CIA2B_HUMAN
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 03-AUG-2022, entry version 160.
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,
GN MIP18 {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=22; IntAct=EBI-744045, EBI-725145;
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=12; 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}.
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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; 107.
DR CORUM; Q9Y3D0; -.
DR IntAct; Q9Y3D0; 57.
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; Q9Y3D0; -.
DR PeptideAtlas; Q9Y3D0; -.
DR PRIDE; Q9Y3D0; -.
DR ProteomicsDB; 86018; -.
DR Antibodypedia; 44224; 185 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 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; 1408004at2759; -.
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; 748 hits in 1080 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 200 other tissues.
DR ExpressionAtlas; Q9Y3D0; baseline and differential.
DR Genevisible; Q9Y3D0; HS.
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; 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; 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
