ID   ZXDC_HUMAN              Reviewed;         858 AA.
AC   Q2QGD7; C5J0H9; Q6DKI8; Q7L3L1; Q8NAU2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   02-SEP-2026, entry version 169.
DE   RecName: Full=Zinc finger protein ZXDC;
DE   AltName: Full=ZXD-like zinc finger protein;
GN   Name=ZXDC; Synonyms=ZXDL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CIITA,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=16600381; DOI=10.1016/j.molimm.2006.02.029;
RA   Al-Kandari W., Jambunathan S., Navalgund V., Koneni R., Freer M.,
RA   Parimi N., Mudhasani R., Fontes J.D.;
RT   "ZXDC, a novel zinc finger protein that binds CIITA and activates MHC gene
RT   transcription.";
RL   Mol. Immunol. 44:311-321(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT LEU-562.
RX   PubMed=19777325; DOI=10.1007/s11010-009-0280-5;
RA   Aleksandrova A., Galkin O., Koneni R., Fontes J.D.;
RT   "An N- and C-terminal truncated isoform of zinc finger X-linked duplicated
RT   C protein represses MHC class II transcription.";
RL   Mol. Cell. Biochem. 337:1-7(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Tang W.W., Tang Z.H., Yu L.;
RT   "Cloning and characterization of the ZXDL gene which encodes a putative
RT   zinc finger protein.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-858 (ISOFORM 2).
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-858 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-710 (ISOFORM 2).
RC   TISSUE=Placenta, Skin, and Testis;
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   [7]
RP   SUMOYLATION AT LYS-660, AND FUNCTION.
RX   PubMed=17696781; DOI=10.1515/bc.2007.106;
RA   Jambunathan S., Fontes J.D.;
RT   "Sumoylation of the zinc finger protein ZXDC enhances the function of its
RT   transcriptional activation domain.";
RL   Biol. Chem. 388:965-972(2007).
RN   [8]
RP   FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH ZXDA AND CIITA.
RX   PubMed=17493635; DOI=10.1016/j.jmb.2007.04.033;
RA   Al-Kandari W., Koneni R., Navalgund V., Aleksandrova A., Jambunathan S.,
RA   Fontes J.D.;
RT   "The zinc finger proteins ZXDA and ZXDC form a complex that binds CIITA and
RT   regulates MHC II gene transcription.";
RL   J. Mol. Biol. 369:1175-1187(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND THR-172, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Cooperates with CIITA to promote transcription of MHC class I
CC       and MHC class II genes. {ECO:0000269|PubMed:16600381,
CC       ECO:0000269|PubMed:17493635, ECO:0000269|PubMed:17696781}.
CC   -!- SUBUNIT: Self-associates. Interacts with ZXDA and CIITA.
CC       {ECO:0000269|PubMed:16600381, ECO:0000269|PubMed:17493635}.
CC   -!- INTERACTION:
CC       Q2QGD7; P54253: ATXN1; NbExp=7; IntAct=EBI-1538838, EBI-930964;
CC       Q2QGD7; P46379-2: BAG6; NbExp=3; IntAct=EBI-1538838, EBI-10988864;
CC       Q2QGD7; Q8N4T8: CBR4; NbExp=3; IntAct=EBI-1538838, EBI-10897344;
CC       Q2QGD7; P33076: CIITA; NbExp=6; IntAct=EBI-1538838, EBI-1538819;
CC       Q2QGD7; O14645: DNALI1; NbExp=3; IntAct=EBI-1538838, EBI-395638;
CC       Q2QGD7; P04792: HSPB1; NbExp=3; IntAct=EBI-1538838, EBI-352682;
CC       Q2QGD7; P42858: HTT; NbExp=3; IntAct=EBI-1538838, EBI-466029;
CC       Q2QGD7; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1538838, EBI-10975473;
CC       Q2QGD7; O14901: KLF11; NbExp=3; IntAct=EBI-1538838, EBI-948266;
CC       Q2QGD7; Q9NQ76: MEPE; NbExp=3; IntAct=EBI-1538838, EBI-1753293;
CC       Q2QGD7; A0A6Q8PF08: PMP22; NbExp=3; IntAct=EBI-1538838, EBI-50433196;
CC       Q2QGD7; Q7Z3K3: POGZ; NbExp=4; IntAct=EBI-1538838, EBI-1389308;
CC       Q2QGD7; P60891: PRPS1; NbExp=3; IntAct=EBI-1538838, EBI-749195;
CC       Q2QGD7; P49810: PSEN2; NbExp=3; IntAct=EBI-1538838, EBI-2010251;
CC       Q2QGD7; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1538838, EBI-396669;
CC       Q2QGD7; P00441: SOD1; NbExp=3; IntAct=EBI-1538838, EBI-990792;
CC       Q2QGD7; P51687: SUOX; NbExp=3; IntAct=EBI-1538838, EBI-3921347;
CC       Q2QGD7; P02766: TTR; NbExp=3; IntAct=EBI-1538838, EBI-711909;
CC       Q2QGD7; P61964: WDR5; NbExp=6; IntAct=EBI-1538838, EBI-540834;
CC       Q2QGD7; O76024: WFS1; NbExp=3; IntAct=EBI-1538838, EBI-720609;
CC       Q2QGD7; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1538838, EBI-746595;
CC       Q2QGD7; P98168: ZXDA; NbExp=5; IntAct=EBI-1538838, EBI-1538980;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q2QGD7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2QGD7-2; Sequence=VSP_026437, VSP_026438;
CC       Name=3; Synonyms=ZXDC2;
CC         IsoId=Q2QGD7-3; Sequence=VSP_047464, VSP_026437, VSP_026438;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in heart, kidney, liver
CC       and testis, at moderate levels in brain and stomach, and at low levels
CC       in lung, muscle, placenta, small intestine and spleen.
