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Sal-like protein 1 (Spalt-like transcription factor 1) (Zinc finger protein 794) (Zinc finger protein SALL1) (Zinc finger protein Spalt-1) (HSal1) (Sal-1)

 SALL1_HUMAN             Reviewed;        1324 AA.
Q9NSC2; Q99881; Q9NSC3; Q9P1R0;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
13-FEB-2019, entry version 166.
RecName: Full=Sal-like protein 1;
AltName: Full=Spalt-like transcription factor 1;
AltName: Full=Zinc finger protein 794;
AltName: Full=Zinc finger protein SALL1;
AltName: Full=Zinc finger protein Spalt-1;
Short=HSal1;
Short=Sal-1;
Name=SALL1; Synonyms=SAL1, ZNF794;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS SER-150
DEL; SER-150 INS AND GLY-159, AND INVOLVEMENT IN TBS1.
PubMed=9973281; DOI=10.1086/302238;
Kohlhase J., Taschner P.E.M., Burfeind P., Pasche B., Newman B.,
Blanck C., Breuning M.H., ten Kate L.P., Maaswinkel-Mooy P.,
Mitulla B., Seidel J., Kirkpatrick S.J., Pauli R.M., Wargowski D.S.,
Devriendt K., Proesmans W., Gabrielli O., Coppa G.V.,
Wesby-van Swaay E., Trembath R.C., Schinzel A.A., Reardon W.,
Seemanova E., Engel W.;
"Molecular analysis of SALL1 mutations in Townes-Brocks syndrome.";
Am. J. Hum. Genet. 64:435-445(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 (ISOFORM 1), INVOLVEMENT IN
TBS1, AND VARIANTS SER-164 DEL AND GLU-1265.
PubMed=10533063;
DOI=10.1002/(SICI)1098-1004(199911)14:5<377::AID-HUMU3>3.0.CO;2-A;
Marlin S., Blanchard S., Lacombe D., Denoyelle F., Alessandri J.-L.,
Calzolari E., Drouin-Garraud V., Ferraz F.G., Fourmaintraux A.,
Philip N., Toublanc J.E., Petit C.;
"Townes-Brocks syndrome: detection of a SALL1 mutation hot spot and
evidence for a position effect in one patient.";
Hum. Mutat. 14:377-386(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-1324 (ISOFORM 1).
PubMed=8975705; DOI=10.1006/geno.1996.0631;
Kohlhase J., Schuh R., Dowe G., Kuehnlein R.P., Jaeckle H.,
Schroeder B., Schulz-Schaeffer W., Kretzschmar H.A., Koehler A.,
Mueller U., Raab-Vetter M., Burkhardt E., Engel W., Stick R.;
"Isolation, characterization, and organ-specific expression of two
novel human zinc finger genes related to the Drosophila gene spalt.";
Genomics 38:291-298(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-345 (ISOFORM 1), AND
INVOLVEMENT IN TBS1.
PubMed=9425907; DOI=10.1038/ng0198-81;
Kohlhase J., Wischermann A., Reichenbach H., Froster U., Engel W.;
"Mutations in the SALL1 putative transcription factor gene cause
Townes-Brocks syndrome.";
Nat. Genet. 18:81-83(1998).
[7]
INTERACTION WITH CCNQ.
PubMed=18297069; DOI=10.1038/ng.86;
Unger S., Boehm D., Kaiser F.J., Kaulfuss S., Borozdin W., Buiting K.,
Burfeind P., Boehm J., Barrionuevo F., Craig A., Borowski K.,
Keppler-Noreuil K., Schmitt-Mechelke T., Steiner B., Bartholdi D.,
Lemke J., Mortier G., Sandford R., Zabel B., Superti-Furga A.,
Kohlhase J.;
"Mutations in the cyclin family member FAM58A cause an X-linked
dominant disorder characterized by syndactyly, telecanthus and
anogenital and renal malformations.";
Nat. Genet. 40:287-289(2008).
[8]
DISEASE.
PubMed=10928856; DOI=10.1136/jmg.37.6.458;
Engels S., Kohlhase J., McGaughran J.;
"A SALL1 mutation causes a branchio-oto-renal syndrome-like
phenotype.";
J. Med. Genet. 37:458-460(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593; SER-595; SER-941
AND SER-943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-439; LYS-947 AND LYS-982,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-439; LYS-673; LYS-690;
LYS-701; LYS-947; LYS-982; LYS-1086; LYS-1219; LYS-1299 AND LYS-1319,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcriptional repressor involved in organogenesis.
{ECO:0000250}.
