ID ZN462_MOUSE Reviewed; 2495 AA.
AC B1AWL2; A2SW42;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Zinc finger protein 462 {ECO:0000303|PubMed:17207666};
DE AltName: Full=Zinc finger PBX1-interacting protein {ECO:0000303|PubMed:17353115};
DE Short=ZFPIP {ECO:0000303|PubMed:17353115};
GN Name=Znf462 {ECO:0000305}; Synonyms=Zfp462 {ECO:0000312|MGI:MGI:107690};
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] {ECO:0000312|EMBL:ABC79685.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1 {ECO:0000312|EMBL:ABC79685.1};
RC TISSUE=Brain {ECO:0000312|EMBL:ABC79685.1};
RX PubMed=17207666; DOI=10.1016/j.modgep.2006.11.009;
RA Chang Y.S., Stoykova A., Chowdhury K., Gruss P.;
RT "Graded expression of Zfp462 in the embryonic mouse cerebral cortex.";
RL Gene Expr. Patterns 7:405-412(2007).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PBX1 ISOFORM PBX1B, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17353115; DOI=10.1016/j.mod.2007.01.008;
RA Laurent A., Bihan R., Deschamps S., Guerrier D., Dupe V., Omilli F.,
RA Burel A., Pellerin I.;
RT "Identification of a new type of PBX1 partner that contains zinc finger
RT motifs and inhibits the binding of HOXA9-PBX1 to DNA.";
RL Mech. Dev. 124:364-376(2007).
RN [4] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20219459; DOI=10.1016/j.yexcr.2010.02.024;
RA Masse J., Laurent A., Nicol B., Guerrier D., Pellerin I., Deschamps S.;
RT "Involvement of ZFPIP/Zfp462 in chromatin integrity and survival of P19
RT pluripotent cells.";
RL Exp. Cell Res. 316:1190-1201(2010).
RN [6] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21570965; DOI=10.1016/j.yexcr.2011.04.015;
RA Masse J., Piquet-Pellorce C., Viet J., Guerrier D., Pellerin I.,
RA Deschamps S.;
RT "ZFPIP/Zfp462 is involved in P19 cell pluripotency and in their neuronal
RT fate.";
RL Exp. Cell Res. 317:1922-1934(2011).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27621227; DOI=10.1111/gbb.12339;
RA Wang B., Zheng Y., Shi H., Du X., Zhang Y., Wei B., Luo M., Wang H., Wu X.,
RA Hua X., Sun M., Xu X.;
RT "Zfp462 deficiency causes anxiety-like behaviors with excessive self-
RT grooming in mice.";
RL Genes Brain Behav. 16:296-307(2017).
CC -!- FUNCTION: Zinc finger nuclear factor involved in transcription by
CC regulating chromatin structure and organization (PubMed:20219459,
CC PubMed:21570965). Involved in the pluripotency and differentiation of
CC embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG
CC (PubMed:21570965). By binding PBX1, prevents the heterodimerization of
CC PBX1 and HOXA9 and their binding to DNA (PubMed:17353115). Regulates
CC neuronal development and neural cell differentiation (PubMed:21570965,
CC PubMed:27621227). {ECO:0000269|PubMed:17353115,
CC ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965,
CC ECO:0000269|PubMed:27621227}.
CC -!- SUBUNIT: Interacts with PBX1 isoform PBX1b; this interaction prevents
CC PBX1-HOXA9 heterodimer from forming and binding to DNA.
CC {ECO:0000269|PubMed:17353115}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353115,
CC ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex (at protein level)
CC (PubMed:17207666, PubMed:27621227). Expressed in embryonic stem cells
CC (at protein level) (PubMed:20219459). Expressed in heart, liver,
CC kidney, muscle, and female and male genital tracts (at protein level)
CC (PubMed:27621227, PubMed:17353115). {ECO:0000269|PubMed:17207666,
CC ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459,
CC ECO:0000269|PubMed:27621227}.
