PRDM1_MOUSE
ID PRDM1_MOUSE Reviewed; 856 AA.
AC Q60636; A2VDE8; Q3UET9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=PR domain zinc finger protein 1;
DE EC=2.1.1.-;
DE AltName: Full=B lymphocyte-induced maturation protein 1;
DE Short=Blimp-1;
DE AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
DE AltName: Full=PR domain-containing protein 1;
GN Name=Prdm1; Synonyms=Blimp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=B-cell;
RX PubMed=8168136; DOI=10.1016/0092-8674(94)90321-2;
RA Turner C.A., Mack D.H., Davis M.M.;
RT "Blimp-1, a novel zinc finger-containing protein that can drive the
RT maturation of B lymphocytes into immunoglobulin-secreting cells.";
RL Cell 77:297-306(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 5),
RP AND TISSUE SPECIFICITY.
RC STRAIN=129;
RX PubMed=11121475; DOI=10.1093/nar/28.24.4846;
RA Tunyaplin C., Shapiro M.A., Calame K.L.;
RT "Characterization of the B lymphocyte-induced maturation protein-1 (Blimp-
RT 1) gene, mRNA isoforms and basal promoter.";
RL Nucleic Acids Res. 28:4846-4855(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1-253 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 INTERACTION WITH PRMT5.
RX PubMed=16699504; DOI=10.1038/ncb1413;
RA Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA Kouzarides T., Surani M.A.;
RT "Blimp1 associates with Prmt5 and directs histone arginine methylation in
RT mouse germ cells.";
RL Nat. Cell Biol. 8:623-630(2006).
RN [6]
RP ALTERNATIVE PROMOTER USAGE (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo, Placenta, and Yolk sac;
RX PubMed=19737919; DOI=10.1128/mcb.00670-09;
RA Morgan M.A., Magnusdottir E., Kuo T.C., Tunyaplin C., Harper J.,
RA Arnold S.J., Calame K., Robertson E.J., Bikoff E.K.;
RT "Blimp-1/Prdm1 alternative promoter usage during mouse development and
RT plasma cell differentiation.";
RL Mol. Cell. Biol. 29:5813-5827(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN LYMPHOCYTE T CELLS,
RP TISSUE SPECIFICITY, AND INDUCTION (MICROBIAL INFECTION).
RX PubMed=27102484; DOI=10.1126/science.aad2035;
RA Mackay L.K., Minnich M., Kragten N.A., Liao Y., Nota B., Seillet C.,
RA Zaid A., Man K., Preston S., Freestone D., Braun A., Wynne-Jones E.,
RA Behr F.M., Stark R., Pellicci D.G., Godfrey D.I., Belz G.T., Pellegrini M.,
RA Gebhardt T., Busslinger M., Shi W., Carbone F.R., van Lier R.A.,
RA Kallies A., van Gisbergen K.P.;
RT "Hobit and Blimp1 instruct a universal transcriptional program of tissue
RT residency in lymphocytes.";
RL Science 352:459-463(2016).
CC -!- FUNCTION: Transcription factor that mediates a transcriptional program
CC in various innate and adaptive immune tissue-resident lymphocyte T cell
CC types such as tissue-resident memory T (Trm), natural killer (trNK) and
CC natural killer T (NKT) cells and negatively regulates gene expression
CC of proteins that promote the egress of tissue-resident T-cell
CC populations from non-lymphoid organs (PubMed:27102484). Plays a role in
CC the development, retention and long-term establishment of adaptive and
CC innate tissue-resident lymphocyte T cell types in non-lymphoid organs,
CC such as the skin and gut, but also in other nonbarrier tissues like
CC liver and kidney, and therefore may provide immediate immunological
CC protection against reactivating infections or viral reinfection
CC (PubMed:27102484). Binds specifically to the PRDI element in the
CC promoter of the beta-interferon gene (By similarity). Drives the
CC maturation of B-lymphocytes into Ig secreting cells (By similarity).
