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NOP16_HUMAN
ID   NOP16_HUMAN             Reviewed;         178 AA.
AC   Q9Y3C1; B4DV13; D6RGD3; Q05D05; Q6IAI6; Q6PIM0; Q8IXL5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Nucleolar protein 16;
DE   AltName: Full=HBV pre-S2 trans-regulated protein 3;
GN   Name=NOP16; ORFNames=CGI-117, HSPC111;
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).
RA   Ji D., Cheng J., Dong J., Liu Y., Wang J.-J., Guo J.;
RT   "Screening and identification of genes trans-regulated by hepatitis B virus
RT   pre-S2 protein by microarray assay.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Small intestine;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Lung, Mammary gland, and Skin;
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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-144, AND
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, 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].
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-74, SUMOYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-166 AND LYS-172 (ISOFORM 2), SUMOYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-167 AND LYS-173 (ISOFORM 3), 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).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y3C1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y3C1-2; Sequence=VSP_045583;
CC       Name=3;
CC         IsoId=Q9Y3C1-3; Sequence=VSP_057393;
CC   -!- SIMILARITY: Belongs to the NOP16 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19331.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAG62525.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=EAW85085.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY561704; AAS66977.1; -; mRNA.
DR   EMBL; AF151875; AAD34112.1; -; mRNA.
DR   EMBL; AF161460; AAF29075.1; -; mRNA.
DR   EMBL; AK300883; BAG62525.1; ALT_FRAME; mRNA.
DR   EMBL; CR457169; CAG33450.1; -; mRNA.
DR   EMBL; AC138956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471195; EAW85084.1; -; Genomic_DNA.
DR   EMBL; CH471195; EAW85085.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BC019331; AAH19331.1; ALT_FRAME; mRNA.
DR   EMBL; BC032424; AAH32424.1; -; mRNA.
DR   EMBL; BC040106; AAH40106.1; -; mRNA.
DR   CCDS; CCDS43403.1; -. [Q9Y3C1-1]
DR   CCDS; CCDS78091.1; -. [Q9Y3C1-3]
DR   RefSeq; NP_001243468.2; NM_001256539.3. [Q9Y3C1-3]
DR   RefSeq; NP_001243469.2; NM_001256540.3.
DR   RefSeq; NP_001278234.1; NM_001291305.2.
DR   RefSeq; NP_001278236.1; NM_001291307.2.
DR   RefSeq; NP_001278237.1; NM_001291308.2.
DR   RefSeq; NP_001304904.1; NM_001317975.1.
DR   RefSeq; NP_057475.2; NM_016391.7. [Q9Y3C1-1]
DR   AlphaFoldDB; Q9Y3C1; -.
DR   SMR; Q9Y3C1; -.
DR   BioGRID; 119568; 183.
DR   IntAct; Q9Y3C1; 60.
DR   MINT; Q9Y3C1; -.
DR   STRING; 9606.ENSP00000480832; -.
DR   GlyGen; Q9Y3C1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3C1; -.
DR   MetOSite; Q9Y3C1; -.
DR   PhosphoSitePlus; Q9Y3C1; -.
DR   SwissPalm; Q9Y3C1; -.
DR   BioMuta; NOP16; -.
DR   DMDM; 115311631; -.
DR   SWISS-2DPAGE; Q9Y3C1; -.
DR   EPD; Q9Y3C1; -.
DR   jPOST; Q9Y3C1; -.
DR   MassIVE; Q9Y3C1; -.
DR   MaxQB; Q9Y3C1; -.
DR   PaxDb; Q9Y3C1; -.
DR   PeptideAtlas; Q9Y3C1; -.
DR   PRIDE; Q9Y3C1; -.
DR   ProteomicsDB; 14665; -.
DR   ProteomicsDB; 86010; -. [Q9Y3C1-1]
DR   TopDownProteomics; Q9Y3C1-1; -. [Q9Y3C1-1]
DR   Antibodypedia; 29078; 166 antibodies from 23 providers.
DR   DNASU; 51491; -.
DR   Ensembl; ENST00000614830.5; ENSP00000480832.2; ENSG00000048162.22. [Q9Y3C1-1]
DR   Ensembl; ENST00000618911.4; ENSP00000483001.1; ENSG00000048162.22. [Q9Y3C1-3]
DR   GeneID; 51491; -.
