CIZ1_HUMAN
ID CIZ1_HUMAN Reviewed; 898 AA.
AC Q9ULV3; A8K9J8; B4E131; B7ZAS8; Q5SYW3; Q5SYW5; Q8WU72; Q9H868; Q9NYM8;
AC Q9UHK4; Q9Y3F9; Q9Y3G0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cip1-interacting zinc finger protein;
DE AltName: Full=CDKN1A-interacting zinc finger protein 1;
DE AltName: Full=Nuclear protein NP94;
DE AltName: Full=Zinc finger protein 356;
GN Name=CIZ1; Synonyms=LSFR1, NP94, ZNF356;
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 [MRNA] (ISOFORM 1).
RX PubMed=10529385; DOI=10.1006/bbrc.1999.1516;
RA Mitsui K., Matsumoto A., Ohtsuka S., Ohtsubo M., Yoshimura A.;
RT "Cloning and characterization of a novel p21(Cip1/Waf1)-interacting zinc
RT finger protein, ciz1.";
RL Biochem. Biophys. Res. Commun. 264:457-464(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-219; GLY-370; PHE-578;
RP MET-638 AND GLN-847.
RG NIEHS SNPs program;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), AND VARIANT
RP MET-638.
RC TISSUE=Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-898 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 50-898 (ISOFORM 2).
RC TISSUE=Medulloblastoma;
RX PubMed=12824700; DOI=10.1159/000071160;
RA Warder D.E., Keherly M.J.;
RT "Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus DNA
RT sequence ARYSR(0-2)YYAC.";
RL J. Biomed. Sci. 10:406-417(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 649-898.
RX PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
RA Gilley J., Fried M.;
RT "Extensive gene order differences within regions of conserved synteny
RT between the Fugu and human genomes: implications for chromosomal evolution
RT and the cloning of disease genes.";
RL Hum. Mol. Genet. 8:1313-1320(1999).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-567, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP POSSIBLE INVOLVEMENT IN ADULT ONSET PRIMARY CERVICAL DYSTONIA, AND VARIANTS
RP SER-47; LEU-50; GLY-264; GLU-394; PHE-577 AND MET-672.
RX PubMed=22447717; DOI=10.1002/ana.23547;
RA Xiao J., Uitti R.J., Zhao Y., Vemula S.R., Perlmutter J.S., Wszolek Z.K.,
RA Maraganore D.M., Auburger G., Leube B., Lehnhoff K., Ledoux M.S.;
RT "Mutations in CIZ1 cause adult onset primary cervical dystonia.";
RL Ann. Neurol. 71:458-469(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; THR-244; SER-350;
RP SER-547; SER-821 AND SER-838, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280; LYS-340; LYS-401; LYS-549;
RP LYS-588; LYS-680; LYS-705; LYS-830 AND LYS-879, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May regulate the subcellular localization of CIP/WAF1.
CC -!- SUBUNIT: Interacts with CIP/WAF1.
CC -!- INTERACTION:
CC Q9ULV3; Q9P0V3: SH3BP4; NbExp=2; IntAct=EBI-2652948, EBI-1049513;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ULV3-1; Sequence=Displayed;
CC Name=2; Synonyms=NP94B;
CC IsoId=Q9ULV3-2; Sequence=VSP_004164, VSP_004165;
CC Name=3;
CC IsoId=Q9ULV3-3; Sequence=VSP_004164, VSP_039894;
CC Name=4;
CC IsoId=Q9ULV3-4; Sequence=VSP_039894;
CC Name=5;
CC IsoId=Q9ULV3-5; Sequence=VSP_044729;
CC -!- DISEASE: Note=Defects in CIZ1 may be a cause of adult onset primary
CC cervical dystonia. Dystonia is defined by the presence of sustained
CC involuntary muscle contractions, often leading to abnormal postures.
CC Cervical dystonia or spasmodic torticollis, the most common form of
CC focal dystonia, is characterized by involuntary contractions of the
CC neck muscles, which produce abnormal posturing of the head upon the
CC trunk.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF37882.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ciz1/";
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DR EMBL; AB030835; BAA85783.1; -; mRNA.
DR EMBL; EF467915; ABO43037.1; -; Genomic_DNA.
DR EMBL; AK023978; BAB14750.1; -; mRNA.
DR EMBL; AK292713; BAF85402.1; -; mRNA.
DR EMBL; AK303636; BAG64643.1; -; mRNA.
DR EMBL; AK316393; BAH14764.1; -; mRNA.
DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87752.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87753.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87754.1; -; Genomic_DNA.
DR EMBL; BC021163; AAH21163.1; -; mRNA.
DR EMBL; AF159027; AAF23231.1; ALT_INIT; mRNA.
DR EMBL; AF234161; AAF37882.1; ALT_INIT; mRNA.
DR EMBL; Y17453; CAB44346.1; -; Genomic_DNA.
DR EMBL; Y17454; CAB44347.1; -; Genomic_DNA.
