ID CZIB_HUMAN Reviewed; 160 AA. AC Q9NWV4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=CXXC motif containing zinc binding protein {ECO:0000305}; DE AltName: Full=UPF0587 protein C1orf123; GN Name=CZIB {ECO:0000312|HGNC:HGNC:26059}; GN Synonyms=C1orf123 {ECO:0000312|HGNC:HGNC:26059}; 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=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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [5] RP PROTEIN SEQUENCE OF 10-26, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] 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 [9] RP CRYSTALLIZATION, AND SUBUNIT. RX PubMed=26919524; DOI=10.1107/s2053230x16002016; RA Rahaman S.N., Mat Yusop J., Mohamed-Hussein Z.A., Ho K.L., Teh A.H., RA Waterman J., Ng C.L.; RT "Cloning, expression, purification, crystallization and X-ray RT crystallographic analysis of recombinant human C1ORF123 protein."; RL Acta Crystallogr. F Struct. Biol. Commun. 72:207-213(2016). RN [10] {ECO:0007744|PDB:5ZLQ} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, RP DOMAIN, AND MUTAGENESIS OF CYS-33; CYS-36; CYS-67 AND CYS-70. RX PubMed=30260988; DOI=10.1371/journal.pone.0204355; RA Furukawa Y., Lim C., Tosha T., Yoshida K., Hagai T., Akiyama S., RA Watanabe S., Nakagome K., Shiro Y.; RT "Identification of a novel zinc-binding protein, C1orf123, as an interactor RT with a heavy metal-associated domain."; RL PLoS ONE 13:e0204355-e0204355(2018). RN [11] {ECO:0007744|PDB:5ZRT} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, RP AND DOMAIN. RX PubMed=30280012; DOI=10.7717/peerj.5377; RA Rahaman S.N., Mat Yusop J., Mohamed-Hussein Z.A., Aizat W.M., Ho K.L., RA Teh A.H., Waterman J., Tan B.K., Tan H.L., Li A.Y., Chen E.S., Ng C.L.; RT "Crystal structure and functional analysis of human C1ORF123."; RL PeerJ 6:E5377-E5377(2018). CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26919524, CC ECO:0000269|PubMed:30260988, ECO:0000269|PubMed:30280012}. CC -!- INTERACTION: CC Q9NWV4; O14618: CCS; NbExp=3; IntAct=EBI-724109, EBI-11668690; CC -!- DOMAIN: The N-terminal and the C-terminal half of the protein have a CC very similar 3D-structure, suggesting they arose from duplication CC (PubMed:30280012). Requires a bound zinc ion for normal folding and CC solubility (PubMed:30260988). {ECO:0000269|PubMed:30260988, CC ECO:0000269|PubMed:30280012}. CC -!- SIMILARITY: Belongs to the UPF0587 family. {ECO:0000305}. CC -!- CAUTION: Was identified as interaction partner for CCS CC (PubMed:30260988). Only misfolded mutant protein forms that lack part CC of the zinc-binding sites interact with CCS. The full-length protein CC does not interact with CCS. Likewise, mutant protein that lacks all CC four zinc-binding residues does not interact with CCS CC (PubMed:30260988). {ECO:0000269|PubMed:30260988}. 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; AK000587; BAA91272.1; -; mRNA. DR EMBL; CR457246; CAG33527.1; -; mRNA. DR EMBL; AL606760; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010908; AAH10908.1; -; mRNA. DR CCDS; CCDS576.1; -. DR RefSeq; NP_001291688.1; NM_001304759.1. DR RefSeq; NP_001291689.1; NM_001304760.1. DR RefSeq; NP_060357.1; NM_017887.2. DR PDB; 5ZLQ; X-ray; 2.00 A; A=1-160. DR PDB; 5ZRT; X-ray; 1.90 A; A/B=1-160. DR PDBsum; 5ZLQ; -. DR PDBsum; 5ZRT; -. DR AlphaFoldDB; Q9NWV4; -. DR SMR; Q9NWV4; -. DR BioGRID; 120322; 29. DR IntAct; Q9NWV4; 5. DR MINT; Q9NWV4; -. DR STRING; 9606.ENSP00000294360; -. DR GlyGen; Q9NWV4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NWV4; -. DR MetOSite; Q9NWV4; -. DR PhosphoSitePlus; Q9NWV4; -. DR BioMuta; C1orf123; -. DR DMDM; 74753033; -. DR REPRODUCTION-2DPAGE; IPI00016605; -. DR EPD; Q9NWV4; -. DR jPOST; Q9NWV4; -. DR MassIVE; Q9NWV4; -. DR MaxQB; Q9NWV4; -. DR PaxDb; 9606-ENSP00000294360; -. DR PeptideAtlas; Q9NWV4; -. DR ProteomicsDB; 82985; -. DR