CASZ1_HUMAN
ID CASZ1_HUMAN Reviewed; 1759 AA.
AC Q86V15; Q078S9; Q2EN02; Q5T9S1; Q6ZNM8; Q8WX49; Q8WX50; Q9BT16; Q9NXC6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger protein castor homolog 1;
DE AltName: Full=Castor-related protein;
DE AltName: Full=Putative survival-related protein;
DE AltName: Full=Zinc finger protein 693;
GN Name=CASZ1; Synonyms=CST, SRG, ZNF693;
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].
RC TISSUE=Heart;
RX PubMed=16322216; DOI=10.1158/0008-5472.can-05-2176;
RA Yuan Z.-R., Wang R., Solomon J., Luo X., Sun H., Zhang L., Shi Y.;
RT "Identification and characterization of survival-related gene, a novel cell
RT survival gene controlling apoptosis and tumorigenesis.";
RL Cancer Res. 65:10716-10724(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16631614; DOI=10.1016/j.bbrc.2006.03.207;
RA Liu Z., Yang X., Tan F., Cullion K., Thiele C.J.;
RT "Molecular cloning and characterization of human Castor, a novel human gene
RT upregulated during cell differentiation.";
RL Biochem. Biophys. Res. Commun. 344:834-844(2006).
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] (ISOFORM 2).
RC TISSUE=Pancreas, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-1759 (ISOFORM 2).
RC TISSUE=Hepatoma, and Rectum;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-981, AND IDENTIFICATION BY
RP 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 [7]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=23639441; DOI=10.1016/j.devcel.2013.03.003;
RA Charpentier M.S., Christine K.S., Amin N.M., Dorr K.M., Kushner E.J.,
RA Bautch V.L., Taylor J.M., Conlon F.L.;
RT "CASZ1 promotes vascular assembly and morphogenesis through the direct
RT regulation of an EGFL7/RhoA-mediated pathway.";
RL Dev. Cell 25:132-143(2013).
RN [8]
RP FUNCTION, VARIANT PRO-38, AND CHARACTERIZATION OF VARIANT PRO-38.
RX PubMed=27693370; DOI=10.1016/j.gene.2016.09.044;
RA Huang R.T., Xue S., Wang J., Gu J.Y., Xu J.H., Li Y.J., Li N., Yang X.X.,
RA Liu H., Zhang X.D., Qu X.K., Xu Y.J., Qiu X.B., Li R.G., Yang Y.Q.;
RT "CASZ1 loss-of-function mutation associated with congenital heart
RT disease.";
RL Gene 595:62-68(2016).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288 AND LYS-975, AND
RP IDENTIFICATION BY MASS 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: Transcriptional activator (PubMed:23639441, PubMed:27693370).
CC Involved in vascular assembly and morphogenesis through direct
CC transcriptional regulation of EGFL7 (PubMed:23639441).
CC {ECO:0000269|PubMed:23639441, ECO:0000269|PubMed:27693370}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16631614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=hCASZ11;
CC IsoId=Q86V15-1; Sequence=Displayed;
CC Name=2; Synonyms=hCASZ5;
CC IsoId=Q86V15-2; Sequence=VSP_027093, VSP_027094;
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, skeletal muscle,
CC pancreas, testis, small intestine, and stomach, but it is not
CC detectable in the adult brain. {ECO:0000269|PubMed:16631614}.
CC -!- MISCELLANEOUS: Endothelial cells depleted in CASZ1 by siRNAs display
CC dramatic alterations in adhesion, morphology and sprouting; normal
CC behavior can be rescued by restoration of EGFL7 expression. The defects
CC are in part due to diminished RhoA expression and impaired focal
CC adhesion localization.
CC -!- CAUTION: According to PubMed:16322216, another protein (SRG) is encoded
CC on the 3'-UTR of the CASZ1 gene. The existence of this protein that may
CC play a role in apoptosis is extremely dubious despite the fact it was
CC localized in the cytoplasm with the help of a polyclonal antibody.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD14411.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAA91089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85474.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CASZ1ID45989ch1p36.html";
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DR EMBL; DQ372703; ABD14411.1; ALT_SEQ; mRNA.
DR EMBL; DQ217660; ABB29845.1; -; mRNA.
DR EMBL; AL139423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004410; AAH04410.2; -; mRNA.
DR EMBL; BC051883; AAH51883.2; -; mRNA.
DR EMBL; AK000328; BAA91089.1; ALT_INIT; mRNA.
DR EMBL; AK130996; BAC85474.1; ALT_SEQ; mRNA.
