ID F161A_HUMAN Reviewed; 660 AA. AC Q3B820; B4DJV7; Q9H8R2; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 24-JAN-2024, entry version 137. DE RecName: Full=Protein FAM161A; GN Name=FAM161A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP MET-107. RC TISSUE=Colon endothelium, and Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 123-660 (ISOFORMS 1/2). RC TISSUE=Ovary, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-660 (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [6] RP INVOLVEMENT IN RP28, AND TISSUE SPECIFICITY. RX PubMed=20705278; DOI=10.1016/j.ajhg.2010.07.018; RA Langmann T., Di Gioia S.A., Rau I., Stohr H., Maksimovic N.S., Corbo J.C., RA Renner A.B., Zrenner E., Kumaramanickavel G., Karlstetter M., RA Arsenijevic Y., Weber B.H., Gal A., Rivolta C.; RT "Nonsense mutations in FAM161A cause RP28-associated recessive retinitis RT pigmentosa."; RL Am. J. Hum. Genet. 87:376-381(2010). RN [7] RP INVOLVEMENT IN RP28, AND TISSUE SPECIFICITY. RX PubMed=20705279; DOI=10.1016/j.ajhg.2010.07.022; RA Bandah-Rozenfeld D., Mizrahi-Meissonnier L., Farhy C., Obolensky A., RA Chowers I., Pe'er J., Merin S., Ben-Yosef T., Ashery-Padan R., Banin E., RA Sharon D.; RT "Homozygosity mapping reveals null mutations in FAM161A as a cause of RT autosomal-recessive retinitis pigmentosa."; RL Am. J. Hum. Genet. 87:382-391(2010). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCA5; CEP290 AND RP SDCCAG8. RX PubMed=22940612; DOI=10.1093/hmg/dds368; RA Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D., RA Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.; RT "FAM161A, associated with retinitis pigmentosa, is a component of the RT cilia-basal body complex and interacts with proteins involved in RT ciliopathies."; RL Hum. Mol. Genet. 21:5174-5184(2012). RN [9] RP INTERACTION WITH MICROTUBULES AND FAM161B. RX PubMed=22791751; DOI=10.1093/hmg/dds268; RA Zach F., Grassmann F., Langmann T., Sorusch N., Wolfrum U., Stohr H.; RT "The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein RT involved in intermolecular protein interaction and microtubule RT association."; RL Hum. Mol. Genet. 21:4573-4586(2012). RN [10] RP INTERACTION WITH POC1B. RX PubMed=25018096; DOI=10.1016/j.ajhg.2014.06.012; RA Roosing S., Lamers I.J., de Vrieze E., van den Born L.I., Lambertus S., RA Arts H.H., Peters T.A., Hoyng C.B., Kremer H., Hetterschijt L., RA Letteboer S.J., van Wijk E., Roepman R., den Hollander A.I., Cremers F.P., RA Boldt K., de Baere E., Klaver C.C., Coppieters F., Koolen D.A., RA Lugtenberg D., Neveling K., van Reeuwijk J., Ueffing M., van Beersum S.E., RA Zonneveld-Vrieling M.N.; RT "Disruption of the basal body protein POC1B results in autosomal-recessive RT cone-rod dystrophy."; RL Am. J. Hum. Genet. 95:131-142(2014). RN [11] RP INTERACTION WITH CEP78. RX PubMed=27588451; DOI=10.1016/j.ajhg.2016.07.009; RA Nikopoulos K., Farinelli P., Giangreco B., Tsika C., Royer-Bertrand B., RA Mbefo M.K., Bedoni N., Kjellstroem U., El Zaoui I., Di Gioia S.A., RA Balzano S., Cisarova K., Messina A., Decembrini S., Plainis S., RA Blazaki S.V., Khan M.I., Micheal S., Boldt K., Ueffing M., Moulin A.P., RA Cremers F.P., Roepman R., Arsenijevic Y., Tsilimbaris M.K., Andreasson S., RA Rivolta C.; RT "Mutations in CEP78 cause cone-rod dystrophy and hearing loss associated RT with primary-cilia defects."; RL Am. J. Hum. Genet. 99:770-776(2016). