ID BCD1_HUMAN Reviewed; 470 AA. AC Q9NWK9; B2RBA1; B4DP13; D3DT20; Q9H278; Q9H3X3; Q9NWN0; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Box C/D snoRNA protein 1; DE AltName: Full=Serologically defined breast cancer antigen NY-BR-75; DE AltName: Full=Zinc finger HIT domain-containing protein 6; GN Name=ZNHIT6; Synonyms=BCD1, C1orf181; 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Hepatoma, and Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 69-470 (ISOFORM 1). RC TISSUE=Mammary gland; RX PubMed=12747765; RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.; RT "Humoral immunity to human breast cancer: antigen definition and RT quantitative analysis of mRNA expression."; RL Cancer Immun. 1:4-4(2001). RN [7] RP FUNCTION, AND INTERACTION WITH FBL; SNU13; NOP58; NUFIP1; RUVBL1; RUVBL2 RP AND TAF9. RX PubMed=17636026; DOI=10.1128/mcb.01097-07; RA McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.; RT "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP RT assembly."; RL Mol. Cell. Biol. 27:6782-6793(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY RP 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 [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143; LYS-162; LYS-200 AND RP LYS-459, AND 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 [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-200, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [13] RP INTERACTION WITH RUVBL1/RUVBL2 COMPLEX. RX PubMed=28561026; DOI=10.1038/ncomms15615; RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E., RA Bouchard A., Faubert D., Chabot B., Coulombe B.; RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 RT to regulate assembly of U5 small nuclear ribonucleoprotein."; RL Nat. Commun. 8:15615-15615(2017). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-108; LYS-118; LYS-138; RP LYS-143; LYS-153; LYS-162; LYS-173; LYS-183; LYS-200 AND LYS-459, 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 [15] RP VARIANT [LARGE SCALE ANALYSIS] HIS-455. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA CC processing, snoRNA transport to the nucleolus and ribosome biogenesis. CC {ECO:0000269|PubMed:17636026}. CC -!- SUBUNIT: Interacts with FBL, SNU13, NOP58, NUFIP1, RUVBL1, RUVBL2 and CC TAF9 (PubMed:17636026). Interacts (via HIT-type zinc finger) with the CC RUVBL1/RUVBL2 complex in the presence of ADP (PubMed:28561026). CC {ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:28561026}. CC -!- INTERACTION: CC Q9NWK9; Q9UHK0: NUFIP1; NbExp=2; IntAct=EBI-2563515, EBI-2563549; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NWK9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NWK9-2; Sequence=VSP_042946; CC -!- SIMILARITY: Belongs to the BCD1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG48263.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA91349.1; Type=Erroneous initiation; 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; AK000736; BAA91349.1; ALT_INIT; mRNA. DR EMBL; AK000767; BAA91371.1; -; mRNA. DR EMBL; AK298149; BAG60425.1; -; mRNA. DR EMBL; AK314566; BAG37148.1; -; mRNA. DR EMBL; AL442074; CAC09440.1; -; mRNA. DR EMBL; AC092807; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099561; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX323040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW73194.1; -; Genomic_DNA. DR EMBL; CH471097; EAW73195.1; -; Genomic_DNA. DR EMBL; BC026236; AAH26236.1; -; mRNA. DR EMBL; BC110898; AAI10899.1; -; mRNA. DR EMBL; AF308296; AAG48263.1; ALT_FRAME; mRNA. DR CCDS; CCDS53338.1; -. [Q9NWK9-2] DR CCDS; CCDS707.1; -. [Q9NWK9-1] DR RefSeq; NP_001164141.1; NM_001170670.1. [Q9NWK9-2] DR RefSeq; NP_060423.3; NM_017953.3. [Q9NWK9-1] DR AlphaFoldDB; Q9NWK9; -. DR SMR; Q9NWK9; -. DR BioGRID; 120099; 93. DR IntAct; Q9NWK9; 25. DR MINT; Q9NWK9; -. DR STRING; 9606.ENSP00000359606; -. DR GlyCosmos; Q9NWK9; 1 site, 1 glycan. DR GlyGen; Q9NWK9; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; Q9NWK9; -. DR PhosphoSitePlus; Q9NWK9; -. DR BioMuta; ZNHIT6; -. DR DMDM; 74753026; -. DR EPD; Q9NWK9; -. DR jPOST; Q9NWK9; -. DR MassIVE; Q9NWK9; -. DR MaxQB; Q9NWK9; -. DR PaxDb; 9606-ENSP00000359606; -. DR