Z280B_HUMAN
ID Z280B_HUMAN Reviewed; 543 AA.
AC Q86YH2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein 280B;
DE AltName: Full=5'OY11.1;
DE AltName: Full=Suppressor of hairy wing homolog 2;
DE AltName: Full=Zinc finger protein 279;
DE AltName: Full=Zinc finger protein 632;
GN Name=ZNF280B; Synonyms=SUHW2, ZNF279, ZNF632;
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=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-256.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-256.
RC TISSUE=Uterus;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-70, AND
RP 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-247 AND LYS-261, VARIANT
RP [LARGE SCALE ANALYSIS] ALA-256, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 function as a transcription factor.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D87009; BAA20005.1; ALT_INIT; Genomic_DNA.
DR EMBL; CR456614; CAG30500.1; -; mRNA.
DR EMBL; BC040020; AAH40020.1; -; mRNA.
DR CCDS; CCDS13799.1; -.
DR RefSeq; NP_542942.2; NM_080764.3.
DR RefSeq; XP_011528195.1; XM_011529893.2.
DR RefSeq; XP_011528197.1; XM_011529895.2.
DR RefSeq; XP_011528198.1; XM_011529896.2.
DR RefSeq; XP_011528199.1; XM_011529897.2.
DR AlphaFoldDB; Q86YH2; -.
DR SMR; Q86YH2; -.
DR BioGRID; 126751; 3.
DR IntAct; Q86YH2; 1.
DR STRING; 9606.ENSP00000480958; -.
DR GlyGen; Q86YH2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86YH2; -.
DR PhosphoSitePlus; Q86YH2; -.
DR BioMuta; ZNF280B; -.
DR DMDM; 313104081; -.
DR EPD; Q86YH2; -.
DR jPOST; Q86YH2; -.
DR MassIVE; Q86YH2; -.
DR MaxQB; Q86YH2; -.
DR PaxDb; Q86YH2; -.
DR PeptideAtlas; Q86YH2; -.
DR PRIDE; Q86YH2; -.
DR ProteomicsDB; 70414; -.
DR Antibodypedia; 73538; 104 antibodies from 21 providers.
DR DNASU; 140883; -.
DR Ensembl; ENST00000613655.1; ENSP00000481008.1; ENSG00000275004.4.
DR Ensembl; ENST00000619852.2; ENSP00000480958.1; ENSG00000275004.4.
DR GeneID; 140883; -.
DR KEGG; hsa:140883; -.
DR UCSC; uc032qhv.2; human.
DR CTD; 140883; -.
DR DisGeNET; 140883; -.
DR GeneCards; ZNF280B; -.
DR HGNC; HGNC:23022; ZNF280B.
DR HPA; ENSG00000275004; Tissue enhanced (testis).
DR neXtProt; NX_Q86YH2; -.
DR PharmGKB; PA162409948; -.
DR VEuPathDB; HostDB:ENSG00000275004; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q86YH2; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q86YH2; -.
DR TreeFam; TF331707; -.
DR PathwayCommons; Q86YH2; -.
DR SignaLink; Q86YH2; -.
DR BioGRID-ORCS; 140883; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; ZNF280B; human.
DR GenomeRNAi; 140883; -.
DR Pharos; Q86YH2; Tdark.
DR PRO; PR:Q86YH2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q86YH2; protein.
DR Bgee; ENSG00000275004; Expressed in testis and 91 other tissues.
DR ExpressionAtlas; Q86YH2; baseline and differential.
DR Genevisible; Q86YH2; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor 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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR025243; DUF4195.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13836; DUF4195; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..543
FT /note="Zinc finger protein 280B"
FT /id="PRO_0000047056"
FT ZN_FING 343..366
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..396
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..483
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 256
FT /note="E -> A (in dbSNP:rs2236729)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:28112733"
FT /id="VAR_028013"
FT VARIANT 522
FT /note="V -> G (in dbSNP:rs12484816)"
FT /id="VAR_028014"
SQ SEQUENCE 543 AA; 61584 MW; F39D795E8478DAD7 CRC64;
MEQSCEEEKE PEPQKNIQET KQVDDEDAEL IFVGVEHVNE DAELIFVGVT SNSKPVVSNI
LNRVTPGSWS RRKKYDHLRK DTARKLQPKS HETVTSEAVT VLPASQLESR STDSPIIIEP
LSKPDYRNSS PQVVPNNSSE LPSPLITFTD SLHHPVSTAL SVGGINESPR VSKQLSTFEV
NSINPKRAKL RDGIIEGNSS ASFPSDTFHT MNTQQSTPSN NVHTSLSHVQ NGAPFPAAFP
KDNIHFKPIN TNLDRENELA KTDILSLTSQ NKTFDPKKEN PIVLLSDFYY GQHKGEGQPE
QKTHTTFKCL SCVKVLKNVK FMNHVKHHLE FEKQRNDSWE NHTTCQHCHR QFPTPFQLQC
HIENVHTAQE PSTVCKICEL SFETDQVLLQ HMKDHHKPGE MPYVCQVCHY RSSVFADVET
HFRTCHENTK NLLCPFCLKI FKTATPYMCH YRGHWGKSAH QCSKCRLQFL TFKEKMEHKT
QCHQMFKKPK QLEGLPPETK VTIQVSLEPL QPGSVDVASI TVSTSDSEPS LPRSKSKISK
KSH
