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Zinc finger protein ZIC 2 (Zinc finger protein of the cerebellum 2)

 ZIC2_HUMAN              Reviewed;         532 AA.
O95409; Q5VYA9; Q9H309;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
22-NOV-2017, entry version 164.
RecName: Full=Zinc finger protein ZIC 2;
AltName: Full=Zinc finger protein of the cerebellum 2;
Name=ZIC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION OF VARIANT HPE5
POLY-ALA INS.
PubMed=9771712; DOI=10.1038/2484;
Brown S.A., Warburton D., Brown L.Y., Yu C.Y., Roeder E.R.,
Stengel-Rutkowski S., Hennekam R.C.M., Muenke M.;
"Holoprosencephaly due to mutations in ZIC2, a homologue of Drosophila
odd-paired.";
Nat. Genet. 20:180-183(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10984499; DOI=10.1074/jbc.M007906200;
Yang Y., Hwang C.K., Junn E., Lee G., Mouradian M.M.;
"ZIC2 and Sp3 repress Sp1-induced activation of the human D1A dopamine
receptor gene.";
J. Biol. Chem. 275:38863-38869(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
INTERACTION WITH DHX9.
PubMed=17251188; DOI=10.1074/jbc.M610821200;
Ishiguro A., Ideta M., Mikoshiba K., Chen D.J., Aruga J.;
"ZIC2-dependent transcriptional regulation is mediated by DNA-
dependent protein kinase, poly(ADP-ribose) polymerase, and RNA
helicase A.";
J. Biol. Chem. 282:9983-9995(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[6]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, 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).
[7]
VARIANTS HPE5 POLY-ALA INS AND PHE-152, AND POLYMORPHISM OF POLY-HIS
REGION.
PubMed=11285244; DOI=10.1093/hmg/10.8.791;
Brown L.Y., Odent S., David V., Blayau M., Dubourg C., Apacik C.,
Delgado M.A., Hall B.D., Reynolds J.F., Sommer A., Wieczorek D.,
Brown S.A., Muenke M.;
"Holoprosencephaly due to mutations in ZIC2: alanine tract expansion
mutations may be caused by parental somatic recombination.";
Hum. Mol. Genet. 10:791-796(2001).
[8]
VARIANTS HPE5 PRO-36 AND PHE-152, AND VARIANTS HIS-239 INS AND HIS-239
DEL.
PubMed=15221788; DOI=10.1002/humu.20056;
Dubourg C., Lazaro L., Pasquier L., Bendavid C., Blayau M.,
Le Duff F., Durou M.-R., Odent S., David V.;
"Molecular screening of SHH, ZIC2, SIX3, and TGIF genes in patients
with features of holoprosencephaly spectrum: mutation review and
genotype-phenotype correlations.";
Hum. Mutat. 24:43-51(2004).
[9]
CHARACTERIZATION OF VARIANTS HPE5 PRO-36; PHE-152 AND POLY-ALA INS.
PubMed=15590697; DOI=10.1093/hmg/ddi037;
Brown L., Paraso M., Arkell R., Brown S.;
"In vitro analysis of partial loss-of-function ZIC2 mutations in
holoprosencephaly: alanine tract expansion modulates DNA binding and
transactivation.";
Hum. Mol. Genet. 14:411-420(2005).
[10]
VARIANTS HPE5 ASN-37; ASN-128; ASN-272; LEU-286; GLN-286; TYR-286;
TYR-291; ARG-304; CYS-314; SER-325; LEU-325; TYR-327; PHE-335;
PRO-373; ASN-402; LYS-403; ARG-404; TRP-409 AND GLN-415.
PubMed=19177455; DOI=10.1002/humu.20982;
Roessler E., Lacbawan F., Dubourg C., Paulussen A., Herbergs J.,
Hehr U., Bendavid C., Zhou N., Ouspenskaia M., Bale S., Odent S.,
David V., Muenke M.;
"The full spectrum of holoprosencephaly-associated mutations within
the ZIC2 gene in humans predicts loss-of-function as the predominant
disease mechanism.";
Hum. Mutat. 30:E541-E554(2009).
-!- FUNCTION: Acts as a transcriptional activator or repressor. Plays
important roles in the early stage of organogenesis of the CNS.
Activates the transcription of the serotonin transporter SERT in
uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine
eye-specific projections in primary visual targets. Its
transcriptional activity is repressed by MDFIC. Involved in the
formation of the ipsilateral retinal projection at the optic
chiasm midline. Drives the expression of EPHB1 on ipsilaterally
projecting growth cones. Binds to the minimal GLI-consensus
sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter
region from ventrotemporal retinal segments of retinal embryos.
-!- SUBUNIT: Interacts with RNF180. Interacts (via the C2H2-type
domains 3, 4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and
5); the interaction reduces its transcriptional activity.
