ID   SALL4_HUMAN             Reviewed;        1053 AA.
AC   Q9UJQ4; A2A2D8; Q540H3; Q6Y8G6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 196.
DE   RecName: Full=Sal-like protein 4;
DE   AltName: Full=Zinc finger protein 797;
DE   AltName: Full=Zinc finger protein SALL4;
GN   Name=SALL4; Synonyms=ZNF797;
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] (ISOFORMS SALL4A AND SALL4B), ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=16763212; DOI=10.1182/blood-2006-02-001594;
RA   Ma Y., Cui W., Yang J., Qu J., Di C., Amin H.M., Lai R., Ritz J.,
RA   Krause D.S., Chai L.;
RT   "SALL4, a novel oncogene, is constitutively expressed in human acute
RT   myeloid leukemia (AML) and induces AML in transgenic mice.";
RL   Blood 108:2726-2735(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SALL4A).
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   INVOLVEMENT IN DRRS.
RX   PubMed=12393809; DOI=10.1093/hmg/11.23.2979;
RA   Kohlhase J., Heinrich M., Schubert L., Liebers M., Kispert A., Laccone F.,
RA   Turnpenny P., Winter R.M., Reardon W.;
RT   "Okihiro syndrome is caused by SALL4 mutations.";
RL   Hum. Mol. Genet. 11:2979-2987(2002).
RN   [6]
RP   DOMAIN.
RX   PubMed=16545361; DOI=10.1016/j.ydbio.2006.02.009;
RA   Sweetman D., Muensterberg A.;
RT   "The vertebrate spalt genes in development and disease.";
RL   Dev. Biol. 293:285-293(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   INTERACTION WITH BEND3.
RX   PubMed=21914818; DOI=10.1242/jcs.086603;
RA   Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
RT   "A BEN-domain-containing protein associates with heterochromatin and
RT   represses transcription.";
RL   J. Cell Sci. 124:3149-3163(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; THR-541; SER-776;
RP   SER-789 AND SER-1019, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   INTERACTION WITH NRBP1.
RX   PubMed=22510880; DOI=10.1038/emboj.2012.91;
RA   Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G.,
RA   Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E.,
RA   Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.;
RT   "Nuclear receptor binding protein 1 regulates intestinal progenitor cell
RT   homeostasis and tumour formation.";
RL   EMBO J. 31:2486-2497(2012).
RN   [11]
RP   FUNCTION, UBIQUITINATION, SUMOYLATION AT LYS-156; LYS-316; LYS-374 AND
RP   LYS-838, PHOSPHORYLATION AT SER-57 AND SER-852, AND INTERACTION WITH
RP   POU5F1.
RX   PubMed=23012367; DOI=10.1074/jbc.m112.391441;
RA   Yang F., Yao Y., Jiang Y., Lu L., Ma Y., Dai W.;
RT   "Sumoylation is important for stability, subcellular localization, and
RT   transcriptional activity of SALL4, an essential stem cell transcription
RT   factor.";
RL   J. Biol. Chem. 287:38600-38608(2012).
RN   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-316 AND LYS-838, AND
RP   IDENTIFICATION BY MASS 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-156; LYS-175; LYS-190; LYS-290;
RP   LYS-316; LYS-372; LYS-374; LYS-436; LYS-550; LYS-597; LYS-623; LYS-838;
RP   LYS-896; LYS-932 AND LYS-947, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [14]
RP   VARIANTS ARG-507 AND LEU-798, AND INVOLVEMENT IN DRRS.
RX   PubMed=12395297; DOI=10.1086/343821;
RA   Al-Baradie R., Yamada K., St Hilaire C., Chan W.-M., Andrews C.,
RA   McIntosh N., Nakano M., Martonyi E.J., Raymond W.R., Okumura S.,
RA   Okihiro M.M., Engle E.C.;
RT   "Duane radial ray syndrome (Okihiro syndrome) maps to 20q13 and results
RT   from mutations in SALL4, a new member of the SAL family.";
RL   Am. J. Hum. Genet. 71:1195-1199(2002).
RN   [15]
RP   VARIANT DRRS ARG-888.
RX   PubMed=16402211; DOI=10.1007/s00439-005-0124-7;
RA   Miertus J., Borozdin W., Frecer V., Tonini G., Bertok S., Amoroso A.,
RA   Miertus S., Kohlhase J.;
RT   "A SALL4 zinc finger missense mutation predicted to result in increased DNA
RT   binding affinity is associated with cranial midline defects and mild
RT   features of Okihiro syndrome.";
RL   Hum. Genet. 119:154-161(2006).
RN   [16]
RP   INVOLVEMENT IN IVIC.
