ID ZBT18_HUMAN Reviewed; 522 AA.
AC Q99592; A8K5U3; Q13397; Q5VU40; Q8N463; Q9UD99;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 211.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE AltName: Full=58 kDa repressor protein;
DE AltName: Full=Transcriptional repressor RP58;
DE AltName: Full=Translin-associated zinc finger protein 1;
DE Short=TAZ-1;
DE AltName: Full=Zinc finger protein 238;
DE AltName: Full=Zinc finger protein C2H2-171;
GN Name=ZBTB18; Synonyms=RP58, TAZ1, ZNF238;
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), AND VARIANT GLY-132.
RC TISSUE=Hippocampus;
RX PubMed=7633419; DOI=10.1093/hmg/4.4.685;
RA Becker K.G., Nagle J.W., Canning R.D., Biddison W.E., Ozato K., Drew P.D.;
RT "Rapid isolation and characterization of 118 novel C2H2-type zinc finger
RT cDNAs expressed in human brain.";
RL Hum. Mol. Genet. 4:685-691(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DNA-BINDING.
RC TISSUE=Spleen;
RX PubMed=9756912; DOI=10.1074/jbc.273.41.26698;
RA Aoki K., Meng G., Suzuki K., Takashi T., Kameoka Y., Nakahara K.,
RA Ishida R., Kasai M.;
RT "RP58 associates with condensed chromatin and mediates a sequence-specific
RT transcriptional repression.";
RL J. Biol. Chem. 273:26698-26704(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=10721697; DOI=10.1016/s0378-1119(99)00477-1;
RA Meng G., Inazawa J., Ishida R., Tokura K., Nakahara K., Aoki K., Kasai M.;
RT "Structural analysis of the gene encoding RP58, a sequence-specific
RT transrepressor associated with heterochromatin.";
RL Gene 242:59-64(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 1-75 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8358434; DOI=10.1038/ng0793-256;
RA Adams M.D., Kerlavage A.R., Fields C., Venter J.C.;
RT "3,400 new expressed sequence tags identify diversity of transcripts in
RT human brain.";
RL Nat. Genet. 4:256-267(1993).
RN [8]
RP INTERACTION WITH DNMT3A.
RX PubMed=11350943; DOI=10.1093/emboj/20.10.2536;
RA Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.;
RT "Dnmt3a binds deacetylases and is recruited by a sequence-specific
RT repressor to silence transcription.";
RL EMBO J. 20:2536-2544(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516 AND SER-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP INVOLVEMENT IN MRD22.
RX PubMed=24193349; DOI=10.1038/ejhg.2013.249;
RA de Munnik S.A., Garcia-Minaur S., Hoischen A., van Bon B.W., Boycott K.M.,
RA Schoots J., Hoefsloot L.H., Knoers N.V., Bongers E.M., Brunner H.G.;
RT "A de novo non-sense mutation in ZBTB18 in a patient with features of the
RT 1q43q44 microdeletion syndrome.";
RL Eur. J. Hum. Genet. 22:844-846(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-273, 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).
RN [12]
RP VARIANT 186-ARG--LYS-522 DEL.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: Transcriptional repressor that plays a role in various
CC developmental processes such as myogenesis and brain development. Plays
CC a key role in myogenesis by directly repressing the expression of ID2
CC and ID3, 2 inhibitors of skeletal myogenesis. Also involved in
CC controlling cell division of progenitor cells and regulating the
CC survival of postmitotic cortical neurons. Specifically binds the
CC consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E
CC box core, and acts by recruiting chromatin remodeling multiprotein
CC complexes. May also play a role in the organization of chromosomes in
CC the nucleus. {ECO:0000269|PubMed:9756912}.
CC -!- SUBUNIT: Interacts with DNMT3A. {ECO:0000269|PubMed:11350943}.
CC -!- INTERACTION:
CC Q99592; Q13363: CTBP1; NbExp=5; IntAct=EBI-3232046, EBI-908846;
CC Q99592; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-3232046, EBI-10171858;
CC Q99592; P56545: CTBP2; NbExp=7; IntAct=EBI-3232046, EBI-741533;
CC Q99592; P56545-3: CTBP2; NbExp=6; IntAct=EBI-3232046, EBI-10171902;
CC Q99592; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-3232046, EBI-6952711;
CC Q99592; Q92569: PIK3R3; NbExp=3; IntAct=EBI-3232046, EBI-79893;
CC Q99592; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-3232046, EBI-2515601;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with condensed
CC chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99592-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99592-2; Sequence=VSP_035381;
CC -!- TISSUE SPECIFICITY: Lymphoid tissues, testis, heart, brain, skeletal
CC muscle, and pancreas and, at much lower level, other tissues.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 22
CC (MRD22) [MIM:612337]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Additional MRD22 patients have limited or no speech, and variable but
CC characteristic facial features, including round face, prominent
CC forehead, flat nasal bridge, hypertelorism, epicanthal folds, and low-
CC set ears. Other features may include hypotonia, poor growth,
CC microcephaly, agenesis of the corpus callosum, and seizures.
CC {ECO:0000269|PubMed:24193349}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZBTB18 subfamily. {ECO:0000305}.
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DR EMBL; U38896; AAA81368.1; -; mRNA.
DR EMBL; X95072; CAA64468.1; -; mRNA.
DR EMBL; AJ001388; CAA04718.1; -; mRNA.
DR EMBL; AJ223321; CAA11262.1; -; Genomic_DNA.
DR EMBL; AK291408; BAF84097.1; -; mRNA.
DR EMBL; AL590483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036677; AAH36677.2; -; mRNA.
