ID   C102B_HUMAN             Reviewed;         513 AA.
AC   Q68D86; A1A4H1; Q7Z467; Q8NDK7; Q9H5C1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 4.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Coiled-coil domain-containing protein 102B;
GN   Name=CCDC102B; Synonyms=C18orf14;
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), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 189-513 (ISOFORM 2), AND VARIANTS ASN-153 AND
RP   ARG-298.
RC   TISSUE=Salivary gland, and Testis;
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=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-513 (ISOFORM 1).
RC   TISSUE=Lung;
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   [5]
RP   FUNCTION, INTERACTION WITH CEP250; CROCC; LRRC45 AND NEK2, SUBCELLULAR
RP   LOCATION, PHOSPHORYLATION AT SER-21; SER-22; SER-34; SER-135; SER-142;
RP   SER-194; SER-210; SER-401; SER-404 AND SER-406, AND MUTAGENESIS OF SER-21;
RP   SER-22; SER-34; SER-135; SER-142; SER-194; SER-210; SER-401; SER-404 AND
RP   SER-406.
RX   PubMed=30404835; DOI=10.1242/jcs.222901;
RA   Xia Y., Huang N., Chen Z., Li F., Fan G., Ma D., Chen J., Teng J.;
RT   "CCDC102B functions in centrosome linker assembly and centrosome
RT   cohesion.";
RL   J. Cell Sci. 131:0-0(2018).
CC   -!- FUNCTION: During interphase, forms fibers at the proximal ends of
CC       centrioles to maintain centrosome cohesion (PubMed:30404835). During
CC       mitosis, dissociates from the centrosome following phosphorylation to
CC       allow centrosome separation (PubMed:30404835). Contributes to
CC       CROCC/rootletin filament formation (PubMed:30404835).
CC       {ECO:0000269|PubMed:30404835}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with centriolar protein
CC       CEP250/CNAP1; the interaction results in recruitment of CCDC102B to the
CC       proximal ends of centrioles (PubMed:30404835). Interacts (via N-
CC       terminus) with CROCC/rootletin and LRRC45 (PubMed:30404835). Interacts
CC       (via N-terminus) with serine/threonine-protein kinase NEK2; the
CC       interaction results in phosphorylation of CCDC102B (PubMed:30404835).
CC       {ECO:0000269|PubMed:30404835}.
CC   -!- INTERACTION:
CC       Q68D86; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-10171570, EBI-743598;
CC       Q68D86; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-10171570, EBI-11096309;
CC       Q68D86; Q96MA6: AK8; NbExp=3; IntAct=EBI-10171570, EBI-8466265;
CC       Q68D86; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-10171570, EBI-5661893;
CC       Q68D86; P40617: ARL4A; NbExp=3; IntAct=EBI-10171570, EBI-2875746;
CC       Q68D86; P49703: ARL4D; NbExp=4; IntAct=EBI-10171570, EBI-711726;
CC       Q68D86; Q13895: BYSL; NbExp=6; IntAct=EBI-10171570, EBI-358049;
CC       Q68D86; A1L168: C20orf202; NbExp=3; IntAct=EBI-10171570, EBI-18396958;
CC       Q68D86; O00305: CACNB4; NbExp=3; IntAct=EBI-10171570, EBI-714838;
CC       Q68D86; P20807-4: CAPN3; NbExp=3; IntAct=EBI-10171570, EBI-11532021;
CC       Q68D86; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-10171570, EBI-744556;
CC       Q68D86; Q96HB5-4: CCDC120; NbExp=4; IntAct=EBI-10171570, EBI-10185348;
CC       Q68D86; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-10171570, EBI-10175300;
CC       Q68D86; Q07002: CDK18; NbExp=3; IntAct=EBI-10171570, EBI-746238;
CC       Q68D86; Q96LK0: CEP19; NbExp=6; IntAct=EBI-10171570, EBI-741885;
CC       Q68D86; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-10171570, EBI-10181988;
CC       Q68D86; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-10171570, EBI-5453285;
