ID ZN593_HUMAN Reviewed; 134 AA. AC O00488; B2R4S0; Q5T2H7; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 2. DT 27-MAR-2024, entry version 188. DE RecName: Full=Zinc finger protein 593; DE AltName: Full=Zinc finger protein T86; GN Name=ZNF593; Synonyms=ZT86; 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]. RC TISSUE=Cerebellum; 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 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 [3] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-134, FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=T-cell lymphoma; RX PubMed=9115366; DOI=10.1093/nar/25.10.1984; RA Terunuma A., Shiba K., Noda T.; RT "A novel genetic system to isolate a dominant negative effector on DNA- RT binding activity of Oct-2."; RL Nucleic Acids Res. 25:1984-1990(1997). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] 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 [9] RP IDENTIFICATION BY 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 [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [13] RP STRUCTURE BY NMR OF 20-134 IN COMPLEX WITH ZINC IONS, AND DOMAIN. RX PubMed=18287285; DOI=10.1110/ps.073290408; RA Hayes P.L., Lytle B.L., Volkman B.F., Peterson F.C.; RT "The solution structure of ZNF593 from Homo sapiens reveals a zinc finger RT in a predominantly unstructured protein."; RL Protein Sci. 17:571-576(2008). RN [14] {ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.13 ANGSTROMS) IN COMPLEX WITH PRE-60S RP RIBOSOMAL PARTICLES, FUNCTION, AND INTERACTION WITH PRE-60S RIBOSOMAL RP PARTICLES. RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x; RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.; RT "Structural snapshots of human pre-60S ribosomal particles before and after RT nuclear export."; RL Nat. Commun. 11:3542-3542(2020). CC -!- FUNCTION: Involved in pre-60S ribosomal particles maturation by CC promoting the nuclear export of the 60S ribosome (PubMed:32669547). CC Negatively modulates the DNA binding activity of Oct-2 and therefore CC its transcriptional regulatory activity (PubMed:9115366). CC {ECO:0000269|PubMed:9115366, ECO:0000305|PubMed:32669547}. CC -!- SUBUNIT: Associates with pre-60S ribosomal particles. CC {ECO:0000269|PubMed:32669547}. CC -!- INTERACTION: CC O00488; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-726769, EBI-742054; CC O00488; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-726769, EBI-739832; CC O00488; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-726769, EBI-79165; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. CC Cytoplasm {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the CC nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q08004}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, prostate, testis, CC small intestine, colon and to a minor level in thymus and peripheral CC blood leukocytes. {ECO:0000269|PubMed:9115366}. CC -!- DOMAIN: The protein is largely disordered, with the exception of the CC zinc finger domain. {ECO:0000269|PubMed:18287285}. CC -!- SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH02580.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH19267.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA20369.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG34867.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK311926; BAG34867.1; ALT_INIT; mRNA. DR EMBL; AL391650; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07843.1; -; Genomic_DNA. DR EMBL; BC002580; AAH02580.1; ALT_INIT; mRNA. DR EMBL; BC019267; AAH19267.1; ALT_INIT; mRNA. DR EMBL; D45213; BAA20369.1; ALT_INIT; mRNA. DR CCDS; CCDS275.2; -. DR RefSeq; NP_056955.2; NM_015871.4. DR PDB; 1ZR9; NMR; -; A=20-134. DR PDB; 6LSS; EM; 3.23 A; 9=1-134. DR PDB; 6LU8; EM; 3.13 A; 9=1-134. DR PDB; 8FL2; EM; 2.67 A; NP=1-134. DR PDB; 8FL3; EM; 2.53 A; NP=1-134. DR PDB; 8FL4; EM; 2.89 A; NP=1-134. DR PDB; 8FL6; EM; 2.62 A; NP=1-134. DR PDB; 8FL7; EM; 2.55 A; NP=1-134. DR PDB; 8FL9; EM; 2.75 A; NP=1-134. DR PDB; 8FLA; EM; 2.63 A; NP=1-134. DR PDB; 8FLB; EM; 2.55 A; NP=1-134. DR PDB; 8FLC; EM; 2.76 A; NP=1-134. DR PDB; 8FLD; EM; 2.58 A; NP=1-134. DR PDB; 8FLE; EM; 2.48 A; NP=1-134. DR PDB; 8FLF; EM; 2.65 A; NP=1-134. DR PDB; 8IDT; EM; 2.80 A; 9=1-134. DR PDB; 8IDY; EM; 3.00 A; 9=1-134. DR PDB; 8IE3; EM; 3.30 A; 9=1-134. DR PDB; 8INE; EM; 3.20 A; 9=1-134. DR PDB; 8INF; EM; 3.00 A; 9=1-134. DR PDB; 8INK; EM; 3.20 A; 9=1-134. DR PDB; 8IPD; EM; 3.20 A; 9=1-134. DR PDB; 8IPX; EM; 