POC1B_HUMAN
ID POC1B_HUMAN Reviewed; 478 AA.
AC Q8TC44; G3V1X0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=POC1 centriolar protein homolog B {ECO:0000305};
DE AltName: Full=Pix1;
DE AltName: Full=Proteome of centriole protein 1B;
DE AltName: Full=WD repeat-containing protein 51B;
GN Name=POC1B {ECO:0000312|HGNC:HGNC:30836}; Synonyms=WDR51B;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 SUBCELLULAR LOCATION.
RX PubMed=18068700; DOI=10.1016/j.yexcr.2007.10.019;
RA Hames R.S., Hames R., Prosser S.L., Euteneuer U., Lopes C.A., Moore W.,
RA Woodland H.R., Fry A.M.;
RT "Pix1 and Pix2 are novel WD40 microtubule-associated proteins that
RT colocalize with mitochondria in Xenopus germ plasm and centrosomes in human
RT cells.";
RL Exp. Cell Res. 314:574-589(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20008567; DOI=10.1083/jcb.200908019;
RA Pearson C.G., Osborn D.P., Giddings T.H. Jr., Beales P.L., Winey M.;
RT "Basal body stability and ciliogenesis requires the conserved component
RT Poc1.";
RL J. Cell Biol. 187:905-920(2009).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19109428; DOI=10.1091/mbc.e08-06-0619;
RA Keller L.C., Geimer S., Romijn E., Yates J. III, Zamora I., Marshall W.F.;
RT "Molecular architecture of the centriole proteome: the conserved WD40
RT domain protein POC1 is required for centriole duplication and length
RT control.";
RL Mol. Biol. Cell 20:1150-1166(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POC1A, AND
RP PHOSPHORYLATION.
RX PubMed=23015594; DOI=10.1242/jcs.111203;
RA Venoux M., Tait X., Hames R.S., Straatman K.R., Woodland H.R., Fry A.M.;
RT "Poc1A and Poc1B act together in human cells to ensure centriole
RT integrity.";
RL J. Cell Sci. 126:163-175(2013).
RN [11]
RP INTERACTION WITH FAM161A, INVOLVEMENT IN CORD20, VARIANTS CORD20 GLN-67 DEL
RP AND PRO-106, AND CHARACTERIZATION OF VARIANTS CORD20 GLN-67 DEL AND
RP PRO-106.
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 [12]
RP FUNCTION, TISSUE SPECIFICITY, AND VARIANT CORD20 PRO-106.
RX PubMed=25044745; DOI=10.1002/humu.22618;
RA Beck B.B., Phillips J.B., Bartram M.P., Wegner J., Thoenes M., Pannes A.,
RA Sampson J., Heller R., Goebel H., Koerber F., Neugebauer A., Hedergott A.,
RA Nuernberg G., Nuernberg P., Thiele H., Altmueller J., Toliat M.R.,
RA Staubach S., Boycott K.M., Valente E.M., Janecke A.R., Eisenberger T.,
RA Bergmann C., Tebbe L., Wang Y., Wu Y., Fry A.M., Westerfield M.,
RA Wolfrum U., Bolz H.J.;
RT "Mutation of POC1B in a severe syndromic retinal ciliopathy.";
RL Hum. Mutat. 35:1153-1162(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP44.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
RN [14]
RP VARIANT CORD20 PRO-106.
RX PubMed=24945461; DOI=10.1001/jamaophthalmol.2014.1658;
RA Durlu Y.K., Koeroglu C., Tolun A.;
RT "Novel recessive cone-rod dystrophy caused by POC1B mutation.";
RL JAMA Ophthalmol. 132:1185-1191(2014).
CC -!- FUNCTION: Plays an important role in centriole assembly and/or
CC stability and ciliogenesis (PubMed:20008567, PubMed:32060285). Involved
CC in early steps of centriole duplication, as well as in the later steps
CC of centriole length control (PubMed:19109428). Acts in concert with
CC POC1A to ensure centriole integrity and proper mitotic spindle
CC formation (PubMed:32060285). Required for primary cilia formation,
CC ciliary length and also cell proliferation (PubMed:23015594). Required
CC for retinal integrity (PubMed:25044745). {ECO:0000269|PubMed:19109428,
CC ECO:0000269|PubMed:20008567, ECO:0000269|PubMed:23015594,
CC ECO:0000269|PubMed:25044745, ECO:0000269|PubMed:32060285}.
