MPH6_HUMAN
ID MPH6_HUMAN Reviewed; 160 AA.
AC Q99547; B2RAF0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=M-phase phosphoprotein 6 {ECO:0000305};
GN Name=MPHOSPH6 {ECO:0000312|HGNC:HGNC:7214};
GN Synonyms=MPP6 {ECO:0000303|PubMed:26166824};
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].
RC TISSUE=Lymphoblast;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Urinary bladder;
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 [5]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11719186; DOI=10.1016/s0092-8674(01)00578-5;
RA Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M.,
RA Stoecklin G., Moroni C., Mann M., Karin M.;
RT "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.";
RL Cell 107:451-464(2001).
RN [6]
RP INTERACTION WITH ARHGAP18.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [7]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16396833; DOI=10.1093/nar/gki982;
RA Schilders G., Raijmakers R., Raats J.M., Pruijn G.J.;
RT "MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA
RT maturation.";
RL Nucleic Acids Res. 33:6795-6804(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC10 AND MTREX.
RX PubMed=17412707; DOI=10.1093/nar/gkm082;
RA Schilders G., van Dijk E., Pruijn G.J.M.;
RT "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are
RT involved in pre-rRNA processing.";
RL Nucleic Acids Res. 35:2564-2572(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND THR-147, AND
RP IDENTIFICATION BY 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 [13]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=20531386; DOI=10.1038/emboj.2010.121;
RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A.,
RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S.,
RA Stepien P.P., Dziembowski A., Jensen T.H.;
RT "The human core exosome interacts with differentially localized processive
RT RNases: hDIS3 and hDIS3L.";
RL EMBO J. 29:2342-2357(2010).
RN [14]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20531389; DOI=10.1038/emboj.2010.122;
RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
RA Heck A.J., Raijmakers R., Pruijn G.J.;
RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome.";
RL EMBO J. 29:2358-2367(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION BY
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND THR-147, AND
RP IDENTIFICATION BY 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 [18]
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 [19]
RP FUNCTION.
RX PubMed=26166824; DOI=10.1016/j.bbrc.2015.07.032;
RA Yoshikatsu Y., Ishida Y., Sudo H., Yuasa K., Tsuji A., Nagahama M.;
RT "NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and
RT is involved in pre-rRNA processing.";
RL Biochem. Biophys. Res. Commun. 464:780-786(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37; LYS-86; LYS-127 AND LYS-150,
RP AND 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 [22] {ECO:0007744|PDB:6D6Q, ECO:0007744|PDB:6D6R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS), AND SUBUNIT.
RX PubMed=29906447; DOI=10.1016/j.cell.2018.05.041;
RA Weick E.M., Puno M.R., Januszyk K., Zinder J.C., DiMattia M.A., Lima C.D.;
RT "Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human
RT Nuclear RNA Exosome-MTR4 Complex.";
RL Cell 173:1663-1677.e21(2018).
CC -!- FUNCTION: RNA-binding protein that associates with the RNA exosome
CC complex. Involved in the 3'-processing of the 7S pre-RNA to the mature
CC 5.8S rRNA and play a role in recruiting the RNA exosome complex to pre-
CC rRNA; this function may include C1D. {ECO:0000269|PubMed:17412707,
CC ECO:0000269|PubMed:26166824}.
CC -!- SUBUNIT: Associates with the RNA exosome complex, probably mediated by
CC EXOSC10 (PubMed:29906447). Interacts with ARHGAP18, EXOSC10 and MTREX.
CC {ECO:0000269|PubMed:15231747, ECO:0000269|PubMed:17412707,
CC ECO:0000269|PubMed:29906447}.
CC -!- INTERACTION:
CC Q99547; P05067: APP; NbExp=3; IntAct=EBI-373187, EBI-77613;
CC Q99547; Q01780: EXOSC10; NbExp=4; IntAct=EBI-373187, EBI-358236;
CC Q99547; Q13868: EXOSC2; NbExp=3; IntAct=EBI-373187, EBI-301735;
CC Q99547; P42285: MTREX; NbExp=2; IntAct=EBI-373187, EBI-347612;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Cytoplasmic
CC in M phase.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC -!- SIMILARITY: Belongs to the MPP6 family. {ECO:0000305}.
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DR EMBL; X98263; CAA66916.1; -; mRNA.
DR EMBL; AK314163; BAG36847.1; -; mRNA.