CC       {ECO:0000269|PubMed:16600381}.
CC   -!- PTM: Sumoylated at Lys-660 with SUMO1, SUMO2 and SUMO3; sumoylation
CC       enhances the activity of the transcriptional activation domain.
CC       {ECO:0000269|PubMed:17696781}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Doesn't interact with CIITA. Represses MHC
CC       class II transcription possibly via dominant-negative association with
CC       isoform 1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ZXD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC03805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY936556; AAX23974.1; -; mRNA.
DR   EMBL; FJ980275; ACR56328.1; -; mRNA.
DR   EMBL; DQ079590; AAZ30918.1; -; mRNA.
DR   EMBL; AC024558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK092101; BAC03805.1; ALT_INIT; mRNA.
DR   EMBL; BC002940; AAH02940.2; -; mRNA.
DR   EMBL; BC012729; AAH12729.2; -; mRNA.
DR   EMBL; BC073859; AAH73859.1; -; mRNA.
DR   CCDS; CCDS43145.1; -. [Q2QGD7-1]
DR   CCDS; CCDS43146.1; -. [Q2QGD7-2]
DR   RefSeq; NP_001035743.1; NM_001040653.4. [Q2QGD7-2]
DR   RefSeq; NP_079388.3; NM_025112.5. [Q2QGD7-1]
DR   AlphaFoldDB; Q2QGD7; -.
DR   SMR; Q2QGD7; -.
DR   BioGRID; 122653; 36.
DR   FunCoup; Q2QGD7; 837.
DR   IntAct; Q2QGD7; 34.
DR   MINT; Q2QGD7; -.
DR   NDEx; IQUERY-CP-ZXDC; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000374359; -.
DR   GlyGen; Q2QGD7; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q2QGD7; -.
DR   PhosphoSitePlus; Q2QGD7; -.
DR   BioMuta; ZXDC; -.
DR   DMDM; 296453026; -.
DR   jPOST; Q2QGD7; -.
DR   MassIVE; Q2QGD7; -.
DR   PaxDb; 9606-ENSP00000374359; -.
DR   PeptideAtlas; Q2QGD7; -.
DR   ProteomicsDB; 61437; -. [Q2QGD7-1]
DR   ProteomicsDB; 61438; -. [Q2QGD7-2]
DR   Pumba; Q2QGD7; -.
DR   Antibodypedia; 33073; 111 antibodies from 22 providers.
DR   DNASU; 79364; -.
DR   Ensembl; ENST00000336332.5; ENSP00000337694.5; ENSG00000070476.16. [Q2QGD7-2]
DR   Ensembl; ENST00000389709.8; ENSP00000374359.3; ENSG00000070476.16. [Q2QGD7-1]
DR   GeneID; 79364; -.
DR   KEGG; hsa:79364; -.
DR   MANE-Select; ENST00000389709.8; ENSP00000374359.3; NM_025112.5; NP_079388.3.
DR   UCSC; uc003eiv.3; human. [Q2QGD7-1]
DR   AGR; HGNC:28160; -.
DR   ClinPGx; PA142670466; -.
DR   CTD; 79364; -.
DR   GeneCards; ZXDC; -.
DR   HGNC; HGNC:28160; ZXDC.
DR   HPA; ENSG00000070476; Tissue enhanced (bone).
DR   MIM; 615746; gene.
DR   OpenTargets; ENSG00000070476; -.
DR   VEuPathDB; HostDB:ENSG00000070476; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162216; -.
DR   HOGENOM; CLU_007312_0_0_1; -.
DR   InParanoid; Q2QGD7; -.
DR   OMA; TGVQCIQ; -.
DR   OrthoDB; 6277246at2759; -.
