ID   ZFR_HUMAN               Reviewed;        1074 AA.
AC   Q96KR1; B2RNR5; Q05C08; Q3B7X5; Q6P5A3; Q86UA0; Q9H6V4; Q9NTI1; Q9Y687;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Zinc finger RNA-binding protein;
DE            Short=hZFR;
DE   AltName: Full=M-phase phosphoprotein homolog;
GN   Name=ZFR;
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], AND TISSUE SPECIFICITY.
RX   PubMed=11574164; DOI=10.1016/s0378-1119(01)00620-5;
RA   Kleines M., Gaertner A., Ritter K., Schaade L.;
RT   "Cloning and expression of the human single copy homologue of the mouse
RT   zinc finger protein zfr.";
RL   Gene 275:157-162(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-461 AND THR-520.
RC   TISSUE=Bone marrow, Duodenum, Eye, Lung, and Uterus;
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 [LARGE SCALE MRNA] OF 643-1074.
RC   TISSUE=Pituitary;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 744-1074.
RC   TISSUE=Hepatoma;
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 970-1074.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-509, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
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   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-509; LYS-541 AND LYS-623, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [16]
RP   VARIANT PRO-319.
RX   PubMed=24482476; DOI=10.1126/science.1247363;
RA   Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA   Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA   Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA   Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA   Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA   Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA   Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA   Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA   Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA   Gleeson J.G.;
RT   "Exome sequencing links corticospinal motor neuron disease to common
RT   neurodegenerative disorders.";
RL   Science 343:506-511(2014).
CC   -!- FUNCTION: Involved in postimplantation and gastrulation stages of
CC       development. Involved in the nucleocytoplasmic shuttling of STAU2.
CC       Binds to DNA and RNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Found in a cytoplasmic RNP complex with STAU2. Interacts with
CC       STAU2. Does not interact with STAU1 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96KR1; Q15796: SMAD2; NbExp=2; IntAct=EBI-2513582, EBI-1040141;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cytoplasmic granule {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Associated with chromosome foci in meiotic cells. Localizes in
CC       somatodendritic compartment of primary hippocampal neurons. Colocalizes
CC       with STAU2 in several cytosolic RNA granules (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, liver, lymphocytes, heart,
CC       pancreas, placenta, brain and kidney. {ECO:0000269|PubMed:11574164}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD40385.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH30540.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI07418.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAB15147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC40818.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC40818.1; Type=Frameshift; Evidence={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; AJ314790; CAC40818.1; ALT_SEQ; mRNA.
DR   EMBL; AC008949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030540; AAH30540.1; ALT_SEQ; mRNA.
DR   EMBL; BC051893; AAH51893.1; -; mRNA.
DR   EMBL; BC062986; AAH62986.1; -; mRNA.
DR   EMBL; BC107417; AAI07418.1; ALT_SEQ; mRNA.
DR   EMBL; BC137084; AAI37085.1; -; mRNA.
DR   EMBL; AF100742; AAD40385.1; ALT_INIT; mRNA.
DR   EMBL; AK025481; BAB15147.1; ALT_INIT; mRNA.
DR   EMBL; AL137258; CAB70659.1; -; mRNA.
DR   CCDS; CCDS34139.1; -.
DR   PIR; T46329; T46329.
DR   RefSeq; NP_057191.2; NM_016107.4.
DR   AlphaFoldDB; Q96KR1; -.
DR   SMR; Q96KR1; -.
DR   BioGRID; 119667; 309.
DR   DIP; DIP-47293N; -.
DR   IntAct; Q96KR1; 75.
DR   MINT; Q96KR1; -.
DR   STRING; 9606.ENSP00000265069; -.
DR   GlyConnect; 2868; 1 O-GlcNAc glycan (4 sites).
DR   GlyCosmos; Q96KR1; 54 sites, 2 glycans.
DR   GlyGen; Q96KR1; 68 sites, 2 O-linked glycans (68 sites).
DR   iPTMnet; Q96KR1; -.
DR   MetOSite; Q96KR1; -.
DR   PhosphoSitePlus; Q96KR1; -.
DR   SwissPalm; Q96KR1; -.
DR   BioMuta; ZFR; -.
DR   DMDM; 162416228; -.
DR   EPD; Q96KR1; -.
DR   jPOST; Q96KR1; -.
DR   MassIVE; Q96KR1; -.
DR   MaxQB; Q96KR1; -.
DR   PaxDb; 9606-ENSP00000265069; -.
DR   PeptideAtlas; Q96KR1; -.
DR   ProteomicsDB; 77105; -.
DR   Pumba; Q96KR1; -.
DR   Antibodypedia; 9796; 89 antibodies from 17 providers.
DR   DNASU; 51663; -.
DR   Ensembl; ENST00000265069.13; ENSP00000265069.8; ENSG00000056097.16.
DR   GeneID; 51663; -.
DR   KEGG; hsa:51663; -.
DR   MANE-Select; ENST00000265069.13; ENSP00000265069.8; NM_016107.5; NP_057191.2.
DR   UCSC; uc003jhr.2; human.
DR   AGR; HGNC:17277; -.
DR   CTD; 51663; -.
