ZN649_HUMAN
ID ZN649_HUMAN Reviewed; 505 AA.
AC Q9BS31; A8MYJ5; B2RDC4; Q9H9N2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Zinc finger protein 649;
GN Name=ZNF649;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15950191; DOI=10.1016/j.bbrc.2005.05.101;
RA Yang H., Yuan W., Wang Y., Zhu C., Liu B., Wang Y., Yang D., Li Y.,
RA Wang C., Wu X., Liu M.;
RT "ZNF649, a novel Kruppel type zinc-finger protein, functions as a
RT transcriptional suppressor.";
RL Biochem. Biophys. Res. Commun. 333:206-215(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112, 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 -!- FUNCTION: Transcriptional repressor. Regulator of transcriptional
CC factor complexes and may suppress SRE and AP-1 transcription activities
CC mediated by growth factor signaling pathways.
CC {ECO:0000269|PubMed:15950191}.
CC -!- INTERACTION:
CC Q9BS31; P02545: LMNA; NbExp=3; IntAct=EBI-4395789, EBI-351935;
CC Q9BS31; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-4395789, EBI-5235340;
CC Q9BS31; O43463: SUV39H1; NbExp=2; IntAct=EBI-4395789, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15950191}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, and
CC brain. Lower expression in liver, lung, kidney, pancreas and placenta.
CC {ECO:0000269|PubMed:15950191}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal heart, brain, placenta, lung,
CC liver, skeletal muscle, kidney, and pancreas.
CC {ECO:0000269|PubMed:15950191}.
CC -!- DOMAIN: The KRAB domain is required for transcriptional repression.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK022706; BAB14191.1; -; mRNA.
DR EMBL; AK315487; BAG37871.1; -; mRNA.
DR EMBL; AL713677; CAD28482.1; -; mRNA.
DR EMBL; AC011460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72050.1; -; Genomic_DNA.
DR EMBL; BC005368; AAH05368.1; -; mRNA.
DR CCDS; CCDS12843.1; -.
DR RefSeq; NP_075562.2; NM_023074.3.
DR AlphaFoldDB; Q9BS31; -.
DR SMR; Q9BS31; -.
DR BioGRID; 122414; 8.
DR IntAct; Q9BS31; 6.
DR MINT; Q9BS31; -.
DR STRING; 9606.ENSP00000347043; -.
DR iPTMnet; Q9BS31; -.
DR PhosphoSitePlus; Q9BS31; -.
DR BioMuta; ZNF649; -.
DR DMDM; 74761227; -.
DR EPD; Q9BS31; -.
DR jPOST; Q9BS31; -.
DR MassIVE; Q9BS31; -.
DR MaxQB; Q9BS31; -.
DR PaxDb; Q9BS31; -.
DR PeptideAtlas; Q9BS31; -.
DR PRIDE; Q9BS31; -.
DR ProteomicsDB; 78862; -.
DR Antibodypedia; 19056; 100 antibodies from 19 providers.
DR DNASU; 65251; -.
DR Ensembl; ENST00000354957.8; ENSP00000347043.2; ENSG00000198093.11.
DR GeneID; 65251; -.
DR KEGG; hsa:65251; -.
DR MANE-Select; ENST00000354957.8; ENSP00000347043.2; NM_023074.4; NP_075562.2.
DR UCSC; uc002pxy.4; human.
DR CTD; 65251; -.
DR DisGeNET; 65251; -.
DR GeneCards; ZNF649; -.
DR HGNC; HGNC:25741; ZNF649.
DR HPA; ENSG00000198093; Low tissue specificity.
DR MIM; 611903; gene.
DR neXtProt; NX_Q9BS31; -.
DR OpenTargets; ENSG00000198093; -.
DR PharmGKB; PA143485678; -.
DR VEuPathDB; HostDB:ENSG00000198093; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164046; -.
DR InParanoid; Q9BS31; -.
DR OMA; AFTTKTM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9BS31; -.
DR TreeFam; TF340593; -.
DR PathwayCommons; Q9BS31; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9BS31; -.
DR BioGRID-ORCS; 65251; 8 hits in 1098 CRISPR screens.
DR ChiTaRS; ZNF649; human.
DR GeneWiki; ZNF649; -.
DR GenomeRNAi; 65251; -.
DR Pharos; Q9BS31; Tdark.
DR PRO; PR:Q9BS31; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BS31; protein.
DR Bgee; ENSG00000198093; Expressed in corpus callosum and 108 other tissues.
DR ExpressionAtlas; Q9BS31; baseline and differential.
DR Genevisible; Q9BS31; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..505
FT /note="Zinc finger protein 649"
FT /id="PRO_0000251224"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 178..200
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..228
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..284
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..368
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 455..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 352
FT /note="G -> D (in dbSNP:rs6509593)"
FT /id="VAR_027668"
FT VARIANT 469
FT /note="A -> T (in dbSNP:rs1433083)"
FT /id="VAR_027669"
FT CONFLICT 8
FT /note="L -> V (in Ref. 2; BAB14191)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="G -> E (in Ref. 2; BAB14191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 57683 MW; EC1A70DCA8E01613 CRC64;
MTKAQESLTL EDVAVDFTWE EWQFLSPAQK DLYRDVMLEN YSNLVSVGYQ AGKPDALTKL
EQGEPLWTLE DEIHSPAHPE IEKADDHLQQ PLQNQKILKR TGQRYEHGRT LKSYLGLTNQ
SRRYNRKEPA EFNGDGAFLH DNHEQMPTEI EFPESRKPIS TKSQFLKHQQ THNIEKAHEC
TDCGKAFLKK SQLTEHKRIH TGKKPHVCSL CGKAFYKKYR LTEHERAHRG EKPHGCSLCG
KAFYKRYRLT EHERAHKGEK PYGCSECGKA FPRKSELTEH QRIHTGIKPH QCSECGRAFS
RKSLLVVHQR THTGEKPHTC SECGKGFIQK GNLNIHQRTH TGEKPYGCID CGKAFSQKSC
LVAHQRYHTG KTPFVCPECG QPCSQKSGLI RHQKIHSGEK PYKCSDCGKA FLTKTMLIVH
HRTHTGERPY GCDECEKAYF YMSCLVKHKR IHSREKRGDS VKVENPSTAS HSLSPSEHVQ
GKSPVNMVTV AMVAGQCEFA HILHS
