103710; AAI03711.1; ALT_SEQ; mRNA.
EMBL; AK023876; BAB14710.1; ALT_SEQ; mRNA.
CCDS; CCDS47026.1; -. [Q9P2K1-4]
CCDS; CCDS47027.2; -. [Q9P2K1-5]
CCDS; CCDS54744.1; -. [Q9P2K1-6]
RefSeq; NP_001073991.2; NM_001080522.2. [Q9P2K1-4]
RefSeq; NP_001158192.1; NM_001164720.1. [Q9P2K1-6]
RefSeq; NP_065836.2; NM_020785.2. [Q9P2K1-5]
RefSeq; XP_005248234.1; XM_005248177.1. [Q9P2K1-4]
RefSeq; XP_011512176.1; XM_011513874.2. [Q9P2K1-6]
UniGene; Hs.590928; -.
ProteinModelPortal; Q9P2K1; -.
SMR; Q9P2K1; -.
BioGrid; 121603; 36.
CORUM; Q9P2K1; -.
IntAct; Q9P2K1; 35.
STRING; 9606.ENSP00000398391; -.
iPTMnet; Q9P2K1; -.
PhosphoSitePlus; Q9P2K1; -.
BioMuta; CC2D2A; -.
DMDM; 229462975; -.
EPD; Q9P2K1; -.
MaxQB; Q9P2K1; -.
PaxDb; Q9P2K1; -.
PeptideAtlas; Q9P2K1; -.
PRIDE; Q9P2K1; -.
Ensembl; ENST00000424120; ENSP00000403465; ENSG00000048342. [Q9P2K1-4]
Ensembl; ENST00000438599; ENSP00000401154; ENSG00000048342. [Q9P2K1-5]
Ensembl; ENST00000503292; ENSP00000421809; ENSG00000048342. [Q9P2K1-4]
Ensembl; ENST00000503658; ENSP00000426846; ENSG00000048342. [Q9P2K1-5]
Ensembl; ENST00000507954; ENSP00000427221; ENSG00000048342. [Q9P2K1-6]
Ensembl; ENST00000515124; ENSP00000424368; ENSG00000048342. [Q9P2K1-6]
GeneID; 57545; -.
KEGG; hsa:57545; -.
UCSC; uc003gnq.5; human. [Q9P2K1-4]
CTD; 57545; -.
DisGeNET; 57545; -.
EuPathDB; HostDB:ENSG00000048342.15; -.
GeneCards; CC2D2A; -.
GeneReviews; CC2D2A; -.
HGNC; HGNC:29253; CC2D2A.
HPA; HPA044124; -.
MalaCards; CC2D2A; -.
MIM; 216360; phenotype.
MIM; 612013; gene.
MIM; 612284; phenotype.
MIM; 612285; phenotype.
neXtProt; NX_Q9P2K1; -.
OpenTargets; ENSG00000048342; -.
Orphanet; 1454; Joubert syndrome with hepatic defect.
Orphanet; 2318; Joubert syndrome with oculorenal defect.
Orphanet; 564; Meckel syndrome.
PharmGKB; PA162381194; -.
eggNOG; KOG3639; Eukaryota.
eggNOG; ENOG410XQVY; LUCA.
GeneTree; ENSGT00510000046611; -.
HOGENOM; HOG000068028; -.
HOVERGEN; HBG107545; -.
InParanoid; Q9P2K1; -.
KO; K19352; -.
OMA; ERHWLGC; -.
OrthoDB; EOG091G0IID; -.
PhylomeDB; Q9P2K1; -.
TreeFam; TF324786; -.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
ChiTaRS; CC2D2A; human.
GeneWiki; CC2D2A; -.
GenomeRNAi; 57545; -.
PRO; PR:Q9P2K1; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000048342; -.
CleanEx; HS_CC2D2A; -.
ExpressionAtlas; Q9P2K1; baseline and differential.
Genevisible; Q9P2K1; HS.
GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
GO; GO:0035082; P:axoneme assembly; IEA:Ensembl.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
GO; GO:1904491; P:protein localization to ciliary transition zone; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
InterPro; IPR000008; C2_dom.
InterPro; IPR028928; CC2D2AN-C2.
Pfam; PF00168; C2; 1.
Pfam; PF15625; CC2D2AN-C2; 1.
SMART; SM00239; C2; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Ciliopathy; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Joubert syndrome;
Meckel syndrome; Polymorphism; Reference proteome.
CHAIN 1 1620 Coiled-coil and C2 domain-containing
protein 2A.