Pumba; Q9NWV4; -. DR Antibodypedia; 52610; 70 antibodies from 11 providers. DR DNASU; 54987; -. DR Ensembl; ENST00000294360.5; ENSP00000294360.4; ENSG00000162384.14. DR GeneID; 54987; -. DR KEGG; hsa:54987; -. DR MANE-Select; ENST00000294360.5; ENSP00000294360.4; NM_017887.3; NP_060357.1. DR UCSC; uc001cvd.4; human. DR AGR; HGNC:26059; -. DR CTD; 54987; -. DR GeneCards; CZIB; -. DR HGNC; HGNC:26059; CZIB. DR HPA; ENSG00000162384; Low tissue specificity. DR neXtProt; NX_Q9NWV4; -. DR OpenTargets; ENSG00000162384; -. DR PharmGKB; PA142672441; -. DR VEuPathDB; HostDB:ENSG00000162384; -. DR eggNOG; KOG1296; Eukaryota. DR GeneTree; ENSGT00390000001523; -. DR HOGENOM; CLU_114688_1_0_1; -. DR InParanoid; Q9NWV4; -. DR OMA; TAHFVWR; -. DR OrthoDB; 5490773at2759; -. DR PhylomeDB; Q9NWV4; -. DR TreeFam; TF105959; -. DR PathwayCommons; Q9NWV4; -. DR SignaLink; Q9NWV4; -. DR BioGRID-ORCS; 54987; 18 hits in 1129 CRISPR screens. DR ChiTaRS; C1orf123; human. DR GenomeRNAi; 54987; -. DR Pharos; Q9NWV4; Tdark. DR PRO; PR:Q9NWV4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NWV4; Protein. DR Bgee; ENSG00000162384; Expressed in tendon of biceps brachii and 208 other cell types or tissues. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR InterPro; IPR008584; CXXC_Zn-binding_euk. DR PANTHER; PTHR12857:SF0; CXXC MOTIF CONTAINING ZINC BINDING PROTEIN; 1. DR PANTHER; PTHR12857; UNCHARACTERIZED; 1. DR Pfam; PF05907; CXXC_Zn-b_euk; 1. DR SUPFAM; SSF141678; MAL13P1.257-like; 1. DR Genevisible; Q9NWV4; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Metal-binding; Phosphoprotein; KW Reference proteome; Zinc. FT CHAIN 1..160 FT /note="CXXC motif containing zinc binding protein" FT /id="PRO_0000264151" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:30260988, FT ECO:0000269|PubMed:30280012, ECO:0007744|PDB:5ZLQ, FT ECO:0007744|PDB:5ZRT" FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:30260988, FT ECO:0000269|PubMed:30280012, ECO:0007744|PDB:5ZLQ, FT ECO:0007744|PDB:5ZRT" FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:30260988, FT ECO:0000269|PubMed:30280012, ECO:0007744|PDB:5ZLQ, FT ECO:0007744|PDB:5ZRT" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:30260988, FT ECO:0000269|PubMed:30280012, ECO:0007744|PDB:5ZLQ, FT ECO:0007744|PDB:5ZRT" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MUTAGEN 33 FT /note="C->A: Disrupts protein folding and solubility; when FT associated with A-36; A-67 and A-70." FT /evidence="ECO:0000269|PubMed:30260988" FT MUTAGEN 36 FT /note="C->A: Disrupts protein folding and solubility; when FT associated with A-33; A-67 and A-70." FT /evidence="ECO:0000269|PubMed:30260988" FT MUTAGEN 67 FT /note="C->A: Disrupts protein folding and solubility; when FT associated with A-33; A-36 and A-70." FT /evidence="ECO:0000269|PubMed:30260988" FT MUTAGEN 70 FT /note="C->A: Disrupts protein folding and solubility; when FT associated with A-33; A-36 and A-67." FT /evidence="ECO:0000269|PubMed:30260988" FT STRAND 2..20 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:5ZRT" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:5ZRT" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:5ZRT" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:5ZRT" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:5ZRT" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 95..111 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 116..120 FT /evidence="ECO:0007829|PDB:5ZRT" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:5ZRT" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:5ZRT" FT STRAND 146..159 FT /evidence="ECO:0007829|PDB:5ZRT" SQ SEQUENCE 160 AA; 18048 MW; 7CACEEE7CE781CBC CRC64; MGKIALQLKA TLENITNLRP VGEDFRWYLK MKCGNCGEIS DKWQYIRLMD SVALKGGRGS ASMVQKCKLC ARENSIEILS STIKPYNAED NENFKTIVEF ECRGLEPVDF QPQAGFAAEG VESGTAFSDI NLQEKDWTDY DEKAQESVGI YEVTHQFVKC //