ID ZMIZ1_HUMAN Reviewed; 1067 AA.
AC Q9ULJ6; Q5JSH9; Q7Z7E6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Zinc finger MIZ domain-containing protein 1 {ECO:0000305};
DE AltName: Full=PIAS-like protein Zimp10;
DE AltName: Full=Retinoic acid-induced protein 17;
GN Name=ZMIZ1 {ECO:0000312|HGNC:HGNC:16493}; Synonyms=KIAA1224, RAI17, ZIMP10;
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), FUNCTION, SUBCELLULAR LOCATION,
RP DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH AR, AND SUMOYLATION.
RX PubMed=14609956; DOI=10.1093/emboj/cdg585;
RA Sharma M., Li X., Wang Y., Zarnegar M., Huang C.-Y., Palvimo J.J., Lim B.,
RA Sun Z.;
RT "hZimp10 is an androgen receptor co-activator and forms a complex with
RT SUMO-1 at replication foci.";
RL EMBO J. 22:6101-6114(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP FUNCTION, INTERACTION WITH SMAD3 AND SMAD4, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=16777850; DOI=10.1074/jbc.m508365200;
RA Li X., Thyssen G., Beliakoff J., Sun Z.;
RT "The novel PIAS-like protein hZimp10 enhances Smad transcriptional
RT activity.";
RL J. Biol. Chem. 281:23748-23756(2006).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-834, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-834, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-834, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-834 AND LYS-843, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN NEDDFSA, VARIANTS NEDDFSA
RP ARG-91; THR-287; ILE-296; LYS-296; ILE-298 AND MET-300, AND
RP CHARACTERIZATION OF VARIANTS NEDDFSA ARG-91 AND MET-300.
RX PubMed=30639322; DOI=10.1016/j.ajhg.2018.12.007;
RG Deciphering Developmental Disorders Study;
RG University of Washington Center for Mendelian Genomics;
RA Carapito R., Ivanova E.L., Morlon A., Meng L., Molitor A., Erdmann E.,
RA Kieffer B., Pichot A., Naegely L., Kolmer A., Paul N., Hanauer A.,
RA Tran Mau-Them F., Jean-Marcais N., Hiatt S.M., Cooper G.M., Tvrdik T.,
RA Muir A.M., Dimartino C., Chopra M., Amiel J., Gordon C.T., Dutreux F.,
RA Garde A., Thauvin-Robinet C., Wang X., Leduc M.S., Phillips M.,
RA Crawford H.P., Kukolich M.K., Hunt D., Harrison V., Kharbanda M.,
RA Smigiel R., Gold N., Hung C.Y., Viskochil D.H., Dugan S.L.,
RA Bayrak-Toydemir P., Joly-Helas G., Guerrot A.M., Schluth-Bolard C., Rio M.,
RA Wentzensen I.M., McWalter K., Schnur R.E., Lewis A.M., Lalani S.R.,
RA Mensah-Bonsu N., Ceraline J., Sun Z., Ploski R., Bacino C.A., Mefford H.C.,
RA Faivre L., Bodamer O., Chelly J., Isidor B., Bahram S.;
RT "ZMIZ1 variants cause a syndromic neurodevelopmental disorder.";
RL Am. J. Hum. Genet. 104:319-330(2019).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-118, FUNCTION, AND INTERACTION
RP WITH NOTCH1 AND RBPJ.
RX PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
RA Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y., Alarcon A.S.,
RA Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S., Maillard I.,
RA Samuelson L.C., Cierpicki T., Chiang M.Y.;
RT "The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
RT Notch1 in T cell development and leukemia.";
RL Immunity 43:870-883(2015).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-551.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Acts as a transcriptional coactivator. Increases ligand-
CC dependent transcriptional activity of AR and promotes AR sumoylation.
CC The stimulation of AR activity is dependent upon sumoylation
CC (PubMed:14609956, PubMed:26522984). Also functions as a transcriptional
CC coactivator in the TGF-beta signaling pathway by increasing the
CC activity of the SMAD3/SMAD4 transcriptional complex (PubMed:16777850).
CC Involved in transcriptional activation of a subset of NOTCH1 target
CC genes including MYC. Involved in thymocyte and T cell development (By
CC similarity). Involved in the regulation of postmitotic positioning of
CC pyramidal neurons in the developing cerebral cortex (PubMed:30639322).
CC {ECO:0000250|UniProtKB:Q6P1E1, ECO:0000269|PubMed:14609956,
CC ECO:0000269|PubMed:16777850, ECO:0000269|PubMed:26522984,
CC ECO:0000269|PubMed:30639322}.
CC -!- SUBUNIT: Interacts with AR, but not with ESR1, NR3C1, PGR, THRB nor
CC VDR. Interacts with NOTCH1 and RBPJ (PubMed:14609956, PubMed:26522984).
CC Interacts with SMARCA4 (By similarity). Interacts (via SP-RING-type
CC domain) with SMAD3 and SMAD4 (via MH2 domain) (PubMed:16777850).