CC -!- SUBUNIT: Interacts with POC1A (PubMed:23015594). Interacts with FAM161A
CC (PubMed:25018096). Interacts with CEP44; the interaction is direct and
CC recruits POC1B to centriolar microtubules (PubMed:32060285).
CC {ECO:0000269|PubMed:23015594, ECO:0000269|PubMed:25018096,
CC ECO:0000269|PubMed:32060285}.
CC -!- INTERACTION:
CC Q8TC44; Q9Y266: NUDC; NbExp=3; IntAct=EBI-1176274, EBI-357298;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:23015594,
CC ECO:0000269|PubMed:32060285}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:20008567}. Cytoplasm, cytoskeleton, spindle
CC pole. Note=Component of both mother and daughter centrioles
CC (PubMed:32060285). Localizes to the basal body and centriole adjacent
CC to the connecting cilium of photoreceptors and in synapses of the outer
CC plexiform layer. {ECO:0000250|UniProtKB:Q8BHD1,
CC ECO:0000269|PubMed:32060285}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TC44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TC44-2; Sequence=VSP_047066;
CC -!- TISSUE SPECIFICITY: Expressed in the retina.
CC {ECO:0000269|PubMed:25044745}.
CC -!- PTM: Phosphorylated in mitotic cells that may be mediated by CDK1.
CC {ECO:0000269|PubMed:23015594}.
CC -!- DISEASE: Cone-rod dystrophy 20 (CORD20) [MIM:615973]: A form of cone-
CC rod dystrophy, an inherited retinal dystrophy characterized by retinal
CC pigment deposits visible on fundus examination, predominantly in the
CC macular region, and initial loss of cone photoreceptors followed by rod
CC degeneration. This leads to decreased visual acuity and sensitivity in
CC the central visual field, followed by loss of peripheral vision. Severe
CC loss of vision occurs earlier than in retinitis pigmentosa, due to cone
CC photoreceptors degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:24945461, ECO:0000269|PubMed:25018096,
CC ECO:0000269|PubMed:25044745}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat POC1 family. {ECO:0000305}.
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DR EMBL; AK074772; BAC11198.1; -; mRNA.
DR EMBL; AC010201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97425.1; -; Genomic_DNA.
DR EMBL; BC026080; AAH26080.1; -; mRNA.
DR CCDS; CCDS31869.1; -. [Q8TC44-1]
DR CCDS; CCDS55859.1; -. [Q8TC44-2]
DR RefSeq; NP_001186706.1; NM_001199777.1. [Q8TC44-2]
DR RefSeq; NP_758440.1; NM_172240.2. [Q8TC44-1]
DR AlphaFoldDB; Q8TC44; -.
DR SMR; Q8TC44; -.
DR BioGRID; 129421; 72.
DR IntAct; Q8TC44; 49.
DR MINT; Q8TC44; -.
DR STRING; 9606.ENSP00000323302; -.
DR iPTMnet; Q8TC44; -.
DR PhosphoSitePlus; Q8TC44; -.
DR BioMuta; POC1B; -.
DR DMDM; 74762610; -.
DR EPD; Q8TC44; -.
DR jPOST; Q8TC44; -.
DR MassIVE; Q8TC44; -.
DR MaxQB; Q8TC44; -.
DR PaxDb; Q8TC44; -.
DR PeptideAtlas; Q8TC44; -.
DR PRIDE; Q8TC44; -.
DR ProteomicsDB; 32464; -.
DR ProteomicsDB; 74088; -. [Q8TC44-1]
DR Antibodypedia; 29964; 117 antibodies from 21 providers.
DR DNASU; 282809; -.
DR Ensembl; ENST00000313546.8; ENSP00000323302.3; ENSG00000139323.14. [Q8TC44-1]
DR Ensembl; ENST00000549035.1; ENSP00000447916.1; ENSG00000139323.14. [Q8TC44-2]
DR GeneID; 282809; -.
DR KEGG; hsa:282809; -.
DR MANE-Select; ENST00000313546.8; ENSP00000323302.3; NM_172240.3; NP_758440.1.
