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CZIB_HUMAN
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   03-AUG-2022, entry version 148.
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}.
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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; 22.
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; Q9NWV4; -.
DR   PeptideAtlas; Q9NWV4; -.
DR   PRIDE; Q9NWV4; -.
DR   ProteomicsDB; 82985; -.
DR   Antibodypedia; 52610; 69 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   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; FFMKCKM; -.
DR   OrthoDB; 1398309at2759; -.
DR   PhylomeDB; Q9NWV4; -.
DR   TreeFam; TF105959; -.
DR   PathwayCommons; Q9NWV4; -.
DR   SignaLink; Q9NWV4; -.
DR   BioGRID-ORCS; 54987; 11 hits in 1055 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 206 other tissues.
DR   Genevisible; Q9NWV4; HS.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   InterPro; IPR008584; CXXC_Zn-binding_euk.
DR   PANTHER; PTHR12857; PTHR12857; 1.
DR   Pfam; PF05907; DUF866; 1.
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
 
 
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