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   24-JAN-2024, entry version 167.
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,
GN   ECO:0000312|MGI:MGI:1203484};
GN   Synonyms=Np220 {ECO:0000303|PubMed:8670298}, Zfml
GN   {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}.
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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.ENSMUSP00000144989; -.
DR   GlyGen; Q61464; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61464; -.
DR   PhosphoSitePlus; Q61464; -.
DR   SwissPalm; Q61464; -.
DR   EPD; Q61464; -.
DR   jPOST; Q61464; -.
DR   MaxQB; Q61464; -.
DR   PaxDb; 10090-ENSMUSP00000032088; -.
DR   PeptideAtlas; 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   Pumba; Q61464; -.
DR   Antibodypedia; 31207; 130 antibodies from 22 providers.
DR   DNASU; 18139; -.
DR   Ensembl; ENSMUST00000113835.10; ENSMUSP00000109466.4; ENSMUSG00000030016.15. [Q61464-2]
DR   GeneID; 18139; -.
DR   KEGG; mmu:18139; -.
DR   UCSC; uc009coo.2; mouse. [Q61464-3]
DR   UCSC; uc009coq.2; mouse. [Q61464-2]
DR   AGR; MGI:1203484; -.
DR   CTD; 18139; -.
DR   MGI; MGI:1203484; Zfp638.
DR   VEuPathDB; HostDB:ENSMUSG00000030016; -.
DR   eggNOG; ENOG502QVQ7; Eukaryota.
DR   GeneTree; ENSGT00940000153322; -.
DR   InParanoid; Q61464; -.
DR   OrthoDB; 5362494at2759; -.
DR   PhylomeDB; Q61464; -.
DR   BioGRID-ORCS; 18139; 10 hits in 78 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 274 other cell types or tissues.
DR   ExpressionAtlas; Q61464; baseline and differential.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR   CDD; cd12716; RRM1_2_NP220; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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_RRM1/2.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR15592; MATRIN 3/NUCLEAR PROTEIN 220-RELATED; 1.
DR   PANTHER; PTHR15592:SF1; ZINC FINGER PROTEIN 638; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
DR   Genevisible; Q61464; MM.
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
//