ZN687_HUMAN
ID ZN687_HUMAN Reviewed; 1237 AA.
AC Q8N1G0; D3DV17; Q68DQ8; Q9H937; Q9P2A7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Zinc finger protein 687;
GN Name=ZNF687; Synonyms=KIAA1441;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
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=Brain;
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 [LARGE SCALE MRNA] OF 399-1237 (ISOFORM 2).
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-253; SER-266;
RP SER-271; SER-433; SER-1082; SER-1083; SER-1085; SER-1191 AND SER-1211, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-148 AND SER-495, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-266; SER-1057;
RP SER-1106 AND SER-1118, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-251; SER-253;
RP SER-374; SER-433 AND SER-1057, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-227; SER-242;
RP SER-253; SER-266; SER-271; SER-374; THR-377; SER-433; SER-495; THR-900 AND
RP SER-1057, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-1057 AND SER-1191,
RP AND 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, AND
RP 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, AND
RP IDENTIFICATION BY MASS 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285; LYS-336; LYS-372; LYS-384;
RP LYS-397; LYS-422; LYS-435; LYS-439; LYS-451; LYS-464; LYS-954 AND LYS-1043,
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 [20]
RP VARIANTS PDB6 ILE-242 AND ARG-937, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND CHARACTERIZATION OF VARIANT ARG-937.
RX PubMed=26849110; DOI=10.1016/j.ajhg.2015.12.016;
RA Divisato G., Formicola D., Esposito T., Merlotti D., Pazzaglia L.,
RA Del Fattore A., Siris E., Orcel P., Brown J.P., Nuti R., Strazzullo P.,
RA Benassi M.S., Cancela M.L., Michou L., Rendina D., Gennari L.,
RA Gianfrancesco F.;
RT "ZNF687 mutations in severe paget disease of bone associated with giant
RT cell tumor.";
RL Am. J. Hum. Genet. 98:275-286(2016).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q8N1G0; Q9H2G4: TSPYL2; NbExp=4; IntAct=EBI-1210558, EBI-947459;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26849110}. Nucleus
CC {ECO:0000269|PubMed:26849110}. Note=Predominantly nuclear.
CC {ECO:0000269|PubMed:26849110}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N1G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N1G0-2; Sequence=VSP_018168, VSP_018169;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in obvary,
CC muscle, blood and lung. {ECO:0000269|PubMed:26849110}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during osteoclastogenesis induced by
CC treatment of peripheral blood mononuclear cells with CSF1 and TNFSF11,
CC as well as during osteoblastogenesis. {ECO:0000269|PubMed:26849110}.
CC -!- DISEASE: Paget disease of bone 6 (PDB6) [MIM:616833]: An autosomal
CC dominant form of Paget disease, a disorder of bone remodeling
CC characterized by increased bone turnover affecting one or more sites
CC throughout the skeleton, primarily the axial skeleton. Osteoclastic
CC overactivity followed by compensatory osteoblastic activity leads to a
CC structurally disorganized mosaic of bone (woven bone), which is
CC mechanically weaker, larger, less compact, more vascular, and more
CC susceptible to fracture than normal adult lamellar bone. PDB6 is
CC characterized by adult onset of bone pain associated with polyostotic
CC bone lesions primarily affecting the axial skeleton. In some cases, the
CC pagetic tissue undergoes neoplastic transformation, resulting in
CC osteosarcoma and, less frequently, in giant cell tumor of bone.
CC {ECO:0000269|PubMed:26849110}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92679.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14406.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH18162.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB037862; BAA92679.1; ALT_INIT; mRNA.
DR EMBL; CR749307; CAH18162.1; ALT_FRAME; mRNA.
DR EMBL; AL391069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53452.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53453.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53454.1; -; Genomic_DNA.
DR EMBL; BC032463; AAH32463.1; -; mRNA.
DR EMBL; AK023105; BAB14406.1; ALT_INIT; mRNA.
DR CCDS; CCDS992.1; -. [Q8N1G0-1]
DR RefSeq; NP_001291692.1; NM_001304763.1. [Q8N1G0-1]
DR RefSeq; NP_001291693.1; NM_001304764.1. [Q8N1G0-1]
DR RefSeq; NP_065883.1; NM_020832.2. [Q8N1G0-1]
DR RefSeq; XP_011508114.1; XM_011509812.2. [Q8N1G0-1]
DR RefSeq; XP_011508115.1; XM_011509813.2. [Q8N1G0-1]
DR AlphaFoldDB; Q8N1G0; -.