-!- SUBUNIT: Interacts with HDAC1, HDAC2, RBBP4, RBPP7, MTA1 and MTA2
(By similarity). Interacts with CCNQ. Probably associates with
NuRD histone deacetylase complex (HDAC). {ECO:0000250,
ECO:0000269|PubMed:18297069}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NSC2-1; Sequence=Displayed;
Name=2;
IsoId=Q9NSC2-2; Sequence=VSP_040502;
-!- TISSUE SPECIFICITY: Highest levels in kidney. Lower levels in
adult brain (enriched in corpus callosum, lower expression in
substantia nigra) and liver.
-!- DEVELOPMENTAL STAGE: In fetal brain exclusively in neurons of the
subependymal region of hypothalamus lateral to the third
ventricle.
-!- DISEASE: Townes-Brocks syndrome 1 (TBS1) [MIM:107480]: A form of
Townes-Brocks syndrome, a rare autosomal dominant disease
characterized by the triad of imperforate anus, dysplastic ears,
and thumb malformations. Minor features of the condition include
hearing loss, foot malformations, renal impairment with or without
renal malformations, genitourinary malformations, and congenital
heart disease. {ECO:0000269|PubMed:10533063,
ECO:0000269|PubMed:9425907, ECO:0000269|PubMed:9973281}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. Some individuals with SALL1 mutations manifest a
phenotype overlapping with TBS1 and bronchio-oto-renal syndrome.
Clinical features include dysplastic ears, hypoplastic kidneys
with impaired renal function, gastroesophageal reflux,
hypermetropia, hypospadias, and mild developmental delay. Affected
individuals lack the characteristic anal or hand malformations of
TBS1. {ECO:0000269|PubMed:10928856}.
-!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; Y18265; CAB41400.1; -; mRNA.
EMBL; Y18264; CAB41399.1; -; Genomic_DNA.
EMBL; X98833; CAB41399.1; JOINED; Genomic_DNA.
EMBL; AC009166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK307835; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF017655; AAB99908.1; -; Genomic_DNA.
EMBL; AF074949; AAF19263.1; -; Genomic_DNA.
CCDS; CCDS10747.1; -. [Q9NSC2-1]
CCDS; CCDS45483.1; -. [Q9NSC2-2]
RefSeq; NP_001121364.1; NM_001127892.1. [Q9NSC2-2]
RefSeq; NP_002959.2; NM_002968.2. [Q9NSC2-1]
RefSeq; XP_006721304.1; XM_006721241.3.
RefSeq; XP_011521556.1; XM_011523254.2.
UniGene; Hs.135787; -.
ProteinModelPortal; Q9NSC2; -.
SMR; Q9NSC2; -.
BioGrid; 112206; 20.
ELM; Q9NSC2; -.
IntAct; Q9NSC2; 10.
MINT; Q9NSC2; -.
STRING; 9606.ENSP00000251020; -.
iPTMnet; Q9NSC2; -.
PhosphoSitePlus; Q9NSC2; -.
BioMuta; SALL1; -.
DMDM; 296452895; -.
EPD; Q9NSC2; -.
jPOST; Q9NSC2; -.
MaxQB; Q9NSC2; -.
PaxDb; Q9NSC2; -.
PeptideAtlas; Q9NSC2; -.
PRIDE; Q9NSC2; -.
ProteomicsDB; 82527; -.
ProteomicsDB; 82528; -. [Q9NSC2-2]
DNASU; 6299; -.
Ensembl; ENST00000251020; ENSP00000251020; ENSG00000103449. [Q9NSC2-1]
Ensembl; ENST00000440970; ENSP00000407914; ENSG00000103449. [Q9NSC2-2]
GeneID; 6299; -.
KEGG; hsa:6299; -.
UCSC; uc059ucr.1; human. [Q9NSC2-1]
CTD; 6299; -.
DisGeNET; 6299; -.
EuPathDB; HostDB:ENSG00000103449.11; -.
GeneCards; SALL1; -.
GeneReviews; SALL1; -.
HGNC; HGNC:10524; SALL1.
HPA; HPA049829; -.
MalaCards; SALL1; -.
MIM; 107480; phenotype.
MIM; 602218; gene.
neXtProt; NX_Q9NSC2; -.
OpenTargets; ENSG00000103449; -.
Orphanet; 857; Townes-Brocks syndrome.
PharmGKB; PA34932; -.
eggNOG; KOG1074; Eukaryota.
eggNOG; ENOG410ZE3Z; LUCA.
GeneTree; ENSGT00940000155938; -.
HOGENOM; HOG000231986; -.
HOVERGEN; HBG058921; -.
InParanoid; Q9NSC2; -.
