ZBTB4_HUMAN
ID ZBTB4_HUMAN Reviewed; 1013 AA.
AC Q9P1Z0; B3KVL6; Q7Z697; Q86XJ4; Q8N4V8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Zinc finger and BTB domain-containing protein 4;
DE AltName: Full=KAISO-like zinc finger protein 1;
DE Short=KAISO-L1;
GN Name=ZBTB4; Synonyms=KIAA1538;
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=Fetal brain;
RA Weber A., Klinkhammer B., Glaum A., Bergmann E., Berwanger B., Eilers M.,
RA Christiansen H.;
RT "Identification of a novel zinc-finger-protein encoding gene on 17p13.1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, 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 [7]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INTERACTION WITH ZBTB38.
RX PubMed=16354688; DOI=10.1128/mcb.26.1.169-181.2006;
RA Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E.,
RA Defossez P.A.;
RT "A family of human zinc finger proteins that bind methylated DNA and
RT repress transcription.";
RL Mol. Cell. Biol. 26:169-181(2006).
RN [8]
RP PHOSPHORYLATION AT THR-795; THR-797 AND THR-983 BY HIPK2, MUTAGENESIS OF
RP THR-795; THR-797 AND THR-983, AND INTERACTION WITH HIPK2.
RX PubMed=19448668; DOI=10.1038/onc.2009.109;
RA Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B., Devignot V.,
RA Sasai N., Ravassard P., Mallet J., Sastre-Garau X., Schmitz M.L.,
RA Defossez P.A.;
RT "The human protein kinase HIPK2 phosphorylates and downregulates the
RT methyl-binding transcription factor ZBTB4.";
RL Oncogene 28:2535-2544(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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 [10]
RP INTERACTION WITH CBFA2T3.
RX PubMed=23251453; DOI=10.1371/journal.pone.0051205;
RA Barrett C.W., Smith J.J., Lu L.C., Markham N., Stengel K.R., Short S.P.,
RA Zhang B., Hunt A.A., Fingleton B.M., Carnahan R.H., Engel M.E., Chen X.,
RA Beauchamp R.D., Wilson K.T., Hiebert S.W., Reynolds A.B., Williams C.S.;
RT "Kaiso directs the transcriptional corepressor MTG16 to the Kaiso binding
RT site in target promoters.";
RL PLoS ONE 7:E51205-E51205(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-573 AND LYS-615, 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 repressor with bimodal DNA-binding
CC specificity. Represses transcription in a methyl-CpG-dependent manner.
CC Binds with a higher affinity to methylated CpG dinucleotides in the
CC consensus sequence 5'-CGCG-3' but can also bind to the non-methylated
CC consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso
CC binding site (KBS). Can also bind specifically to a single methyl-CpG
CC pair and can bind hemimethylated DNA but with a lower affinity compared
CC to methylated DNA (PubMed:16354688). Plays a role in postnatal
CC myogenesis, may be involved in the regulation of satellite cells self-
CC renewal (By similarity). {ECO:0000250|UniProtKB:Q5F293,
CC ECO:0000269|PubMed:16354688}.
CC -!- SUBUNIT: Interacts with HIPK2. Interacts with CBFA2T3. Interacts with
CC ZBTB38. {ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:19448668,
CC ECO:0000269|PubMed:23251453}.
CC -!- INTERACTION:
CC Q9P1Z0; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2564133, EBI-11524452;
CC Q9P1Z0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2564133, EBI-739580;
CC Q9P1Z0; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2564133, EBI-10961624;
CC Q9P1Z0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2564133, EBI-739624;
CC Q9P1Z0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2564133, EBI-742887;
CC Q9P1Z0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2564133, EBI-3867333;
CC Q9P1Z0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2564133, EBI-618309;
CC Q9P1Z0; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2564133, EBI-748420;
CC Q9P1Z0; Q53G59: KLHL12; NbExp=3; IntAct=EBI-2564133, EBI-740929;
CC Q9P1Z0; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-2564133, EBI-9640281;
CC Q9P1Z0; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2564133, EBI-14066006;
CC Q9P1Z0; P78424: POU6F2; NbExp=3; IntAct=EBI-2564133, EBI-12029004;
CC Q9P1Z0; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2564133, EBI-11952721;
CC Q9P1Z0; P36406: TRIM23; NbExp=3; IntAct=EBI-2564133, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16354688}. Chromosome
CC {ECO:0000269|PubMed:16354688}. Note=Localizes to chromocenters.