CC Associates with the transcriptional repressor ZNF683 to chromatin at
CC gene promoter regions (PubMed:27102484). {ECO:0000250|UniProtKB:O75626,
CC ECO:0000269|PubMed:27102484}.
CC -!- SUBUNIT: Interacts with PRMT5 (PubMed:16699504). Interacts with FBXO10
CC (By similarity). Interacts with FBXO11 (By similarity). Interacts with
CC multiple nuclear sumoylation E3 ligases, including CBX4, PIAS1, PIAS2,
CC PIAS3, PIAS4, PML and RNF4, but not RANBP2 (By similarity). Interacts
CC with LDB1, SMARCD3 and SMARCC1 (By similarity).
CC {ECO:0000250|UniProtKB:O75626, ECO:0000269|PubMed:16699504}.
CC -!- INTERACTION:
CC Q60636; P63165: SUMO1; Xeno; NbExp=3; IntAct=EBI-7000804, EBI-80140;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8168136}. Cytoplasm
CC {ECO:0000250|UniProtKB:O75626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q60636-1; Sequence=Displayed;
CC Name=2; Synonyms=1A;
CC IsoId=Q60636-2; Sequence=VSP_039189;
CC Name=3; Synonyms=1B;
CC IsoId=Q60636-3; Sequence=VSP_041570;
CC Name=4; Synonyms=1C;
CC IsoId=Q60636-4; Sequence=VSP_041571;
CC Name=5; Synonyms=delta exon 7;
CC IsoId=Q60636-5; Sequence=VSP_041572;
CC -!- TISSUE SPECIFICITY: Expressed in innate lymphocytes, including tissue-
CC resident conventional natural killer (cNK) cells in liver
CC (PubMed:27102484). Expressed also weakly in tissue-resident natural
CC killer (trNK) and natural killer T (NKT) cells in liver
CC (PubMed:27102484). Isoform 1 is detected in bone marrow, spleen and
CC lymph node but not in brain, heart, kidney, liver, ovary or muscle.
CC Weak expression detected in the lung. Isoform 3 is detected only in
CC yolk sac. Isoform 4 is detected in embryo, yolk sac, placenta,
CC splenocytes, and activated T-cells. {ECO:0000269|PubMed:11121475,
CC ECO:0000269|PubMed:19737919, ECO:0000269|PubMed:27102484,
CC ECO:0000269|PubMed:8168136}.
CC -!- INDUCTION: By lymphokines, specifically IL-2 and IL-5. Up-regulated
CC during dendritic cell maturation.
CC -!- INDUCTION: (Microbial infection) Up-regulated in response to Herpes
CC simplex virus (HSV) infection in skin and spleen memory CD8(+) T cells.
CC {ECO:0000269|PubMed:27102484}.
CC -!- INDUCTION: (Microbial infection) Up-regulated in response to
CC Lymphocytic choriomeningitis virus (LCMV) in memory CD8(+) T cells.
CC {ECO:0000269|PubMed:27102484}.
CC -!- PTM: Sumoylation at Lys-847 by PIAS1 increases transcriptional
CC repressor activity, and is critical for plasma cell differentiation (By
CC similarity). Can be sumoylated with SUMO1 and SUMO2 by PML. Degradation
CC of the wild-type protein mostly depends upon sumoylation, rather than
CC ubiquitination (By similarity). Desumoylated by SENP1 and SENP6 (By
CC similarity). {ECO:0000250|UniProtKB:O75626}.
CC -!- PTM: Ubiquitinated by SCF(FBXO11), leading to its degradation by the
CC proteasome. {ECO:0000250|UniProtKB:O75626}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality (PubMed:19737919).