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-468 AND LYS-484, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [13] RP INTERACTION WITH CFAP418, AND TISSUE SPECIFICITY. RX PubMed=36233334; DOI=10.3390/ijms231912033; RA Liu Y., Chen J., Sager R., Sasaki E., Hu H.; RT "Interactions between C8orf37 and FAM161A, Two Ciliary Proteins Essential RT for Photoreceptor Survival."; RL Int. J. Mol. Sci. 23:12033-12033(2022). RN [14] RP VARIANT RP28 315-LYS--HIS-660 DEL. RX PubMed=31236346; DOI=10.18240/ijo.2019.06.06; RA Hu Y.S., Song H., Li Y., Xiao Z.Y., Li T.; RT "Whole-exome sequencing identifies novel mutations in genes responsible for RT retinitis pigmentosa in 2 nonconsanguineous Chinese families."; RL Int. J. Ophthalmol. 12:915-923(2019). CC -!- FUNCTION: Involved in ciliogenesis. {ECO:0000269|PubMed:22940612}. CC -!- SUBUNIT: Interacts (via central region) with CFAP418 (via N-terminus); CC the interaction is direct (PubMed:36233334). Interacts (via C-terminus) CC with microtubules (PubMed:22791751). Interacts with LCA5 CC (PubMed:22940612). Interacts with CEP290 (PubMed:22940612). Interacts CC with SDCCAG8 (PubMed:22940612). Interacts with FAM161B CC (PubMed:22791751). Interacts with POC1B (PubMed:25018096). Interacts CC with CEP78 (PubMed:27588451). {ECO:0000269|PubMed:22791751, CC ECO:0000269|PubMed:22940612, ECO:0000269|PubMed:25018096, CC ECO:0000269|PubMed:27588451, ECO:0000269|PubMed:36233334}. CC -!- INTERACTION: CC Q3B820; P29972: AQP1; NbExp=3; IntAct=EBI-719941, EBI-745213; CC Q3B820; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-719941, EBI-4400025; CC Q3B820; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-719941, EBI-1642333; CC Q3B820; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-719941, EBI-742722; CC Q3B820; Q5T5X7: BEND3; NbExp=3; IntAct=EBI-719941, EBI-1211496; CC Q3B820; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-719941, EBI-724373; CC Q3B820; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-719941, EBI-11975051; CC Q3B820; A2RRN7: CADPS; NbExp=6; IntAct=EBI-719941, EBI-10179719; CC Q3B820; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-719941, EBI-749920; CC Q3B820; Q13137: CALCOCO2; NbExp=6; IntAct=EBI-719941, EBI-739580; CC Q3B820; Q9H257: CARD9; NbExp=4; IntAct=EBI-719941, EBI-751319; CC Q3B820; Q9H257-2: CARD9; NbExp=6; IntAct=EBI-719941, EBI-11530605; CC Q3B820; Q8NA61: CBY2; NbExp=3; IntAct=EBI-719941, EBI-741724; CC Q3B820; Q8NA61-2: CBY2; NbExp=5; IntAct=EBI-719941, EBI-11524851; CC Q3B820; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-719941, EBI-10171570; CC Q3B820; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-719941, EBI-11977221; CC Q3B820; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-719941, EBI-10961312; CC Q3B820; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-719941, EBI-10171416; CC Q3B820; Q8N715: CCDC185; NbExp=3; IntAct=EBI-719941, EBI-740814; CC Q3B820; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-719941, EBI-2808286; CC Q3B820; Q2TAC2-2: CCDC57; NbExp=6; IntAct=EBI-719941, EBI-10961624; CC Q3B820; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-719941, EBI-347573; CC Q3B820; P24863: CCNC; NbExp=3; IntAct=EBI-719941, EBI-395261; CC Q3B820; O95273: CCNDBP1; NbExp=5; IntAct=EBI-719941, EBI-748961; CC Q3B820; Q01850: CDR2; NbExp=6; IntAct=EBI-719941, EBI-1181367; CC Q3B820; Q86X02: CDR2L; NbExp=3; IntAct=EBI-719941, EBI-11063830; CC Q3B820; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-719941, EBI-744115; CC Q3B820; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-719941, EBI-10181988; CC Q3B820; Q96MT8: CEP63; NbExp=3; IntAct=EBI-719941, EBI-741977; CC Q3B820; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-719941, EBI-11522539; CC Q3B820; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-719941, EBI-739624; CC