/FTId=PRO_0000317250.
DOMAIN 1062 1174 C2.
COILED 439 493 {ECO:0000255}.
COILED 532 582 {ECO:0000255}.
COMPBIAS 221 229 Poly-Glu.
COMPBIAS 591 596 Poly-Lys.
COMPBIAS 1491 1494 Poly-Ala.
VAR_SEQ 1 49 Missing (in isoform 2).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_030923.
VAR_SEQ 42 122 PPTAVPKEMVSEKSHLGNPQEPVQEEPKTRLLSMTVRRGPR
SLPPIPSTSRTGFAEFSMRGRMREKLQAARSKAESALLQE
-> KPTPFSRACWQILPHLSAGVPLLGWEHPVQGKSFQATN
CCPQGNGVRKIPPWQPPGACAGGAQDPPPEYDSPERPTERA
GC (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045255.
VAR_SEQ 83 111 SLPPIPSTSRTGFAEFSMRGRMREKLQAA -> RELVVKKS
LGRPGTVTHVCNPSTLEGRGG (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045453.
VAR_SEQ 112 1620 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045454.
VAR_SEQ 123 1620 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045256.
VAR_SEQ 1199 1257 Missing (in isoform 2).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037223.
VARIANT 117 117 S -> R (in JBTS9; unknown pathological
significance; dbSNP:rs186264635).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076881.
VARIANT 376 376 E -> A (in dbSNP:rs16892095).
/FTId=VAR_038489.
VARIANT 507 507 K -> E (in JBTS9; unknown pathological
significance; dbSNP:rs144439937).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076882.
VARIANT 559 559 L -> P (in JBTS9; dbSNP:rs754221308).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076883.
VARIANT 660 660 V -> I (in dbSNP:rs16892134).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_038490.
VARIANT 684 684 L -> I (in dbSNP:rs190698163).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076884.
VARIANT 701 701 L -> V (in dbSNP:rs537906621).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076885.
VARIANT 721 721 P -> S (in JBTS9; dbSNP:rs199768782).
{ECO:0000269|PubMed:19777577}.
/FTId=VAR_062804.
VARIANT 800 800 K -> E (in dbSNP:rs751256652).
{ECO:0000269|PubMed:19777577}.
/FTId=VAR_062805.
VARIANT 1045 1045 V -> A (in JBTS9; dbSNP:rs863225173).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076886.
VARIANT 1096 1096 Q -> H (in JBTS9; dbSNP:rs863225169).
{ECO:0000269|PubMed:18950740,
ECO:0000269|PubMed:22241855}.
/FTId=VAR_055321.
VARIANT 1114 1114 T -> M (in MKS6 and JBTS9;
dbSNP:rs386833752).
{ECO:0000269|PubMed:19466712,
ECO:0000269|PubMed:19777577}.
/FTId=VAR_062293.
VARIANT 1116 1116 T -> M (in COACHS and JBTS9;
dbSNP:rs267606709).
{ECO:0000269|PubMed:19574260,
ECO:0000269|PubMed:22241855}.
/FTId=VAR_063804.
VARIANT 1122 1122 P -> S (in JBTS9; dbSNP:rs118204051).
{ECO:0000269|PubMed:18950740,
ECO:0000269|PubMed:22241855}.
/FTId=VAR_055322.
VARIANT 1126 1126 E -> K (in JBTS9).
{ECO:0000269|PubMed:22425360,
ECO:0000269|PubMed:23012439,
ECO:0000269|PubMed:26477546}.
/FTId=VAR_068169.
VARIANT 1151 1151 V -> A (in JBTS9; dbSNP:rs863225170).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076887.
VARIANT 1182 1182 W -> R (in JBTS9; dbSNP:rs386833755).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075698.
VARIANT 1284 1284 R -> C (in JBTS9; dbSNP:rs779823379).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076888.
VARIANT 1284 1284 R -> H (in JBTS9; dbSNP:rs754586025).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076889.
VARIANT 1330 1330 R -> Q (in JBTS9; unknown pathological
significance; dbSNP:rs763486732).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076890.
VARIANT 1430 1430 V -> A (in JBTS9; dbSNP:rs863225168).
{ECO:0000269|PubMed:22241855}.
/FTId=VAR_076891.
VARIANT 1447 1447 E -> A (in JBTS9; digenic inheritance;
the patient also carries mutation C-360
in CEP41; dbSNP:rs387907058).
{ECO:0000269|PubMed:22246503}.
/FTId=VAR_067535.
