ZFR_HUMAN
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 03-AUG-2022, entry version 163.
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; 253.
DR DIP; DIP-47293N; -.
DR IntAct; Q96KR1; 73.
DR MINT; Q96KR1; -.
DR STRING; 9606.ENSP00000265069; -.
DR GlyConnect; 2868; 1 O-Linked glycan (4 sites).
DR GlyGen; Q96KR1; 54 sites, 2 O-linked glycans (54 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; Q96KR1; -.
DR PeptideAtlas; Q96KR1; -.
DR PRIDE; Q96KR1; -.
DR ProteomicsDB; 77105; -.
DR Antibodypedia; 9796; 80 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 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; QCSQQPA; -.
DR OrthoDB; 612611at2759; -.
DR PhylomeDB; Q96KR1; -.
DR TreeFam; TF320194; -.
DR PathwayCommons; Q96KR1; -.
DR SignaLink; Q96KR1; -.
DR BioGRID-ORCS; 51663; 155 hits in 1081 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 214 other tissues.
DR ExpressionAtlas; Q96KR1; baseline and differential.
DR Genevisible; Q96KR1; HS.
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; 3.30.460.10; -; 1.
DR InterPro; IPR006561; DZF_dom.
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 Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS51703; DZF; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
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 unknown pathological 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