CC {ECO:0000269|PubMed:16354688}.
CC -!- PTM: Phosphorylated by HIPK2. This phosphorylation reduces stability
CC and triggers ZBTB4 protein degradation in response to DNA damage.
CC {ECO:0000269|PubMed:19448668}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96062.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY302699; AAP59447.1; -; mRNA.
DR EMBL; AB040971; BAA96062.2; ALT_INIT; mRNA.
DR EMBL; AK122971; BAG53828.1; -; mRNA.
DR EMBL; CH471108; EAW90185.1; -; Genomic_DNA.
DR EMBL; BC033259; AAH33259.1; -; mRNA.
DR EMBL; BC043352; AAH43352.1; -; mRNA.
DR CCDS; CCDS11107.1; -.
DR RefSeq; NP_001122305.1; NM_001128833.1.
DR RefSeq; NP_065950.2; NM_020899.3.
DR RefSeq; XP_006721626.1; XM_006721563.3.
DR RefSeq; XP_006721627.1; XM_006721564.2.
DR RefSeq; XP_011522274.1; XM_011523972.2.
DR AlphaFoldDB; Q9P1Z0; -.
DR BioGRID; 121693; 24.
DR IntAct; Q9P1Z0; 17.
DR MINT; Q9P1Z0; -.
DR STRING; 9606.ENSP00000307858; -.
DR CarbonylDB; Q9P1Z0; -.
DR iPTMnet; Q9P1Z0; -.
DR PhosphoSitePlus; Q9P1Z0; -.
DR BioMuta; ZBTB4; -.
DR DMDM; 46577564; -.
DR EPD; Q9P1Z0; -.
DR jPOST; Q9P1Z0; -.
DR MassIVE; Q9P1Z0; -.
DR MaxQB; Q9P1Z0; -.
DR PaxDb; Q9P1Z0; -.
DR PeptideAtlas; Q9P1Z0; -.
DR PRIDE; Q9P1Z0; -.
DR ProteomicsDB; 83682; -.
DR Antibodypedia; 24133; 168 antibodies from 23 providers.
DR DNASU; 57659; -.
DR Ensembl; ENST00000311403.4; ENSP00000307858.4; ENSG00000174282.12.
DR Ensembl; ENST00000380599.9; ENSP00000369973.4; ENSG00000174282.12.
DR Ensembl; ENST00000639670.2; ENSP00000492232.1; ENSG00000283868.2.
DR Ensembl; ENST00000639962.1; ENSP00000492616.1; ENSG00000283868.2.
DR GeneID; 57659; -.
DR KEGG; hsa:57659; -.
DR MANE-Select; ENST00000380599.9; ENSP00000369973.4; NM_001128833.2; NP_001122305.1.
DR UCSC; uc002ghc.5; human.
DR CTD; 57659; -.
DR DisGeNET; 57659; -.
DR GeneCards; ZBTB4; -.
DR HGNC; HGNC:23847; ZBTB4.
DR HPA; ENSG00000174282; Low tissue specificity.
DR MIM; 612308; gene.
DR neXtProt; NX_Q9P1Z0; -.
DR OpenTargets; ENSG00000174282; -.
DR PharmGKB; PA134959224; -.
DR VEuPathDB; HostDB:ENSG00000174282; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161268; -.
DR HOGENOM; CLU_007011_1_0_1; -.
DR InParanoid; Q9P1Z0; -.
DR OMA; THEVLCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9P1Z0; -.
DR TreeFam; TF333100; -.
DR PathwayCommons; Q9P1Z0; -.
DR SignaLink; Q9P1Z0; -.
DR SIGNOR; Q9P1Z0; -.
DR BioGRID-ORCS; 57659; 38 hits in 1138 CRISPR screens.
DR ChiTaRS; ZBTB4; human.
DR GenomeRNAi; 57659; -.
DR Pharos; Q9P1Z0; Tbio.
DR PRO; PR:Q9P1Z0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P1Z0; protein.
