ZN638_MOUSE
ID ZN638_MOUSE Reviewed; 1960 AA.
AC Q61464; Q6DFV9; Q8C941;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein 638 {ECO:0000303|PubMed:21602272};
DE AltName: Full=Nuclear protein 220 {ECO:0000303|PubMed:8670298};
DE AltName: Full=Zinc finger matrin-like protein {ECO:0000250|UniProtKB:Q14966};
GN Name=Znf638 {ECO:0000303|PubMed:21602272, ECO:0000312|MGI:MGI:1203484};
GN Synonyms=Np220 {ECO:0000303|PubMed:8670298},
GN Zfml {ECO:0000312|MGI:MGI:1203484}, Zfp638 {ECO:0000312|MGI:MGI:1203484};
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 4; 5 AND 6).
RC TISSUE=Heart;
RX PubMed=8670298; DOI=10.1006/bbrc.1996.0910;
RA Matsushima Y., Ohshima M., Sonoda M., Kitagawa Y.;
RT "A family of novel DNA-binding nuclear proteins having polypyrimidine
RT tract-binding motif and arginine/serine-rich motif.";
RL Biochem. Biophys. Res. Commun. 223:427-433(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 PROTEIN SEQUENCE OF 761-768; 873-891; 1395-1404; 1506-1513 AND 1874-1881,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-1635, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and 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).
RN [6]
RP FUNCTION, INTERACTION WITH CEBPA; CEBPD AND CEBPG, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=21602272; DOI=10.1074/jbc.m110.212506;
RA Meruvu S., Hugendubler L., Mueller E.;
RT "Regulation of adipocyte differentiation by the zinc finger protein
RT ZNF638.";
RL J. Biol. Chem. 286:26516-26523(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25024404; DOI=10.1194/jlr.m047555;
RA Du C., Ma X., Meruvu S., Hugendubler L., Mueller E.;
RT "The adipogenic transcriptional cofactor ZNF638 interacts with splicing
RT regulators and influences alternative splicing.";
RL J. Lipid Res. 55:1886-1896(2014).
RN [8]
RP FUNCTION.
RX PubMed=30487602; DOI=10.1038/s41586-018-0750-6;
RA Zhu Y., Wang G.Z., Cingoez O., Goff S.P.;
RT "NP220 mediates silencing of unintegrated retroviral DNA.";
RL Nature 564:278-282(2018).
CC -!- FUNCTION: Transcription factor that binds to cytidine clusters in
CC double-stranded DNA (By similarity). Plays a key role in the silencing
CC of unintegrated retroviral DNA: some part of the retroviral DNA formed
CC immediately after infection remains unintegrated in the host genome and
CC is transcriptionally repressed (PubMed:30487602). Mediates
CC transcriptional repression of unintegrated viral DNA by specifically
CC binding to the cytidine clusters of retroviral DNA and mediating the
CC recruitment of chromatin silencers, such as the HUSH complex, SETDB1
CC and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as
CC an early regulator of adipogenesis by acting as a transcription
CC cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the
CC expression of PPARG and probably of other proadipogenic genes, such as
CC SREBF1 (PubMed:21602272). May also regulate alternative splicing of
CC target genes during adipogenesis (PubMed:25024404).
CC {ECO:0000250|UniProtKB:Q14966, ECO:0000269|PubMed:21602272,
CC ECO:0000269|PubMed:25024404, ECO:0000269|PubMed:30487602}.
CC -!- SUBUNIT: Interacts with FHL2 (By similarity). Interacts with CEBPA,
CC CEBPD and CEBPG (PubMed:21602272). Interacts with MPHOSPH8 and TASOR
CC components of the HUSH complex; leading to recruitment of the HUSH
CC complex (By similarity). Interacts with SETDB1 (By similarity).
CC Interacts with HDAC1 (By similarity). Interacts with HDAC4 (By
CC similarity). {ECO:0000250|UniProtKB:Q14966,
CC ECO:0000269|PubMed:21602272}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00130, ECO:0000269|PubMed:21602272,
CC ECO:0000269|PubMed:25024404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Alpha {ECO:0000303|PubMed:8670298};
CC IsoId=Q61464-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61464-2; Sequence=VSP_014809, VSP_014812, VSP_014813,
CC VSP_014814;
CC Name=3;
CC IsoId=Q61464-3; Sequence=VSP_014807, VSP_014808;
CC Name=4; Synonyms=Beta {ECO:0000303|PubMed:8670298};
CC IsoId=Q61464-4; Sequence=VSP_014814;
CC Name=5; Synonyms=Gamma {ECO:0000303|PubMed:8670298};
CC IsoId=Q61464-5; Sequence=VSP_014811;
CC Name=6; Synonyms=Delta {ECO:0000303|PubMed:8670298};
CC IsoId=Q61464-7; Sequence=VSP_014810;
CC -!- DEVELOPMENTAL STAGE: In an vitro adipocyte differentiation system,
CC induced at the protein and RNA levels shortly after exposure to the
CC induction mixture. Levels peak before PPARG induction and rapidly
CC decrease during later stages of differentiation.