DR UCSC; uc001tba.4; human. [Q8TC44-1]
DR CTD; 282809; -.
DR DisGeNET; 282809; -.
DR GeneCards; POC1B; -.
DR GeneReviews; POC1B; -.
DR HGNC; HGNC:30836; POC1B.
DR HPA; ENSG00000139323; Low tissue specificity.
DR MalaCards; POC1B; -.
DR MIM; 614784; gene.
DR MIM; 615973; phenotype.
DR neXtProt; NX_Q8TC44; -.
DR OpenTargets; ENSG00000139323; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA165513299; -.
DR VEuPathDB; HostDB:ENSG00000139323; -.
DR eggNOG; ENOG502QSVJ; Eukaryota.
DR GeneTree; ENSGT00940000160413; -.
DR HOGENOM; CLU_000288_57_17_1; -.
DR InParanoid; Q8TC44; -.
DR OMA; HYKAHEA; -.
DR PhylomeDB; Q8TC44; -.
DR TreeFam; TF324210; -.
DR PathwayCommons; Q8TC44; -.
DR SignaLink; Q8TC44; -.
DR BioGRID-ORCS; 282809; 35 hits in 1077 CRISPR screens.
DR ChiTaRS; POC1B; human.
DR GenomeRNAi; 282809; -.
DR Pharos; Q8TC44; Tbio.
DR PRO; PR:Q8TC44; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TC44; protein.
DR Bgee; ENSG00000139323; Expressed in epithelial cell of pancreas and 179 other tissues.
DR ExpressionAtlas; Q8TC44; baseline and differential.
DR Genevisible; Q8TC44; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Coiled coil; Cone-rod dystrophy; Cytoplasm; Cytoskeleton; Disease variant;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..478
FT /note="POC1 centriolar protein homolog B"
FT /id="PRO_0000051410"
FT REPEAT 16..55
FT /note="WD 1"
FT REPEAT 58..99
FT /note="WD 2"
FT REPEAT 101..139
FT /note="WD 3"
FT REPEAT 142..181
FT /note="WD 4"
FT REPEAT 183..223
FT /note="WD 5"
FT REPEAT 226..265
FT /note="WD 6"
FT REPEAT 268..307
FT /note="WD 7"
FT COILED 431..470
FT /evidence="ECO:0000255"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047066"
FT VARIANT 67
FT /note="Missing (in CORD20; disrupts interaction with
FT FAM161A; localization of the mutant is cytosolic without
FT enrichment at specific subcellular sites;
FT dbSNP:rs587777693)"
FT /evidence="ECO:0000269|PubMed:25018096"
FT /id="VAR_071916"
FT VARIANT 106
FT /note="R -> P (in CORD20; disrupts interaction with
FT FAM161A; localization of the mutant is cytosolic without
FT enrichment at specific subcellular sites;
FT dbSNP:rs76216585)"
FT /evidence="ECO:0000269|PubMed:24945461,
FT ECO:0000269|PubMed:25018096, ECO:0000269|PubMed:25044745"
FT /id="VAR_071917"
SQ SEQUENCE 478 AA; 53668 MW; 1D93DBBE05A603E8 CRC64;
MASATEDPVL ERYFKGHKAA ITSLDLSPNG KQLATASWDT FLMLWNFKPH ARAYRYVGHK
DVVTSVQFSP HGNLLASASR DRTVRLWIPD KRGKFSEFKA HTAPVRSVDF SADGQFLATA
SEDKSIKVWS MYRQRFLYSL YRHTHWVRCA KFSPDGRLIV SCSEDKTIKI WDTTNKQCVN
NFSDSVGFAN FVDFNPSGTC IASAGSDQTV KVWDVRVNKL LQHYQVHSGG VNCISFHPSG
NYLITASSDG TLKILDLLEG RLIYTLQGHT GPVFTVSFSK GGELFASGGA DTQVLLWRTN
FDELHCKGLT KRNLKRLHFD SPPHLLDIYP RTPHPHEEKV ETVEINPKLE VIDLQISTPP
VMDILSFDST TTTETSGRTL PDKGEEACGY FLNPSLMSPE CLPTTTKKKT EDMSDLPCES
QRSIPLAVTD ALEHIMEQLN VLTQTVSILE QRLTLTEDKL KDCLENQQKL FSAVQQKS
