CCD92_HUMAN
ID CCD92_HUMAN Reviewed; 331 AA.
AC Q53HC0; B3KNQ0; Q9H697;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Coiled-coil domain-containing protein 92;
DE AltName: Full=Limkain beta-2;
GN Name=CCDC92;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Miyamoto K., Sumi T., Nakamura T.;
RT "Limkain beta 2 associates with the LIM domain of LIM kinase 2 and
RT localizes in the nucleus.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-253.
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [6]
RP INTERACTION WITH CEP164, AND SUBCELLULAR LOCATION.
RX PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA Hildebrandt F.;
RT "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT ciliopathies to DNA damage response signaling.";
RL Cell 150:533-548(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP PHOSPHORYLATION AT SER-209.
RX PubMed=32129703; DOI=10.1091/mbc.e19-06-0334;
RA Bernatik O., Pejskova P., Vyslouzil D., Hanakova K., Zdrahal Z.,
RA Cajanek L.;
RT "Phosphorylation of multiple proteins involved in ciliogenesis by Tau
RT Tubulin kinase 2.";
RL Mol. Biol. Cell 31:1032-1046(2020).
RN [9]
RP FUNCTION, INDUCTION BY INTERFERON, INTERACTION WITH EBOLAVIRUS PROTEIN NP
RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=32528005; DOI=10.1038/s41467-020-16768-7;
RA Kuroda M., Halfmann P.J., Hill-Batorski L., Ozawa M., Lopes T.J.S.,
RA Neumann G., Schoggins J.W., Rice C.M., Kawaoka Y.;
RT "Identification of interferon-stimulated genes that attenuate Ebola virus
RT infection.";
RL Nat. Commun. 11:2953-2953(2020).
CC -!- FUNCTION: Interferon-stimulated protein that plays a role in innate
CC immunity. Strongly inhibits ebolavirus transcription and replication.
CC Forms a complex with viral RNA-bound nucleocapsid NP and thereby
CC prevents the transport of NP to the cell surface.
CC {ECO:0000269|PubMed:32528005}.
CC -!- SUBUNIT: Interacts with CEP164. {ECO:0000269|PubMed:22863007}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein NP;
CC this interaction sequesters NP in the cytoplasm.
CC {ECO:0000269|PubMed:32528005}.
CC -!- INTERACTION:
CC Q53HC0; Q53HC0: CCDC92; NbExp=3; IntAct=EBI-719994, EBI-719994;
CC Q53HC0; Q9UPV0: CEP164; NbExp=5; IntAct=EBI-719994, EBI-3937015;
CC Q53HC0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-719994, EBI-742887;
CC Q53HC0; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-719994, EBI-11988027;
CC Q53HC0; Q14192: FHL2; NbExp=10; IntAct=EBI-719994, EBI-701903;
CC Q53HC0; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-719994, EBI-10175039;
CC Q53HC0; P14373: TRIM27; NbExp=3; IntAct=EBI-719994, EBI-719493;
CC Q53HC0; Q8N7C3: TRIML2; NbExp=6; IntAct=EBI-719994, EBI-11059915;
CC Q53HC0; P14079: tax; Xeno; NbExp=3; IntAct=EBI-719994, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:22863007}. Cytoplasm
CC {ECO:0000269|PubMed:32528005}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53HC0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53HC0-2; Sequence=VSP_056906;
CC -!- INDUCTION: Up to threefold after interferon treatment.
CC {ECO:0000269|PubMed:32528005}.
CC -!- PTM: Phosphorylated at Ser-209 by TTBK2. {ECO:0000269|PubMed:32129703}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB015292; BAB82436.1; -; mRNA.
DR EMBL; AK026124; BAB15366.1; -; mRNA.
DR EMBL; AK054680; BAG51412.1; -; mRNA.
DR EMBL; AK125866; BAG54259.1; -; mRNA.
DR EMBL; AK222661; BAD96381.1; ALT_INIT; mRNA.
DR EMBL; AC068790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017186; AAH17186.1; -; mRNA.
DR CCDS; CCDS76619.1; -. [Q53HC0-2]
DR CCDS; CCDS9256.1; -. [Q53HC0-1]
DR RefSeq; NP_001291886.1; NM_001304957.1. [Q53HC0-1]
DR RefSeq; NP_001291887.1; NM_001304958.1. [Q53HC0-1]
DR RefSeq; NP_001291888.1; NM_001304959.1. [Q53HC0-1]
DR RefSeq; NP_001291889.1; NM_001304960.1. [Q53HC0-1]
DR RefSeq; NP_001291890.1; NM_001304961.1. [Q53HC0-2]
DR RefSeq; NP_079416.1; NM_025140.2. [Q53HC0-1]
DR RefSeq; XP_005253681.1; XM_005253624.2. [Q53HC0-1]
DR RefSeq; XP_016875473.1; XM_017019984.1.
DR AlphaFoldDB; Q53HC0; -.
DR SMR; Q53HC0; -.
DR BioGRID; 123180; 57.
DR CORUM; Q53HC0; -.
DR IntAct; Q53HC0; 42.
DR MINT; Q53HC0; -.
DR STRING; 9606.ENSP00000238156; -.
DR iPTMnet; Q53HC0; -.
