ID   SALL1_HUMAN             Reviewed;        1324 AA.
AC   Q9NSC2; Q99881; Q9NSC3; Q9P1R0;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Sal-like protein 1;
DE   AltName: Full=Spalt-like transcription factor 1;
DE   AltName: Full=Zinc finger protein 794;
DE   AltName: Full=Zinc finger protein SALL1;
DE   AltName: Full=Zinc finger protein Spalt-1;
DE            Short=HSal1;
DE            Short=Sal-1;
GN   Name=SALL1; Synonyms=SAL1, ZNF794;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS SER-150 DEL;
RP   SER-150 INS AND GLY-159, AND INVOLVEMENT IN TBS1.
RX   PubMed=9973281; DOI=10.1086/302238;
RA   Kohlhase J., Taschner P.E.M., Burfeind P., Pasche B., Newman B., Blanck C.,
RA   Breuning M.H., ten Kate L.P., Maaswinkel-Mooy P., Mitulla B., Seidel J.,
RA   Kirkpatrick S.J., Pauli R.M., Wargowski D.S., Devriendt K., Proesmans W.,
RA   Gabrielli O., Coppa G.V., Wesby-van Swaay E., Trembath R.C., Schinzel A.A.,
RA   Reardon W., Seemanova E., Engel W.;
RT   "Molecular analysis of SALL1 mutations in Townes-Brocks syndrome.";
RL   Am. J. Hum. Genet. 64:435-445(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 (ISOFORM 1), INVOLVEMENT IN TBS1,
RP   AND VARIANTS SER-164 DEL AND GLU-1265.
RX   PubMed=10533063;
RX   DOI=10.1002/(sici)1098-1004(199911)14:5<377::aid-humu3>3.0.co;2-a;
RA   Marlin S., Blanchard S., Lacombe D., Denoyelle F., Alessandri J.-L.,
RA   Calzolari E., Drouin-Garraud V., Ferraz F.G., Fourmaintraux A., Philip N.,
RA   Toublanc J.E., Petit C.;
RT   "Townes-Brocks syndrome: detection of a SALL1 mutation hot spot and
RT   evidence for a position effect in one patient.";
RL   Hum. Mutat. 14:377-386(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-1324 (ISOFORM 1).
RX   PubMed=8975705; DOI=10.1006/geno.1996.0631;
RA   Kohlhase J., Schuh R., Dowe G., Kuehnlein R.P., Jaeckle H., Schroeder B.,
RA   Schulz-Schaeffer W., Kretzschmar H.A., Koehler A., Mueller U.,
RA   Raab-Vetter M., Burkhardt E., Engel W., Stick R.;
RT   "Isolation, characterization, and organ-specific expression of two novel
RT   human zinc finger genes related to the Drosophila gene spalt.";
RL   Genomics 38:291-298(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-345 (ISOFORM 1), AND INVOLVEMENT
RP   IN TBS1.
RX   PubMed=9425907; DOI=10.1038/ng0198-81;
RA   Kohlhase J., Wischermann A., Reichenbach H., Froster U., Engel W.;
RT   "Mutations in the SALL1 putative transcription factor gene cause Townes-
RT   Brocks syndrome.";
RL   Nat. Genet. 18:81-83(1998).
RN   [7]
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   [8]
RP   INTERACTION WITH CCNQ.
RX   PubMed=18297069; DOI=10.1038/ng.86;
RA   Unger S., Boehm D., Kaiser F.J., Kaulfuss S., Borozdin W., Buiting K.,
RA   Burfeind P., Boehm J., Barrionuevo F., Craig A., Borowski K.,
RA   Keppler-Noreuil K., Schmitt-Mechelke T., Steiner B., Bartholdi D.,
RA   Lemke J., Mortier G., Sandford R., Zabel B., Superti-Furga A., Kohlhase J.;
RT   "Mutations in the cyclin family member FAM58A cause an X-linked dominant
RT   disorder characterized by syndactyly, telecanthus and anogenital and renal
RT   malformations.";
RL   Nat. Genet. 40:287-289(2008).
RN   [9]
RP   DISEASE.
RX   PubMed=10928856; DOI=10.1136/jmg.37.6.458;
RA   Engels S., Kohlhase J., McGaughran J.;
RT   "A SALL1 mutation causes a branchio-oto-renal syndrome-like phenotype.";
RL   J. Med. Genet. 37:458-460(2000).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593; SER-595; SER-941 AND
RP   SER-943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-439; LYS-947 AND LYS-982, AND
RP   IDENTIFICATION BY MASS 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-439; LYS-673; LYS-690; LYS-701;
RP   LYS-947; LYS-982; LYS-1086; LYS-1219; LYS-1299 AND LYS-1319, 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).
