BCD1_HUMAN
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 03-AUG-2022, entry version 151.
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};
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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; 81.
DR IntAct; Q9NWK9; 25.
DR MINT; Q9NWK9; -.
DR STRING; 9606.ENSP00000359606; -.
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; Q9NWK9; -.
DR PeptideAtlas; Q9NWK9; -.
DR PRIDE; Q9NWK9; -.
DR ProteomicsDB; 82943; -. [Q9NWK9-1]
DR ProteomicsDB; 82944; -. [Q9NWK9-2]
DR Antibodypedia; 19797; 117 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 CTD; 54680; -.
DR DisGeNET; 54680; -.
DR GeneCards; ZNHIT6; -.
DR HGNC; HGNC:26089; ZNHIT6.
DR HPA; ENSG00000117174; Low tissue specificity.
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; 678600at2759; -.
DR PhylomeDB; Q9NWK9; -.
DR TreeFam; TF323923; -.
DR PathwayCommons; Q9NWK9; -.
DR SignaLink; Q9NWK9; -.
DR BioGRID-ORCS; 54680; 484 hits in 1090 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 206 other tissues.
DR Genevisible; Q9NWK9; HS.
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 InterPro; IPR007529; Znf_HIT.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
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
