TZAP_HUMAN
ID TZAP_HUMAN Reviewed; 688 AA.
AC P10074; Q5SY19;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Telomere zinc finger-associated protein {ECO:0000303|PubMed:28082411};
DE Short=TZAP {ECO:0000303|PubMed:28082411};
DE AltName: Full=Krueppel-related zinc finger protein 3 {ECO:0000303|PubMed:9516840};
DE Short=hKR3 {ECO:0000303|Ref.12};
DE AltName: Full=Zinc finger and BTB domain-containing protein 48 {ECO:0000312|HGNC:HGNC:4930};
DE AltName: Full=Zinc finger protein 855 {ECO:0000312|HGNC:HGNC:4930};
GN Name=ZBTB48 {ECO:0000312|HGNC:HGNC:4930};
GN Synonyms=HKR3 {ECO:0000303|PubMed:9516840},
GN TZAP {ECO:0000303|PubMed:28082411}, ZNF855 {ECO:0000312|HGNC:HGNC:4930};
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], DNA-BINDING, AND FUNCTION.
RX PubMed=7969177; DOI=10.1128/mcb.14.12.8438-8450.1994;
RA Sugawara M., Scholl T., Ponath P.D., Strominger J.L.;
RT "A factor that regulates the class II major histocompatibility complex gene
RT DPA is a member of a subfamily of zinc finger proteins that includes a
RT Drosophila developmental control protein.";
RL Mol. Cell. Biol. 14:8438-8450(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9516840; DOI=10.1016/s0959-8049(97)00279-7;
RA Maris J.M., Jensen J., Sulman E.P., Beltinger C.P., Allen C., Biegel J.A.,
RA Brodeur G.M., White P.S.;
RT "Human Kruppel-related 3 (HKR3): a candidate for the 1p36 neuroblastoma
RT tumour suppressor gene?";
RL Eur. J. Cancer 33:1991-1996(1997).
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].
RC TISSUE=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 [GENOMIC DNA] OF 461-488.
RX PubMed=2850480; DOI=10.1128/mcb.8.8.3104-3113.1988;
RA Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T., Law M.L.,
RA Seuanez H.N., O'Brien S.J., Vogelstein B.;
RT "The GLI-Kruppel family of human genes.";
RL Mol. Cell. Biol. 8:3104-3113(1988).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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 [7]
RP FUNCTION, AND INTERACTION WITH EP300.
RX PubMed=24382891; DOI=10.1074/jbc.m113.526855;
RA Yoon J.H., Choi W.I., Jeon B.N., Koh D.I., Kim M.K., Kim M.H., Kim J.,
RA Hur S.S., Kim K.S., Hur M.W.;
RT "Human Kruppel-related 3 (HKR3) is a novel transcription activator of
RT alternate reading frame (ARF) gene.";
RL J. Biol. Chem. 289:4018-4031(2014).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-171 AND SER-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF HIS-596.
RX PubMed=28500257; DOI=10.15252/embr.201744095;
RA Jahn A., Rane G., Paszkowski-Rogacz M., Sayols S., Bluhm A., Han C.T.,
RA Draskovic I., Londono-Vallejo J.A., Kumar A.P., Buchholz F., Butter F.,
RA Kappei D.;
RT "ZBTB48 is both a vertebrate telomere-binding protein and a transcriptional
RT activator.";
RL EMBO Rep. 18:929-946(2017).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143 AND LYS-263, 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).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=28082411; DOI=10.1126/science.aah6752;
RA Li J.S., Miralles Fuste J., Simavorian T., Bartocci C., Tsai J.,
RA Karlseder J., Lazzerini Denchi E.;
RT "TZAP: A telomere-associated protein involved in telomere length control.";
RL Science 355:638-641(2017).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 2-120.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human BTB domain of the krueppel-related zinc
RT finger protein 3 (hKR3).";
RL Submitted (NOV-2007) to the PDB data bank.
CC -!- FUNCTION: Telomere-binding protein that acts as a regulator of telomere
CC length (PubMed:28500257, PubMed:28082411). Directly binds the telomeric
CC double-stranded 5'-TTAGGG-3' repeat (PubMed:28500257, PubMed:28082411).
CC Preferentially binds to telomeres that have a low concentration of
CC shelterin complex and acts as a regulator of telomere length by
CC initiating telomere trimming, a process that prevents the accumulation
CC of aberrantly long telomeres (PubMed:28082411). Also acts as a
CC transcription regulator that binds to promoter regions (PubMed:7969177,
CC PubMed:24382891, PubMed:28500257). Regulates expression of a small
CC subset of genes, including MTFP1 (PubMed:28500257). Regulates
CC expression the J and/or S elements in MHC II promoter (PubMed:7969177).