KO; K19871; -.
OMA; EKGQPNR; -.
OrthoDB; 244207at2759; -.
PhylomeDB; Q9NSC2; -.
TreeFam; TF317003; -.
Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
SIGNOR; Q9NSC2; -.
GeneWiki; SALL1; -.
GenomeRNAi; 6299; -.
PRO; PR:Q9NSC2; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103449; Expressed in 144 organ(s), highest expression level in metanephros.
ExpressionAtlas; Q9NSC2; baseline and differential.
Genevisible; Q9NSC2; HS.
GO; GO:0010369; C:chromocenter; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEP:UniProtKB.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0048566; P:embryonic digestive tract development; IMP:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
GO; GO:0008406; P:gonad development; IEP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0031129; P:inductive cell-cell signaling; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; IMP:UniProtKB.
GO; GO:0072073; P:kidney epithelium development; ISS:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IEP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0021889; P:olfactory bulb interneuron differentiation; ISS:UniProtKB.
GO; GO:0061034; P:olfactory bulb mitral cell layer development; IMP:UniProtKB.
GO; GO:0021553; P:olfactory nerve development; ISS:UniProtKB.
GO; GO:0042473; P:outer ear morphogenesis; IMP:UniProtKB.
GO; GO:0021983; P:pituitary gland development; IEP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
GO; GO:0072092; P:ureteric bud invasion; ISS:UniProtKB.
GO; GO:0003281; P:ventricular septum development; ISS:UniProtKB.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 6.
SMART; SM00355; ZnF_C2H2; 9.
SUPFAM; SSF57667; SSF57667; 5.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Deafness; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1324 Sal-like protein 1.
/FTId=PRO_0000047020.
ZN_FING 449 471 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 477 499 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 706 728 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 734 756 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 766 788 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1001 1023 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1029 1051 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1134 1156 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1162 1184 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 150 159 Poly-Ser.
COMPBIAS 160 163 Poly-Gly.
COMPBIAS 237 240 Poly-Gln.
COMPBIAS 294 297 Poly-Ala.
COMPBIAS 371 375 Poly-Ser.
COMPBIAS 1144 1147 Poly-Ser.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ER74}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 943 943 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 673 673 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 690 690 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 701 701 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 947 947 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 982 982 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1086 1086 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1219 1219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1299 1299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1319 1319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 97 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040502.
VARIANT 150 150 S -> SS. {ECO:0000269|PubMed:9973281}.
/FTId=VAR_013156.
VARIANT 150 150 Missing. {ECO:0000269|PubMed:9973281}.
/FTId=VAR_013155.
VARIANT 159 159 S -> G (in dbSNP:rs13336129).
{ECO:0000269|PubMed:9973281}.
/FTId=VAR_013157.
VARIANT 164 164 Missing. {ECO:0000269|PubMed:10533063}.
/FTId=VAR_013158.
VARIANT 1265 1265 G -> E (in dbSNP:rs149302006).
{ECO:0000269|PubMed:10533063}.
/FTId=VAR_013159.
CONFLICT 79 79 A -> G (in Ref. 1; CAB41400).
{ECO:0000305}.
CONFLICT 562 562 T -> S (in Ref. 1; CAB41400/CAB41399).
{ECO:0000305}.
CONFLICT 1275 1275 V -> I (in Ref. 1; CAB41400/CAB41399).
{ECO:0000305}.
