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CCD89_MOUSE
ID   CCD89_MOUSE             Reviewed;         370 AA.
AC   Q9DA73;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Coiled-coil domain-containing protein 89 {ECO:0000250|UniProtKB:Q8N998};
DE   AltName: Full=Bc8 orange-interacting protein {ECO:0000303|PubMed:14648848};
GN   Name=Ccdc89 {ECO:0000312|MGI:MGI:1917304};
GN   Synonyms=Boip {ECO:0000303|PubMed:14648848};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAB24410.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-370.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB24410.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB24410.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION, INTERACTION WITH HEY1, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14648848; DOI=10.1002/dvdy.10406;
RA   Van Wayenbergh R., Taelman V., Pichon B., Fischer A., Kricha S.,
RA   Gessler M., Christophe D., Bellefroid E.J.;
RT   "Identification of BOIP, a novel cDNA highly expressed during
RT   spermatogenesis that encodes a protein interacting with the orange domain
RT   of the hairy-related transcription factor HRT1/Hey1 in Xenopus and mouse.";
RL   Dev. Dyn. 228:716-725(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBUNIT: Interacts with HEY1. {ECO:0000269|PubMed:14648848}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7ZW57}. Nucleus
CC       {ECO:0000250|UniProtKB:Q7ZW57}. Note=Uniformly distributed within the
CC       cell, but becomes recruited to the nucleus upon binding to HEY1.
CC       {ECO:0000250|UniProtKB:Q7ZW57}.
CC   -!- TISSUE SPECIFICITY: Expression is restricted to the adult testis, where
CC       localization is almost exclusive to round spermatids.
CC       {ECO:0000269|PubMed:14648848}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adults but not embryos.
CC       {ECO:0000269|PubMed:14648848}.
CC   -!- SIMILARITY: Belongs to the CCDC89 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24410.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB24410.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AC100322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK006105; BAB24410.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS52308.1; -.
DR   RefSeq; NP_081574.1; NM_027298.1.
DR   AlphaFoldDB; Q9DA73; -.
DR   SMR; Q9DA73; -.
DR   IntAct; Q9DA73; 1.
DR   STRING; 10090.ENSMUSP00000060309; -.
DR   iPTMnet; Q9DA73; -.
DR   PhosphoSitePlus; Q9DA73; -.
DR   PaxDb; Q9DA73; -.
DR   PRIDE; Q9DA73; -.
DR   ProteomicsDB; 265602; -.
DR   Antibodypedia; 49524; 85 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000061391; ENSMUSP00000060309; ENSMUSG00000044362.
DR   GeneID; 70054; -.
DR   KEGG; mmu:70054; -.
DR   UCSC; uc012fox.1; mouse.
DR   CTD; 220388; -.
DR   MGI; MGI:1917304; Ccdc89.
DR   VEuPathDB; HostDB:ENSMUSG00000044362; -.
DR   eggNOG; ENOG502QU10; Eukaryota.
DR   GeneTree; ENSGT00390000016046; -.
DR   HOGENOM; CLU_066884_0_0_1; -.
DR   InParanoid; Q9DA73; -.
DR   OMA; AMLCSRI; -.
DR   OrthoDB; 1122259at2759; -.
DR   PhylomeDB; Q9DA73; -.
DR   TreeFam; TF333232; -.
DR   BioGRID-ORCS; 70054; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q9DA73; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9DA73; protein.
DR   Bgee; ENSMUSG00000044362; Expressed in seminiferous tubule of testis and 98 other tissues.
DR   Genevisible; Q9DA73; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:MGI.
DR   InterPro; IPR043450; CCDC89-like.
DR   PANTHER; PTHR34768; PTHR34768; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Coiled-coil domain-containing protein 89"
FT                   /id="PRO_0000370201"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..346
FT                   /evidence="ECO:0000255"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        107
FT                   /note="K -> E (in Ref. 2; BAB24410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116..117
FT                   /note="QK -> KM (in Ref. 2; BAB24410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224..225
FT                   /note="EL -> DV (in Ref. 2; BAB24410)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  43241 MW;  197E380266AC2064 CRC64;
     MPQEEKTLRM DTPPPDEILG KQNENLQNQD EELGFKEMDG LREALANLRG LSEEEKGEKA
     MLRSRIQEQS QLICILKRRS DEALERCQIL ELLNSELEEK RLQEMEKLKA QSEHIQKLEN
     HFMILASNHE QMIRFKDAHK SENVKLKEEN ARLRQENNSL FSQALKDQEA KVLELTTLNK
     ALVEELEVLK QRCAHEASQA QAREEELLGL QNQQACDHAK ETEELRSQLQ SIKQQHQQAT
     EQMGKEQEAN LNLNQELQAR LQTVLREKEE LLQLSMERGK VLQNKQAEIR QLEEKLETAA
     MAKKHALERF EQEAVAVDSN LRVRELQRRV DGIQKAYDEL RLQSEAFKKH SLDLLSKERE
     LNAKLRHLFP
 
 
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