DR CCDS; CCDS1622.1; -. [Q99592-2]
DR PIR; I39200; I39200.
DR RefSeq; NP_001265125.1; NM_001278196.1. [Q99592-1]
DR RefSeq; NP_006343.2; NM_006352.4. [Q99592-1]
DR RefSeq; NP_991331.1; NM_205768.2. [Q99592-2]
DR RefSeq; XP_005273063.1; XM_005273006.2. [Q99592-1]
DR RefSeq; XP_016855549.1; XM_017000060.1. [Q99592-1]
DR AlphaFoldDB; Q99592; -.
DR SMR; Q99592; -.
DR BioGRID; 115735; 52.
DR IntAct; Q99592; 317.
DR STRING; 9606.ENSP00000351539; -.
DR iPTMnet; Q99592; -.
DR PhosphoSitePlus; Q99592; -.
DR BioMuta; ZBTB18; -.
DR DMDM; 20141020; -.
DR EPD; Q99592; -.
DR jPOST; Q99592; -.
DR MassIVE; Q99592; -.
DR PaxDb; 9606-ENSP00000351539; -.
DR PeptideAtlas; Q99592; -.
DR ProteomicsDB; 78345; -. [Q99592-1]
DR ProteomicsDB; 78346; -. [Q99592-2]
DR Antibodypedia; 34710; 144 antibodies from 25 providers.
DR DNASU; 10472; -.
DR Ensembl; ENST00000358704.4; ENSP00000351539.4; ENSG00000179456.12. [Q99592-2]
DR Ensembl; ENST00000622512.1; ENSP00000481278.1; ENSG00000179456.12. [Q99592-1]
DR Ensembl; ENST00000696616.1; ENSP00000512756.1; ENSG00000179456.12. [Q99592-1]
DR Ensembl; ENST00000696618.1; ENSP00000512758.1; ENSG00000179456.12. [Q99592-1]
DR GeneID; 10472; -.
DR KEGG; hsa:10472; -.
DR MANE-Select; ENST00000358704.4; ENSP00000351539.4; NM_205768.3; NP_991331.1. [Q99592-2]
DR UCSC; uc001iad.6; human. [Q99592-1]
DR AGR; HGNC:13030; -.
DR CTD; 10472; -.
DR DisGeNET; 10472; -.
DR GeneCards; ZBTB18; -.
DR HGNC; HGNC:13030; ZBTB18.
DR HPA; ENSG00000179456; Tissue enhanced (brain).
DR MalaCards; ZBTB18; -.
DR MIM; 608433; gene.
DR MIM; 612337; phenotype.
DR neXtProt; NX_Q99592; -.
DR OpenTargets; ENSG00000179456; -.
DR Orphanet; 36367; Distal deletion 1q.
DR PharmGKB; PA37608; -.
DR VEuPathDB; HostDB:ENSG00000179456; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155092; -.
DR HOGENOM; CLU_034521_0_0_1; -.
DR InParanoid; Q99592; -.
DR OMA; GASDYDM; -.
DR OrthoDB; 783166at2759; -.
DR PhylomeDB; Q99592; -.
DR TreeFam; TF337437; -.
DR PathwayCommons; Q99592; -.
DR SignaLink; Q99592; -.
DR BioGRID-ORCS; 10472; 25 hits in 1215 CRISPR screens.
DR ChiTaRS; ZBTB18; human.
DR GeneWiki; ZNF238; -.
DR GenomeRNAi; 10472; -.
DR Pharos; Q99592; Tbio.
DR PRO; PR:Q99592; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99592; Protein.
DR Bgee; ENSG00000179456; Expressed in cerebellar vermis and 213 other cell types or tissues.
DR Genevisible; Q99592; HS.
DR GO; GO:0000792; C:heterochromatin; IDA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR CDD; cd18324; BTB_POZ_ZBTB18_RP58; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF18; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 18; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF13894; zf-C2H2_4; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..522
FT /note="Zinc finger and BTB domain-containing protein 18"
FT /id="PRO_0000047477"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 370..392
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..489
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 121..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..427
FT /note="Interaction with DNMT3A"
FT /evidence="ECO:0000269|PubMed:11350943"
FT COMPBIAS 121..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKY3"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MCPKGYEDSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035381"
FT VARIANT 132
FT /note="E -> G (in dbSNP:rs1048824)"
FT /evidence="ECO:0000269|PubMed:7633419"
FT /id="VAR_012768"
FT VARIANT 186..522
FT /note="Missing (found in a patient with Rett syndrome-like
FT phenotype; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079032"
FT CONFLICT 51
FT /note="L -> I (in Ref. 6; AAH36677)"
FT /evidence="ECO:0000305"
FT CONFLICT 166..262
FT /note="KLNILPSKRDLAAEPGNMWMRLPSDSAGIPQAGGEAEPHATAAGKTVASPCS
FT STESLSQRSVTSVRDSADVDCVLDLSVKSSLSGVENLNSSYFSSQ -> IEHPAQQKGL
FT GGRAWEHVDAIALRLSRHPPGWRRGRATRHSSWKNSSQPLQLNRVFVPE (in Ref.
FT 1; AAA81368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58354 MW; DE024B66E02DCE75 CRC64;
MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
ATTEADSTKK EEDASSCSDK VESLSDGSSH IAGDLPSDED EGEDEKLNIL PSKRDLAAEP
GNMWMRLPSD SAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL
DLSVKSSLSG VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG MESSLLPYVS
NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR SKPAADVNVP TCSLCGKTFS
CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD
LYRHIRKFHC ELVNSLSVKS EALSLPTVRD WTLEDSSQEL WK
//
