ID CIA2B_HUMAN Reviewed; 163 AA. AC Q9Y3D0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Cytosolic iron-sulfur assembly component 2B {ECO:0000305}; DE AltName: Full=MSS19-interacting protein of 18 kDa; DE AltName: Full=Mitotic spindle-associated MMXD complex subunit MIP18; DE AltName: Full=Protein FAM96B; GN Name=CIAO2B {ECO:0000312|HGNC:HGNC:24261}; GN Synonyms=CIAB {ECO:0000303|PubMed:23891004}, FAM96B, MIP18 GN {ECO:0000303|PubMed:23585563}; ORFNames=CGI-128, HSPC118; 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]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, and Uterus; 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 PROTEIN SEQUENCE OF 2-22; 117-134 AND 142-162, CLEAVAGE OF INITIATOR RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [5] RP FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH ERCC2 AND MMS19, RP AND SUBCELLULAR LOCATION. RX PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029; RA Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., RA Kuraoka I., Hiraoka Y., Tanaka K.; RT "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome RT segregation."; RL Mol. Cell 39:632-640(2010). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP IDENTIFICATION IN THE CIA COMPLEX, AND FUNCTION. RX PubMed=22678362; DOI=10.1126/science.1219723; RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T., RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.; RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and RT genomic integrity."; RL Science 337:195-199(2012). RN [9] RP IDENTIFICATION IN THE CIA COMPLEX, AND FUNCTION. RX PubMed=22678361; DOI=10.1126/science.1219664; RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.; RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism."; RL Science 337:243-245(2012). RN [10] RP FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CIAO1; RP ERCC2; MMS19 AND POLD1. RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015; RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B., RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.; RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and RT maturation of different subsets of cytosolic-nuclear iron-sulfur RT proteins."; RL Cell Metab. 18:187-198(2013). RN [11] RP ERRATUM OF PUBMED:23891004. RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009; RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B., RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.; RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur RT Proteins."; RL Cell Metab. 27:263-263(2018). RN [12] RP IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION RP WITH CIAO1; MMS19 AND ERCC2. RX PubMed=23585563; DOI=10.1074/jbc.m112.416602; RA Seki M., Takeda Y., Iwai K., Tanaka K.; RT "IOP1 protein is an external component of the human cytosolic iron-sulfur RT cluster assembly (CIA) machinery and functions in the MMS19 protein- RT dependent CIA pathway."; RL J. Biol. Chem. 288:16680-16689(2013). RN [13] 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 [14] RP FUNCTION, INTERACTION WITH KIF4A, AND SUBCELLULAR LOCATION. RX PubMed=29848660; DOI=10.1242/jcs.211433; RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E., RA Muehlenhoff U., Lill R., Ben-Aroya S.; RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its RT subcellular localization during mitosis."; RL J. Cell Sci. 131:0-0(2018). RN [15] RP INTERACTION WITH CCDC117. RX PubMed=30742009; DOI=10.1038/s41598-019-39078-5; RA Horton A.J., Brooker J., Streitfeld W.S., Flessa M.E., Pillai B., RA Simpson R., Clark C.D., Gooz M.B., Sutton K.K., Foley A.C., Lee K.H.; RT "Nkx2-5 Second Heart Field Target Gene Ccdc117 Regulates DNA Metabolism and RT Proliferation."; RL Sci. Rep. 9:1738-1738(2019). 