GNL3_HUMAN
ID GNL3_HUMAN Reviewed; 549 AA.
AC Q9BVP2; B2RDC1; Q5PU80; Q96SV6; Q96SV7; Q9UJY0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Guanine nucleotide-binding protein-like 3;
DE AltName: Full=E2-induced gene 3 protein;
DE AltName: Full=Novel nucleolar protein 47;
DE Short=NNP47;
DE AltName: Full=Nucleolar GTP-binding protein 3;
DE AltName: Full=Nucleostemin;
GN Name=GNL3; Synonyms=E2IG3, NS;
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), AND VARIANTS GLN-39 AND MET-367.
RX PubMed=11085516;
RA Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J.,
RA Gaddis S., MacLeod M.C., Aldaz C.M.;
RT "Effects of estrogen on global gene expression: identification of novel
RT targets of estrogen action.";
RL Cancer Res. 60:5977-5983(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANTS GLN-39 AND MET-367.
RX PubMed=16012751;
RA Han C., Zhang X., Xu W., Wang W., Qian H., Chen Y.;
RT "Cloning of the nucleostemin gene and its function in transforming human
RT embryonic bone marrow mesenchymal stem cells into F6 tumor cells.";
RL Int. J. Mol. Med. 16:205-213(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [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] (ISOFORM 1), AND VARIANTS GLN-39 AND
RP MET-367.
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9;
RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H.,
RA Mann M., Lamond A.I.;
RT "Directed proteomic analysis of the human nucleolus.";
RL Curr. Biol. 12:1-11(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
RX PubMed=12464630; DOI=10.1101/gad.55671;
RA Tsai R.Y.L., McKay R.D.G.;
RT "A nucleolar mechanism controlling cell proliferation in stem and cancer
RT cells.";
RL Genes Dev. 16:2991-3003(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490 AND SER-517, AND
RP IDENTIFICATION BY 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).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-99; LYS-114; LYS-179;
RP LYS-196; LYS-253; LYS-267 AND LYS-275, AND IDENTIFICATION BY MASS
RP 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 [15]
RP VARIANT [LARGE SCALE ANALYSIS] MET-367, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May be required to maintain the proliferative capacity of
CC stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence
CC proteasomal degradation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12464630, ECO:0000269|PubMed:16012751}.
CC -!- SUBUNIT: Interacts with MDM2; this interaction stabilizes MDM2.
CC Interaction with MDM2 occurs in the nucleoplasm and is triggered by a
CC nucleolar release mechanism, such as mitosis-induced nucleolar
CC disassembly (By similarity). Indirectly interacts with TP53, via MDM2-
CC binding (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BVP2; Q9UKV8: AGO2; NbExp=3; IntAct=EBI-641642, EBI-528269;
CC Q9BVP2; Q96LK0: CEP19; NbExp=4; IntAct=EBI-641642, EBI-741885;
CC Q9BVP2; Q00987: MDM2; NbExp=3; IntAct=EBI-641642, EBI-389668;
CC Q9BVP2; Q15172: PPP2R5A; NbExp=3; IntAct=EBI-641642, EBI-641666;
CC Q9BVP2; P40763: STAT3; NbExp=2; IntAct=EBI-641642, EBI-518675;
CC Q9BVP2; O14746: TERT; NbExp=3; IntAct=EBI-641642, EBI-1772203;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q811S9}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:12464630}. Note=Shuttles between the nucleus and
CC nucleolus. {ECO:0000250|UniProtKB:Q811S9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVP2-2; Sequence=VSP_013411;
CC -!- TISSUE SPECIFICITY: Increased levels in lung tissue in cancer patients.
CC {ECO:0000269|PubMed:16012751}.
CC -!- DOMAIN: The basic domain (B) allows nucleolar localization in the
CC absence of GTP. The intermediate domain (I) inhibits nucleolar
CC localization by the B domain and is required for exit from the
CC nucleolus. Exit from the nucleolus to the nucleoplasm requires both the
CC I and the acidic (A) domains, and may be triggered by GTP hydrolysis
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF09482.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF191018; AAF09482.1; ALT_FRAME; mRNA.
DR EMBL; AY825265; AAV74413.1; -; mRNA.
DR EMBL; AK027514; BAB55168.1; -; mRNA.
DR EMBL; AK027516; BAB55169.1; -; mRNA.
DR EMBL; AK315484; BAG37868.1; -; mRNA.
DR EMBL; AC104446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001024; AAH01024.1; -; mRNA.
DR CCDS; CCDS2861.1; -. [Q9BVP2-1]
DR CCDS; CCDS43100.1; -. [Q9BVP2-2]
DR RefSeq; NP_055181.3; NM_014366.4. [Q9BVP2-1]
DR RefSeq; NP_996561.1; NM_206825.1. [Q9BVP2-2]
DR RefSeq; NP_996562.1; NM_206826.1. [Q9BVP2-2]
DR AlphaFoldDB; Q9BVP2; -.
DR SMR; Q9BVP2; -.
DR BioGRID; 117690; 253.
DR CORUM; Q9BVP2; -.
DR IntAct; Q9BVP2; 85.
DR MINT; Q9BVP2; -.
DR STRING; 9606.ENSP00000395772; -.