DR   PAN-GO; Q2QGD7; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q2QGD7; -.
DR   PathwayCommons; Q2QGD7; -.
DR   SignaLink; Q2QGD7; -.
DR   SIGNOR; Q2QGD7; -.
DR   Agora; ENSG00000070476; -.
DR   BioGRID-ORCS; 79364; 18 hits in 1178 CRISPR screens.
DR   ChiTaRS; ZXDC; human.
DR   GenomeRNAi; 79364; -.
DR   Pharos; Q2QGD7; Tbio.
DR   PRO; PR:Q2QGD7; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q2QGD7; protein.
DR   Bgee; ENSG00000070476; Expressed in gastrocnemius and 189 other cell types or tissues.
DR   ExpressionAtlas; Q2QGD7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR   GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IMP:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   FunFam; 3.30.160.60:FF:000543; Zinc finger protein 384 like; 1.
DR   FunFam; 3.30.160.60:FF:000872; zinc finger X-linked protein ZXDB; 1.
DR   FunFam; 3.30.160.60:FF:000257; ZXD family zinc finger C; 3.
DR   FunFam; 3.30.160.60:FF:000499; ZXD family zinc finger C; 1.
DR   FunFam; 3.30.160.60:FF:001192; ZXD family zinc finger C; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR46179; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR46179:SF5; ZINC FINGER PROTEIN ZXDC; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..858
FT                   /note="Zinc finger protein ZXDC"
FT                   /id="PRO_0000292803"
FT   ZN_FING         175..199
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         208..232
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         238..262
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         268..290
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         297..321
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         328..352
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..382
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         388..412
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         418..442
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         451..476
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..688
FT                   /note="Required for transcriptional activation"
FT   REGION          660..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..858
FT                   /note="Interaction with CIITA"
FT   REGION          837..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..35
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..97
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         172
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CROSSLNK        660
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:17696781"
FT   VAR_SEQ         1..258
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19777325"
FT                   /id="VSP_047464"
FT   VAR_SEQ         710
FT                   /note="E -> V (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19777325"
FT                   /id="VSP_026437"
FT   VAR_SEQ         711..858
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19777325"
FT                   /id="VSP_026438"
FT   VARIANT         562
FT                   /note="P -> L (in dbSNP:rs16837497)"
FT                   /evidence="ECO:0000269|PubMed:19777325"
FT                   /id="VAR_057464"
FT   CONFLICT        118
FT                   /note="P -> A (in Ref. 1; AAX23974 and 3; AAZ30918)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        683
FT                   /note="Q -> H (in Ref. 5; AAH73859)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   858 AA;  89988 MW;  8C35F5685CF1E695 CRC64;
     MDLPALLPAP TARGGQHGGG PGPLRRAPAP LGASPARRRL LLVRGPEDGG PGARPGEASG
     PSPPPAEDDS DGDSFLVLLE VPHGGAAAEA AGSQEAEPGS RVNLASRPEQ GPSGPAAPPG
     PGVAPAGAVT ISSQDLLVRL DRGVLALSAP PGPATAGAAA PRRAPQASGP STPGYRCPEP
     QCALAFAKKH QLKVHLLTHG GGQGRRPFKC PLEGCGWAFT TSYKLKRHLQ SHDKLRPFGC
     PVGGCGKKFT TVYNLKAHMK GHEQESLFKC EVCAERFPTH AKLSSHQRSH FEPERPYKCD
     FPGCEKTFIT VSALFSHNRA HFREQELFSC SFPGCSKQYD KACRLKIHLR SHTGERPFIC
     DSDSCGWTFT SMSKLLRHRR KHDDDRRFTC PVEGCGKSFT RAEHLKGHSI THLGTKPFEC
     PVEGCCARFS ARSSLYIHSK KHVQDVGAPK SRCPVSTCNR LFTSKHSMKA HMVRQHSRRQ
     DLLPQLEAPS SLTPSSELSS PGQSELTNMD LAALFSDTPA NASGSAGGSD EALNSGILTI
     DVTSVSSSLG GNLPANNSSL GPMEPLVLVA HSDIPPSLDS PLVLGTAATV LQQGSFSVDD
     VQTVSAGALG CLVALPMKNL SDDPLALTSN SNLAAHITTP TSSSTPRENA SVPELLAPIK
     VEPDSPSRPG AVGQQEGSHG LPQSTLPSPA EQHGAQDTEL SAGTGNFYLE SGGSARTDYR
     AIQLAKEKKQ RGAGSNAGAS QSTQRKIKEG KMSPPHFHAS QNSWLCGSLV VPSGGRPGPA
     PAAGVQCGAQ GVQVQLVQDD PSGEGVLPSA RGPATFLPFL TVDLPVYVLQ EVLPSSGGPA
     GPEATQFPGS TINLQDLQ
//