CC   -!- FUNCTION: Transcriptional repressor involved in organogenesis. Plays an
CC       essential role in ureteric bud invasion during kidney development.
CC       {ECO:0000250|UniProtKB:Q9ER74}.
CC   -!- SUBUNIT: May associate with NuRD histone deacetylase complex (HDAC) (By
CC       similarity). Interacts with components of HDAC complex including HDAC1,
CC       HDAC2, RBBP4, RBPP7, MTA1 and MTA2 (By similarity). Interacts with CCNQ
CC       (PubMed:18297069). Interacts with NSD2 (via PHD-type zinc fingers 1, 2
CC       and 3) (By similarity). {ECO:0000250|UniProtKB:Q9ER74,
CC       ECO:0000269|PubMed:18297069}.
CC   -!- INTERACTION:
CC       Q9NSC2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-11317266, EBI-1105153;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ER74}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NSC2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NSC2-2; Sequence=VSP_040502;
CC   -!- TISSUE SPECIFICITY: Highest levels in kidney. Lower levels in adult
CC       brain (enriched in corpus callosum, lower expression in substantia
CC       nigra) and liver.
CC   -!- DEVELOPMENTAL STAGE: In fetal brain exclusively in neurons of the
CC       subependymal region of hypothalamus lateral to the third ventricle.
CC   -!- DISEASE: Townes-Brocks syndrome 1 (TBS1) [MIM:107480]: A form of
CC       Townes-Brocks syndrome, a rare autosomal dominant disease characterized
CC       by the triad of imperforate anus, dysplastic ears, and thumb
CC       malformations. Minor features of the condition include hearing loss,
CC       foot malformations, renal impairment with or without renal
CC       malformations, genitourinary malformations, and congenital heart
CC       disease. {ECO:0000269|PubMed:10533063, ECO:0000269|PubMed:9425907,
CC       ECO:0000269|PubMed:9973281}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry. Some individuals with
CC       SALL1 mutations manifest a phenotype overlapping with TBS1 and
CC       bronchio-oto-renal syndrome. Clinical features include dysplastic ears,
CC       hypoplastic kidneys with impaired renal function, gastroesophageal
CC       reflux, hypermetropia, hypospadias, and mild developmental delay.
CC       Affected individuals lack the characteristic anal or hand malformations
CC       of TBS1. {ECO:0000269|PubMed:10928856}.
CC   -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; Y18265; CAB41400.1; -; mRNA.
DR   EMBL; Y18264; CAB41399.1; -; Genomic_DNA.
DR   EMBL; X98833; CAB41399.1; JOINED; Genomic_DNA.
DR   EMBL; AC009166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK307835; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF017655; AAB99908.1; -; Genomic_DNA.
DR   EMBL; AF074949; AAF19263.1; -; Genomic_DNA.
DR   CCDS; CCDS10747.1; -. [Q9NSC2-1]
DR   CCDS; CCDS45483.1; -. [Q9NSC2-2]
DR   RefSeq; NP_001121364.1; NM_001127892.1. [Q9NSC2-2]
DR   RefSeq; NP_002959.2; NM_002968.2. [Q9NSC2-1]
DR   RefSeq; XP_006721304.1; XM_006721241.3.
DR   RefSeq; XP_011521556.1; XM_011523254.2.
DR   AlphaFoldDB; Q9NSC2; -.
DR   BioGRID; 112206; 91.
DR   ELM; Q9NSC2; -.
DR   IntAct; Q9NSC2; 26.
DR   MINT; Q9NSC2; -.
DR   STRING; 9606.ENSP00000251020; -.
DR   GlyGen; Q9NSC2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NSC2; -.
DR   PhosphoSitePlus; Q9NSC2; -.
DR   BioMuta; SALL1; -.
DR   DMDM; 296452895; -.
DR   EPD; Q9NSC2; -.
DR   jPOST; Q9NSC2; -.
DR   MassIVE; Q9NSC2; -.
DR   MaxQB; Q9NSC2; -.
DR   PaxDb; 9606-ENSP00000251020; -.
DR   PeptideAtlas; Q9NSC2; -.
DR   ProteomicsDB; 82527; -. [Q9NSC2-1]
DR   ProteomicsDB; 82528; -. [Q9NSC2-2]
DR   Pumba; Q9NSC2; -.