DR CCDS; CCDS120.2; -. [Q86V15-2]
DR CCDS; CCDS41246.1; -. [Q86V15-1]
DR RefSeq; NP_001073312.1; NM_001079843.2. [Q86V15-1]
DR RefSeq; NP_060236.3; NM_017766.4. [Q86V15-2]
DR AlphaFoldDB; Q86V15; -.
DR BioGRID; 120243; 30.
DR IntAct; Q86V15; 15.
DR MINT; Q86V15; -.
DR STRING; 9606.ENSP00000366221; -.
DR GlyGen; Q86V15; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86V15; -.
DR PhosphoSitePlus; Q86V15; -.
DR BioMuta; CASZ1; -.
DR DMDM; 300669712; -.
DR EPD; Q86V15; -.
DR jPOST; Q86V15; -.
DR MassIVE; Q86V15; -.
DR MaxQB; Q86V15; -.
DR PaxDb; Q86V15; -.
DR PeptideAtlas; Q86V15; -.
DR PRIDE; Q86V15; -.
DR ProteomicsDB; 69945; -. [Q86V15-1]
DR ProteomicsDB; 69946; -. [Q86V15-2]
DR Antibodypedia; 27940; 178 antibodies from 25 providers.
DR DNASU; 54897; -.
DR Ensembl; ENST00000344008.5; ENSP00000339445.5; ENSG00000130940.15. [Q86V15-2]
DR Ensembl; ENST00000377022.8; ENSP00000366221.3; ENSG00000130940.15. [Q86V15-1]
DR GeneID; 54897; -.
DR KEGG; hsa:54897; -.
DR MANE-Select; ENST00000377022.8; ENSP00000366221.3; NM_001079843.3; NP_001073312.1.
DR UCSC; uc001aro.6; human. [Q86V15-1]
DR CTD; 54897; -.
DR DisGeNET; 54897; -.
DR GeneCards; CASZ1; -.
DR HGNC; HGNC:26002; CASZ1.
DR HPA; ENSG00000130940; Tissue enhanced (skin).
DR MIM; 609895; gene.
DR neXtProt; NX_Q86V15; -.
DR OpenTargets; ENSG00000130940; -.
DR Orphanet; 1606; 1p36 deletion syndrome.
DR PharmGKB; PA142672203; -.
DR VEuPathDB; HostDB:ENSG00000130940; -.
DR eggNOG; KOG4377; Eukaryota.
DR GeneTree; ENSGT00390000008187; -.
DR HOGENOM; CLU_003385_0_0_1; -.
DR InParanoid; Q86V15; -.
DR OMA; WPVHASP; -.
DR OrthoDB; 31485at2759; -.
DR PhylomeDB; Q86V15; -.
DR TreeFam; TF324787; -.
DR PathwayCommons; Q86V15; -.
DR SignaLink; Q86V15; -.
DR SIGNOR; Q86V15; -.
DR BioGRID-ORCS; 54897; 24 hits in 1065 CRISPR screens.
DR ChiTaRS; CASZ1; human.
DR GeneWiki; CASZ1; -.
DR GenomeRNAi; 54897; -.
DR Pharos; Q86V15; Tbio.
DR PRO; PR:Q86V15; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86V15; protein.
DR Bgee; ENSG00000130940; Expressed in skin of leg and 176 other tissues.
DR ExpressionAtlas; Q86V15; baseline and differential.
DR Genevisible; Q86V15; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR InterPro; IPR040373; CASZ1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12451; PTHR12451; 2.