Q3B820; Q9P209: CEP72; NbExp=3; IntAct=EBI-719941, EBI-739498; CC Q3B820; Q96NL8: CFAP418; NbExp=5; IntAct=EBI-719941, EBI-11904873; CC Q3B820; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-719941, EBI-11962928; CC Q3B820; Q7L7V1: DHX32; NbExp=9; IntAct=EBI-719941, EBI-2807297; CC Q3B820; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-719941, EBI-10174653; CC Q3B820; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-719941, EBI-10174566; CC Q3B820; O60447: EVI5; NbExp=3; IntAct=EBI-719941, EBI-852291; CC Q3B820; Q3B820: FAM161A; NbExp=4; IntAct=EBI-719941, EBI-719941; CC Q3B820; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-719941, EBI-10175124; CC Q3B820; A1L4K1: FSD2; NbExp=3; IntAct=EBI-719941, EBI-5661036; CC Q3B820; P51114-2: FXR1; NbExp=3; IntAct=EBI-719941, EBI-11022345; CC Q3B820; O95995: GAS8; NbExp=3; IntAct=EBI-719941, EBI-1052570; CC Q3B820; Q08379: GOLGA2; NbExp=5; IntAct=EBI-719941, EBI-618309; CC Q3B820; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-719941, EBI-5916454; CC Q3B820; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-719941, EBI-2349758; CC Q3B820; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-719941, EBI-11519926; CC Q3B820; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-719941, EBI-717919; CC Q3B820; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-719941, EBI-5460660; CC Q3B820; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-719941, EBI-2549423; CC Q3B820; Q9UJC3: HOOK1; NbExp=5; IntAct=EBI-719941, EBI-746704; CC Q3B820; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-719941, EBI-10961706; CC Q3B820; Q13422: IKZF1; NbExp=3; IntAct=EBI-719941, EBI-745305; CC Q3B820; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-719941, EBI-769401; CC Q3B820; O75564-2: JRK; NbExp=3; IntAct=EBI-719941, EBI-17181882; CC Q3B820; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-719941, EBI-2556193; CC Q3B820; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-719941, EBI-749265; CC Q3B820; Q92993: KAT5; NbExp=3; IntAct=EBI-719941, EBI-399080; CC Q3B820; O60341: KDM1A; NbExp=3; IntAct=EBI-719941, EBI-710124; CC Q3B820; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-719941, EBI-2805604; CC Q3B820; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-719941, EBI-3437878; CC Q3B820; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-719941, EBI-14069005; CC Q3B820; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-719941, EBI-10172290; CC Q3B820; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-719941, EBI-10171774; CC Q3B820; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-719941, EBI-10172052; CC Q3B820; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-719941, EBI-14065470; CC Q3B820; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-719941, EBI-11987425; CC Q3B820; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-719941, EBI-3958099; CC Q3B820; O95751: LDOC1; NbExp=3; IntAct=EBI-719941, EBI-740738; CC Q3B820; P02545: LMNA; NbExp=3; IntAct=EBI-719941, EBI-351935; CC Q3B820; Q8IV03: LURAP1L; NbExp=3; IntAct=EBI-719941, EBI-12898559; CC Q3B820; Q9Y250: LZTS1; NbExp=5; IntAct=EBI-719941, EBI-1216080; CC Q3B820; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-719941, EBI-741037; CC Q3B820; P43364: MAGEA11; NbExp=3; IntAct=EBI-719941, EBI-739552; CC Q3B820; P23508: MCC; NbExp=3; IntAct=EBI-719941, EBI-307531; CC Q3B820; Q14566: MCM6; NbExp=3; IntAct=EBI-719941, EBI-374900; CC Q3B820; Q99750: MDFI; NbExp=6; IntAct=EBI-719941, EBI-724076; CC Q3B820; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-719941, EBI-10172526; CC