Interacts with GLI1 and GLI2 (By similarity). Interacts (via C2H2-
type domain 3) with DHX9 (PubMed:17251188).
{ECO:0000250|UniProtKB:Q62520, ECO:0000269|PubMed:17251188}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
Note=Localizes in the cytoplasm in presence of MDFIC
overexpression. Both phosphorylated and unphosphorylated forms are
localized in the nucleus (By similarity). {ECO:0000250}.
-!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary
for transcription activation. {ECO:0000250}.
-!- PTM: Phosphorylated.
-!- PTM: Ubiquitinated by RNF180, leading to its degradation.
-!- POLYMORPHISM: The poly-His region between amino acids 231-239 of
ZIC2 is polymorphic and the number of His can vary from 8 to 12.
{ECO:0000269|PubMed:11285244}.
-!- DISEASE: Holoprosencephaly 5 (HPE5) [MIM:609637]: A structural
anomaly of the brain, in which the developing forebrain fails to
correctly separate into right and left hemispheres.
Holoprosencephaly is genetically heterogeneous and associated with
several distinct facies and phenotypic variability.
{ECO:0000269|PubMed:11285244, ECO:0000269|PubMed:15221788,
ECO:0000269|PubMed:15590697, ECO:0000269|PubMed:19177455,
ECO:0000269|PubMed:9771712}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AF104902; AAC96325.1; -; mRNA.
EMBL; AF193855; AAG28409.1; -; mRNA.
EMBL; AL355338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS9495.1; -.
RefSeq; NP_009060.2; NM_007129.3.
UniGene; Hs.653700; -.
ProteinModelPortal; O95409; -.
SMR; O95409; -.
BioGrid; 113378; 15.
IntAct; O95409; 2.
MINT; MINT-2798893; -.
STRING; 9606.ENSP00000365514; -.
iPTMnet; O95409; -.
PhosphoSitePlus; O95409; -.
BioMuta; ZIC2; -.
EPD; O95409; -.
MaxQB; O95409; -.
PaxDb; O95409; -.
PeptideAtlas; O95409; -.
PRIDE; O95409; -.
DNASU; 7546; -.
Ensembl; ENST00000376335; ENSP00000365514; ENSG00000043355.
GeneID; 7546; -.
KEGG; hsa:7546; -.
UCSC; uc001von.4; human.
CTD; 7546; -.
DisGeNET; 7546; -.
EuPathDB; HostDB:ENSG00000043355.10; -.
GeneCards; ZIC2; -.
GeneReviews; ZIC2; -.
HGNC; HGNC:12873; ZIC2.
HPA; HPA055031; -.
MalaCards; ZIC2; -.
MIM; 603073; gene.
MIM; 609637; phenotype.
neXtProt; NX_O95409; -.
OpenTargets; ENSG00000043355; -.
Orphanet; 93925; Alobar holoprosencephaly.
Orphanet; 93924; Lobar holoprosencephaly.
Orphanet; 280200; Microform holoprosencephaly.
Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
Orphanet; 220386; Semilobar holoprosencephaly.
Orphanet; 280195; Septopreoptic holoprosencephaly.
PharmGKB; PA37462; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOGENOM; HOG000232057; -.
HOVERGEN; HBG007135; -.
InParanoid; O95409; -.
KO; K06235; -.
OMA; DSAHMGA; -.
OrthoDB; EOG091G0M59; -.
PhylomeDB; O95409; -.
TreeFam; TF351425; -.
SignaLink; O95409; -.
SIGNOR; O95409; -.
GeneWiki; ZIC2; -.
GenomeRNAi; 7546; -.
PRO; PR:O95409; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000043355; -.
CleanEx; HS_ZIC2; -.
ExpressionAtlas; O95409; baseline and differential.
Genevisible; O95409; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0007420; P:brain development; TAS:ProtInc.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; ISS:UniProtKB.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Disease mutation; DNA-binding; Holoprosencephaly;
Isopeptide bond; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 532 Zinc finger protein ZIC 2.
/FTId=PRO_0000047247.
ZN_FING 256 291 C2H2-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 300 327 C2H2-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 333 357 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 363 387 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 393 415 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 100 255 Necessary for interaction with MDFIC and
transcriptional activation or repression.
{ECO:0000250}.
COMPBIAS 20 23 Poly-His.
COMPBIAS 25 33 Poly-Ala.
COMPBIAS 89 97 Poly-Ala.
COMPBIAS 226 230 Poly-Ala.
COMPBIAS 231 239 Poly-His.
COMPBIAS 456 470 Poly-Ala.
COMPBIAS 490 508 Poly-Gly.
MOD_RES 191 191 Phosphoserine.
