ZN521_HUMAN
ID ZN521_HUMAN Reviewed; 1311 AA.
AC Q96K83; A3QVP7; B0YJB7; Q8IXI0; Q8TES6; Q9C065; Q9HAL5; Q9UFK4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger protein 521;
DE AltName: Full=Early hematopoietic zinc finger protein;
DE AltName: Full=LYST-interacting protein 3;
GN Name=ZNF521; Synonyms=EHZF, LIP3;
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], FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, AND
RP INTERACTION WITH EBF1; SMAD1 AND SMAD4.
RX PubMed=14630787; DOI=10.1182/blood-2003-07-2388;
RA Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N.,
RA De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M.,
RA Morrone G., Venuta S.;
RT "Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse
RT Evi3, is highly expressed in primitive human hematopoietic cells.";
RL Blood 103:2062-2070(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-1311, AND CHROMOSOMAL TRANSLOCATION WITH
RP PAX5.
RX PubMed=17344859; DOI=10.1038/nature05690;
RA Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
RA Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H.,
RA Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
RT "Genome-wide analysis of genetic alterations in acute lymphoblastic
RT leukaemia.";
RL Nature 446:758-764(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 729-1311.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1311, AND INTERACTION WITH LYST.
RX PubMed=11984006; DOI=10.1007/bf03402003;
RA Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y.,
RA Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S.,
RA Kingsmore S.F.;
RT "The Chediak-Higashi protein interacts with SNARE complex and signal
RT transduction proteins.";
RL Mol. Med. 8:56-64(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-608, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1146, 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).
CC -!- FUNCTION: Transcription factor that can both act as an activator or a
CC repressor depending on the context. Involved in BMP signaling and in
CC the regulation of the immature compartment of the hematopoietic system.
CC Associates with SMADs in response to BMP2 leading to activate
CC transcription of BMP target genes. Acts as a transcriptional repressor
CC via its interaction with EBF1, a transcription factor involved
CC specification of B-cell lineage; this interaction preventing EBF1 to
CC bind DNA and activate target genes. {ECO:0000269|PubMed:14630787}.
CC -!- SUBUNIT: Interacts with EBF1. Interacts with SMAD1 and SMAD4.
CC {ECO:0000269|PubMed:11984006, ECO:0000269|PubMed:14630787}.
CC -!- INTERACTION:
CC Q96K83; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-6597673, EBI-750700;
CC Q96K83; P54136: RARS1; NbExp=3; IntAct=EBI-6597673, EBI-355482;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic cells.
CC Present in organs and tissues that contain stem and progenitor cells,
CC myeloid and/or lymphoid: placenta, spleen, lymph nodes, thymus, bone
CC marrow and fetal liver. Within the hematopoietic system, it is abundant
CC in CD34(+) cells but undetectable in mature peripheral blood
CC leukocytes, and its levels rapidly decrease during the differentiation
CC of CD34(+) cells in response to hemopoietins.
CC {ECO:0000269|PubMed:14630787}.
CC -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC regulate the distinct BMP-Smad and hematopoietic system. {ECO:0000250}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZNF521 is found in
CC acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2) with
CC PAX5. The translocation generates the PAX5-ZNF521 oncogene consisting
CC of the N-terminus part of PAX5 and the C-terminus part of ZNF521.
CC {ECO:0000269|PubMed:17344859}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI33104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB13829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ518106; CAD57322.1; -; mRNA.
DR EMBL; AK021452; BAB13829.1; ALT_INIT; mRNA.
DR EMBL; AK027354; BAB55056.1; -; mRNA.
DR EMBL; AK074046; BAB84872.1; -; mRNA.
DR EMBL; EF445043; ACA06095.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01201.1; -; Genomic_DNA.
DR EMBL; BC113622; AAI13623.1; -; mRNA.
DR EMBL; BC113648; AAI13649.1; -; mRNA.
DR EMBL; DQ845345; ABI33104.1; ALT_INIT; mRNA.