CC {ECO:0000269|PubMed:21602272}.
CC -!- DOMAIN: The matrin-type zinc finger domain is required for localization
CC to nuclear speckles. {ECO:0000269|PubMed:25024404}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
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; D83033; BAA11749.1; -; mRNA.
DR EMBL; AK043029; BAC31439.1; -; mRNA.
DR EMBL; BC076615; AAH76615.1; -; mRNA.
DR CCDS; CCDS20288.1; -. [Q61464-4]
DR CCDS; CCDS51823.1; -. [Q61464-2]
DR PIR; JC4842; JC4842.
DR RefSeq; NP_001159843.1; NM_001166371.1. [Q61464-2]
DR RefSeq; NP_032743.2; NM_008717.3.
DR AlphaFoldDB; Q61464; -.
DR SMR; Q61464; -.
DR BioGRID; 201815; 12.
DR IntAct; Q61464; 1.
DR MINT; Q61464; -.
DR STRING; 10090.ENSMUSP00000032088; -.
DR iPTMnet; Q61464; -.
DR PhosphoSitePlus; Q61464; -.
DR SwissPalm; Q61464; -.
DR EPD; Q61464; -.
DR jPOST; Q61464; -.
DR MaxQB; Q61464; -.
DR PaxDb; Q61464; -.
DR PeptideAtlas; Q61464; -.
DR PRIDE; Q61464; -.
DR ProteomicsDB; 275022; -. [Q61464-1]
DR ProteomicsDB; 275023; -. [Q61464-2]
DR ProteomicsDB; 275024; -. [Q61464-3]
DR ProteomicsDB; 275025; -. [Q61464-4]
DR ProteomicsDB; 275026; -. [Q61464-5]
DR ProteomicsDB; 275027; -. [Q61464-7]
DR Antibodypedia; 31207; 103 antibodies from 22 providers.
DR DNASU; 18139; -.
DR Ensembl; ENSMUST00000113835; ENSMUSP00000109466; ENSMUSG00000030016. [Q61464-2]
DR GeneID; 18139; -.
DR KEGG; mmu:18139; -.
DR UCSC; uc009coo.2; mouse. [Q61464-3]
DR UCSC; uc009coq.2; mouse. [Q61464-2]
DR CTD; 18139; -.
DR MGI; MGI:1203484; Zfp638.
DR VEuPathDB; HostDB:ENSMUSG00000030016; -.
DR eggNOG; ENOG502QVQ7; Eukaryota.
DR GeneTree; ENSGT00940000153322; -.
DR InParanoid; Q61464; -.
DR OrthoDB; 301913at2759; -.
DR PhylomeDB; Q61464; -.
DR BioGRID-ORCS; 18139; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp638; mouse.
DR PRO; PR:Q61464; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61464; protein.
DR Bgee; ENSMUSG00000030016; Expressed in undifferentiated genital tubercle and 270 other tissues.
DR ExpressionAtlas; Q61464; baseline and differential.
