ID   SALL4_MOUSE             Reviewed;        1067 AA.
AC   Q8BX22; A2AV00; Q6S7E8; Q6S7E9; Q7TST6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=Sal-like protein 4;
DE   AltName: Full=Zinc finger protein SALL4;
GN   Name=Sall4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA   Ma Y., Di C., Kang Q., Lai R., Theus J., Chai L.;
RT   "Characterization of the murine Okihiro syndrome gene (Sall4): sequence,
RT   expression and alternative splicing.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-958.
RC   STRAIN=129/Sv;
RA   Kohlhase J., Kispert A., Heinrich M.;
RT   "Cloning and expression of Sall4.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH NANOG.
RX   PubMed=16840789; DOI=10.1074/jbc.c600122200;
RA   Wu Q., Chen X., Zhang J., Loh Y.-H., Low T.-Y., Zhang W., Zhang W.,
RA   Sze S.-K., Lim B., Ng H.-H.;
RT   "Sall4 interacts with Nanog and co-occupies Nanog genomic sites in
RT   embryonic stem cells.";
RL   J. Biol. Chem. 281:24090-24094(2006).
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 NSD2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=19483677; DOI=10.1038/nature08086;
RA   Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J.,
RA   Kaneda Y.;
RT   "A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-
RT   Hirschhorn syndrome.";
RL   Nature 460:287-291(2009).
RN   [9]
RP   INTERACTION WITH NRBP1.
RX   PubMed=22510880; DOI=10.1038/emboj.2012.91;
RA   Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G.,
RA   Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E.,
RA   Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.;
RT   "Nuclear receptor binding protein 1 regulates intestinal progenitor cell
RT   homeostasis and tumour formation.";
RL   EMBO J. 31:2486-2497(2012).
CC   -!- FUNCTION: Transcription factor with a key role in the maintenance and
CC       self-renewal of embryonic and hematopoietic stem cells. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with POU5F1/OCT4 (By similarity). Interacts with
CC       NANOG (PubMed:16840789). Interacts with BEND3 (By similarity).
CC       Interacts with NSD2 (via PHD-type zinc fingers 1, 2 and 3)
CC       (PubMed:19483677). Interacts with NRBP1 (PubMed:22510880).
CC       {ECO:0000250|UniProtKB:Q9UJQ4, ECO:0000269|PubMed:16840789,
CC       ECO:0000269|PubMed:19483677, ECO:0000269|PubMed:22510880}.
CC   -!- INTERACTION:
CC       Q8BX22; Q9R190: Mta2; NbExp=3; IntAct=EBI-2312582, EBI-904134;
CC       Q8BX22; Q7TSZ8: Nacc1; NbExp=4; IntAct=EBI-2312582, EBI-5691985;
CC       Q8BX22; Q8BVE8-2: Nsd2; NbExp=3; IntAct=EBI-2312582, EBI-11518042;
CC       Q8BX22; O70230: Znf143; NbExp=2; IntAct=EBI-2312582, EBI-5691478;
CC       Q8BX22; Q9UHY1: NRBP1; Xeno; NbExp=2; IntAct=EBI-2312582, EBI-749731;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000269|PubMed:19483677}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Sall4a;
CC         IsoId=Q8BX22-1; Sequence=Displayed;
CC       Name=2; Synonyms=Sall4b;
CC         IsoId=Q8BX22-2; Sequence=VSP_021687;
CC       Name=3; Synonyms=Sall4c;
CC         IsoId=Q8BX22-3; Sequence=VSP_021686;
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryonic heart (at protein
CC       level). {ECO:0000269|PubMed:19483677}.
CC   -!- PTM: Sumoylation with both SUMO1 and SUMO2 regulates the stability,
CC       subcellular localization, transcriptional activity, and may reduce
CC       interaction with POU5F1/OCT4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AY463371; AAR91796.1; -; mRNA.
DR   EMBL; AY463372; AAR91797.1; -; mRNA.
DR   EMBL; AY463373; AAR91798.1; -; mRNA.
DR   EMBL; AK049188; BAC33598.1; -; mRNA.
DR   EMBL; AL929248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466551; EDL06559.1; -; Genomic_DNA.