4.30 A; 9=1-134. DR PDB; 8IPY; EM; 3.20 A; 9=1-134. DR PDB; 8IR3; EM; 3.50 A; 9=1-134. DR PDBsum; 1ZR9; -. DR PDBsum; 6LSS; -. DR PDBsum; 6LU8; -. DR PDBsum; 8FL2; -. DR PDBsum; 8FL3; -. DR PDBsum; 8FL4; -. DR PDBsum; 8FL6; -. DR PDBsum; 8FL7; -. DR PDBsum; 8FL9; -. DR PDBsum; 8FLA; -. DR PDBsum; 8FLB; -. DR PDBsum; 8FLC; -. DR PDBsum; 8FLD; -. DR PDBsum; 8FLE; -. DR PDBsum; 8FLF; -. DR PDBsum; 8IDT; -. DR PDBsum; 8IDY; -. DR PDBsum; 8IE3; -. DR PDBsum; 8INE; -. DR PDBsum; 8INF; -. DR PDBsum; 8INK; -. DR PDBsum; 8IPD; -. DR PDBsum; 8IPX; -. DR PDBsum; 8IPY; -. DR PDBsum; 8IR3; -. DR AlphaFoldDB; O00488; -. DR EMDB; EMD-0964; -. DR EMDB; EMD-0978; -. DR EMDB; EMD-29265; -. DR EMDB; EMD-29266; -. DR EMDB; EMD-29267; -. DR EMDB; EMD-29268; -. DR EMDB; EMD-29269; -. DR EMDB; EMD-29271; -. DR EMDB; EMD-29272; -. DR EMDB; EMD-29273; -. DR EMDB; EMD-29274; -. DR EMDB; EMD-29275; -. DR EMDB; EMD-29276; -. DR EMDB; EMD-29277; -. DR EMDB; EMD-35370; -. DR EMDB; EMD-35371; -. DR EMDB; EMD-35375; -. DR EMDB; EMD-35596; -. DR EMDB; EMD-35597; -. DR EMDB; EMD-35599; -. DR EMDB; EMD-35639; -. DR EMDB; EMD-35649; -. DR EMDB; EMD-35651; -. DR EMDB; EMD-35673; -. DR SMR; O00488; -. DR BioGRID; 119241; 61. DR IntAct; O00488; 23. DR MINT; O00488; -. DR STRING; 9606.ENSP00000363384; -. DR iPTMnet; O00488; -. DR PhosphoSitePlus; O00488; -. DR BioMuta; ZNF593; -. DR EPD; O00488; -. DR jPOST; O00488; -. DR MassIVE; O00488; -. DR MaxQB; O00488; -. DR PaxDb; 9606-ENSP00000363384; -. DR PeptideAtlas; O00488; -. DR ProteomicsDB; 47933; -. DR Pumba; O00488; -. DR Antibodypedia; 30564; 77 antibodies from 19 providers. DR DNASU; 51042; -. DR Ensembl; ENST00000374266.7; ENSP00000363384.5; ENSG00000142684.9. DR GeneID; 51042; -. DR KEGG; hsa:51042; -. DR MANE-Select; ENST00000374266.7; ENSP00000363384.5; NM_015871.5; NP_056955.2. DR UCSC; uc001bll.5; human. DR AGR; HGNC:30943; -. DR CTD; 51042; -. DR DisGeNET; 51042; -. DR GeneCards; ZNF593; -. DR HGNC; HGNC:30943; ZNF593. DR HPA; ENSG00000142684; Low tissue specificity. DR MIM; 616698; gene. DR neXtProt; NX_O00488; -. DR OpenTargets; ENSG00000142684; -. DR PharmGKB; PA134962156; -. DR VEuPathDB; HostDB:ENSG00000142684; -. DR eggNOG; KOG3408; Eukaryota. DR GeneTree; ENSGT00390000004173; -. DR HOGENOM; CLU_117291_1_2_1; -. DR InParanoid; O00488; -. DR OMA; MKDHFRS; -. DR OrthoDB; 230013at2759; -. DR PhylomeDB; O00488; -. DR TreeFam; TF315114; -. DR PathwayCommons; O00488; -. DR SignaLink; O00488; -. DR BioGRID-ORCS; 51042; 187 hits in 1177 CRISPR screens. DR ChiTaRS; ZNF593; human. DR EvolutionaryTrace; O00488; -. DR GeneWiki; ZNF593; -. DR GenomeRNAi; 51042; -. DR Pharos; O00488; Tbio. DR PRO; PR:O00488; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O00488; Protein. DR Bgee; ENSG00000142684; Expressed in gastrocnemius and 175 other cell types or tissues. DR ExpressionAtlas; O00488; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:1990275; F:preribosome binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA. DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IGI:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR DisProt; DP00549; -. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. 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; PTHR46095; ZINC FINGER PROTEIN 593; 1. DR PANTHER; PTHR46095:SF1; ZINC FINGER PROTEIN 593; 1. DR Pfam; PF12171; zf-C2H2_jaz; 1. DR SMART; SM00451; ZnF_U1; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR SWISS-2DPAGE; O00488; -. DR Genevisible; O00488; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-binding; Metal-binding; Nucleus; KW Reference proteome; Ribosome biogenesis; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..134 FT /note="Zinc finger protein 593" FT /id="PRO_0000047684" FT ZN_FING 61..85 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 82..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 6 FT /note="R -> Q (in dbSNP:rs2232649)" FT /id="VAR_059924" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1ZR9" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:1ZR9" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:1ZR9" FT HELIX 73..79 FT /evidence="ECO:0007829|PDB:1ZR9" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:1ZR9" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:1ZR9" SQ SEQUENCE 134 AA; 15199 MW; 883BCE4F72459818 CRC64; MGRSRRTGAH RAHSLARQMK AKRRRPDLDE IHRELRPQGS ARPQPDPNAE FDPDLPGGGL HRCLACARYF IDSTNLKTHF RSKDHKKRLK QLSVEPYSQE EAERAAGMGS YVPPRRLAVP TEVSTEVPEM DTST //