SALL1_HUMAN
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 03-AUG-2022, entry version 184.
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; 71.
DR ELM; Q9NSC2; -.
DR IntAct; Q9NSC2; 26.
DR MINT; Q9NSC2; -.
DR STRING; 9606.ENSP00000251020; -.
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; Q9NSC2; -.
DR PeptideAtlas; Q9NSC2; -.
DR PRIDE; Q9NSC2; -.
DR ProteomicsDB; 82527; -. [Q9NSC2-1]
DR ProteomicsDB; 82528; -. [Q9NSC2-2]
DR Antibodypedia; 28330; 169 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 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; 244207at2759; -.
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; 20 hits in 1090 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 141 other tissues.
DR ExpressionAtlas; Q9NSC2; baseline and differential.
DR Genevisible; Q9NSC2; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
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