RX   PubMed=17256792; DOI=10.1002/ajmg.a.31603;
RA   Paradisi I., Arias S.;
RT   "IVIC syndrome is caused by a c.2607delA mutation in the SALL4 locus.";
RL   Am. J. Med. Genet. A 143:326-332(2007).
CC   -!- FUNCTION: Transcription factor with a key role in the maintenance and
CC       self-renewal of embryonic and hematopoietic stem cells.
CC       {ECO:0000269|PubMed:23012367}.
CC   -!- SUBUNIT: Interacts with POU5F1/OCT4 (PubMed:23012367). Interacts with
CC       NANOG (By similarity). Interacts with BEND3 (PubMed:21914818).
CC       Interacts with NSD2 (via PHD-type zinc fingers 1, 2 and 3) (By
CC       similarity). Interacts with NRBP1 (PubMed:22510880).
CC       {ECO:0000250|UniProtKB:Q8BX22, ECO:0000269|PubMed:21914818,
CC       ECO:0000269|PubMed:22510880, ECO:0000269|PubMed:23012367}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=SALL4A;
CC         IsoId=Q9UJQ4-1; Sequence=Displayed;
CC       Name=SALL4B;
CC         IsoId=Q9UJQ4-2; Sequence=VSP_046525;
CC   -!- TISSUE SPECIFICITY: Expressed in testis. Constitutively expressed in
CC       acute myeloid leukemia (AML). {ECO:0000269|PubMed:16763212}.
CC   -!- PTM: Isoform SALL4B exists primarily as a ubiquitinated form.
CC       {ECO:0000269|PubMed:23012367}.
CC   -!- PTM: Sumoylation with both SUMO1 and SUMO2 regulates the stability,
CC       subcellular localization, transcriptional activity, and may reduce
CC       interaction with POU5F1/OCT4. {ECO:0000269|PubMed:23012367}.
CC   -!- DISEASE: Duane-radial ray syndrome (DRRS) [MIM:607323]: Disorder
CC       characterized by the association of forearm malformations with Duane
CC       retraction syndrome. {ECO:0000269|PubMed:12393809,
CC       ECO:0000269|PubMed:12395297, ECO:0000269|PubMed:16402211}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: IVIC syndrome (IVIC) [MIM:147750]: An autosomal dominant
CC       condition characterized by upper limbs anomalies (radial ray defects,
CC       carpal bones fusion), extraocular motor disturbances, congenital
CC       bilateral non-progressive mixed hearing loss. Other less consistent
CC       malformations include heart involvement, mild thrombocytopenia and
CC       leukocytosis (before age 50), shoulder girdle hypoplasia, imperforate
CC       anus, kidney malrotation or rectovaginal fistula. The IVIC syndrome is
CC       an allelic disorder of Duane-radial ray syndrome with a similar
CC       phenotype. {ECO:0000269|PubMed:17256792}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY172738; AAO44950.1; -; mRNA.
DR   EMBL; AY170621; AAO16566.1; -; mRNA.
DR   EMBL; AL034420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75595.1; -; Genomic_DNA.
DR   EMBL; BC111714; AAI11715.1; -; mRNA.
DR   CCDS; CCDS13438.1; -. [Q9UJQ4-1]
DR   CCDS; CCDS82629.1; -. [Q9UJQ4-2]
DR   RefSeq; NP_001304960.1; NM_001318031.1. [Q9UJQ4-2]
DR   RefSeq; NP_065169.1; NM_020436.4. [Q9UJQ4-1]
DR   PDB; 5XWR; X-ray; 2.69 A; C/D=1-12.
DR   PDB; 6UML; X-ray; 3.58 A; E=405-432.
DR   PDB; 7BQU; X-ray; 1.90 A; B=410-432.
DR   PDB; 7BQV; X-ray; 1.80 A; B=410-432.
DR   PDB; 7Y3I; X-ray; 2.45 A; A/B/C/D=855-930.
DR   PDB; 7Y3K; X-ray; 2.50 A; A/B=855-930.
DR   PDB; 7Y3M; X-ray; 2.72 A; A/B/C/F/I/J=378-453.
DR   PDB; 8CUC; X-ray; 2.09 A; E/F/G/H=864-929.
DR   PDBsum; 5XWR; -.
DR   PDBsum; 6UML; -.
DR   PDBsum; 7BQU; -.
DR   PDBsum; 7BQV; -.
DR   PDBsum; 7Y3I; -.
DR   PDBsum; 7Y3K; -.
DR   PDBsum; 7Y3M; -.
DR   PDBsum; 8CUC; -.
DR   AlphaFoldDB; Q9UJQ4; -.
DR   SMR; Q9UJQ4; -.
DR   BioGRID; 121420; 26.
