ZF69B_HUMAN
ID ZF69B_HUMAN Reviewed; 534 AA.
AC Q9UJL9; Q5QPL4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Zinc finger protein 69 homolog B;
DE AltName: Full=Zinc finger protein 643;
GN Name=ZFP69B; Synonyms=ZNF643;
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 2).
RA Rhodes S., Huckle E.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-86 (ISOFORM 1).
RX PubMed=15146197; DOI=10.1038/nbt971;
RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA Stanton L.W.;
RT "Transcriptome characterization elucidates signaling networks that control
RT human ES cell growth and differentiation.";
RL Nat. Biotechnol. 22:707-716(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-534 (ISOFORM 1).
RC TISSUE=B-cell;
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37; LYS-40; LYS-178 AND LYS-235,
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29851555; DOI=10.1091/mbc.e17-11-0693;
RA Serebrenik Y.V., Hellerschmied D., Toure M., Lopez-Giraldez F.,
RA Brookner D., Crews C.M.;
RT "Targeted protein unfolding uncovers a Golgi-specific transcriptional
RT stress response.";
RL Mol. Biol. Cell 29:1284-1298(2018).
CC -!- FUNCTION: May be involved in transcriptional regulation. Essential for
CC Golgi structural integrity (PubMed:29851555).
CC {ECO:0000269|PubMed:29851555}.
CC -!- INTERACTION:
CC Q9UJL9; Q6A162: KRT40; NbExp=3; IntAct=EBI-10322364, EBI-10171697;
CC Q9UJL9; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10322364, EBI-1567797;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29851555}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJL9-2; Sequence=VSP_041647;
CC -!- INDUCTION: Up-regulated by Golgi stress-inducing agent nigericin.
CC {ECO:0000269|PubMed:29851555}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17498.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL137241; CAB70626.1; -; mRNA.
DR EMBL; AL031985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CN256362; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017498; AAH17498.1; ALT_INIT; mRNA.
DR CCDS; CCDS452.2; -. [Q9UJL9-1]
DR RefSeq; NP_075558.2; NM_023070.2. [Q9UJL9-1]
DR RefSeq; XP_005271194.1; XM_005271137.2.
DR RefSeq; XP_005271196.1; XM_005271139.3. [Q9UJL9-2]
DR AlphaFoldDB; Q9UJL9; -.
DR SMR; Q9UJL9; -.
DR BioGRID; 122409; 12.
DR IntAct; Q9UJL9; 4.
DR STRING; 9606.ENSP00000399664; -.
DR iPTMnet; Q9UJL9; -.
DR PhosphoSitePlus; Q9UJL9; -.
DR BioMuta; ZFP69B; -.
DR DMDM; 342187319; -.
DR jPOST; Q9UJL9; -.
DR MassIVE; Q9UJL9; -.
DR PaxDb; Q9UJL9; -.
DR PeptideAtlas; Q9UJL9; -.
DR PRIDE; Q9UJL9; -.
DR Antibodypedia; 32086; 101 antibodies from 15 providers.
DR DNASU; 65243; -.
DR Ensembl; ENST00000361584.5; ENSP00000354547.4; ENSG00000187801.15. [Q9UJL9-1]
DR Ensembl; ENST00000411995.6; ENSP00000399664.2; ENSG00000187801.15. [Q9UJL9-1]
DR GeneID; 65243; -.
DR KEGG; hsa:65243; -.
DR MANE-Select; ENST00000361584.5; ENSP00000354547.4; NM_023070.3; NP_075558.2.
DR UCSC; uc001cfn.3; human. [Q9UJL9-1]
DR CTD; 65243; -.
DR DisGeNET; 65243; -.
DR GeneCards; ZFP69B; -.
DR HGNC; HGNC:28053; ZFP69B.
DR HPA; ENSG00000187801; Low tissue specificity.
DR neXtProt; NX_Q9UJL9; -.
DR OpenTargets; ENSG00000187801; -.
DR VEuPathDB; HostDB:ENSG00000187801; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163434; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; Q9UJL9; -.
DR OMA; QRMGEGQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UJL9; -.
DR TreeFam; TF337055; -.
DR PathwayCommons; Q9UJL9; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9UJL9; -.
DR BioGRID-ORCS; 65243; 290 hits in 1098 CRISPR screens.
DR GenomeRNAi; 65243; -.
DR Pharos; Q9UJL9; Tdark.
DR PRO; PR:Q9UJL9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UJL9; protein.
DR Bgee; ENSG00000187801; Expressed in cortical plate and 104 other tissues.
DR ExpressionAtlas; Q9UJL9; baseline and differential.
DR Genevisible; Q9UJL9; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; IPR003309; SCAN_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..534
FT /note="Zinc finger protein 69 homolog B"
FT /id="PRO_0000047697"
FT DOMAIN 74..145
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 279..301
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..385
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 391..413
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 419..441
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 447..469
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 475..497
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 503..525
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_041647"
FT VARIANT 115
FT /note="C -> Y (in dbSNP:rs2272994)"
FT /id="VAR_033584"
FT VARIANT 359
FT /note="G -> R (in dbSNP:rs12407929)"
FT /id="VAR_052884"
SQ SEQUENCE 534 AA; 61481 MW; 7F63EF062570CEBE CRC64;
MLQQLLITLP TEASTWVKLR HPKAATERVA LWEDVTKMFK AEALLSQDAD ETQGESLESR
VTLGSLTAES QELLTFKDVS VDFTQEEWGQ LAPAHRNLYR EVMLENYGNL VSVGCQLSKP
GVISQLEKGE EPWLMERDIS GVPSSDLKSK TKTKESALQN DISWEELHCG LMMERFTKGS
SMYSTLGRIS KCNKLESQQE NQRMGKGQIP LMCKKTFTQE RGQESNRFEK RINVKSEVMP
GPIGLPRKRD RKYDTPGKRS RYNIDLVNHS RSYTKMKTFE CNICEKIFKQ LIHLTEHMRI
HTGEKPFRCK ECGKAFSQSS SLIPHQRIHT GEKPYECKEC GKTFRHPSSL TQHVRIHTGE
KPYECRVCEK AFSQSIGLIQ HLRTHVREKP FTCKDCGKAF FQIRHLRQHE IIHTGVKPYI
CNVCSKTFSH STYLTQHQRT HTGERPYKCK ECGKAFSQRI HLSIHQRVHT GVKPYECSHC
GKAFRHDSSF AKHQRIHTGE KPYDCNECGK AFSCSSSLIR HCKTHLRNTF SNVV
