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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.
22-NOV-2017, entry version 154.
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. [Q9NSC2-1]
RefSeq; XP_011521556.1; XM_011523254.2. [Q9NSC2-1]
UniGene; Hs.135787; -.
ProteinModelPortal; Q9NSC2; -.
SMR; Q9NSC2; -.
BioGrid; 112206; 20.
ELM; Q9NSC2; -.
IntAct; Q9NSC2; 9.
STRING; 9606.ENSP00000251020; -.
iPTMnet; Q9NSC2; -.
PhosphoSitePlus; Q9NSC2; -.
BioMuta; SALL1; -.
DMDM; 296452895; -.
EPD; Q9NSC2; -.
MaxQB; Q9NSC2; -.
PaxDb; Q9NSC2; -.
PeptideAtlas; Q9NSC2; -.
PRIDE; Q9NSC2; -.
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; ENSGT00550000074555; -.
HOGENOM; HOG000231986; -.
HOVERGEN; HBG058921; -.
InParanoid; Q9NSC2; -.
KO; K19871; -.
OMA; CTKNQLV; -.
OrthoDB; EOG091G00R1; -.
PhylomeDB; Q9NSC2; -.
TreeFam; TF317003; -.
Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
GeneWiki; SALL1; -.
GenomeRNAi; 6299; -.
PRO; PR:Q9NSC2; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103449; -.
CleanEx; HS_SALL1; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific 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:0016575; P:histone deacetylation; IEA:GOC.
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 from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
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 from RNA polymerase II promoter; 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:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
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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