CIA2B_MOUSE
ID CIA2B_MOUSE Reviewed; 163 AA.
AC Q9D187;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytosolic iron-sulfur assembly component 2B {ECO:0000305};
DE AltName: Full=Mitotic spindle-associated MMXD complex subunit MIP18 {ECO:0000305};
GN Name=Ciao2b {ECO:0000312|MGI:MGI:1915773}; Synonyms=Fam96b, Mip18;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 -!- FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA)
CC complex, a multiprotein complex that mediates the incorporation of
CC iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA
CC complex component and in collaboration with CIAO1 and MMS19, binds to
CC and facilitates the assembly of most cytosolic-nuclear Fe/S proteins.
CC As part of the mitotic spindle-associated MMXD complex it plays a role
CC in chromosome segregation, probably by facilitating iron-sulfur cluster
CC assembly into ERCC2/XPD. Together with MMS19, facilitates the transfer
CC of Fe-S clusters to the motor protein KIF4A, which ensures proper
CC localization of KIF4A to mitotic machinery components to promote the
CC progression of mitosis. {ECO:0000250|UniProtKB:Q9Y3D0}.
CC -!- SUBUNIT: Component of the CIA complex. Component of the MMXD complex,
CC which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with
CC CIAO1, ERCC2 and MMS19; the interactions are direct. Interacts with
CC KIF4A; the interaction facilitates the transfer of Fe-S clusters to
CC KIF4A to ensure proper localization of KIF4A to the mitotic machinery.
CC Interacts with CCDC117; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y3D0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3D0}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Y3D0}.
CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
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DR EMBL; AK003830; BAB23024.1; -; mRNA.
DR EMBL; BC055880; AAH55880.1; -; mRNA.
DR CCDS; CCDS52649.1; -.
DR RefSeq; NP_081029.1; NM_026753.2.
DR AlphaFoldDB; Q9D187; -.
DR SMR; Q9D187; -.
DR BioGRID; 212906; 6.
DR IntAct; Q9D187; 2.
DR MINT; Q9D187; -.
DR STRING; 10090.ENSMUSP00000132725; -.
DR PhosphoSitePlus; Q9D187; -.
DR SwissPalm; Q9D187; -.
DR REPRODUCTION-2DPAGE; Q9D187; -.
DR EPD; Q9D187; -.
DR MaxQB; Q9D187; -.
DR PaxDb; Q9D187; -.
DR PeptideAtlas; Q9D187; -.
DR PRIDE; Q9D187; -.
DR ProteomicsDB; 290252; -.
DR Antibodypedia; 44224; 185 antibodies from 30 providers.
DR DNASU; 68523; -.
DR Ensembl; ENSMUST00000164884; ENSMUSP00000132725; ENSMUSG00000031879.
DR GeneID; 68523; -.
DR KEGG; mmu:68523; -.
DR UCSC; uc033jhf.1; mouse.
DR CTD; 51647; -.
DR MGI; MGI:1915773; Ciao2b.
DR VEuPathDB; HostDB:ENSMUSG00000031879; -.
DR eggNOG; KOG3381; Eukaryota.
DR GeneTree; ENSGT00390000017697; -.
DR HOGENOM; CLU_075876_3_1_1; -.
DR InParanoid; Q9D187; -.
DR OMA; NQCISAR; -.
DR OrthoDB; 1408004at2759; -.
DR PhylomeDB; Q9D187; -.
DR TreeFam; TF105940; -.
DR BioGRID-ORCS; 68523; 28 hits in 67 CRISPR screens.
DR ChiTaRS; Ciao2b; mouse.
DR PRO; PR:Q9D187; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D187; protein.
DR Bgee; ENSMUSG00000031879; Expressed in embryonic brain and 265 other tissues.
DR ExpressionAtlas; Q9D187; baseline and differential.
DR Genevisible; Q9D187; MM.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0071817; C:MMXD complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IEA:InterPro.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR039796; MIP18.
DR InterPro; IPR002744; MIP18-like.
DR PANTHER; PTHR12377; PTHR12377; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..163
FT /note="Cytosolic iron-sulfur assembly component 2B"
FT /id="PRO_0000212692"
SQ SEQUENCE 163 AA; 17667 MW; D3171D52CF3AD02F CRC64;
MVGGGGSGGG LLENANPLIY ERSGERPVTA GEEDEEVPDS IDAREIFDLI RSINDPEHPL
TLEELNVVEQ VRIQVSDPES TVAVAFTPTI PHCSMATLIG LSIKVKLLRS LPQRFKMDVH
ITPGTHASEH AVNKQLADKE RVAAALENTH LLEVVNQCLS ARS