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Cip1-interacting zinc finger protein (CDKN1A-interacting zinc finger protein 1) (Nuclear protein NP94) (Zinc finger protein 356)

 CIZ1_HUMAN              Reviewed;         898 AA.
Q9ULV3; A8K9J8; B4E131; B7ZAS8; Q5SYW3; Q5SYW5; Q8WU72; Q9H868;
Q9NYM8; Q9UHK4; Q9Y3F9; Q9Y3G0;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 151.
RecName: Full=Cip1-interacting zinc finger protein;
AltName: Full=CDKN1A-interacting zinc finger protein 1;
AltName: Full=Nuclear protein NP94;
AltName: Full=Zinc finger protein 356;
Name=CIZ1; Synonyms=LSFR1, NP94, ZNF356;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10529385; DOI=10.1006/bbrc.1999.1516;
Mitsui K., Matsumoto A., Ohtsuka S., Ohtsubo M., Yoshimura A.;
"Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
zinc finger protein, ciz1.";
Biochem. Biophys. Res. Commun. 264:457-464(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-219; GLY-370;
PHE-578; MET-638 AND GLN-847.
NIEHS SNPs program;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), AND
VARIANT MET-638.
TISSUE=Testis, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-898 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 50-898 (ISOFORM 2).
TISSUE=Medulloblastoma;
PubMed=12824700; DOI=10.1007/BF02256432;
Warder D.E., Keherly M.J.;
"Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus DNA
sequence ARYSR(0-2)YYAC.";
J. Biomed. Sci. 10:406-417(2003).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 649-898.
PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
Gilley J., Fried M.;
"Extensive gene order differences within regions of conserved synteny
between the Fugu and human genomes: implications for chromosomal
evolution and the cloning of disease genes.";
Hum. Mol. Genet. 8:1313-1320(1999).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-567, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
POSSIBLE INVOLVEMENT IN ADULT ONSET PRIMARY CERVICAL DYSTONIA, AND
VARIANTS SER-47; LEU-50; GLY-264; GLU-394; PHE-577 AND MET-672.
PubMed=22447717; DOI=10.1002/ana.23547;
Xiao J., Uitti R.J., Zhao Y., Vemula S.R., Perlmutter J.S.,
Wszolek Z.K., Maraganore D.M., Auburger G., Leube B., Lehnhoff K.,
Ledoux M.S.;
"Mutations in CIZ1 cause adult onset primary cervical dystonia.";
Ann. Neurol. 71:458-469(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; THR-244; SER-350;
SER-547; SER-821 AND SER-838, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-705, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280; LYS-340; LYS-401;
LYS-549; LYS-588; LYS-680; LYS-705; LYS-830 AND LYS-879, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: May regulate the subcellular localization of CIP/WAF1.
-!- SUBUNIT: Interacts with CIP/WAF1.
-!- INTERACTION:
Q9P0V3:SH3BP4; NbExp=2; IntAct=EBI-2652948, EBI-1049513;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9ULV3-1; Sequence=Displayed;
Name=2; Synonyms=NP94B;
IsoId=Q9ULV3-2; Sequence=VSP_004164, VSP_004165;
Name=3;
IsoId=Q9ULV3-3; Sequence=VSP_004164, VSP_039894;
Name=4;
IsoId=Q9ULV3-4; Sequence=VSP_039894;
Name=5;
IsoId=Q9ULV3-5; Sequence=VSP_044729;
Note=No experimental confirmation available.;
-!- DISEASE: Note=Defects in CIZ1 may be a cause of adult onset
primary cervical dystonia. Dystonia is defined by the presence of
sustained involuntary muscle contractions, often leading to
abnormal postures. Cervical dystonia or spasmodic torticollis, the
most common form of focal dystonia, is characterized by
involuntary contractions of the neck muscles, which produce
abnormal posturing of the head upon the trunk.
-!- SEQUENCE CAUTION:
Sequence=AAF23231.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF37882.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ciz1/";
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EMBL; AB030835; BAA85783.1; -; mRNA.
EMBL; EF467915; ABO43037.1; -; Genomic_DNA.
EMBL; AK023978; BAB14750.1; -; mRNA.
EMBL; AK292713; BAF85402.1; -; mRNA.
EMBL; AK303636; BAG64643.1; -; mRNA.
EMBL; AK316393; BAH14764.1; -; mRNA.
EMBL; AL590708; CAI13828.1; -; Genomic_DNA.
