PIAS2_MOUSE
ID PIAS2_MOUSE Reviewed; 621 AA.
AC Q8C5D8; O54987; Q8C384; Q8CDQ8; Q8K208; Q99JX5; Q9D5W7; Q9QZ63;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=E3 SUMO-protein ligase PIAS2;
DE EC=2.3.2.27;
DE AltName: Full=Androgen receptor-interacting protein 3;
DE Short=ARIP3;
DE AltName: Full=DAB2-interacting protein;
DE Short=DIP;
DE AltName: Full=Msx-interacting zinc finger protein;
DE AltName: Full=Protein inhibitor of activated STAT x;
DE AltName: Full=Protein inhibitor of activated STAT2;
DE AltName: Full=RING-type E3 ubiquitin transferase PIAS2 {ECO:0000305};
GN Name=Pias2; Synonyms=Miz1, Piasx;
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] (ISOFORM 2), AND INTERACTION WITH DAB2.
RC STRAIN=129; TISSUE=Teratocarcinoma;
RX PubMed=11104669; DOI=10.1042/bj3520645;
RA Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.;
RT "p67 isoform of mouse disabled 2 protein acts as a transcriptional
RT activator during the differentiation of F9 cells.";
RL Biochem. J. 352:645-650(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung, and Testis;
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 MRNA] (ISOFORMS 3 AND 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-621 (ISOFORM 1), AND INTERACTION WITH
RP MSX2.
RC TISSUE=Embryo;
RX PubMed=9256341; DOI=10.1016/s0925-4773(97)00032-4;
RA Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.;
RT "Miz1, a novel zinc finger transcription factor that interacts with Msx2
RT and enhances its affinity for DNA.";
RL Mech. Dev. 65:3-17(1997).
RN [5]
RP ERRATUM OF PUBMED:9256341.
RA Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.;
RL Mech. Dev. 69:219-219(1997).
RN [6]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH
RP GTF2I AND GTF2IRD1.
RX PubMed=12193603; DOI=10.1074/jbc.m207635200;
RA Tussie-Luna M.I., Michel B., Hakre S., Roy A.L.;
RT "The SUMO ubiquitin-protein isopeptide ligase family member
RT Miz1/PIASxbeta/Siz2 is a transcriptional cofactor for TFII-I.";
RL J. Biol. Chem. 277:43185-43193(2002).
RN [7]
RP INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, AND SUMOYLATION.
RX PubMed=12077349; DOI=10.1128/mcb.22.14.5222-5234.2002;
RA Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.;
RT "PIAS proteins modulate transcription factors by functioning as SUMO-1
RT ligases.";
RL Mol. Cell. Biol. 22:5222-5234(2002).
RN [8]
RP INTERACTION WITH IKFZ1.
RX PubMed=15767674; DOI=10.1128/mcb.25.7.2688-2697.2005;
RA Gomez-del Arco P., Koipally J., Georgopoulos K.;
RT "Ikaros SUMOylation: switching out of repression.";
RL Mol. Cell. Biol. 25:2688-2697(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO)
CC ligase, stabilizing the interaction between UBE2I and the substrate,
CC and as a SUMO-tethering factor. Plays a crucial role as a
CC transcriptional coregulation in various cellular pathways, including
CC the STAT pathway, the p53 pathway and the steroid hormone signaling
CC pathway. The effects of this transcriptional coregulation,
CC transactivation or silencing may vary depending upon the biological
CC context and PIAS2 isoform studied. However, it seems to be mostly
CC involved in gene silencing. Binds to sumoylated ELK1 and enhances its
CC transcriptional activity by preventing recruitment of HDAC2 by ELK1,
CC thus reversing SUMO-mediated repression of ELK1 transactivation
CC activity. Isoform PIASx-beta, but not isoform PIASx-alpha, promotes
CC MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation.
CC Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than
CC isoform PIASx-alpha (By similarity). Sumoylates PML at'Lys-65' and
CC 'Lys-160' (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7,
CC TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with
CC STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts
CC also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with
CC several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and
CC with NCOA2. Sumoylation of a target protein seems to enhance the
CC interaction. Binds to sumoylated ELK1. Interacts with PLAG1 (By
CC similarity). Binds DNA, such as CDKN1A promoter, in a sequence-specific
CC manner. Interacts with KLF8; the interaction results in SUMO ligation
CC and repression of KLF8 transcriptional activity and of its cell cycle
CC progression into G(1) phase (By similarity). Interacts with IFIH1/MDA5
CC (By similarity). Interacts with PML (By similarity). Interacts with
CC PRDM1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O75928}.
CC -!- INTERACTION:
CC Q8C5D8; P98078: Dab2; NbExp=2; IntAct=EBI-6305825, EBI-1391846;
CC Q8C5D8; P98078-3: Dab2; NbExp=3; IntAct=EBI-6305825, EBI-6305891;
CC Q8C5D8-1; P08152: Egr2; NbExp=5; IntAct=EBI-8064899, EBI-7070449;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12077349}.
CC Nucleus, PML body {ECO:0000250|UniProtKB:O75928}. Nucleus
CC {ECO:0000269|PubMed:12193603}. Note=Colocalizes at least partially with
CC promyelocytic leukemia nuclear bodies (PML NBs) (By similarity).
CC Colocalizes with SUMO1 in nuclear granules (PubMed:12077349).