CC {ECO:0000250|UniProtKB:Q6P1E1, ECO:0000269|PubMed:14609956,
CC ECO:0000269|PubMed:16777850, ECO:0000269|PubMed:26522984}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14609956, ECO:0000269|PubMed:16777850}. Cytoplasm
CC {ECO:0000269|PubMed:14609956}. Nucleus {ECO:0000269|PubMed:30639322}.
CC Note=Enriched at replication foci throughout S phase.
CC {ECO:0000269|PubMed:14609956}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULJ6-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9ULJ6-3; Sequence=VSP_061581;
CC -!- TISSUE SPECIFICITY: Expressed most abundantly in ovary and, at lower
CC levels, in prostate, spleen and testis. Weak expression, if any, in
CC thymus, small intestine, colon and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:14609956}.
CC -!- DOMAIN: The SP-RING-type domain mediates interaction with SMAD3 and
CC SMAD4. {ECO:0000269|PubMed:16777850}.
CC -!- DOMAIN: The C-terminal proline-rich domain possesses a significant
CC intrinsic transcriptional activity. This activity is inhibited by the
CC N-terminus in the full-length protein. {ECO:0000269|PubMed:14609956}.
CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies and distal
CC skeletal anomalies (NEDDFSA) [MIM:618659]: An autosomal dominant
CC disorder characterized by intellectual disability, developmental delay,
CC poor language acquisition, behavioral abnormalities, growth failure,
CC feeding difficulties, microcephaly, facial dysmorphism, and mild
CC skeletal anomalies of the hands and feet.
CC {ECO:0000269|PubMed:30639322}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86538.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033050; BAA86538.2; ALT_INIT; mRNA.
DR EMBL; AY235683; AAP13542.1; -; mRNA.
DR EMBL; AL391665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS7357.1; -. [Q9ULJ6-1]
DR RefSeq; NP_065071.1; NM_020338.3. [Q9ULJ6-1]
DR RefSeq; XP_011538282.1; XM_011539980.2.
DR RefSeq; XP_016871931.1; XM_017016442.1.
DR PDB; 5AIZ; X-ray; 1.70 A; A=1-118.
DR PDBsum; 5AIZ; -.
DR AlphaFoldDB; Q9ULJ6; -.
DR SMR; Q9ULJ6; -.
DR BioGRID; 121427; 39.
DR IntAct; Q9ULJ6; 21.
DR MINT; Q9ULJ6; -.
DR STRING; 9606.ENSP00000334474; -.
DR GlyGen; Q9ULJ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULJ6; -.
DR PhosphoSitePlus; Q9ULJ6; -.
DR BioMuta; ZMIZ1; -.
DR DMDM; 56404979; -.
DR EPD; Q9ULJ6; -.
DR jPOST; Q9ULJ6; -.
DR MassIVE; Q9ULJ6; -.
DR MaxQB; Q9ULJ6; -.
DR PaxDb; 9606-ENSP00000334474; -.
DR PeptideAtlas; Q9ULJ6; -.
DR ProteomicsDB; 85048; -. [Q9ULJ6-1]
DR Pumba; Q9ULJ6; -.
DR Antibodypedia; 29855; 210 antibodies from 26 providers.
DR DNASU; 57178; -.
DR Ensembl; ENST00000334512.10; ENSP00000334474.5; ENSG00000108175.19. [Q9ULJ6-1]
DR GeneID; 57178; -.
DR KEGG; hsa:57178; -.
DR MANE-Select; ENST00000334512.10; ENSP00000334474.5; NM_020338.4; NP_065071.1.
DR UCSC; uc001kaf.3; human. [Q9ULJ6-1]
DR AGR; HGNC:16493; -.
DR CTD; 57178; -.
DR DisGeNET; 57178; -.
DR GeneCards; ZMIZ1; -.
DR HGNC; HGNC:16493; ZMIZ1.
DR HPA; ENSG00000108175; Low tissue specificity.
DR MalaCards; ZMIZ1; -.
DR MIM; 607159; gene.
DR MIM; 618659; phenotype.
DR neXtProt; NX_Q9ULJ6; -.
DR OpenTargets; ENSG00000108175; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA162409804; -.
DR VEuPathDB; HostDB:ENSG00000108175; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_009461_1_0_1; -.
DR InParanoid; Q9ULJ6; -.
DR OMA; PPMAMNQ; -.
DR OrthoDB; 20246at2759; -.
DR PhylomeDB; Q9ULJ6; -.
DR TreeFam; TF316952; -.
DR PathwayCommons; Q9ULJ6; -.
DR SignaLink; Q9ULJ6; -.
DR SIGNOR; Q9ULJ6; -.
DR BioGRID-ORCS; 57178; 62 hits in 1180 CRISPR screens.
DR ChiTaRS; ZMIZ1; human.
DR GeneWiki; ZMIZ1; -.
DR GenomeRNAi; 57178; -.
DR Pharos; Q9ULJ6; Tbio.