CC       Q68D86; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-10171570, EBI-11988027;
CC       Q68D86; Q96BY6: DOCK10; NbExp=3; IntAct=EBI-10171570, EBI-748520;
CC       Q68D86; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10171570, EBI-2349927;
CC       Q68D86; Q08426: EHHADH; NbExp=4; IntAct=EBI-10171570, EBI-2339219;
CC       Q68D86; Q9H0I2: ENKD1; NbExp=6; IntAct=EBI-10171570, EBI-744099;
CC       Q68D86; O00471: EXOC5; NbExp=3; IntAct=EBI-10171570, EBI-949824;
CC       Q68D86; Q3B820: FAM161A; NbExp=6; IntAct=EBI-10171570, EBI-719941;
CC       Q68D86; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-10171570, EBI-19153639;
CC       Q68D86; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-10171570, EBI-10244131;
CC       Q68D86; P07954: FH; NbExp=3; IntAct=EBI-10171570, EBI-1050358;
CC       Q68D86; O75955: FLOT1; NbExp=3; IntAct=EBI-10171570, EBI-603643;
CC       Q68D86; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-10171570, EBI-744935;
CC       Q68D86; P55040: GEM; NbExp=3; IntAct=EBI-10171570, EBI-744104;
CC       Q68D86; Q9HD26: GOPC; NbExp=3; IntAct=EBI-10171570, EBI-349832;
CC       Q68D86; Q9HD26-2: GOPC; NbExp=4; IntAct=EBI-10171570, EBI-11102276;
CC       Q68D86; Q9P0W2: HMG20B; NbExp=6; IntAct=EBI-10171570, EBI-713401;
CC       Q68D86; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-10171570, EBI-747204;
CC       Q68D86; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10171570, EBI-2125614;
CC       Q68D86; O00505: KPNA3; NbExp=3; IntAct=EBI-10171570, EBI-358297;
CC       Q68D86; O95678: KRT75; NbExp=3; IntAct=EBI-10171570, EBI-2949715;
CC       Q68D86; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-10171570, EBI-10241252;
CC       Q68D86; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-10171570, EBI-726510;
CC       Q68D86; P61968: LMO4; NbExp=6; IntAct=EBI-10171570, EBI-2798728;
CC       Q68D86; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-10171570, EBI-739832;
CC       Q68D86; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-10171570, EBI-1216080;
CC       Q68D86; Q9Y586: MAB21L2; NbExp=3; IntAct=EBI-10171570, EBI-6659161;
CC       Q68D86; Q96A72: MAGOHB; NbExp=6; IntAct=EBI-10171570, EBI-746778;
CC       Q68D86; P33993: MCM7; NbExp=3; IntAct=EBI-10171570, EBI-355924;
CC       Q68D86; P50221: MEOX1; NbExp=3; IntAct=EBI-10171570, EBI-2864512;
CC       Q68D86; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10171570, EBI-16439278;
CC       Q68D86; P55081: MFAP1; NbExp=3; IntAct=EBI-10171570, EBI-1048159;
CC       Q68D86; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-10171570, EBI-14086479;
CC       Q68D86; P00540: MOS; NbExp=3; IntAct=EBI-10171570, EBI-1757866;
CC       Q68D86; P35548: MSX2; NbExp=3; IntAct=EBI-10171570, EBI-6447480;
CC       Q68D86; Q9GZT8: NIF3L1; NbExp=6; IntAct=EBI-10171570, EBI-740897;
CC       Q68D86; O00746: NME4; NbExp=3; IntAct=EBI-10171570, EBI-744871;
CC       Q68D86; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-10171570, EBI-741158;
CC       Q68D86; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-10171570, EBI-752122;
CC       Q68D86; Q16877: PFKFB4; NbExp=3; IntAct=EBI-10171570, EBI-764534;
CC       Q68D86; Q9BSU1: PHAF1; NbExp=5; IntAct=EBI-10171570, EBI-946080;
CC       Q68D86; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10171570, EBI-79165;
CC       Q68D86; Q96PV4: PNMA5; NbExp=8; IntAct=EBI-10171570, EBI-10171633;
CC       Q68D86; P01189: POMC; NbExp=3; IntAct=EBI-10171570, EBI-12219503;
CC       Q68D86; Q969H6: POP5; NbExp=6; IntAct=EBI-10171570, EBI-366525;