DR   KEGG; hsa:51491; -.
DR   MANE-Select; ENST00000614830.5; ENSP00000480832.2; NM_016391.8; NP_057475.2.
DR   UCSC; uc032vuv.2; human. [Q9Y3C1-1]
DR   UCSC; uc063jyi.1; human.
DR   CTD; 51491; -.
DR   DisGeNET; 51491; -.
DR   GeneCards; NOP16; -.
DR   HGNC; HGNC:26934; NOP16.
DR   HPA; ENSG00000048162; Low tissue specificity.
DR   MIM; 612861; gene.
DR   neXtProt; NX_Q9Y3C1; -.
DR   OpenTargets; ENSG00000048162; -.
DR   PharmGKB; PA164724025; -.
DR   VEuPathDB; HostDB:ENSG00000048162; -.
DR   eggNOG; KOG4706; Eukaryota.
DR   GeneTree; ENSGT00390000003426; -.
DR   HOGENOM; CLU_115103_0_0_1; -.
DR   InParanoid; Q9Y3C1; -.
DR   OMA; MRSVKHG; -.
DR   OrthoDB; 1431164at2759; -.
DR   PhylomeDB; Q9Y3C1; -.
DR   TreeFam; TF323541; -.
DR   PathwayCommons; Q9Y3C1; -.
DR   SignaLink; Q9Y3C1; -.
DR   BioGRID-ORCS; 51491; 780 hits in 1088 CRISPR screens.
DR   ChiTaRS; NOP16; human.
DR   GenomeRNAi; 51491; -.
DR   Pharos; Q9Y3C1; Tdark.
DR   PRO; PR:Q9Y3C1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y3C1; protein.
DR   Bgee; ENSG00000048162; Expressed in gastrocnemius and 201 other tissues.
DR   ExpressionAtlas; Q9Y3C1; baseline and differential.
DR   Genevisible; Q9Y3C1; HS.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   InterPro; IPR019002; Ribosome_biogenesis_Nop16.
DR   PANTHER; PTHR13243; PTHR13243; 1.
DR   Pfam; PF09420; Nop16; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..178
FT                   /note="Nucleolar protein 16"
FT                   /id="PRO_0000050817"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         90
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         144
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         132..178
FT                   /note="AMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE -> S
FT                   GKTSSILCRRGRWRWSDWFTSQLPQAEASPGPVKLEPGCKARRCCVAPEELARSHGIRR
FT                   LHTRAHSPLWGRNCSQRLQFIFIWGFTEKPEPAVFRVGDVNIVCT (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045583"
FT   VAR_SEQ         132..178
FT                   /note="AMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE -> Q
FT                   SGKTSSILCRRGRWRWSDWFTSQLPQAEASPGPVKLEPGCKARRCCVAPEELARSHGIR
FT                   RLHTHVHTPRSGEGTVLRGSNLYSSGGSRKSQNLLFSGWVM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057393"
FT   CONFLICT        32..33
FT                   /note="PR -> RG (in Ref. 2; AAD34112 and 3; AAF29075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="E -> D (in Ref. 5; CAG33450)"
FT                   /evidence="ECO:0000305"
FT   CROSSLNK        Q9Y3C1-2:166
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        Q9Y3C1-2:172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CONFLICT        Q9Y3C1-2:171
FT                   /note="C -> F (in Ref. 4; BAG62525)"
FT                   /evidence="ECO:0000305"
FT   CROSSLNK        Q9Y3C1-3:167
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        Q9Y3C1-3:173
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   178 AA;  21188 MW;  D9139BE32DA81FC5 CRC64;
     MPKAKGKTRR QKFGYSVNRK RLNRNARRKA APRIECSHIR HAWDHAKSVR QNLAEMGLAV
     DPNRAVPLRK RKVKAMEVDI EERPKELVRK PYVLNDLEAE ASLPEKKGNT LSRDLIDYVR
     YMVENHGEDY KAMARDEKNY YQDTPKQIRS KINVYKRFYP AEWQDFLDSL QKRKMEVE
 
 
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