DR   IntAct; Q9UJQ4; 2.
DR   MINT; Q9UJQ4; -.
DR   STRING; 9606.ENSP00000217086; -.
DR   BindingDB; Q9UJQ4; -.
DR   GlyGen; Q9UJQ4; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q9UJQ4; -.
DR   PhosphoSitePlus; Q9UJQ4; -.
DR   BioMuta; SALL4; -.
DR   DMDM; 24212387; -.
DR   EPD; Q9UJQ4; -.
DR   jPOST; Q9UJQ4; -.
DR   MassIVE; Q9UJQ4; -.
DR   MaxQB; Q9UJQ4; -.
DR   PaxDb; 9606-ENSP00000217086; -.
DR   PeptideAtlas; Q9UJQ4; -.
DR   ProteomicsDB; 190; -.
DR   ProteomicsDB; 84639; -. [Q9UJQ4-1]
DR   ABCD; Q9UJQ4; 1 sequenced antibody.
DR   Antibodypedia; 13868; 368 antibodies from 41 providers.
DR   DNASU; 57167; -.
DR   Ensembl; ENST00000217086.9; ENSP00000217086.4; ENSG00000101115.13. [Q9UJQ4-1]
DR   Ensembl; ENST00000395997.3; ENSP00000379319.3; ENSG00000101115.13. [Q9UJQ4-2]
DR   GeneID; 57167; -.
DR   KEGG; hsa:57167; -.
DR   MANE-Select; ENST00000217086.9; ENSP00000217086.4; NM_020436.5; NP_065169.1.
DR   UCSC; uc002xwh.5; human. [Q9UJQ4-1]
DR   AGR; HGNC:15924; -.
DR   CTD; 57167; -.
DR   DisGeNET; 57167; -.
DR   GeneCards; SALL4; -.
DR   GeneReviews; SALL4; -.
DR   HGNC; HGNC:15924; SALL4.
DR   HPA; ENSG00000101115; Tissue enhanced (testis, thyroid gland).
DR   MalaCards; SALL4; -.
DR   MIM; 147750; phenotype.
DR   MIM; 607323; phenotype.
DR   MIM; 607343; gene.
DR   neXtProt; NX_Q9UJQ4; -.
DR   OpenTargets; ENSG00000101115; -.
DR   Orphanet; 959; Acro-renal-ocular syndrome.
DR   Orphanet; 233; Duane retraction syndrome.
DR   Orphanet; 2307; IVIC syndrome.
DR   Orphanet; 261638; Okihiro syndrome due to 20q13 microdeletion.
DR   Orphanet; 261647; Okihiro syndrome due to a point mutation.
DR   PharmGKB; PA34936; -.
DR   VEuPathDB; HostDB:ENSG00000101115; -.
DR   eggNOG; KOG1074; Eukaryota.
DR   GeneTree; ENSGT00940000155384; -.
DR   HOGENOM; CLU_005740_1_0_1; -.
DR   InParanoid; Q9UJQ4; -.
DR   OMA; YGRSSIH; -.
DR   OrthoDB; 2880677at2759; -.
DR   PhylomeDB; Q9UJQ4; -.
DR   TreeFam; TF317003; -.
DR   PathwayCommons; Q9UJQ4; -.
DR   Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
DR   Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
DR   Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR   SignaLink; Q9UJQ4; -.
DR   SIGNOR; Q9UJQ4; -.
DR   BioGRID-ORCS; 57167; 14 hits in 1169 CRISPR screens.
DR   ChiTaRS; SALL4; human.
DR   GeneWiki; SALL4; -.
DR   GenomeRNAi; 57167; -.
DR   Pharos; Q9UJQ4; Tbio.
DR   PRO; PR:Q9UJQ4; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9UJQ4; Protein.
DR   Bgee; ENSG00000101115; Expressed in secondary oocyte and 106 other cell types or tissues.