DR Genevisible; Q61464; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033096; ZNF638.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15592:SF1; PTHR15592:SF1; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1960
FT /note="Zinc finger protein 638"
FT /id="PRO_0000082012"
FT DOMAIN 676..751
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 902..976
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 1876..1906
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..573
FT /note="Involved in localization to nuclear speckles"
FT /evidence="ECO:0000269|PubMed:25024404"
FT REGION 749..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1930..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..553
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 54
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 1635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT CROSSLNK 1804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14966"
FT VAR_SEQ 438..454
FT /note="DWIQHQNTSTHIESCRQ -> VSVFKRLLYNDAQCPGF (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014807"
FT VAR_SEQ 456..1960
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014808"
FT VAR_SEQ 810..832
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014809"
FT VAR_SEQ 1147..1866
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8670298"
FT /id="VSP_014810"
FT VAR_SEQ 1147..1832
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8670298"
FT /id="VSP_014811"
FT VAR_SEQ 1147..1200
FT /note="KEEPKQALCESDFAIQTLELEAQGAEVSIEIPLVASTPANIELFSENIDESA
FT LN -> PGSETVTQKDLKTMPERHLAAKTPMKRVRIGKSSPSQKVAEPTKGEEAFQMSE
FT G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014812"
FT VAR_SEQ 1201..1832
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014813"
FT VAR_SEQ 1833..1866
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8670298"
FT /id="VSP_014814"
FT CONFLICT 32
FT /note="V -> L (in Ref. 3; AAH76615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1960 AA; 218134 MW; 27DF6740BFE410ED CRC64;
MSRPRFNPRG TFPLQRPRAP NPPGMRPPGP FVRPGSMGLP RFYPAGRARG IPHRFPGHGS
YQNMGPQRMN VQVTQHRTDP RLTKEKLDFP EAQQKKGKPH GSRWDDESHI TPPVEVKQSS
VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR
KMSRRLPNLP SHSRNKETLS NETVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVKN
EFQPQQSISA TVSTPNVICN SVFPGGDMFR QMDFPGESSS QSFFPVESGT KMSGLHISGQ
SVLEPVKSIS QSISQTVSQT TSQSLNPPSM NQVPFTFELD AVLRQQERIS QKSVISSADA
HGGPTESKKD YQSEADLPIR SPFGIVKASW LPKFTQAGAQ KMKRLPTPSM MNDYYAASPR
IFPHLCSLCN VECSHLKDWI QHQNTSTHIE SCRQLRQQYP DWNPEILPSR RNESNRKENE
TPRRRSHSPS PRHSRRSSSG HRIRRSRSPV RYIYRPRSRS PRICHRFISK YRSRSRSRSR
SRSPYRSRNL LRRSPKSYRS ASPERTSRKS VRSDRKKALE DGGQRSVHGT EVTKQKHTET
VDKGLSPAQK PKLASGTKPS AKSLSSVKSD SHLGAYSAHK SENLEDDTLP EGKQESGKSA
LAQRKPQKDQ SLSSNSILLV SELPEDGFTE EDIRKAFLPF GKISDVLLVP CRNEAYLEME
LRKAVTSIMK YIETMPLVIK GKSVKVCVPG KKKPQNKEMK KKPSDIKKSS ASALKKETDA
SKTMETVSSS SSAKSGQIKS STVKVNKCAG KSAGSVKSVV TVAAKGKASI KTAKSGKKSL
EAKKSGNIKN KDSNKPVTVP ANSEIKASSE DKATGKSAEE SPSGTLEATE KEPVNKESEE
MSVVFISNLP NKGYSTEEIY NLAKPFGALK DILVLSSHKK AYIEINKKSA DSMVKFYTCF
PISMDGNQLS ISMAPEHVDL KDEEALFTTL IQENDPEANI DKIYNRFVHL DNLPEDGLQC
VLCVGHQFGK VDRYMFMSNK NKVILQLESP ESALSMYNFL KQNPQNIGEH VLTCTLSPKT
DSEVQRKNDL ELGKGSTFSP DLKNSPVDES EVQTAADSSS VKPSEVEEET TSNIGTETSV
HQEELGKEEP KQALCESDFA IQTLELEAQG AEVSIEIPLV ASTPANIELF SENIDESALN
QQMYTSDFEK EEAEVTNPET ELAVSDSVFI EERNIKGIIE DSPSETEDIF SGIVQPMVDA
IAEVDKHETV SEVLPSACNV TQAPGSYIED EKVVSKKDIA EKVILDEKEE DEFNVKETRM
DLQVKTEKAE KNEAIIFKEK LEKIIAAIRE KPIESSVIKA DPTKGLDQTS KPDETGKSSV
LTVSNVYSSK SSIKATVVSS PKAKSTPSKT ESHSTFPKPV LREQIKADKK VSAKEFGLLK
NTRSGLAESN SKSKPTQIGV NRGCSGRISA LQCKDSKVDY KDITKQSQET ETKPPIMKRD
DSNNKALALQ NTKNSKSTTD RSSKSKEEPL FTFNLDEFVT VDEVIEEVNP SQAKQNPLKG
KRKEALKISP SPELNLKKKK GKTSVPHSVE GELSFVTLDE IGEEEDATVQ ALVTVDEVID
EEELNMEEMV KNSNSLLTLD ELIDQDDCIP HSGPKDVTVL SMAEEQDLQQ ERLVTVDEIG
EVEESADITF ATLNAKRDKR DSIGFISSQM PEDPSTLVTV DEIQDDSSDF HLMTLDEVTE
EDENSLADFN NLKEELNFVT VDEVGDEEDG DNDSKVELAR GKIEHHTDKK GNRKRRAVDP
KKSKLDSFSQ VGPGSETVTQ KDLKTMPERH LAAKTPMKRV RLGKSSPSQK VAEPTKGEEA
FQMSEGVDDA ELKDSEPDEK RRKTQDSSVG KSMTSDVPGD LDFLVPKAGF FCPICSLFYS
GEKAMANHCK STRHKQNTEK FMAKQRKEKE QNETEERSSR