CC       Q68D86; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-10171570, EBI-1105153;
CC       Q68D86; Q6NYC8: PPP1R18; NbExp=6; IntAct=EBI-10171570, EBI-2557469;
CC       Q68D86; Q99633: PRPF18; NbExp=3; IntAct=EBI-10171570, EBI-2798416;
CC       Q68D86; P25786: PSMA1; NbExp=6; IntAct=EBI-10171570, EBI-359352;
CC       Q68D86; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-10171570, EBI-3437896;
CC       Q68D86; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-10171570, EBI-743428;
CC       Q68D86; Q9UHP6: RSPH14; NbExp=6; IntAct=EBI-10171570, EBI-748350;
CC       Q68D86; Q9BWD3: RTL8A; NbExp=3; IntAct=EBI-10171570, EBI-741643;
CC       Q68D86; Q17RB0: RTL8B; NbExp=3; IntAct=EBI-10171570, EBI-10238588;
CC       Q68D86; A6ZKI3: RTL8C; NbExp=3; IntAct=EBI-10171570, EBI-10174072;
CC       Q68D86; O00560: SDCBP; NbExp=3; IntAct=EBI-10171570, EBI-727004;
CC       Q68D86; P31947: SFN; NbExp=3; IntAct=EBI-10171570, EBI-476295;
CC       Q68D86; Q96ES7: SGF29; NbExp=3; IntAct=EBI-10171570, EBI-743117;
CC       Q68D86; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-10171570, EBI-2130111;
CC       Q68D86; Q9GZT3: SLIRP; NbExp=3; IntAct=EBI-10171570, EBI-1050793;
CC       Q68D86; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-10171570, EBI-358489;
CC       Q68D86; O95295: SNAPIN; NbExp=3; IntAct=EBI-10171570, EBI-296723;
CC       Q68D86; O60504: SORBS3; NbExp=3; IntAct=EBI-10171570, EBI-741237;
CC       Q68D86; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-10171570, EBI-11334239;
CC       Q68D86; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-10171570, EBI-744066;
CC       Q68D86; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-10171570, EBI-742688;
CC       Q68D86; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-10171570, EBI-6872807;
CC       Q68D86; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-10171570, EBI-745392;
CC       Q68D86; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10171570, EBI-11955057;
CC       Q68D86; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-10171570, EBI-3923210;
CC       Q68D86; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10171570, EBI-1105213;
CC       Q68D86; P19237: TNNI1; NbExp=3; IntAct=EBI-10171570, EBI-746692;
CC       Q68D86; Q5VU62: TPM3; NbExp=3; IntAct=EBI-10171570, EBI-10184033;
CC       Q68D86; P14373: TRIM27; NbExp=6; IntAct=EBI-10171570, EBI-719493;
CC       Q68D86; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-10171570, EBI-2130429;
CC       Q68D86; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-10171570, EBI-10241197;
CC       Q68D86; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-10171570, EBI-9090990;
CC       Q68D86; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-10171570, EBI-2799833;
CC       Q68D86; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-10171570, EBI-10188476;
CC       Q68D86; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-10171570, EBI-12287587;
CC       Q68D86; Q53FD0-2: ZC2HC1C; NbExp=6; IntAct=EBI-10171570, EBI-14104088;
CC       Q68D86; P17024: ZNF20; NbExp=6; IntAct=EBI-10171570, EBI-717634;
CC       Q68D86; P15622-3: ZNF250; NbExp=3; IntAct=EBI-10171570, EBI-10177272;
CC       Q68D86; Q7Z3I7: ZNF572; NbExp=6; IntAct=EBI-10171570, EBI-10172590;
CC       Q68D86; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10171570, EBI-4395669;
CC       Q68D86; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-10171570, EBI-4395732;
CC       Q68D86; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-10171570, EBI-10251462;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000269|PubMed:30404835}.