VARIANT 1517 1517 T -> S (in MKS6; unknown pathological
significance; dbSNP:rs780673487).
{ECO:0000269|PubMed:24706459}.
/FTId=VAR_077560.
VARIANT 1520 1520 N -> S (in JBTS9).
{ECO:0000269|PubMed:23012439,
ECO:0000269|PubMed:26477546}.
/FTId=VAR_069045.
VARIANT 1528 1528 R -> C (in JBTS9 and COACHS;
dbSNP:rs118204052).
{ECO:0000269|PubMed:18950740,
ECO:0000269|PubMed:19574260,
ECO:0000269|PubMed:22241855}.
/FTId=VAR_055323.
VARIANT 1551 1551 L -> P (in JBTS9; dbSNP:rs763425007).
{ECO:0000269|PubMed:18950740}.
/FTId=VAR_055324.
VARIANT 1556 1556 D -> V (in JBTS9; dbSNP:rs201502401).
{ECO:0000269|PubMed:19777577,
ECO:0000269|PubMed:22241855,
ECO:0000269|PubMed:22425360,
ECO:0000269|PubMed:23012439,
ECO:0000269|PubMed:26477546}.
/FTId=VAR_062806.
VARIANT 1568 1568 Y -> H (in JBTS9).
{ECO:0000269|PubMed:23012439,
ECO:0000269|PubMed:26477546}.
/FTId=VAR_069046.
CONFLICT 524 524 R -> S (in Ref. 5; AAI03711).
{ECO:0000305}.
SEQUENCE 1620 AA; 186185 MW; 1AF2635A40B3EF4A CRC64;
MNPREEKVKI ITEEFIENDE DADMGRQNKN SKVRRQPRKK QPPTAVPKEM VSEKSHLGNP
QEPVQEEPKT RLLSMTVRRG PRSLPPIPST SRTGFAEFSM RGRMREKLQA ARSKAESALL
QEIPTPRPRR LRSPSKKELE TEFGTEPGKE VERTQQEVDS QSYSRVKFHD SARKIKPKPQ
VPPGFPSAEE AYNFFTFNFD PEPEGSEEKP KARHRAGTNQ EEEEGEEEEP PAQGGGKEMD
EEELLNGDDA EDFLLGLDHV ADDFVAVRPA DYESIHDRLQ MEREMLFIPS RQTVPTYKKL
PENVQPRFLE DEGLYTGVRP EVARTNQNIM ENRLLMQDPE RRWFGDDGRI LALPNPIKPF
PSRPPVLTQE QSIKAELETL YKKAVKYVHS SQHVIRSGDP PGNFQLDIDI SGLIFTHHPC
FSREHVLAAK LAQLYDQYLA RHQRNKAKFL TDKLQALRNA VQTGLDPEKP HQSLDTIQKT
INEYKSEIRQ TRKFRDAEQE KDRTLLKTII KVWKEMKSLR EFQRFTNTPL KLVLRKEKAD
QKADEEAYEA EIQAEISELL EEHTEEYAQK MEEYRTSLQQ WKAWRKVQRA KKKKRKQAAE
EHPGDEIAEP YPEEDLVKPS PPEPTDRAVI EQEVRERAAQ SRRRPWEPTL VPELSLAGSV
TPNDQCPRAE VSRREDVKKR SVYLKVLFNN KEVSRTVSRP LGADFRVHFG QIFNLQIVNW
PESLTLQVYE TVGHSSPTLL AEVFLPIPET TVVTGRAPTE EVEFSSNQHV TLDHEGVGSG
VPFSFEADGS NQLTLMTSGK VSHSVAWAIG ENGIPLIPPL SQQNIGFRSA LKKADAISSI
GTSGLTDMKK LAKWAAESKL DPNDPNNAPL MQLISVATSG ESYVPDFFRL EQLQQEFNFV
SDQELNRSKR FRLLHLRSQE VPEFRNYKQV PVYDREIMEK VFQDYEKRLR DRNVIETKEH
IDTHRAIVAK YLQQVRESVI NRFLIAKQYF LLADMIVEEE VPNISILGLS LFKLAEQKRP
LRPRRKGRKK VTAQNLSDGD IKLLVNIVRA YDIPVRKPAV SKFQQPSRSS RMFSEKHAAS
PSTYSPTHNA DYPLGQVLVR PFVEVSFQRT VCHTTTAEGP NPSWNEELEL PFRAPNGDYS
TASLQSVKDV VFINIFDEVL HDVLEDDRER GSGIHTRIER HWLGCVKMPF STIYFQARID
GTFKIDIPPV LLGYSKERNM ILERGFDSVR SLSEGSYITL FITIEPQLVP GESIREKFES
QEDEKLLQAT EKFQAECALK FPNRQCLTTV IDISGKTVFI TRYLKPLNPP QELLNVYPNN
LQATAELVAR YVSLIPFLPD TVSFGGICDL WSTSDQFLDL LAGDEEEHAV LLCNYFLSLG
KKAWLLMGNA IPEGPTAYVL TWEQGRYLIW NPCSGHFYGQ FDTFCPLKNV GCLIGPDNIW
FNIQRYESPL RINFDVTRPK LWKSFFSRSL PYPGLSSVQP EELIYQRSDK AAAAELQDRI
EKILKEKIMD WRPRHLTRWN RYCTSTLRHF LPLLEKSQGE DVEDDHRAEL LKQLGDYRFS
GFPLHMPYSE VKPLIDAVYS TGVHNIDVPN VEFALAVYIH PYPKNVLSVW IYVASLIRNR


Related products :

Catalog number Product name Quantity
EIAAB07128 C9orf49,CHCHD2P9,CHCHD9,Coiled-coil-helix-coiled-coil-helix domain-containing 2 pseudogene 9,Homo sapiens,Human,Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitocho
EIAAB46890 CCDC131,Coiled-coil domain-containing protein 131,Homo sapiens,Human,KIAA0546,Proline_serine-rich coiled-coil protein 2,PSRC2,ZFC3H1,Zinc finger C3H1 domain-containing protein
EIAAB06031 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,D19Ertd678e,mCyclon,MNCb-4327,Mouse,Mus musculus
EIAAB05828 C6orf184,C6orf185,CCDC162,CCDC162P,Coiled-coil domain-containing protein 162,Coiled-coil domain-containing protein 162 pseudogene,Homo sapiens,Human
EIAAB06030 CCDC86,Coiled-coil domain-containing protein 86,CYCLON,Cytokine-induced protein with coiled-coil domain,Homo sapiens,Human
EIAAB06029 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,Rat,Rattus norvegicus
EIAAB05061 Calcium-binding and coiled-coil domain-containing protein 1,Calcoco1,CocoA,Coiled-coil coactivator protein,Kiaa1536,Mouse,Mus musculus
EIAAB05058 Calcium-binding and coiled-coil domain-containing protein 1,CALCOCO1,Calphoglin,Coiled-coil coactivator protein,Homo sapiens,Human,KIAA1536,PP13275,Sarcoma antigen NY-SAR-3,UNQ2436_PRO4996
EIAAB05742 Ccdc115,Ccp1,Coiled-coil domain-containing protein 115,Coiled-coil protein 1,Mouse,Mus musculus
EIAAB07114 AAG10,Aging-associated gene 10 protein,C7orf17,CHCHD2,Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial,HCV NS2 trans-regulated protein,Homo sapiens,Human,NS2TP
EIAAB07126 CHCHD8,Coiled-coil-helix-coiled-coil-helix domain-containing protein 8,E2IG2,E2-induced gene 2 protein,Homo sapiens,Human
EIAAB07111 C22orf16,CHCHD10,Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial,Homo sapiens,Human,Protein N27C7-4
EIAAB11296 CCD1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,DIXDC1,Dixin,Homo sapiens,Human,KIAA1735
EIAAB07113 C10orf34,CHCHD1,Coiled-coil-helix-coiled-coil-helix domain-containing protein 1,Homo sapiens,Human,Nuclear protein C2360
EIAAB11295 Ccd1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,Dixdc1,Dixin,Kiaa1735,Mouse,Mus musculus
CSB-EL005324HU Human Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial(CHCHD9) ELISA kit SpeciesHuman 96T
CHCH3_BOVIN ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial; organism: Bovine; gene name: CHCHD3 96T
G5255 Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial (CHCHD9), Human, ELISA Kit 96T
CHCH3_HUMAN ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial; organism: Human; gene name: CHCHD3 96T
CHC10_HUMAN ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial; organism: Human; gene name: CHCHD10 96T
CHCH3_MOUSE ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial; organism: Mouse; gene name: Chchd3 96T
CSB-EL005324HU Human Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial(CHCHD9) ELISA kit 96T
CHCH2_MOUSE ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial; organism: Mouse; gene name: Chchd2 96T
CHCH2_HUMAN ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial; organism: Human; gene name: CHCHD2 96T
EIAAB11294 Ccd1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,Dixdc1,Dixin,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur