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Protein FAM161A

 F161A_HUMAN             Reviewed;         660 AA.
Q3B820; B4DJV7; Q9H8R2;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 2.
27-SEP-2017, entry version 101.
RecName: Full=Protein FAM161A;
Name=FAM161A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
MET-107.
TISSUE=Colon endothelium, and Retina;
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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-660 (ISOFORMS 1/2).
TISSUE=Ovary, and Thalamus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-660 (ISOFORM 1).
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).
[5]
INVOLVEMENT IN RP28, AND TISSUE SPECIFICITY.
PubMed=20705278; DOI=10.1016/j.ajhg.2010.07.018;
Langmann T., Di Gioia S.A., Rau I., Stohr H., Maksimovic N.S.,
Corbo J.C., Renner A.B., Zrenner E., Kumaramanickavel G.,
Karlstetter M., Arsenijevic Y., Weber B.H., Gal A., Rivolta C.;
"Nonsense mutations in FAM161A cause RP28-associated recessive
retinitis pigmentosa.";
Am. J. Hum. Genet. 87:376-381(2010).
[6]
INVOLVEMENT IN RP28, AND TISSUE SPECIFICITY.
PubMed=20705279; DOI=10.1016/j.ajhg.2010.07.022;
Bandah-Rozenfeld D., Mizrahi-Meissonnier L., Farhy C., Obolensky A.,
Chowers I., Pe'er J., Merin S., Ben-Yosef T., Ashery-Padan R.,
Banin E., Sharon D.;
"Homozygosity mapping reveals null mutations in FAM161A as a cause of
autosomal-recessive retinitis pigmentosa.";
Am. J. Hum. Genet. 87:382-391(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCA5; CEP290 AND
SDCCAG8.
PubMed=22940612; DOI=10.1093/hmg/dds368;
Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D.,
Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.;
"FAM161A, associated with retinitis pigmentosa, is a component of the
cilia-basal body complex and interacts with proteins involved in
ciliopathies.";
Hum. Mol. Genet. 21:5174-5184(2012).
[8]
INTERACTION WITH MICROTUBULES AND FAM161B.
PubMed=22791751; DOI=10.1093/hmg/dds268;
Zach F., Grassmann F., Langmann T., Sorusch N., Wolfrum U., Stohr H.;
"The retinitis pigmentosa 28 protein FAM161A is a novel ciliary
protein involved in intermolecular protein interaction and microtubule
association.";
Hum. Mol. Genet. 21:4573-4586(2012).
[9]
INTERACTION WITH POC1B.
PubMed=25018096; DOI=10.1016/j.ajhg.2014.06.012;
Roosing S., Lamers I.J., de Vrieze E., van den Born L.I.,
Lambertus S., Arts H.H., Peters T.A., Hoyng C.B., Kremer H.,
Hetterschijt L., Letteboer S.J., van Wijk E., Roepman R.,
den Hollander A.I., Cremers F.P., Boldt K., de Baere E., Klaver C.C.,
Coppieters F., Koolen D.A., Lugtenberg D., Neveling K.,
van Reeuwijk J., Ueffing M., van Beersum S.E.,
Zonneveld-Vrieling M.N.;
"Disruption of the basal body protein POC1B results in autosomal-
recessive cone-rod dystrophy.";
Am. J. Hum. Genet. 95:131-142(2014).
[10]
INTERACTION WITH CEP78.
PubMed=27588451; DOI=10.1016/j.ajhg.2016.07.009;
Nikopoulos K., Farinelli P., Giangreco B., Tsika C.,
Royer-Bertrand B., Mbefo M.K., Bedoni N., Kjellstroem U., El Zaoui I.,
Di Gioia S.A., Balzano S., Cisarova K., Messina A., Decembrini S.,
Plainis S., Blazaki S.V., Khan M.I., Micheal S., Boldt K., Ueffing M.,
Moulin A.P., Cremers F.P., Roepman R., Arsenijevic Y.,
Tsilimbaris M.K., Andreasson S., Rivolta C.;
"Mutations in CEP78 cause cone-rod dystrophy and hearing loss
associated with primary-cilia defects.";
Am. J. Hum. Genet. 99:770-776(2016).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-468 AND LYS-484, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Involved in ciliogenesis. {ECO:0000269|PubMed:22940612}.
-!- SUBUNIT: Interacts (via C-terminus) with microtubules. Interacts
with LCA5, CEP290 and SDCCAG8. Interacts with FAM161B. Interacts
with POC1B. Interacts with CEP78 (PubMed:27588451).
{ECO:0000269|PubMed:22791751, ECO:0000269|PubMed:22940612,
ECO:0000269|PubMed:25018096, ECO:0000269|PubMed:27588451}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-719941, EBI-719941;
Q5T5X7:BEND3; NbExp=3; IntAct=EBI-719941, EBI-1211496;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-719941, EBI-724373;
A2RRN7:CADPS; NbExp=7; IntAct=EBI-719941, EBI-10179719;
Q9P1Z2:CALCOCO1; NbExp=3; IntAct=EBI-719941, EBI-749920;
Q13137:CALCOCO2; NbExp=5; IntAct=EBI-719941, EBI-739580;
Q9H257:CARD9; NbExp=3; IntAct=EBI-719941, EBI-751319;
Q9H257-2:CARD9; NbExp=4; IntAct=EBI-719941, EBI-11530605;
Q68D86:CCDC102B; NbExp=5; IntAct=EBI-719941, EBI-10171570;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-719941, EBI-10171416;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-719941, EBI-749265;
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-719941, EBI-2808286;
Q2TAC2-2:CCDC57; NbExp=4; IntAct=EBI-719941, EBI-10961624;
O95273:CCNDBP1; NbExp=6; IntAct=EBI-719941, EBI-748961;
Q01850:CDR2; NbExp=5; IntAct=EBI-719941, EBI-1181367;
Q9C0F1:CEP44; NbExp=3; IntAct=EBI-719941, EBI-744115;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-719941, EBI-10181988;
Q96MT8:CEP63; NbExp=3; IntAct=EBI-719941, EBI-741977;
Q8NHQ1:CEP70; NbExp=7; IntAct=EBI-719941, EBI-739624;
Q7L7V1:DHX32; NbExp=7; IntAct=EBI-719941, EBI-2807297;
Q8NF50-2:DOCK8; NbExp=3; IntAct=EBI-719941, EBI-10174653;
A2ABF9:EHMT2; NbExp=3; IntAct=EBI-719941, EBI-10174566;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-719941, EBI-10175124;
A1L4K1:FSD2; NbExp=3; IntAct=EBI-719941, EBI-5661036;
Q08379:GOLGA2; NbExp=4; IntAct=EBI-719941, EBI-618309;
Q6NT76:HMBOX1; NbExp=7; IntAct=EBI-719941, EBI-2549423;
Q13422:IKZF1; NbExp=3; IntAct=EBI-719941, EBI-745305;
Q2KHM9:KIAA0753; NbExp=3; IntAct=EBI-719941, EBI-2805604;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-719941, EBI-10172290;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-719941, EBI-10172052;
P26371:KRTAP5-9; NbExp=5; IntAct=EBI-719941, EBI-3958099;
Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-719941, EBI-741037;
Q14566:MCM6; NbExp=3; IntAct=EBI-719941, EBI-374900;
Q99750:MDFI; NbExp=5; IntAct=EBI-719941, EBI-724076;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-719941, EBI-10172526;
Q8TD10:MIPOL1; NbExp=5; IntAct=EBI-719941, EBI-2548751;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-719941, EBI-742948;
Q5JR59-3:MTUS2; NbExp=4; IntAct=EBI-719941, EBI-11522433;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-719941, EBI-10172876;
Q9Y2I6:NINL; NbExp=3; IntAct=EBI-719941, EBI-719716;
Q86Y26:NUTM1; NbExp=3; IntAct=EBI-719941, EBI-10178410;
Q5VU43:PDE4DIP; NbExp=3; IntAct=EBI-719941, EBI-1105124;
Q8TBR0:PDE4DIP; NbExp=3; IntAct=EBI-719941, EBI-10240575;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-719941, EBI-713786;
Q9UL42:PNMA2; NbExp=3; IntAct=EBI-719941, EBI-302355;
Q8NA72:POC5; NbExp=4; IntAct=EBI-719941, EBI-2561090;
Q13136:PPFIA1; NbExp=3; IntAct=EBI-719941, EBI-745426;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-719941, EBI-726876;
Q59EK9:RUNDC3A; NbExp=3; IntAct=EBI-719941, EBI-747225;
Q8NA61:SPERT; NbExp=3; IntAct=EBI-719941, EBI-741724;
Q8NA61-2:SPERT; NbExp=6; IntAct=EBI-719941, EBI-11524851;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-719941, EBI-2212028;
O75558:STX11; NbExp=3; IntAct=EBI-719941, EBI-714135;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-719941, EBI-6872807;
Q9UBB9:TFIP11; NbExp=7; IntAct=EBI-719941, EBI-1105213;
O75069-4:TMCC2; NbExp=3; IntAct=EBI-719941, EBI-10177480;
Q15025:TNIP1; NbExp=5; IntAct=EBI-719941, EBI-357849;
Q13077:TRAF1; NbExp=5; IntAct=EBI-719941, EBI-359224;
Q12933:TRAF2; NbExp=4; IntAct=EBI-719941, EBI-355744;
Q9C019:TRIM15; NbExp=3; IntAct=EBI-719941, EBI-2342111;
O94972:TRIM37; NbExp=3; IntAct=EBI-719941, EBI-741602;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-719941, EBI-2130429;
Q8N3L3:TXLNB; NbExp=3; IntAct=EBI-719941, EBI-6116822;
Q9Y2K1:ZBTB1; NbExp=5; IntAct=EBI-719941, EBI-2682961;
O43829:ZBTB14; NbExp=3; IntAct=EBI-719941, EBI-10176632;
O43298:ZBTB43; NbExp=3; IntAct=EBI-719941, EBI-740718;
Q96BR9:ZBTB8A; NbExp=5; IntAct=EBI-719941, EBI-742740;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:22940612}. Cell projection, cilium
{ECO:0000269|PubMed:22940612}. Note=Localized to the region
between the outer and inner photoreceptor segments, corresponding
to the photoreceptor connecting cilium.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q3B820-1; Sequence=Displayed;
Name=2;
IsoId=Q3B820-2; Sequence=VSP_032935;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q3B820-3; Sequence=VSP_039126;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed
with highest levels in retina and testis, with isoform 1 being the
most abundant in all tissues tested. {ECO:0000269|PubMed:20705278,
ECO:0000269|PubMed:20705279}.
-!- DISEASE: Retinitis pigmentosa 28 (RP28) [MIM:606068]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:20705278,
ECO:0000269|PubMed:20705279}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FAM161 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG58969.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; BX648834; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX649029; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC107081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK023367; BAB14544.1; -; mRNA.
EMBL; AK296255; BAG58969.1; ALT_INIT; mRNA.
EMBL; BC107162; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC107163; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS42687.2; -. [Q3B820-1]
CCDS; CCDS56120.1; -. [Q3B820-3]
RefSeq; NP_001188472.1; NM_001201543.1. [Q3B820-3]
RefSeq; NP_115556.2; NM_032180.2. [Q3B820-1]
RefSeq; XP_016860561.1; XM_017005072.1. [Q3B820-2]
UniGene; Hs.440466; -.
ProteinModelPortal; Q3B820; -.
BioGrid; 123909; 70.
IntAct; Q3B820; 137.
iPTMnet; Q3B820; -.
PhosphoSitePlus; Q3B820; -.
BioMuta; FAM161A; -.
DMDM; 182705173; -.
EPD; Q3B820; -.
MaxQB; Q3B820; -.
PeptideAtlas; Q3B820; -.
PRIDE; Q3B820; -.
DNASU; 84140; -.
Ensembl; ENST00000404929; ENSP00000385158; ENSG00000170264. [Q3B820-3]
Ensembl; ENST00000405894; ENSP00000385893; ENSG00000170264. [Q3B820-1]
GeneID; 84140; -.
KEGG; hsa:84140; -.
UCSC; uc002sbm.5; human. [Q3B820-1]
CTD; 84140; -.
DisGeNET; 84140; -.