CC       Note=Concentrated at the proximal ends of centrioles where it forms
CC       fibers (PubMed:30404835). Centrosomal localization becomes weak when
CC       cells enter prophase and is significantly decreased in metaphase
CC       (PubMed:30404835). {ECO:0000269|PubMed:30404835}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q68D86-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68D86-2; Sequence=VSP_014688, VSP_014689;
CC   -!- PTM: Phosphorylated directly or indirectly by NEK2 during mitosis which
CC       causes dissociation of CCDC102B from the centrosome and allows for
CC       centrosome separation. {ECO:0000269|PubMed:30404835}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56269.1; Type=Miscellaneous discrepancy; Note=wrong intron-exon boundaries.; Evidence={ECO:0000305};
CC       Sequence=AAI26449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI26451.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15706.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD38721.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD38721.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR749520; CAH18334.2; -; mRNA.
DR   EMBL; AL833863; CAD38721.2; ALT_SEQ; mRNA.
DR   EMBL; AC022035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC056269; AAH56269.1; ALT_SEQ; mRNA.
DR   EMBL; BC126448; AAI26449.1; ALT_INIT; mRNA.
DR   EMBL; BC126450; AAI26451.1; ALT_INIT; mRNA.
DR   EMBL; AK027247; BAB15706.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11996.2; -. [Q68D86-1]
DR   RefSeq; NP_001087198.1; NM_001093729.1. [Q68D86-1]
DR   RefSeq; NP_079057.2; NM_024781.2. [Q68D86-1]
DR   RefSeq; XP_016881464.1; XM_017025975.1.
DR   AlphaFoldDB; Q68D86; -.
DR   SMR; Q68D86; -.
DR   BioGRID; 122930; 151.
DR   IntAct; Q68D86; 149.
DR   STRING; 9606.ENSP00000353377; -.
DR   iPTMnet; Q68D86; -.
DR   PhosphoSitePlus; Q68D86; -.
DR   BioMuta; CCDC102B; -.
DR   DMDM; 215274243; -.
DR   EPD; Q68D86; -.
DR   jPOST; Q68D86; -.
DR   MassIVE; Q68D86; -.
DR   MaxQB; Q68D86; -.
DR   PaxDb; 9606-ENSP00000353377; -.
DR   PeptideAtlas; Q68D86; -.
DR   ProteomicsDB; 66059; -. [Q68D86-1]
DR   ProteomicsDB; 66060; -. [Q68D86-2]
DR   Antibodypedia; 49098; 146 antibodies from 22 providers.
DR   DNASU; 79839; -.
DR   Ensembl; ENST00000360242.9; ENSP00000353377.5; ENSG00000150636.17. [Q68D86-1]
DR   Ensembl; ENST00000584156.5; ENSP00000463111.1; ENSG00000150636.17. [Q68D86-2]
DR   GeneID; 79839; -.
DR   KEGG; hsa:79839; -.
DR   MANE-Select; ENST00000360242.9; ENSP00000353377.5; NM_024781.3; NP_079057.3.
DR   UCSC; uc002lki.2; human. [Q68D86-1]
DR   AGR; HGNC:26295; -.
DR   CTD; 79839; -.
DR   DisGeNET; 79839; -.
DR   GeneCards; CCDC102B; -.
DR   HGNC; HGNC:26295; CCDC102B.
DR   HPA; ENSG00000150636; Tissue enhanced (placenta).
DR   neXtProt; NX_Q68D86; -.
DR   OpenTargets; ENSG00000150636; -.
DR   PharmGKB; PA134948675; -.
DR   VEuPathDB; HostDB:ENSG00000150636; -.
DR   eggNOG; ENOG502QSJ6; Eukaryota.
DR   GeneTree; ENSGT00940000163731; -.
DR   HOGENOM; CLU_033486_2_0_1; -.
DR   InParanoid; Q68D86; -.
DR   OMA; DWDICEE; -.
DR   OrthoDB; 3028315at2759; -.
DR   PhylomeDB; Q68D86; -.
DR   TreeFam; TF320856; -.
DR   PathwayCommons; Q68D86; -.
DR   SignaLink; Q68D86; -.
DR   BioGRID-ORCS; 79839; 18 hits in 1151 CRISPR screens.
DR   ChiTaRS; CCDC102B; human.
DR   GenomeRNAi; 79839; -.
DR   Pharos; Q68D86; Tbio.
DR   PRO; PR:Q68D86; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q68D86; Protein.