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 CC (PubMed:23891004, PubMed:22678362, PubMed:22678361, PubMed:29848660). CC As a CIA complex component and in collaboration with CIAO1 and MMS19, CC binds to and facilitates the assembly of most cytosolic-nuclear Fe/S CC proteins (PubMed:23891004, PubMed:29848660). As part of the mitotic CC spindle-associated MMXD complex it plays a role in chromosome CC segregation, probably by facilitating iron-sulfur cluster assembly into CC ERCC2/XPD (PubMed:20797633). Together with MMS19, facilitates the CC transfer of Fe-S clusters to the motor protein KIF4A, which ensures CC proper localization of KIF4A to mitotic machinery components to promote CC the progression of mitosis (PubMed:29848660). CC {ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361, CC ECO:0000269|PubMed:22678362, ECO:0000269|PubMed:23891004, CC ECO:0000269|PubMed:29848660}. CC -!- SUBUNIT: Component of the CIA complex (PubMed:22678361, CC PubMed:22678362, PubMed:23585563). Component of the MMXD complex, which CC includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5 (PubMed:20797633). CC Interacts with CIAO1, ERCC2 and MMS19; the interactions are direct CC (PubMed:22678362, PubMed:23585563). Interacts with KIF4A; the CC interaction facilitates the transfer of Fe-S clusters to KIF4A to CC ensure proper localization of KIF4A to the mitotic machinery CC (PubMed:29848660). Interacts with CCDC117; the interaction is direct CC (PubMed:30742009). {ECO:0000269|PubMed:20797633, CC ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362, CC ECO:0000269|PubMed:23585563, ECO:0000269|PubMed:29848660, CC ECO:0000269|PubMed:30742009}. CC -!- INTERACTION: CC Q9Y3D0; P55212: CASP6; NbExp=3; IntAct=EBI-744045, EBI-718729; CC Q9Y3D0; P06307: CCK; NbExp=3; IntAct=EBI-744045, EBI-6624398; CC Q9Y3D0; O76071: CIAO1; NbExp=24; IntAct=EBI-744045, EBI-725145; CC Q9Y3D0; P18074: ERCC2; NbExp=2; IntAct=EBI-744045, EBI-6380590; CC Q9Y3D0; P22607: FGFR3; NbExp=3; IntAct=EBI-744045, EBI-348399; CC Q9Y3D0; Q14957: GRIN2C; NbExp=3; IntAct=EBI-744045, EBI-8285963; CC Q9Y3D0; P28799: GRN; NbExp=3; IntAct=EBI-744045, EBI-747754; CC Q9Y3D0; P06396: GSN; NbExp=3; IntAct=EBI-744045, EBI-351506; CC Q9Y3D0; P04792: HSPB1; NbExp=3; IntAct=EBI-744045, EBI-352682; CC Q9Y3D0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-744045, EBI-10975473; CC Q9Y3D0; P13473-2: LAMP2; NbExp=3; IntAct=EBI-744045, EBI-21591415; CC Q9Y3D0; Q96T76: MMS19; NbExp=15; IntAct=EBI-744045, EBI-1044169; CC Q9Y3D0; P16284: PECAM1; NbExp=3; IntAct=EBI-744045, EBI-716404; CC Q9Y3D0; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-744045, EBI-5280197; CC Q9Y3D0; P60891: PRPS1; NbExp=3; IntAct=EBI-744045, EBI-749195; CC Q9Y3D0; P20339: RAB5A; NbExp=3; IntAct=EBI-744045, EBI-399437; CC Q9Y3D0; P62826: RAN; NbExp=3; IntAct=EBI-744045, EBI-286642; CC Q9Y3D0; P02766: TTR; NbExp=3; IntAct=EBI-744045, EBI-711909; CC Q9Y3D0; P61086: UBE2K; NbExp=3; IntAct=EBI-744045, EBI-473850; CC Q9Y3D0; P08670: VIM; NbExp=3; IntAct=EBI-744045, EBI-353844; CC Q9Y3D0; O76024: WFS1; NbExp=3; IntAct=EBI-744045, EBI-720609; CC Q9Y3D0; Q9Y649; NbExp=3; IntAct=EBI-744045, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:20797633, CC ECO:0000269|PubMed:29848660}. Midbody {ECO:0000269|PubMed:29848660}. CC Note=In mitosis, localizes to the spindle during metaphase and the CC spindle midbody during telophase (PubMed:29848660). Co-localizes with CC KIF4A to the spindle midzone and midbody during telophase and CC cytokinesis (PubMed:29848660). {ECO:0000269|PubMed:29848660}. CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF151886; AAD34123.1; -; mRNA. DR EMBL; AF161467; AAF29082.1; -; mRNA. DR EMBL; BC001733; AAH01733.1; -; mRNA. DR EMBL; BC005023; AAH05023.1; -; mRNA. DR CCDS; CCDS45506.1; -. DR RefSeq; NP_057146.1; NM_016062.3. DR AlphaFoldDB; Q9Y3D0; -. DR SMR; Q9Y3D0; -. DR BioGRID; 119656; 119. DR ComplexPortal; CPX-2837; CIAO1-CIAO2B-CIAO3-MMS19 cytosolic iron-sulfur protein assembly complex. DR CORUM; Q9Y3D0; -. DR IntAct; Q9Y3D0; 60. DR MINT; Q9Y3D0; -. DR STRING; 9606.ENSP00000387471; -. DR ChEMBL; CHEMBL4295989; -. DR GlyGen; Q9Y3D0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y3D0; -. DR PhosphoSitePlus; Q9Y3D0; -. DR BioMuta; FAM96B; -. DR EPD; Q9Y3D0; -. DR jPOST; Q9Y3D0; -. DR MassIVE; Q9Y3D0; -. DR MaxQB; Q9Y3D0; -. DR PaxDb; 9606-ENSP00000387471; -. DR PeptideAtlas; Q9Y3D0; -. DR ProteomicsDB; 86018; -. DR Pumba; Q9Y3D0; -. DR Antibodypedia; 44224; 214 antibodies from 30 providers. DR DNASU; 51647; -. DR Ensembl; ENST00000422424.7; ENSP00000387471.2; ENSG00000166595.12. DR GeneID; 51647; -. DR KEGG; hsa:51647; -. DR MANE-Select; ENST00000422424.7; ENSP00000387471.2; NM_016062.4; NP_057146.1. DR UCSC; uc059vme.1; human. DR AGR; HGNC:24261; -. DR CTD; 51647; -. DR DisGeNET; 51647; -. DR GeneCards; CIAO2B; -. DR HGNC; HGNC:24261; CIAO2B. DR HPA; ENSG00000166595; Low tissue specificity. DR MIM; 614778; gene. DR neXtProt; NX_Q9Y3D0; -. DR OpenTargets; ENSG00000166595; -. DR PharmGKB; PA142671830; -. DR VEuPathDB; HostDB:ENSG00000166595; -. DR eggNOG; KOG3381; Eukaryota. DR GeneTree; ENSGT00390000017697; -. DR HOGENOM; CLU_075876_3_1_1; -. DR InParanoid; Q9Y3D0; -. DR OMA; NQCISAR; -. DR OrthoDB; 7394at2759; -. DR PhylomeDB; Q9Y3D0; -. DR TreeFam; TF105940; -. DR PathwayCommons; Q9Y3D0; -. DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly. DR SignaLink; Q9Y3D0; -. DR BioGRID-ORCS; 51647; 781 hits in 1153 CRISPR screens. DR ChiTaRS; FAM96B; human. DR GenomeRNAi; 51647; -. DR Pharos; Q9Y3D0; Tbio. DR PRO; PR:Q9Y3D0; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9Y3D0; Protein. DR Bgee; ENSG00000166595; Expressed in lower esophagus mucosa and 202 other cell types or tissues. DR ExpressionAtlas; Q9Y3D0; baseline and differential. DR GO; GO:0097361; C:CIA complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0071817; C:MMXD complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP: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; IMP:UniProtKB. DR Gene3D; 6.10.250.1280; -; 1. DR Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1. DR InterPro; IPR034904; FSCA_dom_sf. DR InterPro; IPR039796; MIP18. DR InterPro; IPR002744; MIP18-like. DR PANTHER; PTHR12377:SF0; CYTOSOLIC IRON-SULFUR ASSEMBLY COMPONENT 2B; 1. DR PANTHER; PTHR12377; UNCHARACTERIZED; 1. DR Pfam; PF01883; FeS_assembly_P; 1. DR SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1. DR Genevisible; Q9Y3D0; HS. PE 1: Evidence at protein level; KW Chromosome partition; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Nucleus; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.4" FT CHAIN 2..163 FT /note="Cytosolic iron-sulfur assembly component 2B" FT /id="PRO_0000212691" SQ SEQUENCE 163 AA; 17663 MW; 323004BAB92B1486 CRC64; MVGGGGVGGG LLENANPLIY QRSGERPVTA GEEDEQVPDS IDAREIFDLI RSINDPEHPL TLEELNVVEQ VRVQVSDPES TVAVAFTPTI PHCSMATLIG LSIKVKLLRS LPQRFKMDVH ITPGTHASEH AVNKQLADKE RVAAALENTH LLEVVNQCLS ARS //