DR EMBL; AC138304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005242; AAH05242.1; -; mRNA.
DR EMBL; BC011020; AAH11020.1; -; mRNA.
DR EMBL; BC031017; AAH31017.1; -; mRNA.
DR CCDS; CCDS10937.1; -.
DR RefSeq; NP_005783.2; NM_005792.2.
DR PDB; 6D6Q; EM; 3.45 A; L=1-160.
DR PDB; 6D6R; EM; 3.45 A; L=1-160.
DR PDB; 6H25; EM; 3.80 A; K=1-160.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 6H25; -.
DR AlphaFoldDB; Q99547; -.
DR SMR; Q99547; -.
DR BioGRID; 115495; 71.
DR CORUM; Q99547; -.
DR DIP; DIP-31131N; -.
DR IntAct; Q99547; 37.
DR MINT; Q99547; -.
DR STRING; 9606.ENSP00000258169; -.
DR GlyGen; Q99547; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99547; -.
DR PhosphoSitePlus; Q99547; -.
DR SwissPalm; Q99547; -.
DR BioMuta; MPHOSPH6; -.
DR DMDM; 296438296; -.
DR EPD; Q99547; -.
DR jPOST; Q99547; -.
DR MassIVE; Q99547; -.
DR MaxQB; Q99547; -.
DR PaxDb; Q99547; -.
DR PeptideAtlas; Q99547; -.
DR PRIDE; Q99547; -.
DR ProteomicsDB; 78320; -.
DR Antibodypedia; 3289; 172 antibodies from 25 providers.
DR DNASU; 10200; -.
DR Ensembl; ENST00000258169.9; ENSP00000258169.4; ENSG00000135698.10.
DR GeneID; 10200; -.
DR KEGG; hsa:10200; -.
DR MANE-Select; ENST00000258169.9; ENSP00000258169.4; NM_005792.2; NP_005783.2.
DR UCSC; uc002fgw.4; human.
DR CTD; 10200; -.
DR DisGeNET; 10200; -.
DR GeneCards; MPHOSPH6; -.
DR HGNC; HGNC:7214; MPHOSPH6.
DR HPA; ENSG00000135698; Low tissue specificity.
DR MIM; 605500; gene.
DR neXtProt; NX_Q99547; -.
DR OpenTargets; ENSG00000135698; -.
DR PharmGKB; PA30920; -.
DR VEuPathDB; HostDB:ENSG00000135698; -.
DR eggNOG; KOG4531; Eukaryota.
DR GeneTree; ENSGT00390000009212; -.
DR InParanoid; Q99547; -.
DR OMA; EKLMVLM; -.
DR OrthoDB; 1436304at2759; -.
DR PhylomeDB; Q99547; -.
DR TreeFam; TF323810; -.
DR PathwayCommons; Q99547; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q99547; -.
DR BioGRID-ORCS; 10200; 137 hits in 1077 CRISPR screens.
DR ChiTaRS; MPHOSPH6; human.
DR GeneWiki; MPHOSPH6; -.
DR GenomeRNAi; 10200; -.
DR Pharos; Q99547; Tbio.
DR PRO; PR:Q99547; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q99547; protein.
DR Bgee; ENSG00000135698; Expressed in oocyte and 203 other tissues.
DR ExpressionAtlas; Q99547; baseline and differential.
DR Genevisible; Q99547; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
DR InterPro; IPR019324; MPP6.
DR PANTHER; PTHR13582; PTHR13582; 1.
DR Pfam; PF10175; MPP6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..160
FT /note="M-phase phosphoprotein 6"
FT /id="PRO_0000122437"
FT MOTIF 116..133
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VARIANT 58
FT /note="I -> V (in dbSNP:rs2303267)"
FT /id="VAR_056150"
FT CONFLICT 8
FT /note="R -> K (in Ref. 1; CAA66916, 2; BAG36847 and 4;
FT AAH05242/AAH11020/AAH31017)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:6D6Q"
SQ SEQUENCE 160 AA; 19024 MW; 506D5274C839BD7E CRC64;
MAAERKTRLS KNLLRMKFMQ RGLDSETKKQ LEEEEKKIIS EEHWYLDLPE LKEKESFIIE
EQSFLLCEDL LYGRMSFRGF NPEVEKLMLQ MNAKHKAEEV EDETVELDVS DEEMARRYET
LVGTIGKKFA RKRDHANYEE DENGDITPIK AKKMFLKPQD