DR EMBL; AL117615; CAB56016.1; -; mRNA.
DR EMBL; AF141339; AAG49442.1; -; mRNA.
DR CCDS; CCDS32806.1; -.
DR PIR; T17326; T17326.
DR RefSeq; NP_001295154.1; NM_001308225.1.
DR RefSeq; NP_056276.1; NM_015461.2.
DR RefSeq; XP_011524213.1; XM_011525911.1.
DR RefSeq; XP_016881187.1; XM_017025698.1.
DR AlphaFoldDB; Q96K83; -.
DR BioGRID; 117425; 29.
DR IntAct; Q96K83; 19.
DR STRING; 9606.ENSP00000354794; -.
DR iPTMnet; Q96K83; -.
DR PhosphoSitePlus; Q96K83; -.
DR BioMuta; ZNF521; -.
DR DMDM; 74760909; -.
DR EPD; Q96K83; -.
DR jPOST; Q96K83; -.
DR MassIVE; Q96K83; -.
DR PaxDb; Q96K83; -.
DR PeptideAtlas; Q96K83; -.
DR PRIDE; Q96K83; -.
DR ProteomicsDB; 77052; -.
DR Antibodypedia; 7815; 204 antibodies from 23 providers.
DR DNASU; 25925; -.
DR Ensembl; ENST00000361524.8; ENSP00000354794.3; ENSG00000198795.11.
DR Ensembl; ENST00000538137.6; ENSP00000440768.2; ENSG00000198795.11.
DR GeneID; 25925; -.
DR KEGG; hsa:25925; -.
DR MANE-Select; ENST00000361524.8; ENSP00000354794.3; NM_015461.3; NP_056276.1.
DR UCSC; uc002kvk.3; human.
DR CTD; 25925; -.
DR DisGeNET; 25925; -.
DR GeneCards; ZNF521; -.
DR HGNC; HGNC:24605; ZNF521.
DR HPA; ENSG00000198795; Tissue enhanced (brain).
DR MIM; 610974; gene.
DR neXtProt; NX_Q96K83; -.
DR OpenTargets; ENSG00000198795; -.
DR PharmGKB; PA134956321; -.
DR VEuPathDB; HostDB:ENSG00000198795; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159287; -.
DR HOGENOM; CLU_004018_0_0_1; -.
DR InParanoid; Q96K83; -.
DR OMA; LACMYCT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96K83; -.
DR TreeFam; TF331504; -.
DR PathwayCommons; Q96K83; -.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR SignaLink; Q96K83; -.
DR SIGNOR; Q96K83; -.
DR BioGRID-ORCS; 25925; 17 hits in 1096 CRISPR screens.
DR ChiTaRS; ZNF521; human.
DR GenomeRNAi; 25925; -.
DR Pharos; Q96K83; Tbio.
DR PRO; PR:Q96K83; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96K83; protein.
DR Bgee; ENSG00000198795; Expressed in cerebellar vermis and 175 other tissues.
DR ExpressionAtlas; Q96K83; baseline and differential.
DR Genevisible; Q96K83; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048663; P:neuron fate commitment; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 30.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24.