DR SMART; SM00355; ZnF_C2H2; 11.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disease variant; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1759
FT /note="Zinc finger protein castor homolog 1"
FT /id="PRO_0000046912"
FT ZN_FING 551..575
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 610..634
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 668..692
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1031..1055
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1300..1324
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1457..1481
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1515..1537
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1571..1595
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1719
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWL2"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWL2"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 975
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1166
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027093"
FT VAR_SEQ 1167..1759
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027094"
FT VARIANT 38
FT /note="L -> P (probable disease-associated variant found in
FT a patient with congenital heart defect; severe decrease of
FT positive regulation of transcription from TH promoter)"
FT /evidence="ECO:0000269|PubMed:27693370"
FT /id="VAR_077466"
FT CONFLICT 192
FT /note="D -> N (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> P (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> N (in Ref. 4; BAA91089)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="Y -> H (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="K -> E (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="L -> P (in Ref. 3; AAH51883)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="M -> T (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="F -> S (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="G -> E (in Ref. 4; BAA91089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="N -> S (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 1501
FT /note="C -> R (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
FT CONFLICT 1549
FT /note="C -> R (in Ref. 2; ABB29845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1759 AA; 190069 MW; 4F5146BE72606654 CRC64;
MDLGTAEGTR CTDPPAGKPA MAPKRKGGLK LNAICAKLSR QVVVEKRADA GSHTEGSPSQ
PRDQERSGPE SGAARAPRSE EDKRRAVIEK WVNGEYSEEP APTPVLGRIA REGLELPPEG
VYMVQPQGCS DEEDHAEEPS KDGGALEEKD SDGAASKEDS GPSTRQASGE ASSLRDYAAS
TMTEFLGMFG YDDQNTRDEL ARKISFEKLH AGSTPEAATS SMLPTSEDTL SKRARFSKYE
EYIRKLKAGE QLSWPAPSTK TEERVGKEVV GTLPGLRLPS STAHLETKAT ILPLPSHSSV
QMQNLVARAS KYDFFIQKLK TGENLRPQNG STYKKPSKYD LENVKYLHLF KPGEGSPDMG
GAIAFKTGKV GRPSKYDVRG IQKPGPAKVP PTPSLAPAPL ASVPSAPSAP GPGPEPPASL
SFNTPEYLKS TFSKTDSITT GTVSTVKNGL PTDKPAVTED VNIYQKYIAR FSGSQHCGHI
HCAYQYREHY HCLDPECNYQ RFTSKQDVIR HYNMHKKRDN SLQHGFMRFS PLDDCSVYYH
GCHLNGKSTH YHCMQVGCNK VYTSTSDVMT HENFHKKNTQ LINDGFQRFR ATEDCGTADC
QFYGQKTTHF HCRRPGCTFT FKNKCDIEKH KSYHIKDDAY AKDGFKKFYK YEECKYEGCV
YSKATNHFHC IRAGCGFTFT STSQMTSHKR KHERRHIRSS GALGLPPSLL GAKDTEHEES
SNDDLVDFSA LSSKNSSLSA SPTSQQSSAS LAAATAATEA GPSATKPPNS KISGLLPQGL
PGSIPLALAL SNSGLPTPTP YFPILAGRGS TSLPVGTPSL LGAVSSGSAA SATPDTPTLV
ASGAGDSAPV AAASVPAPPA SIMERISASK GLISPMMARL AAAALKPSAT FDPGSGQQVT
PARFPPAQVK PEPGESTGAP GPHEASQDRS LDLTVKEPSN ESNGHAVPAN SSLLSSLMNK
MSQGNPGLGS LLNIKAEAEG SPAAEPSPFL GKAVKALVQE KLAEPWKVYL RRFGTKDFCD
GQCDFLHKAH FHCVVEECGA LFSTLDGAIK HANFHFRTEG GAAKGNTEAA FPASAAETKP
PMAPSSPPVP PVTTATVSSL EGPAPSPASV PSTPTLLAWK QLASTIPQMP QIPASVPHLP
ASPLATTSLE NAKPQVKPGF LQFQENDPCL ATDCKYANKF HFHCLFGNCK YVCKTSGKAE
SHCLDHINPN NNLVNVRDQF AYYSLQCLCP NQHCEFRMRG HYHCLRTGCY FVTNITTKLP
WHIKKHEKAE RRAANGFKYF TKREECGRLG CKYNQVNSHF HCIREGCQFS FLLKHQMTSH
ARKHMRRMLG KNFDRVPPSQ GPPGLMDAET DECMDYTGCS PGAMSSESST MDRSCSSTPV
GNESTAAGNT ISMPTASGAK KRFWIIEDMS PFGKRRKTAS SRKMLDEGMM LEGFRRFDLY
EDCKDAACQF SLKVTHYHCT RENCGYKFCG RTHMYKHAQH HDRVDNLVLD DFKRFKASLS
CHFADCPFSG TSTHFHCLRC RFRCTDSTKV TAHRKHHGKQ DVISAAGFCQ FSSSADCAVP
DCKYKLKCSH FHCTFPGCRH TVVGMSQMDS HKRKHEKQER GEPAAEGPAP GPPISLDGSL
SLGAEPGSLL FLQSAAAGLG LALGDAGDPG PPDAAAPGPR EGAAAAAAAA GESSQEDEEE
ELELPEEEAE DDEDEDDDED DDDEDDDEDD DDEDLRTDSE ESLPEAAAEA AGAGARTPAL
AALAALGAPG PAPTAASSP