DR GlyGen; Q9BVP2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVP2; -.
DR MetOSite; Q9BVP2; -.
DR PhosphoSitePlus; Q9BVP2; -.
DR SwissPalm; Q9BVP2; -.
DR BioMuta; GNL3; -.
DR DMDM; 229462872; -.
DR SWISS-2DPAGE; Q9BVP2; -.
DR CPTAC; CPTAC-76; -.
DR CPTAC; CPTAC-77; -.
DR EPD; Q9BVP2; -.
DR jPOST; Q9BVP2; -.
DR MassIVE; Q9BVP2; -.
DR MaxQB; Q9BVP2; -.
DR PaxDb; Q9BVP2; -.
DR PeptideAtlas; Q9BVP2; -.
DR PRIDE; Q9BVP2; -.
DR ProteomicsDB; 79223; -. [Q9BVP2-1]
DR ProteomicsDB; 79224; -. [Q9BVP2-2]
DR Antibodypedia; 31298; 544 antibodies from 40 providers.
DR DNASU; 26354; -.
DR Ensembl; ENST00000394799.6; ENSP00000378278.2; ENSG00000163938.17. [Q9BVP2-2]
DR Ensembl; ENST00000418458.6; ENSP00000395772.1; ENSG00000163938.17. [Q9BVP2-1]
DR GeneID; 26354; -.
DR KEGG; hsa:26354; -.
DR MANE-Select; ENST00000418458.6; ENSP00000395772.1; NM_014366.5; NP_055181.3.
DR UCSC; uc003dfd.4; human. [Q9BVP2-1]
DR CTD; 26354; -.
DR DisGeNET; 26354; -.
DR GeneCards; GNL3; -.
DR HGNC; HGNC:29931; GNL3.
DR HPA; ENSG00000163938; Low tissue specificity.
DR MIM; 608011; gene.
DR neXtProt; NX_Q9BVP2; -.
DR OpenTargets; ENSG00000163938; -.
DR PharmGKB; PA134952132; -.
DR VEuPathDB; HostDB:ENSG00000163938; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000158320; -.
DR HOGENOM; CLU_011106_5_6_1; -.
DR InParanoid; Q9BVP2; -.
DR OMA; FKLDGLW; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q9BVP2; -.
DR TreeFam; TF313085; -.
DR PathwayCommons; Q9BVP2; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9BVP2; -.
DR BioGRID-ORCS; 26354; 766 hits in 1087 CRISPR screens.
DR ChiTaRS; GNL3; human.
DR GeneWiki; GNL3; -.
DR GenomeRNAi; 26354; -.
DR Pharos; Q9BVP2; Tbio.
DR PRO; PR:Q9BVP2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BVP2; protein.
DR Bgee; ENSG00000163938; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; Q9BVP2; baseline and differential.
DR Genevisible; Q9BVP2; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0017145; P:stem cell division; IDA:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; GTP-binding;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..549
FT /note="Guanine nucleotide-binding protein-like 3"
FT /id="PRO_0000122444"
FT DOMAIN 131..312
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..46
FT /note="Basic"
FT /evidence="ECO:0000250"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..456
FT /note="Intermediate"
FT /evidence="ECO:0000250"
FT REGION 465..543
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 474..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..95
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 261..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 305..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811S9"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI11"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013411"
FT VARIANT 39
FT /note="R -> Q (in dbSNP:rs11177)"
FT /evidence="ECO:0000269|PubMed:11085516,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16012751"
FT /id="VAR_022160"
FT VARIANT 367
FT /note="V -> M (in dbSNP:rs2289247)"
FT /evidence="ECO:0000269|PubMed:11085516,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16012751,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_022161"
FT CONFLICT 3
FT /note="R -> K (in Ref. 2; AAV74413)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="L -> Q (in Ref. 2; AAV74413)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="N -> D (in Ref. 2; AAV74413)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="I -> M (in Ref. 3; BAB55169)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="V -> A (in Ref. 2; AAV74413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 61993 MW; F3928FE1C77C77F4 CRC64;
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV PNSAPFKEAL
LREAELRKQR LEELKQQQKL DRQKELEKKR KLETNPDIKP SNVEPMEKEF GLCKTENKAK
SGKQNSKKLY CQELKKVIEA SDVVLEVLDA RDPLGCRCPQ VEEAIVQSGQ KKLVLILNKS
DLVPKENLES WLNYLKKELP TVVFRASTKP KDKGKITKRV KAKKNAAPFR SEVCFGKEGL
WKLLGGFQET CSKAIRVGVI GFPNVGKSSI INSLKQEQMC NVGVSMGLTR SMQVVPLDKQ
ITIIDSPSFI VSPLNSSSAL ALRSPASIEV VKPMEAASAI LSQADARQVV LKYTVPGYRN
SLEFFTVLAQ RRGMHQKGGI PNVEGAAKLL WSEWTGASLA YYCHPPTSWT PPPYFNESIV
VDMKSGFNLE ELEKNNAQSI RAIKGPHLAN SILFQSSGLT NGIIEEKDIH EELPKRKERK
QEEREDDKDS DQETVDEEVD ENSSGMFAAE ETGEALSEET TAGEQSTRSF ILDKIIEEDD
AYDFSTDYV