CC Acts as a negative regulator of cell proliferation by specifically
CC activating expression of ARF, a tumor suppressor isoform of CDKN2A
CC (PubMed:24382891). {ECO:0000269|PubMed:24382891,
CC ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257,
CC ECO:0000269|PubMed:7969177}.
CC -!- SUBUNIT: Interacts with EP300 (PubMed:24382891).
CC {ECO:0000269|PubMed:24382891}.
CC -!- INTERACTION:
CC P10074; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-744864, EBI-739624;
CC P10074; Q92997: DVL3; NbExp=4; IntAct=EBI-744864, EBI-739789;
CC P10074; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-744864, EBI-5666657;
CC P10074; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-744864, EBI-11959885;
CC P10074; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-744864, EBI-10172150;
CC P10074; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-744864, EBI-10172290;
CC P10074; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-744864, EBI-739909;
CC P10074; P02545: LMNA; NbExp=3; IntAct=EBI-744864, EBI-351935;
CC P10074; P23508: MCC; NbExp=3; IntAct=EBI-744864, EBI-307531;
CC P10074; Q9Y5B8: NME7; NbExp=6; IntAct=EBI-744864, EBI-744782;
CC P10074; Q96CV9: OPTN; NbExp=3; IntAct=EBI-744864, EBI-748974;
CC P10074; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-744864, EBI-12023934;
CC P10074; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-744864, EBI-741515;
CC P10074; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-744864, EBI-725997;
CC P10074; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-744864, EBI-947459;
CC P10074; P61964: WDR5; NbExp=3; IntAct=EBI-744864, EBI-540834;
CC P10074; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-744864, EBI-3918996;
CC P10074; P10074: ZBTB48; NbExp=4; IntAct=EBI-744864, EBI-744864;
CC P10074; Q15916: ZBTB6; NbExp=3; IntAct=EBI-744864, EBI-7227791;
CC P10074; Q96BR9: ZBTB8A; NbExp=7; IntAct=EBI-744864, EBI-742740;
CC P10074; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-744864, EBI-395708;
CC P10074; Q96PQ6: ZNF317; NbExp=3; IntAct=EBI-744864, EBI-1210473;
CC P10074; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-744864, EBI-347633;
CC P10074; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-744864, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
CC Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat
CC (PubMed:28500257, PubMed:28082411). According to a report,
CC preferentially binds to long telomeres that have a low concentration of
CC shelterin complex, competing with the telomeric repeat binding factors
CC TERF1 and TERF2 (PubMed:28082411). According to another report, binds
CC telomeres regardless of their length (PubMed:28500257).
CC {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
CC -!- TISSUE SPECIFICITY: Detected in adrenal gland and neuroblastoma.
CC {ECO:0000269|PubMed:9516840}.
CC -!- DOMAIN: The C2H2-type zinc fingers mediate binding to the telomeric
CC double-stranded 5'-TTAGGG-3' repeats (PubMed:28082411). The last C2H2-
CC type zinc finger is required for telomeric-binding (PubMed:28500257).
CC {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- CAUTION: According to a study, preferentially binds to long telomeres
CC that have a low concentration of shelterin complex (PubMed:28082411).
CC According to another report, binds telomeres regardless of their length
CC (PubMed:28500257). {ECO:0000269|PubMed:28082411,
CC ECO:0000269|PubMed:28500257}.
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DR EMBL; L16896; AAA65124.1; -; mRNA.
DR EMBL; U45325; AAB08973.1; -; Genomic_DNA.
DR EMBL; U45324; AAB08973.1; JOINED; Genomic_DNA.
DR EMBL; AL591866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013573; AAH13573.1; -; mRNA.
DR EMBL; M20677; AAA35989.1; -; Genomic_DNA.
DR CCDS; CCDS84.1; -.
DR PIR; A56360; A56360.
DR RefSeq; NP_001265576.1; NM_001278647.1.
DR RefSeq; NP_001265577.1; NM_001278648.1.
DR RefSeq; NP_005332.1; NM_005341.3.
DR PDB; 3B84; X-ray; 1.74 A; A=4-120.
DR PDB; 5YJ3; X-ray; 2.85 A; C/D=516-620.
DR PDBsum; 3B84; -.
DR PDBsum; 5YJ3; -.
DR AlphaFoldDB; P10074; -.
DR SMR; P10074; -.
DR BioGRID; 109349; 143.
DR IntAct; P10074; 103.
DR MINT; P10074; -.
DR STRING; 9606.ENSP00000366902; -.
DR iPTMnet; P10074; -.
DR PhosphoSitePlus; P10074; -.
DR BioMuta; ZBTB48; -.
DR DMDM; 1708212; -.
DR EPD; P10074; -.
DR jPOST; P10074; -.
DR MassIVE; P10074; -.
DR MaxQB; P10074; -.
DR PaxDb; P10074; -.
DR PeptideAtlas; P10074; -.
DR PRIDE; P10074; -.
