SALL4_HUMAN
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 03-AUG-2022, entry version 188.
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 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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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). {ECO:0000250|UniProtKB:Q8BX22,
CC ECO:0000269|PubMed:21914818, 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}.
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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 PDBsum; 5XWR; -.
DR PDBsum; 6UML; -.
DR PDBsum; 7BQU; -.
DR PDBsum; 7BQV; -.
DR AlphaFoldDB; Q9UJQ4; -.
DR SMR; Q9UJQ4; -.
DR BioGRID; 121420; 24.
DR IntAct; Q9UJQ4; 2.
DR MINT; Q9UJQ4; -.
DR STRING; 9606.ENSP00000217086; -.
DR GlyGen; Q9UJQ4; 1 site, 1 O-linked glycan (1 site).
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; Q9UJQ4; -.
DR PeptideAtlas; Q9UJQ4; -.
DR PRIDE; Q9UJQ4; -.
DR ProteomicsDB; 190; -.
DR ProteomicsDB; 84639; -. [Q9UJQ4-1]
DR ABCD; Q9UJQ4; 1 sequenced antibody.
DR Antibodypedia; 13868; 302 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 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; 244207at2759; -.
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; 12 hits in 1090 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 105 other tissues.
DR ExpressionAtlas; Q9UJQ4; baseline and differential.
DR Genevisible; Q9UJQ4; HS.
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:0032991; C:protein-containing complex; IEA:Ensembl.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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 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"
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