CC {ECO:0000250|UniProtKB:O75928, ECO:0000269|PubMed:12077349}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=PIASx-beta, Miz1;
CC IsoId=Q8C5D8-1; Sequence=Displayed;
CC Name=2; Synonyms=PIASx-alpha, ARIP3;
CC IsoId=Q8C5D8-2; Sequence=VSP_012199, VSP_012201;
CC Name=3;
CC IsoId=Q8C5D8-3; Sequence=VSP_012198, VSP_012199, VSP_012201;
CC Name=4;
CC IsoId=Q8C5D8-4; Sequence=VSP_012200, VSP_012202;
CC Name=5;
CC IsoId=Q8C5D8-5; Sequence=VSP_012198;
CC -!- DOMAIN: The LXXLL motif is a transcriptional coregulator signature.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:12077349}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB96678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29594.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF201391; AAF12825.1; -; mRNA.
DR EMBL; AK029716; BAC26579.1; -; mRNA.
DR EMBL; AK014871; BAB29594.1; ALT_FRAME; mRNA.
DR EMBL; AK078813; BAC37407.1; -; mRNA.
DR EMBL; AK086653; BAC39710.1; -; mRNA.
DR EMBL; BC005596; AAH05596.1; -; mRNA.
DR EMBL; BC034711; AAH34711.1; -; mRNA.
DR EMBL; AF039567; AAB96678.1; ALT_INIT; mRNA.
DR CCDS; CCDS37866.1; -. [Q8C5D8-1]
DR RefSeq; NP_001157639.1; NM_001164167.1. [Q8C5D8-4]
DR RefSeq; NP_001157640.1; NM_001164168.1.
DR RefSeq; NP_001157641.1; NM_001164169.1. [Q8C5D8-2]
DR RefSeq; NP_001157642.1; NM_001164170.1.
DR RefSeq; NP_032628.3; NM_008602.4. [Q8C5D8-1]
DR AlphaFoldDB; Q8C5D8; -.
DR SMR; Q8C5D8; -.
DR BioGRID; 201429; 14.
DR IntAct; Q8C5D8; 7.
DR MINT; Q8C5D8; -.
DR STRING; 10090.ENSMUSP00000110425; -.
DR iPTMnet; Q8C5D8; -.
DR PhosphoSitePlus; Q8C5D8; -.
DR EPD; Q8C5D8; -.
DR jPOST; Q8C5D8; -.
DR MaxQB; Q8C5D8; -.
DR PaxDb; Q8C5D8; -.
DR PRIDE; Q8C5D8; -.
DR ProteomicsDB; 287712; -. [Q8C5D8-1]
DR ProteomicsDB; 287713; -. [Q8C5D8-2]
DR ProteomicsDB; 287714; -. [Q8C5D8-3]
DR ProteomicsDB; 287715; -. [Q8C5D8-4]
DR ProteomicsDB; 287716; -. [Q8C5D8-5]
DR Antibodypedia; 9110; 535 antibodies from 41 providers.
DR DNASU; 17344; -.
DR Ensembl; ENSMUST00000114777; ENSMUSP00000110425; ENSMUSG00000025423. [Q8C5D8-1]
DR GeneID; 17344; -.
DR KEGG; mmu:17344; -.
DR UCSC; uc008frb.1; mouse. [Q8C5D8-2]
DR UCSC; uc008frc.2; mouse. [Q8C5D8-1]
DR UCSC; uc012bfb.1; mouse. [Q8C5D8-4]
DR CTD; 9063; -.
DR MGI; MGI:1096566; Pias2.
DR VEuPathDB; HostDB:ENSMUSG00000025423; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR InParanoid; Q8C5D8; -.
DR OMA; DPQQYCP; -.
DR OrthoDB; 1205949at2759; -.
DR PhylomeDB; Q8C5D8; -.
DR TreeFam; TF323787; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 17344; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Pias2; mouse.
DR PRO; PR:Q8C5D8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C5D8; protein.
DR Bgee; ENSMUSG00000025423; Expressed in seminiferous tubule of testis and 270 other tissues.
DR ExpressionAtlas; Q8C5D8; baseline and differential.
DR Genevisible; Q8C5D8; MM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0061665; F:SUMO ligase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0016925; P:protein sumoylation; IDA:MGI.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027228; PIAS2.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF12; PTHR10782:SF12; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..621
FT /note="E3 SUMO-protein ligase PIAS2"
FT /id="PRO_0000218977"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 134..299
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 331..412
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 467..473
FT /note="SUMO1-binding"
FT /evidence="ECO:0000250"
FT REGION 577..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..23
FT /note="LXXLL motif"
FT MOTIF 484..492
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12193603"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75928"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012198"
FT VAR_SEQ 551..572
FT /note="LDFLSLIPVDPQYCPPMFLDSL -> EQRRNDINNEVQLGASSDTVQQ (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11104669,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012199"
FT VAR_SEQ 563..580
FT /note="YCPPMFLDSLTSPLTASS -> SHLTLNSKQYVCHHHQPP (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012200"
FT VAR_SEQ 573..621
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11104669,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012201"
FT VAR_SEQ 581..621
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012202"
FT CONFLICT 73
FT /note="C -> S (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="P -> A (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="T -> A (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="G -> E (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> T (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="D -> E (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> G (in Ref. 2; BAC26579)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="G -> A (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="N -> Q (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="R -> K (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="L -> P (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="Q -> R (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> A (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="S -> I (in Ref. 2; BAC37407)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="V -> G (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..466
FT /note="KKK -> GTR (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8C5D8-2:555
FT /note="N -> T (in Ref. 1; AAF12825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 68426 MW; E980B834C2A9C58E CRC64;
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL
YRRRYPRTLE GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG IHSLPSTSIT PHSPSSPVGS
VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI
FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP
LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT
SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV
TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE
DGSWCPMRPK KEAMKVTSQP CTKVESSSVF SKPCSVTVAS DASKKKIDVI DLTIESSSDE
EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP
VSSMSSDLPG LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSPHE SSTHVSSSSS
RSETGVITSS GRNIPDIISL D