CC -!- DEVELOPMENTAL STAGE: Detected at 6.5 days post coitum (dpc) in the
CC developing central nervous system (PubMed:17207666). At 7.75 dpc,
CC expression is limited to the headfolds (PubMed:17207666). At 8 dpc,
CC transcripts are detected in the midline neural groove
CC (PubMed:17207666). Between 8 dpc and 9.5 dpc, it is found in the
CC developing forebrain, brainstem, spinal cord, branchial arches, otic
CC vesicles, midbrain and hindbrain folds (PubMed:17207666,
CC PubMed:17353115). At 10.5 dpc, expression is detected in the
CC telencephalic vesicles, branchial arches, otic vesicles, dorsal root
CC ganglia, somites, spinal cord and forelimb buds, specifically in
CC migratory muscle progenitor cells (PubMed:17207666). At 11.5 dpc, it is
CC detected in telencephalic vesicles, midbrain-hindbrain boundary, the
CC spinal cord, branchial arches, dorsal root ganglia, fore- and hindlimb
CC buds and somites (PubMed:17207666, PubMed:17353115). Also detected at
CC 11.5 dpc throughout the wall of the telencephalic vesicle and the
CC medial and lateral ganglionic eminence (PubMed:17353115). At 14.5 dpc,
CC expression is detected in the entire cerebral cortex, with higher
CC levels in the developing hippocampus and septal area (PubMed:17207666).
CC Expression becomes more graded by 16.5 and 18.5 dpc, where it is
CC detected in the caudal and medial cerebral cortex, hippocampus and
CC retrosplenial cortex (PubMed:17207666). Detected at 16.5 dpc in female
CC genital tract (PubMed:17353115). It is also detected in the olfactory
CC bud at 18.5 dpc (PubMed:17207666). Detected at 9.5 dpc in embryos
CC (PubMed:20219459). Detected from 7.5 dpc in the brain, with highest
CC levels of expression being detected at postnatal day 1
CC (PubMed:27621227). Expression remains at high levels at postnatal day 7
CC and begins to decrease by postnatal day 14 (PubMed:27621227).
CC Expression is decreased further by postnatal day 30 (PubMed:27621227).
CC {ECO:0000269|PubMed:17207666, ECO:0000269|PubMed:17353115,
CC ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:27621227}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:27621227). Knockout mice
CC do not develop past 18.5 days post coitum and exhibit smaller sized
CC eyes with neural-tube defects (PubMed:27621227). Heterozygous mice
CC exhibit decreased expression and delayed development (PubMed:27621227).
CC Heterozygous mice grow slower, weigh less than wild-type mice and have
CC significantly reduced brain weight (PubMed:27621227). They also exhibit
CC lowered levels of PBX1 and HOXB8 (PubMed:27621227). Mice also exhibit
CC anxiety-like behaviors with excessive grooming, resulting in gradual
CC hair loss (PubMed:27621227). {ECO:0000269|PubMed:27621227}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ355518; ABC79685.1; -; mRNA.
DR EMBL; AL772186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38764.1; -.
DR RefSeq; NP_766455.2; NM_172867.3.
DR AlphaFoldDB; B1AWL2; -.
DR IntAct; B1AWL2; 4.
DR MINT; B1AWL2; -.
DR STRING; 10090.ENSMUSP00000095677; -.
DR GlyGen; B1AWL2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; B1AWL2; -.
DR PhosphoSitePlus; B1AWL2; -.
DR MaxQB; B1AWL2; -.
DR PaxDb; 10090-ENSMUSP00000095677; -.
DR PeptideAtlas; B1AWL2; -.
DR ProteomicsDB; 345506; -.
DR Pumba; B1AWL2; -.
DR Antibodypedia; 14859; 91 antibodies from 19 providers.
DR DNASU; 242466; -.
DR Ensembl; ENSMUST00000098070.10; ENSMUSP00000095677.4; ENSMUSG00000060206.12.
DR GeneID; 242466; -.
DR KEGG; mmu:242466; -.
DR UCSC; uc008sxi.1; mouse.
DR AGR; MGI:107690; -.
DR CTD; 242466; -.
DR MGI; MGI:107690; Zfp462.