EMBL; AL590708; CAI13829.1; -; Genomic_DNA.
EMBL; AL590708; CAI13831.1; -; Genomic_DNA.
EMBL; CH471090; EAW87752.1; -; Genomic_DNA.
EMBL; CH471090; EAW87753.1; -; Genomic_DNA.
EMBL; CH471090; EAW87754.1; -; Genomic_DNA.
EMBL; BC021163; AAH21163.1; -; mRNA.
EMBL; AF159027; AAF23231.1; ALT_INIT; mRNA.
EMBL; AF234161; AAF37882.1; ALT_INIT; mRNA.
EMBL; Y17453; CAB44346.1; -; Genomic_DNA.
EMBL; Y17454; CAB44347.1; -; Genomic_DNA.
CCDS; CCDS48033.1; -. [Q9ULV3-3]
CCDS; CCDS48034.1; -. [Q9ULV3-4]
CCDS; CCDS59147.1; -. [Q9ULV3-5]
CCDS; CCDS6894.1; -. [Q9ULV3-1]
RefSeq; NP_001124487.1; NM_001131015.1. [Q9ULV3-4]
RefSeq; NP_001124488.1; NM_001131016.1. [Q9ULV3-1]
RefSeq; NP_001124489.1; NM_001131017.1.
RefSeq; NP_001124490.1; NM_001131018.1. [Q9ULV3-3]
RefSeq; NP_001244904.1; NM_001257975.1.
RefSeq; NP_001244905.1; NM_001257976.1. [Q9ULV3-5]
RefSeq; NP_036259.2; NM_012127.2. [Q9ULV3-1]
RefSeq; XP_005251945.2; XM_005251888.3. [Q9ULV3-1]
RefSeq; XP_005251948.2; XM_005251891.3. [Q9ULV3-4]
RefSeq; XP_005251950.4; XM_005251893.4. [Q9ULV3-3]
RefSeq; XP_006717102.2; XM_006717039.3. [Q9ULV3-2]
RefSeq; XP_016870085.1; XM_017014596.1. [Q9ULV3-4]
UniGene; Hs.212395; -.
ProteinModelPortal; Q9ULV3; -.
BioGrid; 117325; 27.
IntAct; Q9ULV3; 11.
STRING; 9606.ENSP00000362029; -.
iPTMnet; Q9ULV3; -.
PhosphoSitePlus; Q9ULV3; -.
BioMuta; CIZ1; -.
DMDM; 296434448; -.
EPD; Q9ULV3; -.
PaxDb; Q9ULV3; -.
PeptideAtlas; Q9ULV3; -.
PRIDE; Q9ULV3; -.
Ensembl; ENST00000372938; ENSP00000362029; ENSG00000148337. [Q9ULV3-1]
Ensembl; ENST00000372948; ENSP00000362039; ENSG00000148337. [Q9ULV3-4]
Ensembl; ENST00000372954; ENSP00000362045; ENSG00000148337. [Q9ULV3-3]
Ensembl; ENST00000629610; ENSP00000486816; ENSG00000148337. [Q9ULV3-5]
Ensembl; ENST00000634901; ENSP00000489425; ENSG00000148337. [Q9ULV3-1]
GeneID; 25792; -.
KEGG; hsa:25792; -.
UCSC; uc004btt.4; human. [Q9ULV3-1]
CTD; 25792; -.
DisGeNET; 25792; -.
EuPathDB; HostDB:ENSG00000148337.20; -.
GeneCards; CIZ1; -.
HGNC; HGNC:16744; CIZ1.
HPA; HPA020380; -.
HPA; HPA020387; -.
MIM; 611420; gene.
neXtProt; NX_Q9ULV3; -.
OpenTargets; ENSG00000148337; -.
PharmGKB; PA134883336; -.
eggNOG; ENOG410II97; Eukaryota.
eggNOG; ENOG4111HAM; LUCA.
GeneTree; ENSGT00440000039084; -.
HOVERGEN; HBG002558; -.
InParanoid; Q9ULV3; -.
PhylomeDB; Q9ULV3; -.
TreeFam; TF332388; -.
ChiTaRS; CIZ1; human.
GeneWiki; CIZ1; -.
GenomeRNAi; 25792; -.
PRO; PR:Q9ULV3; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148337; -.
CleanEx; HS_CIZ1; -.
ExpressionAtlas; Q9ULV3; baseline and differential.