{ECO:0000250|UniProtKB:Q62520}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:Q62520}.
CROSSLNK 253 253 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 36 36 Q -> P (in HPE5; 2-fold increase in
luciferase activity).
{ECO:0000269|PubMed:15221788,
ECO:0000269|PubMed:15590697}.
/FTId=VAR_023793.
VARIANT 37 37 D -> N (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058592.
VARIANT 128 128 D -> N (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058593.
VARIANT 152 152 D -> F (in HPE5; requires 2 nucleotide
substitutions; 50% reduction of
luciferase activity).
{ECO:0000269|PubMed:11285244,
ECO:0000269|PubMed:15221788,
ECO:0000269|PubMed:15590697}.
/FTId=VAR_023794.
VARIANT 239 239 H -> HH. {ECO:0000269|PubMed:15221788}.
/FTId=VAR_023795.
VARIANT 239 239 Missing. {ECO:0000269|PubMed:15221788}.
/FTId=VAR_023796.
VARIANT 272 272 S -> N (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058594.
VARIANT 286 286 H -> L (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058595.
VARIANT 286 286 H -> Q (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058596.
VARIANT 286 286 H -> Y (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058597.
VARIANT 291 291 H -> Y (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058598.
VARIANT 304 304 W -> R (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058599.
VARIANT 314 314 F -> C (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058600.
VARIANT 325 325 R -> L (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058601.
VARIANT 325 325 R -> S (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058602.
VARIANT 327 327 H -> Y (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058603.
VARIANT 335 335 C -> F (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058604.
VARIANT 373 373 R -> P (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058605.
VARIANT 402 402 Y -> N (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058606.
VARIANT 403 403 T -> K (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058607.
VARIANT 404 404 H -> R (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058608.
VARIANT 409 409 R -> W (in HPE5).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058609.
VARIANT 415 415 H -> Q (in HPE5; dbSNP:rs794729641).
{ECO:0000269|PubMed:19177455}.
/FTId=VAR_058610.
VARIANT 470 470 A -> AAAAAAAAAAA (in HPE5; near-complete
loss of luciferase activity).
/FTId=VAR_008856.
CONFLICT 124 128 RGFGD -> ARLPGT (in Ref. 1; AAC96325).
{ECO:0000305}.
SEQUENCE 532 AA; 55006 MW; BA3E6455DAF97EAC CRC64;
MLLDAGPQFP AIGVGSFARH HHHSAAAAAA AAAEMQDREL SLAAAQNGFV DSAAAHMGAF
KLNPGAHELS PGQSSAFTSQ GPGAYPGSAA AAAAAAALGP HAAHVGSYSG PPFNSTRDFL
FRSRGFGDSA PGGGQHGLFG PGAGGLHHAH SDAQGHLLFP GLPEQHGPHG SQNVLNGQMR
LGLPGEVFGR SEQYRQVASP RTDPYSAAQL HNQYGPMNMN MGMNMAAAAA HHHHHHHHHP
GAFFRYMRQQ CIKQELICKW IDPEQLSNPK KSCNKTFSTM HELVTHVSVE HVGGPEQSNH
VCFWEECPRE GKPFKAKYKL VNHIRVHTGE KPFPCPFPGC GKVFARSENL KIHKRTHTGE
KPFQCEFEGC DRRFANSSDR KKHMHVHTSD KPYLCKMCDK SYTHPSSLRK HMKVHESSPQ
GSESSPAASS GYESSTPPGL VSPSAEPQSS SNLSPAAAAA AAAAAAAAAA VSAVHRGGGS
GSGGAGGGSG GGSGSGGGGG GAGGGGGGSS GGGSGTAGGH SGLSSNFNEW YV


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EIAAB47907 GIOT2,GIOT-2,Gonadotropin-inducible ovary transcription repressor 2,Homo sapiens,Human,KOX7,Zinc finger protein 44,Zinc finger protein 55,Zinc finger protein 58,Zinc finger protein KOX7,ZNF44,ZNF55,ZN
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EIAAB47892 Homo sapiens,Human,KOX17,Retinoic acid suppression protein A,RSG-A,Zinc finger and SCAN domain-containing protein 3,Zinc finger protein 191,Zinc finger protein 24,Zinc finger protein KOX17,ZNF191,ZNF2
18-003-42388 Zinc finger protein 24 - Zinc finger protein 191; Zinc finger protein KOX17; Retinoic acid suppression protein A; RSG-A; Zinc finger and SCAN domain-containing protein 3 Polyclonal 0.05 mg Aff Pur
EIAAB47372 Homo sapiens,Human,Zinc finger protein 135-like,Zinc finger protein 140-like,Zinc finger protein 302,Zinc finger protein 327,ZNF135L,ZNF140L,ZNF302,ZNF327


 

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