CC Compound heterozygotes display germ cell defects and a rudimentary or
CC missing fifth digit of the forelimb (PubMed:19737919). Conditional
CC knockout in lymphocyte T cells show a weak reduction in tissue-resident
CC memory T (Trm) cell population maintenance in the skin, gut, liver and
CC kidney but not of splenic T cells (PubMed:27102484). Double knockouts
CC for PRDM1/BLIMP1 and ZNF683 result in a strong inhibition of Trm cell
CC population maintenance but not of circulating memory cells
CC (PubMed:27102484). Display an enhancement of natural killer T (NKT)
CC cells migration preferentially to the white pulp of the spleen in
CC response to chemotactic stimuli (PubMed:27102484).
CC {ECO:0000269|PubMed:19737919, ECO:0000269|PubMed:27102484}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage of
CC isoform 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage of
CC isoform 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 1. Does not bind DNA. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI29802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U08185; AAA19252.1; -; mRNA.
DR EMBL; AF305539; AAG42212.1; -; Genomic_DNA.
DR EMBL; AF305534; AAG42212.1; JOINED; Genomic_DNA.
DR EMBL; AF305535; AAG42212.1; JOINED; Genomic_DNA.
DR EMBL; AF305536; AAG42212.1; JOINED; Genomic_DNA.
DR EMBL; AF305537; AAG42212.1; JOINED; Genomic_DNA.
DR EMBL; AF305538; AAG42212.1; JOINED; Genomic_DNA.
DR EMBL; AK077622; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK149344; BAE28822.1; -; mRNA.
DR EMBL; BC129801; AAI29802.1; ALT_INIT; mRNA.
DR CCDS; CCDS23825.2; -. [Q60636-2]
DR PIR; A53503; A53503.
DR RefSeq; NP_031574.2; NM_007548.4. [Q60636-2]
DR RefSeq; XP_006512565.1; XM_006512502.3. [Q60636-4]
DR RefSeq; XP_006512566.1; XM_006512503.2. [Q60636-3]
DR RefSeq; XP_006512568.1; XM_006512505.2. [Q60636-1]
DR RefSeq; XP_011241411.1; XM_011243109.1. [Q60636-3]
DR AlphaFoldDB; Q60636; -.
DR SMR; Q60636; -.
DR BioGRID; 198355; 9.
DR IntAct; Q60636; 1.
DR MINT; Q60636; -.
DR STRING; 10090.ENSMUSP00000101129; -.
DR iPTMnet; Q60636; -.
DR PhosphoSitePlus; Q60636; -.
DR EPD; Q60636; -.
DR MaxQB; Q60636; -.
DR PaxDb; Q60636; -.
DR PeptideAtlas; Q60636; -.
DR PRIDE; Q60636; -.
DR ProteomicsDB; 291552; -. [Q60636-1]
DR ProteomicsDB; 291553; -. [Q60636-2]
DR ProteomicsDB; 291554; -. [Q60636-3]
DR ProteomicsDB; 291555; -. [Q60636-4]
DR ProteomicsDB; 291556; -. [Q60636-5]
DR Antibodypedia; 19038; 697 antibodies from 39 providers.
DR DNASU; 12142; -.
DR Ensembl; ENSMUST00000039174; ENSMUSP00000039248; ENSMUSG00000038151. [Q60636-1]
DR Ensembl; ENSMUST00000105490; ENSMUSP00000101129; ENSMUSG00000038151. [Q60636-2]
DR Ensembl; ENSMUST00000218369; ENSMUSP00000151237; ENSMUSG00000038151. [Q60636-4]
DR GeneID; 12142; -.
DR KEGG; mmu:12142; -.
DR UCSC; uc007ezu.3; mouse. [Q60636-1]
DR UCSC; uc007ezv.3; mouse. [Q60636-2]
DR CTD; 639; -.
DR MGI; MGI:99655; Prdm1.
DR VEuPathDB; HostDB:ENSMUSG00000038151; -.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000154798; -.
DR HOGENOM; CLU_007033_2_1_1; -.
DR InParanoid; Q60636; -.
DR OMA; CQNGMNV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q60636; -.
DR TreeFam; TF316545; -.
DR BioGRID-ORCS; 12142; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Prdm1; mouse.