DR   EMBL; AJ488904; CAD32912.1; -; Genomic_DNA.
DR   CCDS; CCDS17115.1; -. [Q8BX22-1]
DR   CCDS; CCDS17116.1; -. [Q8BX22-2]
DR   CCDS; CCDS17117.1; -. [Q8BX22-3]
DR   RefSeq; NP_780512.2; NM_175303.4. [Q8BX22-1]
DR   RefSeq; NP_958797.2; NM_201395.3. [Q8BX22-2]
DR   RefSeq; NP_958798.2; NM_201396.3. [Q8BX22-3]
DR   PDB; 8A4I; X-ray; 2.76 A; I/J/K/L=871-940.
DR   PDBsum; 8A4I; -.
DR   AlphaFoldDB; Q8BX22; -.
DR   SASBDB; Q8BX22; -.
DR   SMR; Q8BX22; -.
DR   BioGRID; 221236; 72.
DR   DIP; DIP-29926N; -.
DR   IntAct; Q8BX22; 46.
DR   MINT; Q8BX22; -.
DR   STRING; 10090.ENSMUSP00000029061; -.
DR   GlyGen; Q8BX22; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q8BX22; -.
DR   PhosphoSitePlus; Q8BX22; -.
DR   MaxQB; Q8BX22; -.
DR   PaxDb; 10090-ENSMUSP00000029061; -.
DR   PeptideAtlas; Q8BX22; -.
DR   ProteomicsDB; 256691; -. [Q8BX22-1]
DR   ProteomicsDB; 256692; -. [Q8BX22-2]
DR   ProteomicsDB; 256693; -. [Q8BX22-3]
DR   Antibodypedia; 13868; 368 antibodies from 41 providers.
DR   DNASU; 99377; -.
DR   Ensembl; ENSMUST00000029061.12; ENSMUSP00000029061.6; ENSMUSG00000027547.18. [Q8BX22-1]
DR   Ensembl; ENSMUST00000075044.10; ENSMUSP00000074556.4; ENSMUSG00000027547.18. [Q8BX22-3]
DR   Ensembl; ENSMUST00000103074.2; ENSMUSP00000099363.2; ENSMUSG00000027547.18. [Q8BX22-2]
DR   GeneID; 99377; -.
DR   KEGG; mmu:99377; -.
DR   UCSC; uc008obf.1; mouse. [Q8BX22-1]
DR   UCSC; uc008obg.1; mouse. [Q8BX22-2]
DR   UCSC; uc008obh.1; mouse. [Q8BX22-3]
DR   AGR; MGI:2139360; -.
DR   CTD; 57167; -.
DR   MGI; MGI:2139360; Sall4.
DR   VEuPathDB; HostDB:ENSMUSG00000027547; -.
DR   eggNOG; KOG1074; Eukaryota.
DR   GeneTree; ENSGT00940000155384; -.
DR   HOGENOM; CLU_087959_0_0_1; -.
DR   InParanoid; Q8BX22; -.
DR   OMA; YGRSSIH; -.
DR   OrthoDB; 2880677at2759; -.
DR   PhylomeDB; Q8BX22; -.
DR   TreeFam; TF317003; -.
DR   Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR   BioGRID-ORCS; 99377; 4 hits in 62 CRISPR screens.
DR   PRO; PR:Q8BX22; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BX22; Protein.
DR   Bgee; ENSMUSG00000027547; Expressed in primitive streak and 122 other cell types or tissues.