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


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EIAAB37220 Homo sapiens,hSal2,Human,KIAA0360,SAL2,Sal-2,SALL2,Sal-like protein 2,Zinc finger protein 795,Zinc finger protein SALL2,Zinc finger protein Spalt-2,ZNF795
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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[SALL1 SAL1 ZNF794] Sal-like protein 1 (Spalt-like transcription factor 1) (Zinc finger protein 794) (Zinc finger protein SALL1) (Zinc finger protein Spalt-1) (HSal1) (Sal-1)
[SALL2 KIAA0360 SAL2 ZNF795] Sal-like protein 2 (Zinc finger protein 795) (Zinc finger protein SALL2) (Zinc finger protein Spalt-2) (Sal-2) (hSal2)
[Sall2 Sal2] Sal-like protein 2 (Spalt-like protein 2) (Zinc finger protein Spalt-2) (Sal-2) (mSal-2)
[SALL4 ZNF797] Sal-like protein 4 (Zinc finger protein 797) (Zinc finger protein SALL4)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[EGR1 KROX24 ZNF225] Early growth response protein 1 (EGR-1) (AT225) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor ETR103) (Transcription factor Zif268) (Zinc finger protein 225) (Zinc finger protein Krox-24)
[ZBTB17 MIZ1 ZNF151 ZNF60] Zinc finger and BTB domain-containing protein 17 (Myc-interacting zinc finger protein 1) (Miz-1) (Zinc finger protein 151) (Zinc finger protein 60)
[Znf423 Ebfaz Kiaa0760 Nur12 Oaz Zfp423] Zinc finger protein 423 (Early B-cell factor-associated zinc finger protein) (Olf1/EBF-associated zinc finger protein) (Smad- and Olf-interacting zinc finger protein)
[ZFHX3 ATBF1] Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3)
[Zfhx3 Atbf1] Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3)
[ZBTB18 RP58 TAZ1 ZNF238] Zinc finger and BTB domain-containing protein 18 (58 kDa repressor protein) (Transcriptional repressor RP58) (Translin-associated zinc finger protein 1) (TAZ-1) (Zinc finger protein 238) (Zinc finger protein C2H2-171)
[ZEB1 AREB6 TCF8] Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8)
[ZFPM1 FOG1 ZFN89A] Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein 89A) (Zinc finger protein multitype 1)
[ZBTB7B ZBTB15 ZFP67 ZNF857B] Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (hcKrox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger and BTB domain-containing protein 15) (Zinc finger protein 67 homolog) (Zfp-67) (Zinc finger protein 857B) (Zinc finger protein Th-POK)
[Zbtb17 Zfp100 Znf151] Zinc finger and BTB domain-containing protein 17 (LP-1) (Polyomavirus late initiator promoter-binding protein) (Zinc finger protein 100) (Zfp-100) (Zinc finger protein 151) (Zinc finger protein Z13)
[Zbtb7b Thpok Zfp67] Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (c-Krox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger protein 67) (Zfp-67) (Zinc finger protein Th-POK)
[ZIC1 ZIC ZNF201] Zinc finger protein ZIC 1 (Zinc finger protein 201) (Zinc finger protein of the cerebellum 1)
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)
[Zfpm1 Fog Fog1] Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein multitype 1)
[Zkscan3 Skz1 Zfp306 Zfp307 Zfp47] Zinc finger protein with KRAB and SCAN domains 3 (SCAN-KRAB-zinc finger protein) (Zinc finger protein 306) (Zinc finger protein 307) (Zinc finger protein 47 homolog) (Zf47) (Zfp-47)
[ZKSCAN3 ZFP47 ZNF306 ZNF309 ZSCAN13] Zinc finger protein with KRAB and SCAN domains 3 (Zinc finger and SCAN domain-containing protein 13) (Zinc finger protein 306) (Zinc finger protein 309) (Zinc finger protein 47 homolog) (Zf47) (Zfp-47)
[ZNF274 ZKSCAN19 SP2114] Neurotrophin receptor-interacting factor homolog (Zinc finger protein 274) (Zinc finger protein HFB101) (Zinc finger protein with KRAB and SCAN domains 19) (Zinc finger protein zfp2) (Zf2)
[ZNF423 KIAA0760 NPHP14 OAZ] Zinc finger protein 423 (Olf1/EBF-associated zinc finger protein) (hOAZ) (Smad- and Olf-interacting zinc finger protein)
[DPF2 BAF45D REQ UBID4] Zinc finger protein ubi-d4 (Apoptosis response zinc finger protein) (BRG1-associated factor 45D) (BAF45D) (D4, zinc and double PHD fingers family 2) (Protein requiem)
[RC3H1 KIAA2025 RNF198] Roquin-1 (Roquin) (EC 2.3.2.27) (RING finger and C3H zinc finger protein 1) (RING finger and CCCH-type zinc finger domain-containing protein 1) (RING finger protein 198)
[CIZ1 LSFR1 NP94 ZNF356] Cip1-interacting zinc finger protein (CDKN1A-interacting zinc finger protein 1) (Nuclear protein NP94) (Zinc finger protein 356)
[ZC3HAV1 ZC3HDC2 PRO1677] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)
[ZBTB16 PLZF ZNF145] Zinc finger and BTB domain-containing protein 16 (Promyelocytic leukemia zinc finger protein) (Zinc finger protein 145) (Zinc finger protein PLZF)
[Dpf3 Baf45c Cerd4] Zinc finger protein DPF3 (BRG1-associated factor 45C) (BAF45C) (Zinc finger protein cer-d4)
[Rc3h1 Gm551 Kiaa2025] Roquin-1 (Roquin) (EC 2.3.2.27) (Protein Sanroque) (RING finger and C3H zinc finger protein 1) (RING finger and CCCH-type zinc finger domain-containing protein 1)

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