DR PhosphoSitePlus; Q53HC0; -.
DR BioMuta; CCDC92; -.
DR DMDM; 125863297; -.
DR EPD; Q53HC0; -.
DR jPOST; Q53HC0; -.
DR MassIVE; Q53HC0; -.
DR MaxQB; Q53HC0; -.
DR PaxDb; Q53HC0; -.
DR PeptideAtlas; Q53HC0; -.
DR PRIDE; Q53HC0; -.
DR ProteomicsDB; 3505; -.
DR ProteomicsDB; 62503; -. [Q53HC0-1]
DR Antibodypedia; 52615; 120 antibodies from 20 providers.
DR DNASU; 80212; -.
DR Ensembl; ENST00000238156.8; ENSP00000238156.3; ENSG00000119242.9. [Q53HC0-1]
DR Ensembl; ENST00000545135.5; ENSP00000439526.1; ENSG00000119242.9. [Q53HC0-2]
DR Ensembl; ENST00000545891.5; ENSP00000440024.1; ENSG00000119242.9. [Q53HC0-2]
DR Ensembl; ENST00000614047.2; ENSP00000479437.2; ENSG00000275035.2. [Q53HC0-2]
DR Ensembl; ENST00000631749.1; ENSP00000487695.1; ENSG00000275035.2. [Q53HC0-2]
DR Ensembl; ENST00000632401.1; ENSP00000488830.1; ENSG00000275035.2. [Q53HC0-1]
DR GeneID; 80212; -.
DR KEGG; hsa:80212; -.
DR MANE-Select; ENST00000238156.8; ENSP00000238156.3; NM_025140.3; NP_079416.1.
DR UCSC; uc001ufv.2; human. [Q53HC0-1]
DR CTD; 80212; -.
DR DisGeNET; 80212; -.
DR GeneCards; CCDC92; -.
DR HGNC; HGNC:29563; CCDC92.
DR HPA; ENSG00000119242; Low tissue specificity.
DR neXtProt; NX_Q53HC0; -.
DR OpenTargets; ENSG00000119242; -.
DR PharmGKB; PA144596459; -.
DR VEuPathDB; HostDB:ENSG00000119242; -.
DR eggNOG; ENOG502QQWS; Eukaryota.
DR GeneTree; ENSGT00430000031027; -.
DR HOGENOM; CLU_076253_0_0_1; -.
DR InParanoid; Q53HC0; -.
DR OMA; AHRIHHG; -.
DR OrthoDB; 1565079at2759; -.
DR PhylomeDB; Q53HC0; -.
DR TreeFam; TF329066; -.
DR PathwayCommons; Q53HC0; -.
DR SignaLink; Q53HC0; -.
DR BioGRID-ORCS; 80212; 19 hits in 1090 CRISPR screens.
DR ChiTaRS; CCDC92; human.
DR GenomeRNAi; 80212; -.
DR Pharos; Q53HC0; Tbio.
DR PRO; PR:Q53HC0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q53HC0; protein.
DR Bgee; ENSG00000119242; Expressed in anterior cingulate cortex and 95 other tissues.
DR ExpressionAtlas; Q53HC0; baseline and differential.
DR Genevisible; Q53HC0; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR040370; CCDC74A/CCDC74B/CCDC92.
DR InterPro; IPR033224; CCDC92.
DR InterPro; IPR039496; CCDC92/74_CC_dom.
DR PANTHER; PTHR14882; PTHR14882; 1.
DR PANTHER; PTHR14882:SF4; PTHR14882:SF4; 1.
DR Pfam; PF14916; CCDC92; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral protein; Coiled coil; Cytoplasm;
KW Cytoskeleton; Host-virus interaction; Immunity; Innate immunity;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..331
FT /note="Coiled-coil domain-containing protein 92"
FT /id="PRO_0000274500"
FT REGION 171..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..44
FT /evidence="ECO:0000255"
FT COILED 76..152
FT /evidence="ECO:0000255"
FT COMPBIAS 196..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:32129703"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056906"
FT VARIANT 70
FT /note="S -> C (in dbSNP:rs11057401)"
FT /id="VAR_030301"
FT VARIANT 253
FT /note="A -> T (in dbSNP:rs35935939)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_050765"
FT VARIANT 281
FT /note="R -> H (in dbSNP:rs17886730)"
FT /id="VAR_030302"
SQ SEQUENCE 331 AA; 36961 MW; 840D062480338500 CRC64;
MTSPHFSSYD EGPLDVSMAA TNLENQLHSA QKNLLFLQRE HASTLKGLHS EIRRLQQHCT
DLTYELTVKS SEQTGDGTSK SSELKKRCEE LEAQLKVKEN ENAELLKELE QKNAMITVLE
NTIKEREKKY LEELKAKSHK LTLLSSELEQ RASTIAYLTS QLHAAKKKLM SSSGTSDASP
SGSPVLASYK PAPPKDKLPE TPRRRMKKSL SAPLHPEFEE VYRFGAESRK LLLREPVDAM
PDPTPFLLAR ESAEVHLIKE RPLVIPPIAS DRSGEQHSPA REKPHKAHVG VAHRIHHATP
PQAQPEVKTL AVDQVNGGKV VRKHSGTDRT V