DR   Antibodypedia; 28330; 189 antibodies from 26 providers.
DR   DNASU; 6299; -.
DR   Ensembl; ENST00000251020.9; ENSP00000251020.4; ENSG00000103449.13. [Q9NSC2-1]
DR   Ensembl; ENST00000440970.6; ENSP00000407914.2; ENSG00000103449.13. [Q9NSC2-1]
DR   Ensembl; ENST00000570206.2; ENSP00000456777.2; ENSG00000103449.13. [Q9NSC2-2]
DR   Ensembl; ENST00000685868.1; ENSP00000509873.1; ENSG00000103449.13. [Q9NSC2-1]
DR   GeneID; 6299; -.
DR   KEGG; hsa:6299; -.
DR   MANE-Select; ENST00000251020.9; ENSP00000251020.4; NM_002968.3; NP_002959.2.
DR   UCSC; uc059ucr.1; human. [Q9NSC2-1]
DR   AGR; HGNC:10524; -.
DR   CTD; 6299; -.
DR   DisGeNET; 6299; -.
DR   GeneCards; SALL1; -.
DR   GeneReviews; SALL1; -.
DR   HGNC; HGNC:10524; SALL1.
DR   HPA; ENSG00000103449; Tissue enhanced (brain, kidney, liver).
DR   MalaCards; SALL1; -.
DR   MIM; 107480; phenotype.
DR   MIM; 602218; gene.
DR   neXtProt; NX_Q9NSC2; -.
DR   OpenTargets; ENSG00000103449; -.
DR   Orphanet; 857; Townes-Brocks syndrome.
DR   PharmGKB; PA34932; -.
DR   VEuPathDB; HostDB:ENSG00000103449; -.
DR   eggNOG; KOG1074; Eukaryota.
DR   GeneTree; ENSGT00940000155938; -.
DR   InParanoid; Q9NSC2; -.
DR   OMA; QELHKSP; -.
DR   OrthoDB; 2880677at2759; -.
DR   PhylomeDB; Q9NSC2; -.
DR   TreeFam; TF317003; -.
DR   PathwayCommons; Q9NSC2; -.
DR   Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
DR   SignaLink; Q9NSC2; -.
DR   SIGNOR; Q9NSC2; -.
DR   BioGRID-ORCS; 6299; 22 hits in 1173 CRISPR screens.
DR   GeneWiki; SALL1; -.
DR   GenomeRNAi; 6299; -.
DR   Pharos; Q9NSC2; Tbio.
DR   PRO; PR:Q9NSC2; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9NSC2; Protein.
DR   Bgee; ENSG00000103449; Expressed in ventricular zone and 142 other cell types or tissues.
DR   ExpressionAtlas; Q9NSC2; baseline and differential.
DR   GO; GO:0010369; C:chromocenter; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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:0030325; P:adrenal gland development; IEP:UniProtKB.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048566; P:embryonic digestive tract development; IMP:UniProtKB.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
DR   GO; GO:0008406; P:gonad development; IEP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR   GO; GO:0031129; P:inductive cell-cell signaling; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR   GO; GO:0072073; P:kidney epithelium development; ISS:UniProtKB.
DR   GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR   GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IEP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0021889; P:olfactory bulb interneuron differentiation; ISS:UniProtKB.
DR   GO; GO:0061034; P:olfactory bulb mitral cell layer development; IMP:UniProtKB.
DR   GO; GO:0021553; P:olfactory nerve development; ISS:UniProtKB.
DR   GO; GO:0021983; P:pituitary gland development; IEP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR   GO; GO:0072092; P:ureteric bud invasion; ISS:UniProtKB.
DR   GO; GO:0003281; P:ventricular septum development; ISS:UniProtKB.