DR   Bgee; ENSG00000150636; Expressed in sural nerve and 121 other cell types or tissues.
DR   ExpressionAtlas; Q68D86; baseline and differential.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0120283; F:protein serine/threonine kinase binding; IPI:UniProtKB.
DR   GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR   PANTHER; PTHR46292; COILED-COIL DOMAIN-CONTAINING PROTEIN 102A; 1.
DR   PANTHER; PTHR46292:SF2; COILED-COIL DOMAIN-CONTAINING PROTEIN 102B; 1.
DR   Genevisible; Q68D86; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..513
FT                   /note="Coiled-coil domain-containing protein 102B"
FT                   /id="PRO_0000079308"
FT   REGION          1..217
FT                   /note="Required for centriolar localization and for
FT                   interaction with CEP250, CROCC, LRRC45 and NEK2"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   REGION          493..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..142
FT                   /evidence="ECO:0000255"
FT   COILED          268..337
FT                   /evidence="ECO:0000255"
FT   COILED          363..513
FT                   /evidence="ECO:0000255"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         404
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   VAR_SEQ         479..483
FT                   /note="LDDSL -> VLLYE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014688"
FT   VAR_SEQ         484..513
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014689"
FT   VARIANT         153
FT                   /note="K -> N (in dbSNP:rs572020)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_047331"
FT   VARIANT         298
FT                   /note="K -> R (in dbSNP:rs2187094)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_047332"
FT   VARIANT         346
FT                   /note="C -> F (in dbSNP:rs745894)"
FT                   /id="VAR_022893"
FT   VARIANT         370
FT                   /note="E -> G (in dbSNP:rs34102373)"
FT                   /id="VAR_047333"
FT   VARIANT         425
FT                   /note="N -> K (in dbSNP:rs17080065)"
FT                   /id="VAR_047334"
FT   VARIANT         429
FT                   /note="A -> P (in dbSNP:rs9963788)"
FT                   /id="VAR_022894"
FT   MUTAGEN         21
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-22, A-34, A-135, A-142, A-194, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         22
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-34, A-135, A-142, A-194, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         34
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-135, A-142, A-194, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         135
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-142, A-194, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         142
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-194, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         194
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-142, A-210,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         210
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-142, A-194,
FT                   A-401, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         401
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-142, A-194,
FT                   A-210, A-404 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         404
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-142, A-194,
FT                   A-210, A-401 and A-406."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   MUTAGEN         406
FT                   /note="S->A: Substantial decrease in phosphorylation; when
FT                   associated with A-21, A-22, A-34, A-135, A-142, A-194,
FT                   A-210, A-401 and A-404."
FT                   /evidence="ECO:0000269|PubMed:30404835"
FT   CONFLICT        131
FT                   /note="M -> T (in Ref. 1; CAH18334)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="R -> G (in Ref. 1; CAH18334)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="K -> R (in Ref. 1; CAH18334)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  60448 MW;  450D36A80D6D88C8 CRC64;
     MNLDSIHRLI EETQIFQMQQ SSIKSRGDMV APASPPRDTC NTCFPLHGLQ SHAAHNFCAH
     SYNTNKWDIC EELRLRELEE VKARAAQMEK TMRWWSDCTA NWREKWSKVR AERNSAREEG
     RQLRIKLEMA MKELSTLKKK QSLPPQKEAL EAKVTQDLKL PGFVEESCEH TDQFQLSSQM
     HESIREYLVK RQFSTKEDTN NKEQGVVIDS LKLSEEMKPN LDGVDLFNNG GSGNGETKTG
     LRLKAINLPL ENEVTEISAL QVHLDEFQKI LWKEREMRTA LEKEIERLES ALSLWKWKYE
     ELKESKPKNV KEFDILLGQH NDEMQELSGN IKEESKSQNS KDRVICELRA ELERLQAENT
     SEWDKREILE REKQGLEREN RRLKIQVKEM EELLDKKNRL SANSQSPDFK MSQIDLQEKN
     QELLNLQHAY YKLNRQYQAN IAELTHANNR VDQNEAEVKK LRLRVEELKQ GLNQKEDELD
     DSLNQIRKLQ RSLDEEKERN ENLETELRHL QNW
//