Genevisible; Q9ULV3; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR026811; CIZ1.
InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR022755; Znf_C2H2_jaz.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR15491; PTHR15491; 2.
Pfam; PF12171; zf-C2H2_jaz; 1.
SMART; SM00355; ZnF_C2H2; 3.
SMART; SM00451; ZnF_U1; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS50171; ZF_MATRIN; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation; Dystonia;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 898 Cip1-interacting zinc finger protein.
/FTId=PRO_0000089776.
ZN_FING 799 830 Matrin-type. {ECO:0000255|PROSITE-
ProRule:PRU00130}.
COMPBIAS 4 44 Gln-rich.
COMPBIAS 276 470 Gln-rich.
COMPBIAS 741 761 Glu-rich.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 244 244 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 567 567 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 280 280 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 340 340 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 549 549 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 588 588 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 680 680 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 705 705 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 830 830 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 879 879 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 101 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044729.
VAR_SEQ 97 120 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12824700,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_004164.
VAR_SEQ 197 201 Missing (in isoform 2).
{ECO:0000303|PubMed:12824700}.
/FTId=VSP_004165.
VAR_SEQ 377 432 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_039894.
VARIANT 47 47 P -> S (probable disease-associated
mutation found in patients with adult
onset primary cervical dystonia).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067971.
VARIANT 50 50 P -> L (in dbSNP:rs747696276).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067972.
VARIANT 219 219 A -> T (in dbSNP:rs45588035).
{ECO:0000269|Ref.2}.
/FTId=VAR_056820.
VARIANT 264 264 S -> G (probable disease-associated
mutation found in a family with adult
onset primary cervical dystonia; exonic
splicing enhancer mutation resulting in
altered CIZ1 splicing pattern;
dbSNP:rs397514566).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067973.
VARIANT 370 370 E -> G (in dbSNP:rs45554035).
{ECO:0000269|Ref.2}.
/FTId=VAR_063105.
VARIANT 394 394 Q -> E (in dbSNP:rs200010931).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067974.
VARIANT 577 577 S -> F (in dbSNP:rs780188256).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067975.
VARIANT 578 578 S -> F (in dbSNP:rs12334).
{ECO:0000269|Ref.2}.
/FTId=VAR_056821.
VARIANT 638 638 V -> M (in dbSNP:rs11549266).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_056822.
VARIANT 672 672 R -> M (probable disease-associated
mutation found in patients with adult
onset primary cervical dystonia).
{ECO:0000269|PubMed:22447717}.
/FTId=VAR_067976.
VARIANT 847 847 R -> Q (in dbSNP:rs11549260).
{ECO:0000269|Ref.2}.
/FTId=VAR_063106.
CONFLICT 9 9 Missing (in Ref. 7; AAF23231).
{ECO:0000305}.
CONFLICT 35 35 L -> S (in Ref. 7; AAF23231).
{ECO:0000305}.
CONFLICT 101 101 A -> V (in Ref. 3; BAB14750).
{ECO:0000305}.
CONFLICT 232 232 P -> L (in Ref. 1; BAA85783).
{ECO:0000305}.
CONFLICT 500 500 G -> S (in Ref. 7; AAF37882).
{ECO:0000305}.
CONFLICT 549 549 K -> E (in Ref. 3; BAG64643).
{ECO:0000305}.
CONFLICT 555 555 S -> G (in Ref. 1; BAA85783).
{ECO:0000305}.
CONFLICT 568 568 P -> L (in Ref. 7; AAF23231).
{ECO:0000305}.
CONFLICT 634 634 S -> P (in Ref. 7; AAF23231).
{ECO:0000305}.
CONFLICT 677 677 K -> R (in Ref. 7; AAF37882).
{ECO:0000305}.
CONFLICT 678 678 I -> V (in Ref. 3; BAB14750).
{ECO:0000305}.
CONFLICT 682 682 S -> P (in Ref. 3; BAB14750).
{ECO:0000305}.
CONFLICT 698 698 R -> L (in Ref. 8; CAB44346).
{ECO:0000305}.
CONFLICT 735 735 D -> G (in Ref. 7; AAF23231).
{ECO:0000305}.
CONFLICT 757 757 E -> K (in Ref. 3; BAB14750).
{ECO:0000305}.
CONFLICT 810 810 S -> N (in Ref. 7; AAF37882).
{ECO:0000305}.
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


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