DR   CDD; cd20908; SUF4-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23233:SF51; SAL-LIKE PROTEIN 1; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
DR   Genevisible; Q9NSC2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Deafness; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1324
FT                   /note="Sal-like protein 1"
FT                   /id="PRO_0000047020"
FT   ZN_FING         43..65
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000303|PubMed:16545361"
FT   ZN_FING         449..471
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         477..499
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         706..728
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         734..756
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         766..788
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1001..1023
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1029..1051
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1134..1156
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1162..1184
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ER74"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         941
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         943
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CROSSLNK        439
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        690
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        701
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:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        982
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1086
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1219
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1299
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1319
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..97
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040502"
FT   VARIANT         150
FT                   /note="S -> SS"
FT                   /evidence="ECO:0000269|PubMed:9973281"
FT                   /id="VAR_013156"
FT   VARIANT         150
FT                   /note="Missing (in dbSNP:rs113614842)"
FT                   /evidence="ECO:0000269|PubMed:9973281"
FT                   /id="VAR_013155"
FT   VARIANT         159
FT                   /note="S -> G (in dbSNP:rs13336129)"
FT                   /evidence="ECO:0000269|PubMed:9973281"
FT                   /id="VAR_013157"
FT   VARIANT         164
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:10533063"
FT                   /id="VAR_013158"
FT   VARIANT         1265
FT                   /note="G -> E (in dbSNP:rs149302006)"
FT                   /evidence="ECO:0000269|PubMed:10533063"
FT                   /id="VAR_013159"
FT   CONFLICT        79
FT                   /note="A -> G (in Ref. 1; CAB41400)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="T -> S (in Ref. 1; CAB41400/CAB41399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1275
FT                   /note="V -> I (in Ref. 1; CAB41400/CAB41399)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1324 AA;  140405 MW;  41AFA91ADEBEEF8C CRC64;
     MSRRKQAKPQ HFQSDPEVAS LPRRDGDTEK GQPSRPTKSK DAHVCGRCCA EFFELSDLLL
     HKKNCTKNQL VLIVNENPAS PPETFSPSPP PDNPDEQMND TVNKTDQVDC SDLSEHNGLD
     REESMEVEAP VANKSGSGTS SGSHSSTAPS SSSSSSSSSG GGGSSSTGTS AITTSLPQLG
     DLTTLGNFSV INSNVIIENL QSTKVAVAQF SQEARCGGAS GGKLAVPALM EQLLALQQQQ
     IHQLQLIEQI RHQILLLASQ NADLPTSSSP SQGTLRTSAN PLSTLSSHLS QQLAAAAGLA
     QSLASQSASI SGVKQLPPIQ LPQSSSGNTI IPSNSGSSPN MNILAAAVTT PSSEKVASSA
     GASHVSNPAV SSSSSPAFAI SSLLSPASNP LLPQQASANS VFPSPLPNIG TTAEDLNSLS
     ALAQQRKSKP PNVTAFEAKS TSDEAFFKHK CRFCAKVFGS DSALQIHLRS HTGERPFKCN
     ICGNRFSTKG NLKVHFQRHK EKYPHIQMNP YPVPEHLDNI PTSTGIPYGM SIPPEKPVTS
     WLDTKPVLPT LTTSVGLPLP PTLPSLIPFI KTEEPAPIPI SHSATSPPGS VKSDSGGPES
     ATRNLGGLPE EAEGSTLPPS GGKSEESGMV TNSVPTASSS VLSSPAADCG PAGSATTFTN
     PLLPLMSEQF KAKFPFGGLL DSAQASETSK LQQLVENIDK KATDPNECII CHRVLSCQSA
     LKMHYRTHTG ERPFKCKICG RAFTTKGNLK THYSVHRAMP PLRVQHSCPI CQKKFTNAVV
     LQQHIRMHMG GQIPNTPVPD SYSESMESDT GSFDEKNFDD LDNFSDENME DCPEGSIPDT
     PKSADASQDS LSSSPLPLEM SSIAALENQM KMINAGLAEQ LQASLKSVEN GSIEGDVLTN
     DSSSVGGDME SQSAGSPAIS ESTSSMQALS PSNSTQEFHK SPSIEEKPQR AVPSEFANGL
     SPTPVNGGAL DLTSSHAEKI IKEDSLGILF PFRDRGKFKN TACDICGKTF ACQSALDIHY
     RSHTKERPFI CTVCNRGFST KGNLKQHMLT HQMRDLPSQL FEPSSNLGPN QNSAVIPANS
     LSSLIKTEVN GFVHVSPQDS KDTPTSHVPS GPLSSSATSP VLLPALPRRT PKQHYCNTCG
     KTFSSSSALQ IHERTHTGEK PFACTICGRA FTTKGNLKVH MGTHMWNSTP ARRGRRLSVD
     GPMTFLGGNP VKFPEMFQKD LAARSGSGDP SSFWNQYAAA LSNGLAMKAN EISVIQNGGI
     PPIPGSLGSG NSSPVSGLTG NLERLQNSEP NAPLAGLEKM ASSENGTNFR FTRFVEDSKE
     IVTS
//