PE 1: Evidence at protein level;
KW Activator; Chromosomal rearrangement; Developmental protein;
KW Differentiation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1311
FT /note="Zinc finger protein 521"
FT /id="PRO_0000306871"
FT ZN_FING 47..67
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 118..140
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 146..168
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..196
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..269
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..304
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..429
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..460
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..500
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..536
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 560..585
FT /note="C2H2-type 13; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..717
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 722..745
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 752..775
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 783..805
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 809..832
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 886..908
FT /note="C2H2-type 21; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 930..952
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 959..981
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1020..1042
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1065..1083
FT /note="C2H2-type 25; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1138..1161
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1195..1217
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1247
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1256..1279
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1286..1309
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 72..73
FT /note="Breakpoint for translocation to form PAX5-ZNF521"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 1146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 203
FT /note="K -> E (in Ref. 1; CAD57322)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="E -> K (in Ref. 6; ABI33104)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="K -> Q (in Ref. 2; BAB13829)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="F -> L (in Ref. 1; CAD57322)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="K -> E (in Ref. 1; CAD57322)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="N -> S (in Ref. 1; CAD57322 and 6; CAB56016)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="G -> A (in Ref. 1; CAD57322 and 6; CAB56016)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="L -> M (in Ref. 7; AAG49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="P -> T (in Ref. 7; AAG49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="F -> L (in Ref. 7; AAG49442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1311 AA; 147866 MW; C52DCC71C2B16C8F CRC64;
MSRRKQAKPR SLKDPNCKLE DKTEDGEALD CKKRPEDGEE LEDEAVHSCD SCLQVFESLS
DITEHKINQC QLTDGVDVED DPTCSWPASS PSSKDQTSPS HGEGCDFGEE EGGPGLPYPC
QFCDKSFSRL SYLKHHEQSH SDKLPFKCTY CSRLFKHKRS RDRHIKLHTG DKKYHCSECD
AAFSRSDHLK IHLKTHTSNK PYKCAICRRG FLSSSSLHGH MQVHERNKDG SQSGSRMEDW
KMKDTQKCSQ CEEGFDFPED LQKHIAECHP ECSPNEDRAA LQCVYCHELF VEETSLMNHM
EQVHSGEKKN SCSICSESFH TVEELYSHMD SHQQPESCNH SNSPSLVTVG YTSVSSTTPD
SNLSVDSSTM VEAAPPIPKS RGRKRAAQQT PDMTGPSSKQ AKVTYSCIYC NKQLFSSLAV
LQIHLKTMHL DKPEQAHICQ YCLEVLPSLY NLNEHLKQVH EAQDPGLIVS AMPAIVYQCN
FCSEVVNDLN TLQEHIRCSH GFANPAAKDS NAFFCPHCYM GFLTDSSLEE HIRQVHCDLS
GSRFGSPVLG TPKEPVVEVY SCSYCTNSPI FNSVLKLNKH IKENHKNIPL ALNYIHNGKK
SRALSPLSPV AIEQTSLKMM QAVGGAPARP TGEYICNQCG AKYTSLDSFQ THLKTHLDTV
LPKLTCPQCN KEFPNQESLL KHVTIHFMIT STYYICESCD KQFTSVDDLQ KHLLDMHTFV
FFRCTLCQEV FDSKVSIQLH LAVKHSNEKK VYRCTSCNWD FRNETDLQLH VKHNHLENQG
KVHKCIFCGE SFGTEVELQC HITTHSKKYN CKFCSKAFHA IILLEKHLRE KHCVFETKTP
NCGTNGASEQ VQKEEVELQT LLTNSQESHN SHDGSEEDVD TSEPMYGCDI CGAAYTMETL
LQNHQLRDHN IRPGESAIVK KKAELIKGNY KCNVCSRTFF SENGLREHMQ THLGPVKHYM
CPICGERFPS LLTLTEHKVT HSKSLDTGNC RICKMPLQSE EEFLEHCQMH PDLRNSLTGF
RCVVCMQTVT STLELKIHGT FHMQKTGNGS AVQTTGRGQH VQKLYKCASC LKEFRSKQDL
VKLDINGLPY GLCAGCVNLS KSASPGINVP PGTNRPGLGQ NENLSAIEGK GKVGGLKTRC
SSCNVKFESE SELQNHIQTI HRELVPDSNS TQLKTPQVSP MPRISPSQSD EKKTYQCIKC
QMVFYNEWDI QVHVANHMID EGLNHECKLC SQTFDSPAKL QCHLIEHSFE GMGGTFKCPV
CFTVFVQANK LQQHIFSAHG QEDKIYDCTQ CPQKFFFQTE LQNHTMTQHS S