DR BioGRID; 121643; 91.
DR IntAct; Q8N1G0; 43.
DR MINT; Q8N1G0; -.
DR STRING; 9606.ENSP00000319829; -.
DR GlyGen; Q8N1G0; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8N1G0; -.
DR PhosphoSitePlus; Q8N1G0; -.
DR BioMuta; ZNF687; -.
DR DMDM; 74759771; -.
DR EPD; Q8N1G0; -.
DR jPOST; Q8N1G0; -.
DR MassIVE; Q8N1G0; -.
DR MaxQB; Q8N1G0; -.
DR PaxDb; Q8N1G0; -.
DR PeptideAtlas; Q8N1G0; -.
DR PRIDE; Q8N1G0; -.
DR ProteomicsDB; 71597; -. [Q8N1G0-1]
DR ProteomicsDB; 71598; -. [Q8N1G0-2]
DR Antibodypedia; 20323; 94 antibodies from 21 providers.
DR DNASU; 57592; -.
DR Ensembl; ENST00000324048.9; ENSP00000319829.5; ENSG00000143373.18. [Q8N1G0-1]
DR Ensembl; ENST00000336715.11; ENSP00000336620.5; ENSG00000143373.18. [Q8N1G0-1]
DR GeneID; 57592; -.
DR KEGG; hsa:57592; -.
DR MANE-Select; ENST00000336715.11; ENSP00000336620.5; NM_020832.3; NP_065883.1.
DR UCSC; uc001exq.4; human. [Q8N1G0-1]
DR CTD; 57592; -.
DR DisGeNET; 57592; -.
DR GeneCards; ZNF687; -.
DR HGNC; HGNC:29277; ZNF687.
DR HPA; ENSG00000143373; Low tissue specificity.
DR MalaCards; ZNF687; -.
DR MIM; 610568; gene.
DR MIM; 616833; phenotype.
DR neXtProt; NX_Q8N1G0; -.
DR OpenTargets; ENSG00000143373; -.
DR Orphanet; 280110; NON RARE IN EUROPE: Paget disease of bone.
DR PharmGKB; PA142670486; -.
DR VEuPathDB; HostDB:ENSG00000143373; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156524; -.
DR HOGENOM; CLU_006283_1_0_1; -.
DR InParanoid; Q8N1G0; -.
DR OMA; TSWPGSD; -.
DR OrthoDB; 438804at2759; -.
DR PhylomeDB; Q8N1G0; -.
DR TreeFam; TF329009; -.
DR PathwayCommons; Q8N1G0; -.
DR SignaLink; Q8N1G0; -.
DR BioGRID-ORCS; 57592; 182 hits in 1052 CRISPR screens.
DR ChiTaRS; ZNF687; human.
DR GeneWiki; ZNF687; -.
DR GenomeRNAi; 57592; -.
DR Pharos; Q8N1G0; Tbio.
DR PRO; PR:Q8N1G0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N1G0; protein.
DR Bgee; ENSG00000143373; Expressed in kidney epithelium and 129 other tissues.
DR ExpressionAtlas; Q8N1G0; baseline and differential.
