ID ZN219_HUMAN Reviewed; 722 AA. AC Q9P2Y4; Q8IYC1; Q9BW28; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 05-OCT-2010, entry version 91. DE RecName: Full=Zinc finger protein 219; GN Name=ZNF219; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC TISSUE=Testis; RX MEDLINE=20277481; PubMed=10819330; DOI=10.1093/dnares/7.2.137; RA Sakai T., Toyoda A., Hashimoto K., Maeda H.; RT "Isolation and characterization of a novel zinc finger gene, ZNF219, RT and mapping to the human chromosome 14q11 region."; RL DNA Res. 7:137-141(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Kidney; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. CC -!- SIMILARITY: Contains 6 C2H2-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB015427; BAA90526.1; -; mRNA. DR EMBL; BC000694; AAH00694.1; -; mRNA. DR EMBL; BC036105; AAH36105.1; -; mRNA. DR IPI; IPI00002612; -. DR RefSeq; NP_001095142.1; -. DR RefSeq; NP_001095924.1; -. DR RefSeq; NP_057507.2; -. DR UniGene; Hs.250493; -. DR ProteinModelPortal; Q9P2Y4; -. DR SMR; Q9P2Y4; 54-325, 273-555. DR STRING; Q9P2Y4; -. DR PhosphoSite; Q9P2Y4; -. DR PRIDE; Q9P2Y4; -. DR Ensembl; ENST00000360947; ENSP00000354206; ENSG00000165804. DR Ensembl; ENST00000421093; ENSP00000392401; ENSG00000165804. DR Ensembl; ENST00000451119; ENSP00000388558; ENSG00000165804. DR GeneID; 51222; -. DR KEGG; hsa:51222; -. DR UCSC; uc001vzr.2; human. DR CTD; 51222; -. DR GeneCards; GC14M021558; -. DR HGNC; HGNC:13011; ZNF219. DR MIM; 605036; gene. DR PharmGKB; PA37590; -. DR HOGENOM; HBG716587; -. DR HOVERGEN; HBG054187; -. DR InParanoid; Q9P2Y4; -. DR OMA; ADASPPY; -. DR OrthoDB; EOG91G5PC; -. DR PhylomeDB; Q9P2Y4; -. DR NextBio; 54298; -. DR ArrayExpress; Q9P2Y4; -. DR Bgee; Q9P2Y4; -. DR CleanEx; HS_ZNF219; -. DR Genevestigator; Q9P2Y4; -. DR GermOnline; ENSG00000165804; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004969; F:histamine receptor activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003700; F:transcription factor activity; IDA:UniProtKB. DR GO; GO:0016564; F:transcription repressor activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB. DR InterPro; IPR003980; Histamine_H3_recept. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2. DR Pfam; PF00096; zf-C2H2; 1. DR PRINTS; PR01471; HISTAMINEH3R. DR SMART; SM00355; ZnF_C2H2; 9. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1 722 Zinc finger protein 219. FT /FTId=PRO_0000047461. FT ZN_FING 57 79 C2H2-type 1. FT ZN_FING 85 107 C2H2-type 2. FT ZN_FING 163 186 C2H2-type 3. FT ZN_FING 274 296 C2H2-type 4. FT ZN_FING 302 324 C2H2-type 5. FT ZN_FING 498 520 C2H2-type 6. FT MOD_RES 175 175 Phosphoserine. FT CONFLICT 232 233 Missing (in Ref. 2; AAH00694). FT CONFLICT 260 260 P -> T (in Ref. 2; AAH36105). FT CONFLICT 436 436 E -> Q (in Ref. 1; BAA90526). SQ SEQUENCE 722 AA; 76877 MW; AB2B6B37904FC14B CRC64; MEGSRPRAPS GHLAPSPPAF DGELDLQRYS NGPAVSAGSL GMGAVSWSES RAGERRFPCP VCGKRFRFNS ILALHLRAHP GAQAFQCPHC GHRAAQRALL RSHLRTHQPE RPRSPAARLL LELEERALLR EARLGRARSS GGMQATPATE GLARPQAPSS SAFRCPYCKG KFRTSAERER HLHILHRPWK CGLCSFGSSQ EEELLHHSLT AHGAPERPLA ATSAAPPPQP QPQPPPQPEP RSVPQPEPEP EPEREATPTP APAAPEEPPA PPEFRCQVCG QSFTQSWFLK GHMRKHKASF DHACPVCGRC FKEPWFLKNH MKVHASKLGP LRAPGPASGP ARAPQPPDLG LLAYEPLGPA LLLAPAPTPA ERREPPSLLG YLSLRAGEGR PNGEGAEPGP GRSFGGFRPL SSALPARARR HRAEEPEEEE EVVEAEEETW ARGRSLGSLA SLHPRPGEGP GHSASAAGAQ ARSTATQEEN GLLVGGTRPE GGRGATGKDC PFCGKSFRSA HHLKVHLRVH TGERPYKCPH CDYAGTQSGS LKYHLQRHHR EQRSGAGPGP PPEPPPPSQR GSAPQSGAKP SPQPATWVEG ASSPRPPSSG AGPGSRRKPA SPGRTLRNGR GGEAEPLDLS LRAGPGGEAG PGGALHRCLF CPFATGAPEL MALHLQVHHS RRARGRRPPQ ADASPPYARV PSGETPPSPS QEGEEGSGLS RPGEAGLGGQ ER //