Q3B820; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-719941, EBI-2548751; CC Q3B820; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-719941, EBI-373524; CC Q3B820; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-719941, EBI-742948; CC Q3B820; Q5JR59-3: MTUS2; NbExp=5; IntAct=EBI-719941, EBI-11522433; CC Q3B820; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-719941, EBI-10172876; CC Q3B820; Q9Y2I6: NINL; NbExp=3; IntAct=EBI-719941, EBI-719716; CC Q3B820; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-719941, EBI-10178410; CC Q3B820; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-719941, EBI-1051317; CC Q3B820; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-719941, EBI-1105124; CC Q3B820; Q8TBR0: PDE4DIP; NbExp=3; IntAct=EBI-719941, EBI-10240575; CC Q3B820; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-719941, EBI-713786; CC Q3B820; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-719941, EBI-14066006; CC Q3B820; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-719941, EBI-79165; CC Q3B820; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-719941, EBI-949255; CC Q3B820; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-719941, EBI-302345; CC Q3B820; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-719941, EBI-302355; CC Q3B820; Q8NA72: POC5; NbExp=6; IntAct=EBI-719941, EBI-2561090; CC Q3B820; Q8NA72-3: POC5; NbExp=3; IntAct=EBI-719941, EBI-11751537; CC Q3B820; Q13136: PPFIA1; NbExp=5; IntAct=EBI-719941, EBI-745426; CC Q3B820; Q969Q6: PPP2R3C; NbExp=3; IntAct=EBI-719941, EBI-2561661; CC Q3B820; P31321: PRKAR1B; NbExp=3; IntAct=EBI-719941, EBI-2805516; CC Q3B820; P47897: QARS1; NbExp=3; IntAct=EBI-719941, EBI-347462; CC Q3B820; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-719941, EBI-726876; CC Q3B820; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-719941, EBI-1378139; CC Q3B820; Q92622: RUBCN; NbExp=3; IntAct=EBI-719941, EBI-2952709; CC Q3B820; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-719941, EBI-747225; CC Q3B820; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-719941, EBI-748391; CC Q3B820; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-719941, EBI-358489; CC Q3B820; O94964-4: SOGA1; NbExp=3; IntAct=EBI-719941, EBI-14083835; CC Q3B820; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-719941, EBI-5235340; CC Q3B820; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-719941, EBI-2212028; CC Q3B820; O75558: STX11; NbExp=3; IntAct=EBI-719941, EBI-714135; CC Q3B820; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-719941, EBI-6872807; CC Q3B820; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-719941, EBI-529518; CC Q3B820; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-719941, EBI-1644036; CC Q3B820; Q9UBB9: TFIP11; NbExp=9; IntAct=EBI-719941, EBI-1105213; CC Q3B820; Q15025: TNIP1; NbExp=6; IntAct=EBI-719941, EBI-357849; CC Q3B820; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-719941, EBI-2509913; CC Q3B820; Q13077: TRAF1; NbExp=5; IntAct=EBI-719941, EBI-359224; CC Q3B820; Q12933: TRAF2; NbExp=3; IntAct=EBI-719941, EBI-355744; CC Q3B820; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-719941, EBI-492476; CC Q3B820; Q9C019: TRIM15; NbExp=3; IntAct=EBI-719941, EBI-2342111; CC Q3B820; P14373: TRIM27; NbExp=3; IntAct=EBI-719941, EBI-719493; CC Q3B820; O94972: TRIM37; NbExp=3; IntAct=EBI-719941, EBI-741602; CC Q3B820; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-719941, EBI-725997; CC Q3B820; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-719941, EBI-2130429; CC