ID ZN184_HUMAN Reviewed; 751 AA. AC Q99676; B2R715; O60792; Q8TBA9; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 198. DE RecName: Full=Zinc finger protein 184; GN Name=ZNF184; 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], AND VARIANT SER-27. RC TISSUE=Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-27. RC TISSUE=Placenta; 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 [MRNA] OF 26-751, AND VARIANT SER-27. RC TISSUE=Placenta; RX PubMed=9073517; DOI=10.1006/geno.1996.4583; RA Goldwurm S., Menzies M.L., Banyer J.L., Powell B.L.W., Jazwinska E.C.; RT "Identification of a novel Krueppel-related zinc finger gene (ZNF184) RT mapping to 6p21.3."; RL Genomics 40:486-489(1997). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-122, 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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-206, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Predominant expression in testis. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {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; AK312804; BAG35662.1; -; mRNA. DR EMBL; AL021918; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC022992; AAH22992.1; -; mRNA. DR EMBL; U66561; AAC51180.1; -; mRNA. DR CCDS; CCDS4624.1; -. DR RefSeq; NP_001305820.1; NM_001318891.1. DR RefSeq; NP_001305821.1; NM_001318892.1. DR RefSeq; NP_001305822.1; NM_001318893.1. DR RefSeq; NP_001334761.1; NM_001347832.1. DR RefSeq; NP_009080.2; NM_007149.2. DR AlphaFoldDB; Q99676; -. DR SMR; Q99676; -. DR BioGRID; 113524; 64. DR IntAct; Q99676; 17. DR STRING; 9606.ENSP00000211936; -. DR iPTMnet; Q99676; -. DR PhosphoSitePlus; Q99676; -. DR BioMuta; ZNF184; -. DR DMDM; 313104299; -. DR EPD; Q99676; -. DR jPOST; Q99676; -. DR MassIVE; Q99676; -. DR MaxQB; Q99676; -. DR PaxDb; 9606-ENSP00000211936; -. DR PeptideAtlas; Q99676; -. DR ProteomicsDB; 78390; -. DR Pumba; Q99676; -. DR Antibodypedia; 824; 77 antibodies from 16 providers. DR DNASU; 7738; -. DR Ensembl; ENST00000211936.10; ENSP00000211936.6; ENSG00000096654.16. DR Ensembl; ENST00000377419.1; ENSP00000366636.1; ENSG00000096654.16. DR Ensembl; ENST00000683788.1; ENSP00000508298.1; ENSG00000096654.16. DR GeneID; 7738; -. DR KEGG; hsa:7738; -. DR MANE-Select; ENST00000683788.1; ENSP00000508298.1; NM_001318891.2; NP_001305820.1. DR UCSC; uc003nji.4; human. DR AGR; HGNC:12975; -. DR CTD; 7738; -. DR DisGeNET; 7738; -. DR GeneCards; ZNF184; -. DR HGNC; HGNC:12975; ZNF184. DR HPA; ENSG00000096654; Low tissue specificity. DR MIM; 602277; gene. DR neXtProt; NX_Q99676; -. DR OpenTargets; ENSG00000096654; -. DR PharmGKB; PA37557; -. DR VEuPathDB; HostDB:ENSG00000096654; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162941; -. DR HOGENOM; CLU_002678_44_5_1; -. DR InParanoid; Q99676; -. DR OMA; TIPTWER; -. DR OrthoDB; 4622888at2759; -. DR PhylomeDB; Q99676; -. DR TreeFam; TF350822; -. DR PathwayCommons; Q99676; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q99676; -. DR BioGRID-ORCS; 7738; 7 hits in 1171 CRISPR screens. DR ChiTaRS; ZNF184; human. DR GeneWiki; ZNF184; -. DR GenomeRNAi; 7738; -. DR Pharos; Q99676; Tbio. DR PRO; PR:Q99676; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q99676; Protein. DR Bgee; ENSG00000096654; Expressed in Brodmann (1909) area 23 and 177 other cell types or tissues. DR ExpressionAtlas; Q99676; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 19. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24399:SF54; GASTRULA ZINC FINGER PROTEIN XLCGF26.1-LIKE-RELATED; 1. DR PANTHER; PTHR24399; ZINC FINGER AND BTB DOMAIN-CONTAINING; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 19. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 19. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19. DR Genevisible; Q99676; HS. PE 1: Evidence at protein level; KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..751 FT /note="Zinc finger protein 184" FT /id="PRO_0000047443" FT DOMAIN 28..99 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 222..244 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 250..272 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 278..300 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 306..328 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 334..356 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 362..384 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 390..412 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 418..440 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 446..468 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 474..496 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 502..524 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 530..552 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 558..580 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 586..608 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 614..636 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 642..664 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 670..692 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 698..720 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 726..748 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 191..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 206 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 27 FT /note="A -> S (in dbSNP:rs1883216)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9073517" FT /id="VAR_045989" FT CONFLICT 286 FT /note="G -> C (in Ref. 1; BAG35662)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="Q -> R (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="E -> G (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 379..381 FT /note="QHQ -> PHP (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="R -> G (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 526 FT /note="Q -> G (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="K -> E (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 547..549 FT /note="KHE -> QHQ (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" FT CONFLICT 746 FT /note="R -> K (in Ref. 4; AAC51180)" FT /evidence="ECO:0000305" SQ SEQUENCE 751 AA; 86174 MW; 249DFB302C6BC97D CRC64; MEDLSSPDST LLQGGHNLLS SASFQEAVTF KDVIVDFTQE EWKQLDPGQR DLFRDVTLEN YTHLVSIGLQ VSKPDVISQL EQGTEPWIME PSIPVGTCAD WETRLENSVS APEPDISEEE LSPEVIVEKH KRDDSWSSNL LESWEYEGSL ERQQANQQTL PKEIKVTEKT IPSWEKGPVN NEFGKSVNVS SNLVTQEPSP EETSTKRSIK QNSNPVKKEK SCKCNECGKA FSYCSALIRH QRTHTGEKPY KCNECEKAFS RSENLINHQR IHTGDKPYKC DQCGKGFIEG PSLTQHQRIH TGEKPYKCDE CGKAFSQRTH LVQHQRIHTG EKPYTCNECG KAFSQRGHFM EHQKIHTGEK PFKCDECDKT FTRSTHLTQH QKIHTGEKTY KCNECGKAFN GPSTFIRHHM IHTGEKPYEC NECGKAFSQH SNLTQHQKTH TGEKPYDCAE CGKSFSYWSS LAQHLKIHTG EKPYKCNECG KAFSYCSSLT QHRRIHTREK PFECSECGKA FSYLSNLNQH QKTHTQEKAY ECKECGKAFI RSSSLAKHER IHTGEKPYQC HECGKTFSYG SSLIQHRKIH TGERPYKCNE CGRAFNQNIH LTQHKRIHTG AKPYECAECG KAFRHCSSLA QHQKTHTEEK PYQCNKCEKT FSQSSHLTQH QRIHTGEKPY KCNECDKAFS RSTHLTEHQN THTGEKPYNC NECRKTFSQS TYLIQHQRIH SGEKPFGCND CGKSFRYRSA LNKHQRLHPG I //