DR   ExpressionAtlas; Q8BX22; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   GO; GO:0009888; P:tissue development; IMP:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23233:SF19; SAL-LIKE PROTEIN 4; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; Q8BX22; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW   Isopeptide bond; Metal-binding; Nucleus; Oncogene; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1067
FT                   /note="Sal-like protein 4"
FT                   /id="PRO_0000261416"
FT   ZN_FING         68..90
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000303|PubMed:16545361"
FT   ZN_FING         387..409
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         415..437
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         573..595
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         601..623
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         633..655
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         880..902
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         908..930
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   MOD_RES         785
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   MOD_RES         1029
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        170
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        291
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        377
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        379
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        379
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        441
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        557
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        604
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        630
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        846
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        846
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        906
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        942
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   CROSSLNK        957
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT   VAR_SEQ         40..828
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_021686"
FT   VAR_SEQ         386..829
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_021687"
FT   CONFLICT        865
FT                   /note="P -> H (in Ref. 1; AAR91797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        950
FT                   /note="A -> V (in Ref. 1; AAR91797 and 5; CAD32912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        969
FT                   /note="S -> Y (in Ref. 1; AAR91796/AAR91798 and 2;
FT                   BAC33598)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        997
FT                   /note="I -> T (in Ref. 1; AAR91797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1022
FT                   /note="T -> M (in Ref. 1; AAR91797)"
FT                   /evidence="ECO:0000305"
FT   STRAND          883..885
FT                   /evidence="ECO:0007829|PDB:8A4I"
FT   STRAND          889..891
FT                   /evidence="ECO:0007829|PDB:8A4I"
FT   HELIX           892..903
FT                   /evidence="ECO:0007829|PDB:8A4I"
FT   STRAND          911..913
FT                   /evidence="ECO:0007829|PDB:8A4I"
FT   STRAND          916..919
FT                   /evidence="ECO:0007829|PDB:8A4I"
FT   HELIX           920..931
FT                   /evidence="ECO:0007829|PDB:8A4I"
SQ   SEQUENCE   1067 AA;  113110 MW;  23B92F488AAF53E5 CRC64;
     MSRRKQAKPQ HINWEEGQGE QPQQLPSPDL AEALAAEEPG APVNSPGNCD EASEDSIPVK
     RPRREDTHIC NKCCAEFFSL SEFMEHKKSC TKTPPVLIMN DSEGPVPSED FSRAALSHQL
     GSPSNKDSLQ ENGSSSGDLK KLGTDSILYL KTEATQPSTP QDISYLPKGK VANTNVTLQA
     LRGTKVAVNQ RGAEAPMAPM PAAQGIPWVL EQILCLQQQQ LQQIQLTEQI RVQVNMWAAH
     ALHSGVAGAD TLKALSSHVS QQVSVSQQVS AAVALLSQKA SNPALSLDAL KQAKLPHASV
     PSAASPLSSG LTSFTLKPDG TRVLPNFVSR LPSALLPQTP GSVLLQSPFS AVTLDQSKKG
     KGKPQNLSAS ASVLDVKAKD EVVLGKHKCR YCPKVFGTDS SLQIHLRSHT GERPYVCPIC
     GHRFTTKGNL KVHLQRHPEV KANPQLLAEF QDKGAVSAAS HYALPVPVPA DESSLSVDAE
     PVPVTGTPSL GLPQKLTSGP NSRDLMGGSL PNDMQPGPSP ESEAGLPLLG VGMIHNPPKA
     GGFQGTGAPE SGSETLKLQQ LVENIDKATT DPNECLICHR VLSCQSSLKM HYRTHTGERP
     FQCKICGRAF STKGNLKTHL GVHRTNTTVK TQHSCPICQK KFTNAVMLQQ HIRMHMGGQI
     PNTPLPESPC DFTAPEPVAV SENGSASGVC QDDAAEGMEA EEVCSQDVPS GPSTVSLPVP
     SAHLASPSLG FSVLASLDTQ GKGALPALAL QRQSSRENSS LEGGDTGPAN DSSLLVGDQE
     CQSRSPDATE TMCYQAVSPA NSQAGSVKSR SPEGHKAEGV ESCRVDTEGR TSLPPTFIRA
     QPTFVKVEVP GTFVGPPSMP SGMPPLLASQ PQPRRQAKQH CCTRCGKNFS SASALQIHER
     THTGEKPFVC NICGRAFTTK GNLKVHYMTH GANNNSARRG RKLAIENPMA ALSAEGKRAP
     EVFSKELLSP AVSVDPASWN QYTSVLNGGL AMKTNEISVI QSGGIPTLPV SLGASSVVSN
     GTISKLDGSQ TGVSMPMSGN GEKLAVPDGM AKHQFPHFLE ENKIAVS
//