DR PRO; PR:Q9ULJ6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9ULJ6; Protein.
DR Bgee; ENSG00000108175; Expressed in dorsal motor nucleus of vagus nerve and 211 other cell types or tissues.
DR ExpressionAtlas; Q9ULJ6; baseline and differential.
DR Genevisible; Q9ULJ6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0021852; P:pyramidal neuron migration to cerebral cortex; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
DR CDD; cd16822; SP-RING_ZMIZ1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR IDEAL; IID00740; -.
DR InterPro; IPR040797; Zmiz1_N.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10782:SF7; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR Pfam; PF18028; Zmiz1_N; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Disease variant;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1067
FT /note="Zinc finger MIZ domain-containing protein 1"
FT /id="PRO_0000218987"
FT ZN_FING 727..808
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..120
FT /note="Sufficient for transactivation activity; sufficient
FT for interaction with NOTCH1"
FT /evidence="ECO:0000269|PubMed:26522984"
FT REGION 112..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..1067
FT /note="Transactivation domain"
FT /evidence="ECO:0000269|PubMed:26522984"
FT REGION 868..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 758
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 784
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 834
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 843
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 3)"
FT /id="VSP_061581"
FT VARIANT 91
FT /note="K -> R (in NEDDFSA; leads to altered positioning of
FT pyramidal neurons; dbSNP:rs1554817910)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083438"
FT VARIANT 287
FT /note="A -> T (in NEDDFSA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083439"
FT VARIANT 296
FT /note="T -> I (in NEDDFSA)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083440"
FT VARIANT 296
FT /note="T -> K (in NEDDFSA; dbSNP:rs1589579476)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083441"
FT VARIANT 298
FT /note="T -> I (in NEDDFSA; dbSNP:rs1853549548)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083442"
FT VARIANT 300
FT /note="T -> M (in NEDDFSA; leads to altered positioning of
FT pyramidal neurons; decreased transcription coactivator
FT activity; does not affect nuclear localization;
FT dbSNP:rs1589579500)"
FT /evidence="ECO:0000269|PubMed:30639322"
FT /id="VAR_083443"
FT VARIANT 551
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036326"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5AIZ"
FT HELIX 90..110
FT /evidence="ECO:0007829|PDB:5AIZ"
SQ SEQUENCE 1067 AA; 115483 MW; 6C4137488579CC74 CRC64;
MNSMDRHIQQ TNDRLQCIKQ HLQNPANFHN AATELLDWCG DPRAFQRPFE QSLMGCLTVV
SRVAAQQGFD LDLGYRLLAV CAANRDKFTP KSAALLSSWC EELGRLLLLR HQKSRQSDPP
GKLPMQPPLS SMSSMKPTLS HSDGSFPYDS VPWQQNTNQP PGSLSVVTTV WGVTNTSQSQ
VLGNPMANAN NPMNPGGNPM ASGMTTSNPG LNSPQFAGQQ QQFSAKAGPA QPYIQQSMYG
RPNYPGSGGF GASYPGGPNA PAGMGIPPHT RPPADFTQPA AAAAAAAVAA AAATATATAT
ATVAALQETQ NKDINQYGPM GPTQAYNSQF MNQPGPRGPA SMGGSMNPAS MAAGMTPSGM
SGPPMGMNQP RPPGISPFGT HGQRMPQQTY PGPRPQSLPI QNIKRPYPGE PNYGNQQYGP
NSQFPTQPGQ YPAPNPPRPL TSPNYPGQRM PSQPSSGQYP PPTVNMGQYY KPEQFNGQNN
TFSGSSYSNY SQGNVNRPPR PVPVANYPHS PVPGNPTPPM TPGSSIPPYL SPSQDVKPPF
PPDIKPNMSA LPPPPANHND ELRLTFPVRD GVVLEPFRLE HNLAVSNHVF HLRPTVHQTL
MWRSDLELQF KCYHHEDRQM NTNWPASVQV SVNATPLTIE RGDNKTSHKP LHLKHVCQPG
RNTIQITVTA CCCSHLFVLQ LVHRPSVRSV LQGLLKKRLL PAEHCITKIK RNFSSVAASS
GNTTLNGEDG VEQTAIKVSL KCPITFRRIQ LPARGHDCKH VQCFDLESYL QLNCERGTWR
CPVCNKTALL EGLEVDQYMW GILNAIQHSE FEEVTIDPTC SWRPVPIKSD LHIKDDPDGI
PSKRFKTMSP SQMIMPNVME MIAALGPGPS PYPLPPPPGG TNSNDYSSQG NNYQGHGNFD
FPHGNPGGTS MNDFMHGPPQ LSHPPDMPNN MAALEKPLSH PMQETMPHAG SSDQPHPSIQ
QGLHVPHPSS QSGPPLHHSG APPPPPSQPP RQPPQAAPSS HPHSDLTFNP SSALEGQAGA
QGASDMPEPS LDLLPELTNP DELLSYLDPP DLPSNSNDDL LSLFENN
//
