ZN33B_HUMAN
ID ZN33B_HUMAN Reviewed; 778 AA.
AC Q06732; Q06731; Q32MA2; Q86XY8; Q8NDW3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein 33B;
DE AltName: Full=Zinc finger protein 11B;
DE AltName: Full=Zinc finger protein KOX2;
GN Name=ZNF33B; Synonyms=KOX2, ZNF11B;
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 [GENOMIC DNA].
RX PubMed=12566394; DOI=10.1101/gr.644503;
RA Guy J., Hearn T., Crosier M., Mudge J., Viggiano L., Koczan D.,
RA Thiesen H.-J., Bailey J.A., Horvath J.E., Eichler E.E., Earthrowl M.E.,
RA Deloukas P., French L., Rogers J., Bentley D., Jackson M.S.;
RT "Genomic sequence and transcriptional profile of the boundary between
RT pericentromeric satellites and genes on human chromosome arm 10p.";
RL Genome Res. 13:159-172(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-579, AND VARIANT CYS-145.
RC TISSUE=Duodenum;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 76-454 AND 745-778, AND VARIANT
RP CYS-145.
RX PubMed=8464732; DOI=10.1093/nar/21.6.1409;
RA Tunnacliffe A., Liu L., Moore J.K., Leversha M.A., Jackson M.S.,
RA Ferguson-Smith M.A., Thiesen H.-J., Ponder B.A.;
RT "Duplicated KOX zinc finger gene clusters flank the centromere of human
RT chromosome 10: evidence for a pericentric inversion during primate
RT evolution.";
RL Nucleic Acids Res. 21:1409-1417(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 385-440.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-181, 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q06732; P43365: MAGEA12; NbExp=3; IntAct=EBI-474142, EBI-749530;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48313.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ491697; CAD36956.1; -; mRNA.
DR EMBL; AL022345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048313; AAH48313.1; ALT_SEQ; mRNA.
DR EMBL; X68684; CAA48643.1; -; mRNA.
DR EMBL; X68685; CAA48644.1; -; Genomic_DNA.
DR EMBL; X68688; CAA48647.1; -; Genomic_DNA.
DR EMBL; X52333; CAA36559.1; -; mRNA.
DR CCDS; CCDS7198.1; -.
DR PIR; I37959; I37959.
DR PIR; S33989; S33994.
DR PIR; S33993; S33993.
DR RefSeq; NP_001291962.1; NM_001305033.1.
DR RefSeq; NP_001291964.1; NM_001305035.1.
DR RefSeq; NP_001291965.1; NM_001305036.1.
DR RefSeq; NP_001291966.1; NM_001305037.1.
DR RefSeq; NP_001291967.1; NM_001305038.1.
DR RefSeq; NP_001291968.1; NM_001305039.1.
DR RefSeq; NP_001291969.1; NM_001305040.1.
DR RefSeq; NP_008886.1; NM_006955.2.
DR AlphaFoldDB; Q06732; -.
DR SMR; Q06732; -.
DR BioGRID; 113411; 5.
DR IntAct; Q06732; 7.
DR STRING; 9606.ENSP00000352444; -.
DR iPTMnet; Q06732; -.
DR PhosphoSitePlus; Q06732; -.
DR BioMuta; ZNF33B; -.
DR DMDM; 66774229; -.
DR jPOST; Q06732; -.
DR MassIVE; Q06732; -.
DR MaxQB; Q06732; -.
DR PaxDb; Q06732; -.
DR PeptideAtlas; Q06732; -.
DR PRIDE; Q06732; -.
DR ProteomicsDB; 58476; -.
DR Antibodypedia; 55057; 8 antibodies from 4 providers.
DR DNASU; 7582; -.
DR Ensembl; ENST00000359467.8; ENSP00000352444.2; ENSG00000196693.15.
DR GeneID; 7582; -.
DR KEGG; hsa:7582; -.
DR MANE-Select; ENST00000359467.8; ENSP00000352444.2; NM_006955.3; NP_008886.1.
