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 02-OCT-2024, entry version 181. 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}; 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; 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 PDB; 8FKP; EM; 2.85 A; SZ=1-178. DR PDB; 8FKQ; EM; 2.76 A; SZ=1-178. DR PDB; 8FKR; EM; 2.89 A; SZ=1-178. DR PDB; 8FKS; EM; 2.88 A; SZ=1-178. DR PDB; 8FKT; EM; 2.81 A; SZ=1-178. DR PDB; 8FKU; EM; 2.82 A; SZ=1-178. DR PDB; 8FKV; EM; 2.47 A; SZ=1-178. DR PDB; 8FKW; EM; 2.50 A; SZ=1-178. DR PDB; 8FKX; EM; 2.59 A; SZ=1-178. DR PDB; 8FKY; EM; 2.67 A; SZ=1-178. DR PDBsum; 8FKP; -. DR PDBsum; 8FKQ; -. DR PDBsum; 8FKR; -. DR PDBsum; 8FKS; -. DR PDBsum; 8FKT; -. DR PDBsum; 8FKU; -. DR PDBsum; 8FKV; -. DR PDBsum; 8FKW; -. DR PDBsum; 8FKX; -. DR PDBsum; 8FKY; -. DR AlphaFoldDB; Q9Y3C1; -. DR EMDB; EMD-29252; -. DR EMDB; EMD-29253; -. DR EMDB; EMD-29254; -. DR EMDB; EMD-29255; -. DR EMDB; EMD-29256; -. DR EMDB; EMD-29257; -. DR EMDB; EMD-29258; -. DR EMDB; EMD-29259; -. DR EMDB; EMD-29260; -. DR EMDB; EMD-29261; -. DR SMR; Q9Y3C1; -. DR BioGRID; 119568; 214. DR IntAct; Q9Y3C1; 129. DR MINT; Q9Y3C1; -. DR STRING; 9606.ENSP00000483001; -. 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 jPOST; Q9Y3C1; -. DR MassIVE; Q9Y3C1; -. DR PaxDb; 9606-ENSP00000480832; -. DR PeptideAtlas; Q9Y3C1; -. DR ProteomicsDB; 14665; -. DR ProteomicsDB; 86010; -. [Q9Y3C1-1] DR Pumba; Q9Y3C1; -. DR TopDownProteomics; Q9Y3C1-1; -. [Q9Y3C1-1] DR Antibodypedia; 29078; 184 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 AGR; HGNC:26934; -. 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; GIPKQYG; -. DR OrthoDB; 2906817at2759; -. DR PhylomeDB; Q9Y3C1; -. DR TreeFam; TF323541; -. DR PathwayCommons; Q9Y3C1; -. DR SignaLink; Q9Y3C1; -. DR BioGRID-ORCS; 51491; 816 hits in 1175 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 203 other cell types or tissues. DR ExpressionAtlas; Q9Y3C1; baseline and differential. 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; HSPC111 PROTEIN-RELATED; 1. DR PANTHER; PTHR13243:SF1; NUCLEOLAR PROTEIN 16; 1. DR Pfam; PF09420; Nop16; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW 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 //