DR   ExpressionAtlas; Q9UJQ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23233:SF19; SAL-LIKE PROTEIN 4; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; Q9UJQ4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Deafness; Disease variant;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Oncogene;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1053
FT                   /note="Sal-like protein 4"
FT                   /id="PRO_0000047026"
FT   ZN_FING         72..94
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000303|PubMed:16545361"
FT   ZN_FING         382..404
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         410..432
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         566..588
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         594..616
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         626..648
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         870..892
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         898..920
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23012367"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         541
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         776
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         789
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23012367"
FT   MOD_RES         1019
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CROSSLNK        156
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT   CROSSLNK        156
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        175
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        290
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        316
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT   CROSSLNK        316
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        372
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        374
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT   CROSSLNK        374
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        436
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        550
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        597
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        838
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT   CROSSLNK        838
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        896
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        932
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        947
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         385..821
FT                   /note="Missing (in isoform SALL4B)"
FT                   /evidence="ECO:0000303|PubMed:16763212"
FT                   /id="VSP_046525"
FT   VARIANT         507
FT                   /note="L -> R (in dbSNP:rs6126344)"
FT                   /evidence="ECO:0000269|PubMed:12395297"
FT                   /id="VAR_016042"
FT   VARIANT         798
FT                   /note="I -> L (in dbSNP:rs6091375)"
FT                   /evidence="ECO:0000269|PubMed:12395297"
FT                   /id="VAR_016043"
FT   VARIANT         888
FT                   /note="H -> R (in DRRS; dbSNP:rs74315429)"
FT                   /evidence="ECO:0000269|PubMed:16402211"
FT                   /id="VAR_033054"
FT   CONFLICT        130
FT                   /note="K -> E (in Ref. 1; AAO16566)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="M -> I (in Ref. 1; AAO16566)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        865
FT                   /note="R -> G (in Ref. 1; AAO16566)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:5XWR"
FT   TURN            385..387
FT                   /evidence="ECO:0007829|PDB:7Y3M"
FT   HELIX           394..405
FT                   /evidence="ECO:0007829|PDB:7Y3M"
FT   TURN            413..415
FT                   /evidence="ECO:0007829|PDB:7BQV"
FT   STRAND          418..421
FT                   /evidence="ECO:0007829|PDB:7BQV"
FT   HELIX           422..430
FT                   /evidence="ECO:0007829|PDB:7BQV"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:7Y3M"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:7Y3M"
FT   HELIX           446..448
FT                   /evidence="ECO:0007829|PDB:7Y3M"
FT   TURN            873..875
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   STRAND          878..881
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   HELIX           882..893
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   TURN            901..903
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   STRAND          906..909
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   HELIX           910..917
FT                   /evidence="ECO:0007829|PDB:7Y3I"
FT   TURN            918..920
FT                   /evidence="ECO:0007829|PDB:7Y3I"
SQ   SEQUENCE   1053 AA;  112231 MW;  61D0D1F21CB2B337 CRC64;
     MSRRKQAKPQ HINSEEDQGE QQPQQQTPEF ADAAPAAPAA GELGAPVNHP GNDEVASEDE
     ATVKRLRREE THVCEKCCAE FFSISEFLEH KKNCTKNPPV LIMNDSEGPV PSEDFSGAVL
     SHQPTSPGSK DCHRENGGSS EDMKEKPDAE SVVYLKTETA LPPTPQDISY LAKGKVANTN
     VTLQALRGTK VAVNQRSADA LPAPVPGANS IPWVLEQILC LQQQQLQQIQ LTEQIRIQVN
     MWASHALHSS GAGADTLKTL GSHMSQQVSA AVALLSQKAG SQGLSLDALK QAKLPHANIP
     SATSSLSPGL APFTLKPDGT RVLPNVMSRL PSALLPQAPG SVLFQSPFST VALDTSKKGK
     GKPPNISAVD VKPKDEAALY KHKCKYCSKV FGTDSSLQIH LRSHTGERPF VCSVCGHRFT
     TKGNLKVHFH RHPQVKANPQ LFAEFQDKVA AGNGIPYALS VPDPIDEPSL SLDSKPVLVT
     TSVGLPQNLS SGTNPKDLTG GSLPGDLQPG PSPESEGGPT LPGVGPNYNS PRAGGFQGSG
     TPEPGSETLK LQQLVENIDK ATTDPNECLI CHRVLSCQSS LKMHYRTHTG ERPFQCKICG
     RAFSTKGNLK THLGVHRTNT SIKTQHSCPI CQKKFTNAVM LQQHIRMHMG GQIPNTPLPE
     NPCDFTGSEP MTVGENGSTG AICHDDVIES IDVEEVSSQE APSSSSKVPT PLPSIHSASP
     TLGFAMMASL DAPGKVGPAP FNLQRQGSRE NGSVESDGLT NDSSSLMGDQ EYQSRSPDIL
     ETTSFQALSP ANSQAESIKS KSPDAGSKAE SSENSRTEME GRSSLPSTFI RAPPTYVKVE
     VPGTFVGPST LSPGMTPLLA AQPRRQAKQH GCTRCGKNFS SASALQIHER THTGEKPFVC
     NICGRAFTTK GNLKVHYMTH GANNNSARRG RKLAIENTMA LLGTDGKRVS EIFPKEILAP
     SVNVDPVVWN QYTSMLNGGL AVKTNEISVI QSGGVPTLPV SLGATSVVNN ATVSKMDGSQ
     SGISADVEKP SATDGVPKHQ FPHFLEENKI AVS
//