DR UCSC; uc001jaf.1; human.
DR CTD; 7582; -.
DR GeneCards; ZNF33B; -.
DR HGNC; HGNC:13097; ZNF33B.
DR HPA; ENSG00000196693; Low tissue specificity.
DR MIM; 194522; gene.
DR neXtProt; NX_Q06732; -.
DR OpenTargets; ENSG00000196693; -.
DR PharmGKB; PA37672; -.
DR VEuPathDB; HostDB:ENSG00000196693; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162173; -.
DR InParanoid; Q06732; -.
DR OMA; LCIDSFP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q06732; -.
DR TreeFam; TF337898; -.
DR PathwayCommons; Q06732; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q06732; -.
DR BioGRID-ORCS; 7582; 29 hits in 966 CRISPR screens.
DR ChiTaRS; ZNF33B; human.
DR GeneWiki; ZNF33B; -.
DR GenomeRNAi; 7582; -.
DR Pharos; Q06732; Tdark.
DR PRO; PR:Q06732; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q06732; protein.
DR Bgee; ENSG00000196693; Expressed in body of pancreas and 158 other tissues.
DR ExpressionAtlas; Q06732; baseline and differential.
DR Genevisible; Q06732; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; 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; 16.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..778
FT /note="Zinc finger protein 33B"
FT /id="PRO_0000047334"
FT DOMAIN 12..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 329..351
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..379
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 385..407
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..603
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 609..631
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 637..659
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 665..687
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 693..715
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 721..743
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 749..771
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06730"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06730"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06730"
FT CROSSLNK 733
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06730"
FT VARIANT 145
FT /note="R -> C (in dbSNP:rs210280)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8464732"
FT /id="VAR_024192"
FT VARIANT 356
FT /note="H -> R (in dbSNP:rs7914982)"
FT /id="VAR_052752"
FT CONFLICT 392
FT /note="K -> E (in Ref. 5; CAA36559)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="K -> E (in Ref. 5; CAA36559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 90683 MW; D53D23909751DCEF CRC64;
MNKVDQKFQG SVSFKDVTVG FTQEEWQHLD PSQRALYRDV MLENYSNLVS VGYCAHKPEV
IFRLEQGEEP WRLEEEFPSQ SFPEVWTADH LKERSQENQS KHLWEVVFIN NEMLTKEQGN
VIGIPFNMDV SSFPSRKMFC QYDSRGMSFN TVSELVISKI NYLGKKSDEF NACGKLLLNI
KHDETHTREK NEVLKNRNTL SHRENTLQHE KIQTLDHNFE YSICQETLLE KAVFNTRKRE
NAEENNCDYN EFGRTFCDSS SLLFHQIPPS KDSHYEFSDC EKFLCVKSTL SKHDGVPVKH
YDCGESGNNF RRKLCLSQLQ KGDKGEKHFE CNECGKAFWE KSHLTRHQRV HTGEKHFQCN
QCGKTFWEKS NLTKHQRSHT GEKPFECNEC GKAFSHKSAL TLHQRTHTGE KPYQCNACGK
TFYQKSDLTK HQRTHTGQKP YECYECGKSF CMNSHLTVHQ RTHTGEKPFE CLECGKSFCQ
KSHLTQHQRT HIGDKPYECN ACGKTFYHKS VLTRHQIIHT GLKPYECYEC GKTFCLKSDL
TIHQRTHTGE KPFACPECGK FFSHKSTLSQ HYRTHTGEKP YECHECGKIF YNKSYLTKHN
RTHTGEKPYE CNECGKTFCQ KSQLTQHQRI HIGEKPYECN ECGKAFCHKS ALIVHQRTHT
QEKPYKCNEC GKSFCVKSGL ILHERKHTGE KPYECNECGK SFSHKSSLTV HHRAHTGEKS
CQCNECGKIF YRKSDLAKHQ RSHTGEKPYE CNTCRKTFSQ KSNLIVHQRT HIGEKPYE