DR VEuPathDB; HostDB:ENSMUSG00000060206; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156411; -.
DR InParanoid; B1AWL2; -.
DR OMA; CAFQSFS; -.
DR PhylomeDB; B1AWL2; -.
DR TreeFam; TF325534; -.
DR BioGRID-ORCS; 242466; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Zfp462; mouse.
DR PRO; PR:B1AWL2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AWL2; Protein.
DR Bgee; ENSMUSG00000060206; Expressed in undifferentiated genital tubercle and 263 other cell types or tissues.
DR ExpressionAtlas; B1AWL2; baseline and differential.
DR Genevisible; B1AWL2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24403:SF58; ZINC FINGER PROTEIN 462; 1.
DR SMART; SM00355; ZnF_C2H2; 34.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2495
FT /note="Zinc finger protein 462"
FT /id="PRO_0000445627"
FT ZN_FING 4..27
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 108..131
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 162..185
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..463
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 471..493
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 593..616
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 835..858
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 878..900
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 917..940
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1023..1046
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1254..1277
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1459..1482
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1504..1527
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1566..1589
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1649..1672
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1686..1709
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1881..1903
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1957..1981
FT /note="C2H2-type 18; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2014..2037
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2043..2066
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2072..2095
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2180..2203
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2209..2232
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2243..2265
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2289..2311
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2317..2340
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2403..2425
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 215..241
FT /note="Interaction with PBX1"
FT /evidence="ECO:0000269|PubMed:17353115"
FT REGION 278..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2112..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2134..2168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 1993
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 2161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT MOD_RES 2166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 978
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 1935
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 2093
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 2282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CROSSLNK 2493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JM2"
FT CONFLICT 167
FT /note="C -> R (in Ref. 1; ABC79685)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> V (in Ref. 1; ABC79685)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="P -> Q (in Ref. 1; ABC79685)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="V -> VPPQPQ (in Ref. 1; ABC79685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2495 AA; 282713 MW; 5291910B790FDA8C CRC64;
MEVLQCDGCD FRAPSYEDLK AHIQDVHTAF LQPTDVAEDN DDEPLSGSMN ASNQTEVEFS
SIKDEFVIAE DLPGQSATAL GSGGYYGHSP GYYGQHITPN PKPTNKFFQC KFCVRYFRSK
NLLIEHTRKV HGAQAEESPT GPPVPGSLNY NIMMHEGFGK VFSCQFCTYK SPRRARIIKH
QKMYHKNSLK ESTAPPPAPA PLPDPLVPPV SLQDPCKELP AEVVERSILE SMVKPLTKSR
GNFCCEWCSY QTPRRERWCD HMMKKHRSMV KILSSIRQQE GPNVSEAQND NEPSPTSNST
YLSMNAASRE MPNANVSNFR GSMGNSIMRP NSSSTSKFSS SMSYPQMKPK SPHNSGLVNL
TERSRYGMSD MTNSSADLDT NSMLNDSSSD EDLNEVDSEN GLSVLDHQAS GLSAEQLMGS
DGNKLLETKG IPFRRFMNRF QCPFCPFLTM HRRSISRHIE NIHLSGKTAV YKCDECPFTC
KSSLKLGAHK QCHTGTSDWD TVNSQSESLS SSLNEGMVSY ESSSINGRKS GVMLDPLQQQ
QPPQPPPPLP PPPPPPSQPL PQPPPPPLQS PHQVPPPTQQ PQPPTQAPPL HPYKCTMCSY
STMTLKGLRV HQQHKHSFCD NLPKFEGQPS SLPLENETDS HPSSSNTVKK SQTSILGLSS
KNNFVAKANR KLASDFPLDL SPVKKRTRID EIASNLQSKI NQTKLQEDAI INVEDDEEEE
DDNEVEIEVE LDREEEATDP IMEVPTAFSA QQIWARDASE AQKEPNYRSI THDYTATNGA
EIELTLSEDE EDYYGSSASM KDQVSNAALL NTQPAIYGTE PSNENTDFGD SGRLYYCKHC
DFNNKSARSV STHYQRMHPY IKFSFRYILD PNDHSAVYRC LECYIDYTNF EDLQQHYGEH
HPEAMNVLNF DHSDLIYRCR FCSYTSPNVR SLMPHYQRMH PTVKINNAMI FSSYVVEQQE
GLNAESQTLR EILNSAPKSM ATSTPVARGG GLPATFNKNT PPKTFTPECE SQKDPSVNTV
VVYDCDVCSF ASPNMHSVLV HYQKKHPEEK ASYFRIQKTM RMVSVDRGSA LSQLSFEVGA
PMSPKMSNMG SPPPPQPPPP DLSIELYYCK HCSYSNRSVV GVLVHYQKRH PEIKVTAKYI
RQAPPTAAMM RGAEGLQDSP RPPAPLQLNS SERDCPPVET EMFFCQHCDY GNRTVKGVLI
HYQKKHRDFK ANADVIRQHT ATIRSLCDRN QKPASCVLLP ASGMERDKTK LRALKCRQCS
YTSPYFYALR KHIKKDHPAL KATVTSIMRW AFLDGLIEAG YHCEWCIYSH MEPSGLLLHY
QRRHPEHYVD YTYMATKLWA GPDPSSPTLT MSAEAKTYRC RDCVFEAVSI WDITNHYQAF
HPWAMNGDES VLLDIIKEKD GVDKALLAPE ELIGPVNCEN SIPNPLPEQE AECPEDARLS
PEKSIHLASA NPAISSTPYQ CTVCQSEYNN LHGLLTHYGK KHPGMKVKAA DFAQDIDINP
GAVYKCRHCP YINTRIHGVL THYQKRHPAI KVTAEDFVHD VEQSADISQN DVEETSRIFK
QGYGAYRCKL CPYTHGTLEK LKIHYEKYHN QPEFDVFSPP PPKLPVSLEP EITTEVSPSQ
VSVTEEEVGE DPMSTAHFST SHLVSHTVFR CQLCKYFCST RKGIARHYRI KHNNVRAQPE
GKNNLFKCAL CAYTNPIRKG LAAHYQKRHD IDAYYTHCLA ASRTISDKPN KVIIPSPPKD
DSPQLSEELR RAVEKKKCSL CSFQSFSKKG IVSHYMKRHP GVFPKKQHAS KLGGYFTAVY
ADEHEKPPLM EEEERSSFER AEVEGEAQDI EWLPFRCIKC FKLSFSTAEL LCMHYTDHHS
RDLKRDFVIL GSGPRFQNST FQCKHCDSKL QSIAELTSHL NIHNEEFQKR AKRQERRKQL
LSKQKYADGA FADFKQERPF GHLEEVPKIK ERKVVGYKCK FCVEVHPTLR AICNHLRKHV
QYGSVPAVSA AVKGLRSHER SHLALAMFTR EDKYSCQYCS FVSAFRHNLD RHMQTHHGHH
KPFRCKLCSF KSSYNSRLKT HILKAHAGEH AYKCSWCSFS TMTISQLKEH SLKVHGKALT
LPRPRIVSLL SSHAHPSSQK ATPAEEVEDS NDSSYSEPPD VQQQLNHYQS AALARNKSRV
SPVPPSGTAA GTEQKAEAVL HCEFCEFSSG YIQSIRRHYR DKHGGKKLFK CKDCSFYTGF
KSAFTMHVEA GHSAVPEEGP KDLRCPLCLY HTKYKRNMID HIVLHREERV VPIEVCRSKL
SKYLQGVVFR CDKCTFTCSS DESLQQHIEK HNELKPYKCQ LCYYETKHTE ELDTHLRDEH
KVSRNFELVG RVNLDQLEQM KEKIESSSSE DEDKDDEMSS KAEDRELMRF ADRGPGVNTE
KRFPCEFCGR AFSQGSEWER HVLRHGMSLH DTNQVSRNEI HTKEMVEESM QLPSIEAKED
DEPIGIDFPL KSETVTICVV AADKSLLEDA EAKNE
//