PeptideAtlas; Q9NWK9; -. DR ProteomicsDB; 82943; -. [Q9NWK9-1] DR ProteomicsDB; 82944; -. [Q9NWK9-2] DR Pumba; Q9NWK9; -. DR Antibodypedia; 19797; 128 antibodies from 22 providers. DR DNASU; 54680; -. DR Ensembl; ENST00000370574.4; ENSP00000359606.3; ENSG00000117174.11. [Q9NWK9-1] DR Ensembl; ENST00000431532.6; ENSP00000414344.2; ENSG00000117174.11. [Q9NWK9-2] DR GeneID; 54680; -. DR KEGG; hsa:54680; -. DR MANE-Select; ENST00000370574.4; ENSP00000359606.3; NM_017953.4; NP_060423.3. DR UCSC; uc001dlh.4; human. [Q9NWK9-1] DR AGR; HGNC:26089; -. DR CTD; 54680; -. DR DisGeNET; 54680; -. DR GeneCards; ZNHIT6; -. DR HGNC; HGNC:26089; ZNHIT6. DR HPA; ENSG00000117174; Low tissue specificity. DR MIM; 620473; gene. DR neXtProt; NX_Q9NWK9; -. DR OpenTargets; ENSG00000117174; -. DR PharmGKB; PA162410929; -. DR VEuPathDB; HostDB:ENSG00000117174; -. DR eggNOG; KOG2858; Eukaryota. DR GeneTree; ENSGT00390000017201; -. DR HOGENOM; CLU_583884_0_0_1; -. DR InParanoid; Q9NWK9; -. DR OMA; CWHVKLL; -. DR OrthoDB; 162842at2759; -. DR PhylomeDB; Q9NWK9; -. DR TreeFam; TF323923; -. DR PathwayCommons; Q9NWK9; -. DR SignaLink; Q9NWK9; -. DR BioGRID-ORCS; 54680; 515 hits in 1167 CRISPR screens. DR ChiTaRS; ZNHIT6; human. DR GenomeRNAi; 54680; -. DR Pharos; Q9NWK9; Tbio. DR PRO; PR:Q9NWK9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NWK9; Protein. DR Bgee; ENSG00000117174; Expressed in tibia and 208 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:UniProtKB. DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:BHF-UCL. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0051259; P:protein complex oligomerization; IMP:UniProtKB. DR GO; GO:0048254; P:snoRNA localization; IMP:UniProtKB. DR CDD; cd19757; Bbox1; 1. DR Gene3D; 3.30.60.190; -; 1. DR InterPro; IPR007529; Znf_HIT. DR PANTHER; PTHR13483:SF3; BOX C_D SNORNA PROTEIN 1; 1. DR PANTHER; PTHR13483; UNCHARACTERIZED; 1. DR Pfam; PF04438; zf-HIT; 1. DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1. DR PROSITE; PS51083; ZF_HIT; 1. DR Genevisible; Q9NWK9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Isopeptide bond; Metal-binding; Phosphoprotein; KW Reference proteome; Ribosome biogenesis; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..470 FT /note="Box C/D snoRNA protein 1" FT /id="PRO_0000280239" FT ZN_FING 220..254 FT /note="HIT-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 223 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 232 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 235 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 248 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 79 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 108 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 118 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 138 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 143 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 153 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 162 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 173 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 183 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 200 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 459 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 VAR_SEQ 78..116 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042946" FT VARIANT 9 FT /note="G -> R (in dbSNP:rs17399721)" FT /id="VAR_031096" FT VARIANT 455 FT /note="L -> H (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035721" FT CONFLICT 144 FT /note="E -> G (in Ref. 2; CAC09440)" FT /evidence="ECO:0000305" SQ SEQUENCE 470 AA; 53918 MW; 34A50A1C62E4F4E8 CRC64; MEFAAENEGK SGGGLHSVAE GVRLSPEPGR EGVRDLAGAE EFGGGEEGTG LTGIKEIGDG EEGSGQRPEE IPMDLTVVKQ EIIDWPGTEG RLAGQWVEQE VEDRPEVKDE NAGVLEVKQE TDSSLVVKEA KVGEPEVKEE KVKEEVMDWS EVKEEKDNLE IKQEEKFVGQ CIKEELMHGE CVKEEKDFLK KEIVDDTKVK EEPPINHPVG CKRKLAMSRC ETCGTEEAKY RCPRCMRYSC SLPCVKKHKA ELTCNGVRDK TAYISIQQFT EMNLLSDYRF LEDVARTADH ISRDAFLKRP ISNKYMYFMK NRARRQGINL KLLPNGFTKR KENSTFFDKK KQQFCWHVKL QFPQSQAEYI EKRVPDDKTI NEILKPYIDP EKSDPVIRQR LKAYIRSQTG VQILMKIEYM QQNLVRYYEL DPYKSLLDNL RNKVIIEYPT LHVVLKGSNN DMKVLHQVKS ESTKNVGNEN //