DR ProteomicsDB; 52561; -.
DR Antibodypedia; 13109; 148 antibodies from 27 providers.
DR DNASU; 3104; -.
DR Ensembl; ENST00000377674.9; ENSP00000366902.4; ENSG00000204859.13.
DR GeneID; 3104; -.
DR KEGG; hsa:3104; -.
DR MANE-Select; ENST00000377674.9; ENSP00000366902.4; NM_005341.4; NP_005332.1.
DR UCSC; uc001anx.5; human.
DR CTD; 3104; -.
DR DisGeNET; 3104; -.
DR GeneCards; ZBTB48; -.
DR HGNC; HGNC:4930; ZBTB48.
DR HPA; ENSG00000204859; Low tissue specificity.
DR MIM; 165270; gene.
DR neXtProt; NX_P10074; -.
DR OpenTargets; ENSG00000204859; -.
DR PharmGKB; PA162409481; -.
DR VEuPathDB; HostDB:ENSG00000204859; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158981; -.
DR HOGENOM; CLU_002678_70_0_1; -.
DR InParanoid; P10074; -.
DR OMA; HEWEVVV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P10074; -.
DR TreeFam; TF331310; -.
DR PathwayCommons; P10074; -.
DR SignaLink; P10074; -.
DR BioGRID-ORCS; 3104; 14 hits in 1139 CRISPR screens.
DR ChiTaRS; ZBTB48; human.
DR EvolutionaryTrace; P10074; -.
DR GenomeRNAi; 3104; -.
DR Pharos; P10074; Tbio.
DR PRO; PR:P10074; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P10074; protein.
DR Bgee; ENSG00000204859; Expressed in right lobe of liver and 127 other tissues.
DR ExpressionAtlas; P10074; baseline and differential.
DR Genevisible; P10074; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB.
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 Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromosome; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Telomere; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..688
FT /note="Telomere zinc finger-associated protein"
FT /id="PRO_0000047272"
FT DOMAIN 26..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 291..313
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..401
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..430
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..459
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..544
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 675
FT /note="S -> A (in dbSNP:rs2229330)"
FT /id="VAR_052925"
FT MUTAGEN 596
FT /note="H->A: Abolishes binding to the telomeric double-
FT stranded 5'-TTAGGG-3' repeat."
FT /evidence="ECO:0000269|PubMed:28500257"
FT CONFLICT 201
FT /note="P -> S (in Ref. 1; AAA65124)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> S (in Ref. 1; AAA65124)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..351
FT /note="FT -> LP (in Ref. 1; AAA65124)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="N -> K (in Ref. 1; AAA65124)"
FT /evidence="ECO:0000305"
FT HELIX 5..22
FT /evidence="ECO:0007829|PDB:3B84"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3B84"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3B84"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3B84"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:3B84"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:3B84"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:3B84"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:5YJ3"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:5YJ3"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:5YJ3"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:5YJ3"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:5YJ3"
FT HELIX 590..600
FT /evidence="ECO:0007829|PDB:5YJ3"
SQ SEQUENCE 688 AA; 77054 MW; EBECCE3D6CBBD524 CRC64;
MDGSFVQHSV RVLQELNKQR EKGQYCDATL DVGGLVFKAH WSVLACCSHF FQSLYGDGSG
GSVVLPAGFA EIFGLLLDFF YTGHLALTSG NRDQVLLAAR ELRVPEAVEL CQSFKPKTSV
GQAAGGQSGL GPPASQNVNS HVKEPAGLEE EEVSRTLGLV PRDQEPRGSH SPQRPQLHSP
AQSEGPSSLC GKLKQALKPC PLEDKKPEDC KVPPRPLEAE GAQLQGGSNE WEVVVQVEDD
GDGDYMSEPE AVLTRRKSNV IRKPCAAEPA LSAGSLAAEP AENRKGTAVP VECPTCHKKF
LSKYYLKVHN RKHTGEKPFE CPKCGKCYFR KENLLEHEAR NCMNRSEQVF TCSVCQETFR
RRMELRVHMV SHTGEMPYKC SSCSQQFMQK KDLQSHMIKL HGAPKPHACP TCAKCFLSRT
ELQLHEAFKH RGEKLFVCEE CGHRASSRNG LQMHIKAKHR NERPHVCEFC SHAFTQKANL
NMHLRTHTGE KPFQCHLCGK TFRTQASLDK HNRTHTGERP FSCEFCEQRF TEKGPLLRHV
ASRHQEGRPH FCQICGKTFK AVEQLRVHVR RHKGVRKFEC TECGYKFTRQ AHLRRHMEIH
DRVENYNPRQ RKLRNLIIED EKMVVVALQP PAELEVGSAE VIVESLAQGG LASQLPGQRL
CAEESFTGPG VLEPSLIITA AVPEDCDT