Q3B820; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-719941, EBI-11525489; CC Q3B820; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-719941, EBI-6116822; CC Q3B820; P08670: VIM; NbExp=3; IntAct=EBI-719941, EBI-353844; CC Q3B820; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-719941, EBI-2799833; CC Q3B820; Q9Y2K1: ZBTB1; NbExp=6; IntAct=EBI-719941, EBI-2682961; CC Q3B820; O43829: ZBTB14; NbExp=3; IntAct=EBI-719941, EBI-10176632; CC Q3B820; O43298: ZBTB43; NbExp=3; IntAct=EBI-719941, EBI-740718; CC Q3B820; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-719941, EBI-742740; CC Q3B820; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-719941, EBI-11962760; CC Q3B820; P17028: ZNF24; NbExp=3; IntAct=EBI-719941, EBI-707773; CC Q3B820; P15622-3: ZNF250; NbExp=3; IntAct=EBI-719941, EBI-10177272; CC Q3B820; Q8N554: ZNF276; NbExp=3; IntAct=EBI-719941, EBI-750821; CC Q3B820; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-719941, EBI-743265; CC Q3B820; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-719941, EBI-11035148; CC Q3B820; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-719941, EBI-10240849; CC Q3B820; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-719941, EBI-527853; CC Q3B820; O43309: ZSCAN12; NbExp=3; IntAct=EBI-719941, EBI-1210440; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000269|PubMed:22940612}. Cell projection, cilium CC {ECO:0000269|PubMed:22940612}. Note=Localized to the region between the CC outer and inner photoreceptor segments, corresponding to the CC photoreceptor connecting cilium. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3B820-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3B820-2; Sequence=VSP_032935; CC Name=3; CC IsoId=Q3B820-3; Sequence=VSP_039126; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed with CC highest levels in retina and testis, with isoform 1 being the most CC abundant in all tissues tested. {ECO:0000269|PubMed:20705278, CC ECO:0000269|PubMed:20705279, ECO:0000269|PubMed:36233334}. CC -!- DISEASE: Retinitis pigmentosa 28 (RP28) [MIM:606068]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:20705278, CC ECO:0000269|PubMed:20705279, ECO:0000269|PubMed:31236346}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the FAM161 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG58969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX648834; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BX649029; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC107081; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK023367; BAB14544.1; -; mRNA. DR EMBL; AK296255; BAG58969.1; ALT_INIT; mRNA. DR EMBL; BC107162; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC107163; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS42687.2; -. [Q3B820-1] DR CCDS; CCDS56120.1; -. [Q3B820-3] DR RefSeq; NP_001188472.1; NM_001201543.1. [Q3B820-3] DR RefSeq; NP_115556.2; NM_032180.2. [Q3B820-1] DR RefSeq; XP_016860561.1; XM_017005072.1. DR AlphaFoldDB; Q3B820; -. DR SMR; Q3B820; -. DR BioGRID; 123909; 156. DR IntAct; Q3B820; 149. DR MINT; Q3B820; -. DR STRING; 9606.ENSP00000385158; -. DR GlyGen; Q3B820; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3B820; -. DR PhosphoSitePlus; Q3B820; -. DR BioMuta; FAM161A; -. DR DMDM; 182705173; -. DR EPD; Q3B820; -. DR jPOST; Q3B820; -. DR MassIVE; Q3B820; -. DR MaxQB; Q3B820; -. DR PaxDb; 9606-ENSP00000385158; -. DR PeptideAtlas; Q3B820; -. DR ProteomicsDB; 61665; -. [Q3B820-1] DR ProteomicsDB; 61666; -. [Q3B820-2] DR ProteomicsDB; 61667; -. [Q3B820-3] DR Antibodypedia; 30688; 86 antibodies from 11 providers. DR DNASU; 