DR CCDS; CCDS48033.1; -. [Q9ULV3-3]
DR CCDS; CCDS48034.1; -. [Q9ULV3-4]
DR CCDS; CCDS59147.1; -. [Q9ULV3-5]
DR CCDS; CCDS6894.1; -. [Q9ULV3-1]
DR RefSeq; NP_001124487.1; NM_001131015.1. [Q9ULV3-4]
DR RefSeq; NP_001124488.1; NM_001131016.1. [Q9ULV3-1]
DR RefSeq; NP_001124489.1; NM_001131017.1.
DR RefSeq; NP_001124490.1; NM_001131018.1. [Q9ULV3-3]
DR RefSeq; NP_001244904.1; NM_001257975.1.
DR RefSeq; NP_001244905.1; NM_001257976.1. [Q9ULV3-5]
DR RefSeq; NP_036259.2; NM_012127.2. [Q9ULV3-1]
DR RefSeq; XP_005251945.2; XM_005251888.3.
DR RefSeq; XP_005251948.2; XM_005251891.3.
DR RefSeq; XP_005251950.4; XM_005251893.4. [Q9ULV3-3]
DR RefSeq; XP_006717102.2; XM_006717039.3. [Q9ULV3-2]
DR RefSeq; XP_016870085.1; XM_017014596.1. [Q9ULV3-4]
DR AlphaFoldDB; Q9ULV3; -.
DR BioGRID; 117325; 47.
DR IntAct; Q9ULV3; 23.
DR MINT; Q9ULV3; -.
DR STRING; 9606.ENSP00000439244; -.
DR CarbonylDB; Q9ULV3; -.
DR GlyGen; Q9ULV3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULV3; -.
DR PhosphoSitePlus; Q9ULV3; -.
DR BioMuta; CIZ1; -.
DR DMDM; 296434448; -.
DR EPD; Q9ULV3; -.
DR jPOST; Q9ULV3; -.
DR MassIVE; Q9ULV3; -.
DR MaxQB; Q9ULV3; -.
DR PaxDb; Q9ULV3; -.
DR PeptideAtlas; Q9ULV3; -.
DR PRIDE; Q9ULV3; -.
DR ProteomicsDB; 7084; -.
DR ProteomicsDB; 85130; -. [Q9ULV3-1]
DR ProteomicsDB; 85131; -. [Q9ULV3-2]
DR ProteomicsDB; 85132; -. [Q9ULV3-3]
DR ProteomicsDB; 85133; -. [Q9ULV3-4]
DR Antibodypedia; 17368; 106 antibodies from 28 providers.
DR DNASU; 25792; -.
DR Ensembl; ENST00000372938.10; ENSP00000362029.5; ENSG00000148337.22. [Q9ULV3-1]
DR Ensembl; ENST00000372948.7; ENSP00000362039.3; ENSG00000148337.22. [Q9ULV3-4]
DR Ensembl; ENST00000372954.5; ENSP00000362045.1; ENSG00000148337.22. [Q9ULV3-3]
DR Ensembl; ENST00000629610.2; ENSP00000486816.1; ENSG00000148337.22. [Q9ULV3-5]
DR Ensembl; ENST00000634901.1; ENSP00000489425.1; ENSG00000148337.22. [Q9ULV3-1]
DR GeneID; 25792; -.
DR KEGG; hsa:25792; -.
DR MANE-Select; ENST00000372938.10; ENSP00000362029.5; NM_001131016.2; NP_001124488.1.
DR UCSC; uc004btt.4; human. [Q9ULV3-1]
DR CTD; 25792; -.
DR DisGeNET; 25792; -.
DR GeneCards; CIZ1; -.
DR HGNC; HGNC:16744; CIZ1.
DR HPA; ENSG00000148337; Low tissue specificity.
DR MalaCards; CIZ1; -.
DR MIM; 611420; gene.
DR neXtProt; NX_Q9ULV3; -.
DR OpenTargets; ENSG00000148337; -.
DR Orphanet; 420492; Adult-onset cervical dystonia, DYT23 type.
DR PharmGKB; PA134883336; -.
DR VEuPathDB; HostDB:ENSG00000148337; -.
DR eggNOG; ENOG502RYYN; Eukaryota.
DR GeneTree; ENSGT00440000039084; -.
DR HOGENOM; CLU_018344_0_0_1; -.
DR InParanoid; Q9ULV3; -.
DR OrthoDB; 524482at2759; -.
DR PhylomeDB; Q9ULV3; -.
DR TreeFam; TF332388; -.
DR PathwayCommons; Q9ULV3; -.
DR SignaLink; Q9ULV3; -.
DR BioGRID-ORCS; 25792; 21 hits in 1081 CRISPR screens.
DR ChiTaRS; CIZ1; human.
DR GeneWiki; CIZ1; -.
DR GenomeRNAi; 25792; -.
DR Pharos; Q9ULV3; Tbio.
DR PRO; PR:Q9ULV3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9ULV3; protein.
DR Bgee; ENSG00000148337; Expressed in right hemisphere of cerebellum and 197 other tissues.
DR ExpressionAtlas; Q9ULV3; baseline and differential.
DR Genevisible; Q9ULV3; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IEA:Ensembl.