DR   DisGeNET; 51663; -.
DR   GeneCards; ZFR; -.
DR   HGNC; HGNC:17277; ZFR.
DR   HPA; ENSG00000056097; Low tissue specificity.
DR   MalaCards; ZFR; -.
DR   MIM; 615635; gene.
DR   neXtProt; NX_Q96KR1; -.
DR   OpenTargets; ENSG00000056097; -.
DR   Orphanet; 401840; Autosomal recessive spastic paraplegia type 71.
DR   PharmGKB; PA38219; -.
DR   VEuPathDB; HostDB:ENSG00000056097; -.
DR   eggNOG; KOG3792; Eukaryota.
DR   GeneTree; ENSGT00940000155290; -.
DR   HOGENOM; CLU_012026_1_0_1; -.
DR   InParanoid; Q96KR1; -.
DR   OMA; QYSSVLW; -.
DR   OrthoDB; 4565640at2759; -.
DR   PhylomeDB; Q96KR1; -.
DR   TreeFam; TF320194; -.
DR   PathwayCommons; Q96KR1; -.
DR   SignaLink; Q96KR1; -.
DR   BioGRID-ORCS; 51663; 167 hits in 1168 CRISPR screens.
DR   ChiTaRS; ZFR; human.
DR   GenomeRNAi; 51663; -.
DR   Pharos; Q96KR1; Tbio.
DR   PRO; PR:Q96KR1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q96KR1; Protein.
DR   Bgee; ENSG00000056097; Expressed in CA1 field of hippocampus and 216 other cell types or tissues.
DR   ExpressionAtlas; Q96KR1; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.1410.40; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR006561; DZF_dom.
DR   InterPro; IPR049402; DZF_dom_C.
DR   InterPro; IPR049401; DZF_dom_N.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR45762:SF3; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR   Pfam; PF20965; DZF_C; 1.
DR   Pfam; PF07528; DZF_N; 1.
DR   Pfam; PF12874; zf-met; 3.
DR   SMART; SM00572; DZF; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SMART; SM00451; ZnF_U1; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS51703; DZF; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   Genevisible; Q96KR1; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Cytoplasm; Developmental protein; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; Ubl conjugation.
FT   CHAIN           1..1074
FT                   /note="Zinc finger RNA-binding protein"
FT                   /id="PRO_0000312719"
FT   DOMAIN          703..1073
FT                   /note="DZF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT   REGION          120..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1074
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         509
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         516
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O88532"
FT   MOD_RES         1054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   CROSSLNK        509
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        541
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         319
FT                   /note="L -> P (found in a patient with spastic paraplegia;
FT                   uncertain significance; dbSNP:rs587777203)"
FT                   /evidence="ECO:0000269|PubMed:24482476"
FT                   /id="VAR_077851"
FT   VARIANT         461
FT                   /note="V -> I (in dbSNP:rs4867440)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037554"
FT   VARIANT         520
FT                   /note="I -> T (in dbSNP:rs1051489)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037555"
FT   CONFLICT        7
FT                   /note="V -> I (in Ref. 3; AAI07418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        643
FT                   /note="E -> L (in Ref. 4; AAD40385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        659
FT                   /note="M -> I (in Ref. 1; CAC40818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        794
FT                   /note="L -> F (in Ref. 4; AAD40385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        834
FT                   /note="V -> F (in Ref. 4; AAD40385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        913
FT                   /note="Q -> QE (in Ref. 1; CAC40818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1016
FT                   /note="F -> K (in Ref. 1; CAC40818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1074 AA;  117012 MW;  3E43654E7134E9FC CRC64;
     MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA SGVAYSHPTT
     VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA ATAAAYGGYP TAHTATDYGY
     TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA PAVAYDSKQY YQQPTATAAA VAAAAQPQPS
     VAETYYQTAP KAGYSQGATQ YTQAQQTRQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA
     ATVVPSYTQS ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
     AAWTGTTFTK KAPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL EGQKHKKKEA
     ALKASQNTSS SNSSTRGTQN QLRCELCDVS CTGADAYAAH IRGAKHQKVV KLHTKLGKPI
     PSTEPNVVSQ ATSSTAVSAS KPTASPSSIA ANNCTVNTSS VATSSMKGLT TTGNSSLNST
     SNTKVSAVPT NMAAKKTSTP KINFVGGNKL QSTGNKAEDI KGTECVKSTP VTSAVQIPEV
     KQDTVSEPVT PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH
     LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE EEERWRMEMR
     RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL GVRPGMPPQP QGPAPLRRPD
     SSDDRYVMTK HATIYPTEEE LQAVQKIVSI TERALKLVSD SLSEHEKNKN KEGDDKKEGG
     KDRALKGVLR VGVLAKGLLL RGDRNVNLVL LCSEKPSKTL LSRIAENLPK QLAVISPEKY
     DIKCAVSEAA IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL
     DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL VEKAISSASS
     PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA TMTDQQREDI TSSAQFALRL
     LAFRQIHKVL GMDPLPQMSQ RFNIHNNRKR RRDSDGVDGF EAEGKKDKKD YDNF
//