DR Bgee; ENSG00000174282; Expressed in primary visual cortex and 104 other tissues.
DR Genevisible; Q9P1Z0; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA: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:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0010428; F:methyl-CpNpG binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
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 Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1013
FT /note="Zinc finger and BTB domain-containing protein 4"
FT /id="PRO_0000047712"
FT DOMAIN 30..152
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 234..256
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..331
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..388
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 726..748
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..787
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 67..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..348
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000269|PubMed:23251453"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 627..663
FT /evidence="ECO:0000255"
FT COMPBIAS 75..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..657
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:19448668"
FT MOD_RES 797
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:19448668"
FT MOD_RES 983
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:19448668"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 615
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 539
FT /note="A -> V (in dbSNP:rs35231078)"
FT /id="VAR_052913"
FT VARIANT 550
FT /note="M -> I (in dbSNP:rs871990)"
FT /id="VAR_018383"
FT VARIANT 561
FT /note="N -> S (in dbSNP:rs34914463)"
FT /id="VAR_052914"
FT MUTAGEN 795
FT /note="T->A: Impaired HIPK2-mediated phosphorylation; when
FT associated with A-797 and A-983."
FT /evidence="ECO:0000269|PubMed:19448668"
FT MUTAGEN 797
FT /note="T->A: Impaired HIPK2-mediated phosphorylation; when
FT associated with A-795 and A-983."
FT /evidence="ECO:0000269|PubMed:19448668"
FT MUTAGEN 983
FT /note="T->A: Impaired HIPK2-mediated phosphorylation; when
FT associated with A-795 and A-797."
FT /evidence="ECO:0000269|PubMed:19448668"
FT CONFLICT 188
FT /note="P -> S (in Ref. 6; AAH43352)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="R -> C (in Ref. 6; AAH43352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 105114 MW; CA4AB6A5230C2F52 CRC64;
MPPPAEVTDP SHAPAVLRQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAA SSPFFREALL
TSAPLPLPPA TGGAAPNPAT TTAASSSSSS SSSSSSSSSS ASSSSSSSSS SPPPASPPAS
SPPRVLELPG VPAAAFSDVL NFIYSARLAL PGGGGDGAAV AEIGALGRRL GISRLQGLGE
GGDAWVPPTP APMATSQPEE DSFGPGPRPA GEWEGDRAEA QAPDLQCSLP RRPLPCPQCG
KSFIHPKRLQ THEAQCRRGA STRGSTGLGA GGAGPGGPAG VDASALPPPV GFRGGPEHVV
KVVGGHVLYV CAACERSYVT LSSLKRHSNV HSWRRKYPCR YCEKVFALAE YRTKHEVWHT
GERRYQCIFC WETFVTYYNL KTHQRAFHGI SPGLLASEKT PNGGYKPKLN TLKLYRLLPM
RAAKRPYKTY SQGAPEAPLS PTLNTPAPVA MPASPPPGPP PAPEPGPPPS VITFAHPAPS
VIVHGGSSSG GGGSGTASTG GSQAASVITY TAPPRPPKKR EYPPPPPEPA ATPTSPATAV
SPATAAGPAM ATTTEEAKGR NPRAGRTLTY TAKPVGGIGG GGGPPTGAGR GPSQLQAPPP
LCQITVRIGE EAIVKRRISE TDLRPGELSG EEMEESEEDE EEEDEEEEEE DEEESKAGGE
DQLWRPYYSY KPKRKAGAAG GASVGGSGLP RGRRPPRWRQ KLERRSWEET PAAESPAGRA
RTERRHRCGD CAQTFTTLRK LRKHQEAHGG GSHSSRAGRR PSTRFTCPHC AKVCKTAAAL
SRHGQRHAAE RPGGTPTPVI AYSKGSAGTR PGDVKEEAPQ EMQVSSSSGE AGGGSTAAEE
ASETASLQDP IISGGEEPPV VASGGSYVYP PVQEFPLALI GGGREPGGGR GKSGSEGPVG
AGEGDRMEGI GAAKVTFYPE PYPLVYGPQL LAAYPYNFSN LAALPVALNM VLPDEKGAGA
LPFLPGVFGY AVNPQAAPPA PPTPPPPTLP PPIPPKGEGE RAGVERTQKG DVG