84140; -. DR Ensembl; ENST00000404929.6; ENSP00000385158.1; ENSG00000170264.13. [Q3B820-3] DR Ensembl; ENST00000405894.3; ENSP00000385893.3; ENSG00000170264.13. [Q3B820-1] DR GeneID; 84140; -. DR KEGG; hsa:84140; -. DR MANE-Select; ENST00000404929.6; ENSP00000385158.1; NM_001201543.2; NP_001188472.1. [Q3B820-3] DR UCSC; uc002sbm.5; human. [Q3B820-1] DR AGR; HGNC:25808; -. DR CTD; 84140; -. DR DisGeNET; 84140; -. DR GeneCards; FAM161A; -. DR GeneReviews; FAM161A; -. DR HGNC; HGNC:25808; FAM161A. DR HPA; ENSG00000170264; Tissue enriched (retina). DR MalaCards; FAM161A; -. DR MIM; 606068; phenotype. DR MIM; 613596; gene. DR neXtProt; NX_Q3B820; -. DR OpenTargets; ENSG00000170264; -. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA162386876; -. DR VEuPathDB; HostDB:ENSG00000170264; -. DR eggNOG; ENOG502QRC3; Eukaryota. DR GeneTree; ENSGT00940000157824; -. DR HOGENOM; CLU_010955_0_1_1; -. DR InParanoid; Q3B820; -. DR OMA; HIKNMWK; -. DR OrthoDB; 4340341at2759; -. DR PhylomeDB; Q3B820; -. DR TreeFam; TF321199; -. DR PathwayCommons; Q3B820; -. DR SignaLink; Q3B820; -. DR BioGRID-ORCS; 84140; 14 hits in 1155 CRISPR screens. DR ChiTaRS; FAM161A; human. DR GenomeRNAi; 84140; -. DR Pharos; Q3B820; Tbio. DR PRO; PR:Q3B820; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q3B820; Protein. DR Bgee; ENSG00000170264; Expressed in pigmented layer of retina and 146 other cell types or tissues. DR ExpressionAtlas; Q3B820; baseline and differential. DR GO; GO:0000235; C:astral microtubule; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0044782; P:cilium organization; IBA:GO_Central. DR GO; GO:1901985; P:positive regulation of protein acetylation; IDA:UniProtKB. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR InterPro; IPR019579; FAM161A/B. DR PANTHER; PTHR21501:SF3; PROTEIN FAM161A; 1. DR PANTHER; PTHR21501; UNCHARACTERIZED; 1. DR Pfam; PF10595; FAM161A_B; 1. DR Genevisible; Q3B820; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Isopeptide bond; Reference proteome; Retinitis pigmentosa; KW Sensory transduction; Ubl conjugation; Vision. FT CHAIN 1..660 FT /note="Protein FAM161A" FT /id="PRO_0000329052" FT REGION 341..525 FT /note="Required for interaction with CFAP418" FT /evidence="ECO:0000269|PubMed:36233334" FT REGION 605..660 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 93..120 FT /evidence="ECO:0000255" FT COILED 296..320 FT /evidence="ECO:0000255" FT COILED 522..552 FT /evidence="ECO:0000255" FT COMPBIAS 605..629 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..660 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 468 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 484 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..109 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032935" FT VAR_SEQ 527 FT /note="V -> VRRSLEEKKMLEEERNRILTKQKQRMKELQKLLTTRAKAYDSHQSLA FT QISKSRVKCL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_039126" FT VARIANT 107 FT /note="I -> M (in dbSNP:rs11125895)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_060180" FT VARIANT 236 FT /note="I -> V (in dbSNP:rs17513722)" FT /id="VAR_042630" FT VARIANT 273 FT /note="E -> K (in dbSNP:rs6733774)" FT /id="VAR_042631" FT VARIANT 315..660 FT /note="Missing (in RP28)" FT /evidence="ECO:0000269|PubMed:31236346" FT /id="VAR_083934" FT CONFLICT 145 FT /note="E -> G (in Ref. 1; BX648834)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="S -> F (in Ref. 3; BAB14544)" FT /evidence="ECO:0000305" FT CONFLICT 534 FT /note="R -> M (in Ref. 3; BAG58969)" FT /evidence="ECO:0000305" SQ 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 //