DR InterPro; IPR026811; CIZ1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15491; PTHR15491; 2.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Dystonia; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..898
FT /note="Cip1-interacting zinc finger protein"
FT /id="PRO_0000089776"
FT ZN_FING 799..830
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 680
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 705
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 830
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044729"
FT VAR_SEQ 97..120
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12824700,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_004164"
FT VAR_SEQ 197..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12824700"
FT /id="VSP_004165"
FT VAR_SEQ 377..432
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039894"
FT VARIANT 47
FT /note="P -> S (probable disease-associated variant found in
FT patients with adult onset primary cervical dystonia)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067971"
FT VARIANT 50
FT /note="P -> L (in dbSNP:rs747696276)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067972"
FT VARIANT 219
FT /note="A -> T (in dbSNP:rs45588035)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_056820"
FT VARIANT 264
FT /note="S -> G (probable disease-associated variant found in
FT a family with adult onset primary cervical dystonia; exonic
FT splicing enhancer mutation resulting in altered CIZ1
FT splicing pattern; dbSNP:rs397514566)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067973"
FT VARIANT 370
FT /note="E -> G (in dbSNP:rs45554035)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_063105"
FT VARIANT 394
FT /note="Q -> E (in dbSNP:rs200010931)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067974"
FT VARIANT 577
FT /note="S -> F (in dbSNP:rs780188256)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067975"
FT VARIANT 578
FT /note="S -> F (in dbSNP:rs12334)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_056821"
FT VARIANT 638
FT /note="V -> M (in dbSNP:rs11549266)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_056822"
FT VARIANT 672
FT /note="R -> M (probable disease-associated variant found in
FT patients with adult onset primary cervical dystonia)"
FT /evidence="ECO:0000269|PubMed:22447717"
FT /id="VAR_067976"
FT VARIANT 847
FT /note="R -> Q (in dbSNP:rs11549260)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_063106"
FT CONFLICT 9
FT /note="Missing (in Ref. 7; AAF23231)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="L -> S (in Ref. 7; AAF23231)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> V (in Ref. 3; BAB14750)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="P -> L (in Ref. 1; BAA85783)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> S (in Ref. 7; AAF37882)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="K -> E (in Ref. 3; BAG64643)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="S -> G (in Ref. 1; BAA85783)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="P -> L (in Ref. 7; AAF23231)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="S -> P (in Ref. 7; AAF23231)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="K -> R (in Ref. 7; AAF37882)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="I -> V (in Ref. 3; BAB14750)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="S -> P (in Ref. 3; BAB14750)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="R -> L (in Ref. 8; CAB44346)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="D -> G (in Ref. 7; AAF23231)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="E -> K (in Ref. 3; BAB14750)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="S -> N (in Ref. 7; AAF37882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 100045 MW; 5E14389E81A146F1 CRC64;
MFSQQQQQQL QQQQQQLQQL QQQQLQQQQL QQQQLLQLQQ LLQQSPPQAP LPMAVSRGLP
PQQPQQPLLN LQGTNSASLL NGSMLQRALL LQQLQGLDQF AMPPATYDTA GLTMPTATLG
NLRGYGMASP GLAAPSLTPP QLATPNLQQF FPQATRQSLL GPPPVGVPMN PSQFNLSGRN
PQKQARTSSS TTPNRKDSSS QTMPVEDKSD PPEGSEEAAE PRMDTPEDQD LPPCPEDIAK
EKRTPAPEPE PCEASELPAK RLRSSEEPTE KEPPGQLQVK AQPQARMTVP KQTQTPDLLP
EALEAQVLPR FQPRVLQVQA QVQSQTQPRI PSTDTQVQPK LQKQAQTQTS PEHLVLQQKQ
VQPQLQQEAE PQKQVQPQVQ PQAHSQGPRQ VQLQQEAEPL KQVQPQVQPQ AHSQPPRQVQ
LQLQKQVQTQ TYPQVHTQAQ PSVQPQEHPP AQVSVQPPEQ THEQPHTQPQ VSLLAPEQTP
VVVHVCGLEM PPDAVEAGGG MEKTLPEPVG TQVSMEEIQN ESACGLDVGE CENRAREMPG
VWGAGGSLKV TILQSSDSRA FSTVPLTPVP RPSDSVSSTP AATSTPSKQA LQFFCYICKA
SCSSQQEFQD HMSEPQHQQR LGEIQHMSQA CLLSLLPVPR DVLETEDEEP PPRRWCNTCQ
LYYMGDLIQH RRTQDHKIAK QSLRPFCTVC NRYFKTPRKF VEHVKSQGHK DKAKELKSLE
KEIAGQDEDH FITVDAVGCF EGDEEEEEDD EDEEEIEVEE ELCKQVRSRD ISREEWKGSE
TYSPNTAYGV DFLVPVMGYI CRICHKFYHS NSGAQLSHCK SLGHFENLQK YKAAKNPSPT
TRPVSRRCAI NARNALTALF TSSGRPPSQP NTQDKTPSKV TARPSQPPLP RRSTRLKT