DR PRO; PR:Q60636; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q60636; protein.
DR Bgee; ENSMUSG00000038151; Expressed in gastrula and 174 other tissues.
DR Genevisible; Q60636; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0007281; P:germ cell development; IGI:MGI.
DR GO; GO:0003170; P:heart valve development; IMP:MGI.
DR GO; GO:0034969; P:histone arginine methylation; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0033082; P:regulation of extrathymic T cell differentiation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032823; P:regulation of natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0051136; P:regulation of NK T cell differentiation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:1990654; P:sebum secreting cell proliferation; IDA:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR CDD; cd19187; PR-SET_PRDM1; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016608; PRDM1.
DR InterPro; IPR044413; PRDM1_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR PIRSF; PIRSF013212; PRDM1; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative promoter usage; Alternative splicing;
KW Cytoplasm; Developmental protein; DNA-binding; Immunity; Innate immunity;
KW Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..856
FT /note="PR domain zinc finger protein 1"
FT /id="PRO_0000047758"
FT DOMAIN 115..233
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 606..628
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 690..712
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 357..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..605
FT /note="Interaction with PIAS1"
FT /evidence="ECO:0000250"
FT COMPBIAS 370..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75626"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75626"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041570"
FT VAR_SEQ 1..47
FT /note="MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALDSYSTVQ -> M
FT LDLLLEKRVGTTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_039189"
FT VAR_SEQ 1..47
FT /note="MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALDSYSTVQ -> M
FT TPGVPGHRTQQRPQHISALSDKAKDCSK (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_041571"
FT VAR_SEQ 624..666
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_041572"
FT CONFLICT 155
FT /note="N -> K (in Ref. 4; AAI29802)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> M (in Ref. 3; AK077622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 95836 MW; B9AC6FC2E29ECF4A CRC64;
MREAYLRCWI FSWKNVWVRP CQRLHFKTVL LQGSLLYTAL DSYSTVQAAP KSSSGSVKFQ
GLAETGIMKM DMEDADMTLW TEAEFEEKCT YIVNDHPWDS GADGGTSVQA EASLPRNLLF
KYAANNSKEV IGVVSKEYIP KGTRFGPLIG EVYTNDTVPK NANRKYFWRI YSREEFHHFI
DGFNEEKSNW MRYVNPAHSA REQNLAACQN GMNIYFYTIK PIPANQELLV WYCRDFAERL
HYPYPGELTV INLTQTESNP KQYSSEKNEL YPKSVPKREY SVKEILKLDS NPSKRKDIYR
SNISPFTLEK DMDGFRKNGS PDMPFYPRVV YPIRAPLPED FLKASLAYGM ERPTYITHSP
LPSSTTPSPP ASSSPEQSLK SSSPHSSPGN TVSPLAPGLP EHRDSYSYLN VSYGSEGLGS
YPGYAPAPHL PPAFIPSYNA HYPKFLLPPY GISSNGLSTM NNINGINNFS LFPRLYPVYS
NLLSGSSLPH PMLNPASLPS SLPTDGARRL LPPEHPKEVL IPAPHSAFSL TGAAASMKDE
SSPPSGSPTA GTAATSEHVV QPKATSSVMA APSTDGAMNL IKNKRNMTGY KTLPYPLKKQ
NGKIKYECNV CAKTFGQLSN LKVHLRVHSG ERPFKCQTCN KGFTQLAHLQ KHYLVHTGEK
PHECQVCHKR FSSTSNLKTH LRLHSGEKPY QCKVCPAKFT QFVHLKLHKR LHTRERPHKC
AQCHKSYIHL CSLKVHLKGN CPAGPAAGLP LEDLTRINEE IERFDISDNA DRLEDMEDSV
DVTSMVEKEI LAVVRKEKEE TSLKVSLQRN MGNGLLSSGC SLYESSDLSL MKLPHSNPLP
LVPVKVKQET VEPMDP