EuPathDB; HostDB:ENSG00000170264.12; -.
GeneCards; FAM161A; -.
GeneReviews; FAM161A; -.
H-InvDB; HIX0002084; -.
HGNC; HGNC:25808; FAM161A.
HPA; HPA032119; -.
MalaCards; FAM161A; -.
MIM; 606068; phenotype.
MIM; 613596; gene.
neXtProt; NX_Q3B820; -.
OpenTargets; ENSG00000170264; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA162386876; -.
GeneTree; ENSGT00530000063901; -.
HOGENOM; HOG000049209; -.
HOVERGEN; HBG107870; -.
InParanoid; Q3B820; -.
KO; K16772; -.
OMA; AEKHYSN; -.
OrthoDB; EOG091G054R; -.
PhylomeDB; Q3B820; -.
TreeFam; TF321199; -.
GenomeRNAi; 84140; -.
PRO; PR:Q3B820; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000170264; -.
CleanEx; HS_FAM161A; -.
ExpressionAtlas; Q3B820; baseline and differential.
Genevisible; Q3B820; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR019579; UPF0564.
Pfam; PF10595; UPF0564; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Ciliopathy; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Isopeptide bond; Polymorphism;
Reference proteome; Retinitis pigmentosa; Sensory transduction;
Ubl conjugation; Vision.
CHAIN 1 660 Protein FAM161A.
/FTId=PRO_0000329052.
COILED 93 120 {ECO:0000255}.
COILED 296 320 {ECO:0000255}.
COILED 522 552 {ECO:0000255}.
COMPBIAS 47 52 Poly-Glu.
COMPBIAS 609 658 Glu-rich.
CROSSLNK 468 468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 484 484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 109 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032935.
VAR_SEQ 527 527 V -> VRRSLEEKKMLEEERNRILTKQKQRMKELQKLLTTR
AKAYDSHQSLAQISKSRVKCL (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039126.
VARIANT 107 107 I -> M (in dbSNP:rs11125895).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_060180.
VARIANT 236 236 I -> V (in dbSNP:rs17513722).
/FTId=VAR_042630.
VARIANT 273 273 E -> K (in dbSNP:rs6733774).
/FTId=VAR_042631.
CONFLICT 145 145 E -> G (in Ref. 1; BX648834).
{ECO:0000305}.
CONFLICT 167 167 S -> F (in Ref. 3; BAB14544).
{ECO:0000305}.
CONFLICT 534 534 R -> M (in Ref. 3; BAG58969).
{ECO:0000305}.
SEQUENCE 660 AA; 76752 MW; E2C0D443C1A0DAA5 CRC64;
MATSHRVAKL VASSLQTPVN PITGARVAQY EREDPLKALA AAEAILEDEE EEKVAQPAGA
SADLNTSFSG VDEHAPISYE DFVNFPDIHH SNEEYFKKVE ELKAAHIETM AKLEKMYQDK
LHLKEVQPVV IREDSLSDSS RSVSEKNSYH PVSLMTSFSE PDLGQSSSLY VSSSEEELPN
LEKEYPRKNR MMTYAKELIN NMWTDFCVED YIRCKDTGFH AAEKRRKKRK EWVPTITVPE
PFQMMIREQK KKEESMKSKS DIEMVHKALK KQEEDPEYKK KFRANPVPAS VFLPLYHDLV
KQKEERRRSL KEKSKEALLA SQKPFKFIAR EEQKRAAREK QLRDFLKYKK KTNRFKARPI
PRSTYGSTTN DKLKEEELYR NLRTQLRAQE HLQNSSPLPC RSACGCRNPR CPEQAVKLKC
KHKVRCPTPD FEDLPERYQK HLSEHKSPKL LTVCKPFDLH ASPHASIKRE KILADIEADE
ENLKETRWPY LSPRRKSPVR CAGVNPVPCN CNPPVPTVSS RGREQAVRKS EKERMREYQR
ELEEREEKLK KRPLLFERVA QKNARMAAEK HYSNTLKALG ISDEFVSKKG QSGKVLEYFN
NQETKSVTED KESFNEEEKI EERENGEENY FIDTNSQDSY KEKDEANEES EEEKSVEESH


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