DR Genevisible; Q8N1G0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222; PTHR47222; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1237
FT /note="Zinc finger protein 687"
FT /id="PRO_0000234005"
FT ZN_FING 533..552
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 705..727
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..787
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..815
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 827..849
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 858..881
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 963..986
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 993..1016
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1135..1158
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1200..1222
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2D7"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 900
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1060
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2D7"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1101
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2D7"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2D7"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 285
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:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 336
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:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 397
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 451
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 954
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1027..1103
FT /note="YCTEGKRTFSSRLILEKHVQVRHGLQLGAQSPGRGTTLARGSSARAQGPGRK
FT RRQSSDSCSEEPDSTTPPAKSPRGG -> SKGPGLRAVPLLPSCPLPFQVLHRGKTHLQ
FT QPPDPRETCPGPARLAAWGPVPWPGDHLGSGFQCQSPGARSETPPVF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018168"
FT VAR_SEQ 1104..1237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018169"
FT VARIANT 242
FT /note="S -> I (in PDB6; unknown pathological significance;
FT dbSNP:rs869025582)"
FT /evidence="ECO:0000269|PubMed:26849110"
FT /id="VAR_076534"
FT VARIANT 259
FT /note="G -> E (in dbSNP:rs3748545)"
FT /id="VAR_052894"
FT VARIANT 344
FT /note="R -> T (in dbSNP:rs12045766)"
FT /id="VAR_052895"
FT VARIANT 937
FT /note="P -> R (in PDB6; enhances nuclear localization;
FT increases expression levels; R-937 containing osteoclasts
FT induced by treatment of peripheral blood mononuclear cells
FT with CSF1 and TNFSF11 exhibit a greater number of nuclei,
FT as well as a larger surface area than did those from the
FT control individuals; dbSNP:rs148402804)"
FT /evidence="ECO:0000269|PubMed:26849110"
FT /id="VAR_076535"
FT CONFLICT 331
FT /note="R -> W (in Ref. 2; CAH18162)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="K -> E (in Ref. 6; BAB14406)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="R -> G (in Ref. 6; BAB14406)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> V (in Ref. 2; CAH18162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1237 AA; 129529 MW; D2DC99AA2AF44270 CRC64;
MGDMKTPDFD DLLAAFDIPD IDANEAIHSG PEENEGPGGP GKPEPGVGSE SEDTAAASAG
DGPGVPAQAS DHGLPPPDIS VVSVIVKNTV CPEQSEALAG GSAGDGAQAA GVTKEGPVGP
HRMQNGFGSP EPSLPGTPHS PAPPSGGTWK EKGMEGKTPL DLFAHFGPEP GDHSDPLPPS
APSPTREGAL TPPPFPSSFE LAQENGPGMQ PPVSSPPLGA LKQESCSPHH PQVLAQQGSG
SSPKATDIPA SASPPPVAGV PFFKQSPGHQ SPLASPKVPV CQPLKEEDDD EGPVDKSSPG
SPQSPSSGAE AADEDSNDSP ASSSSRPLKV RIKTIKTSCG NITRTVTQVP SDPDPPAPLA
EGAFLAEASL LKLSPATPTS EGPKVVSVQL GDGTRLKGTV LPVATIQNAS TAMLMAASVA
RKAVVLPGGT ATSPKMIAKN VLGLVPQALP KADGRAGLGT GGQKVNGASV VMVQPSKTAT
GPSTGGGTVI SRTQSSLVEA FNKILNSKNL LPAYRPNLSP PAEAGLALPP TGYRCLECGD
AFSLEKSLAR HYDRRSMRIE VTCNHCARRL VFFNKCSLLL HAREHKDKGL VMQCSHLVMR
PVALDQMVGQ PDITPLLPVA VPPVSGPLAL PALGKGEGAI TSSAITTVAA EAPVLPLSTE
PPAAPATSAY TCFRCLECKE QCRDKAGMAA HFQQLGPPAP GATSNVCPTC PMMLPNRCSF
SAHQRMHKNR PPHVCPECGG NFLQANFQTH LREACLHVSR RVGYRCPSCS VVFGGVNSIK
SHIQTSHCEV FHKCPICPMA FKSGPSAHAH LYSQHPSFQT QQAKLIYKCA MCDTVFTHKP
LLSSHFDQHL LPQRVSVFKC PSCPLLFAQK RTMLEHLKNT HQSGRLEETA GKGAGGALLT
PKTEPEELAV SQGGAAPATE ESSSSSEEEE VPSSPEPPRP AKRPRRELGS KGLKGGGGGP
GGWTCGLCHS WFPERDEYVA HMKKEHGKSV KKFPCRLCER SFCSAPSLRR HVRVNHEGIK
RVYPCRYCTE GKRTFSSRLI LEKHVQVRHG LQLGAQSPGR GTTLARGSSA RAQGPGRKRR
QSSDSCSEEP DSTTPPAKSP RGGPGSGGHG PLRYRSSSST EQSLMMGLRV EDGAQQCLDC
GLCFASPGSL SRHRFISHKK RRGVGKASAL GLGDGEEEAP PSRSDPDGGD SPLPASGGPL
TCKVCGKSCD SPLNLKTHFR THGMAFIRAR QGAVGDN
