ID ARID2_HUMAN Reviewed; 1835 AA.
AC Q68CP9; Q15KG9; Q5EB51; Q645I3; Q6ZRY5; Q7Z3I5; Q86T28; Q96SJ6;
AC Q9HCL5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 10-MAY-2017, entry version 134.
DE RecName: Full=AT-rich interactive domain-containing protein 2;
DE Short=ARID domain-containing protein 2;
DE AltName: Full=BRG1-associated factor 200;
DE Short=BAF200;
DE AltName: Full=Zinc finger protein with activation potential;
DE AltName: Full=Zipzap/p200;
GN Name=ARID2; Synonyms=KIAA1557;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP SRF, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Heart;
RX PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Zipzap/p200 is a novel zinc finger protein contributing to cardiac
RT gene regulation.";
RL Biochem. Biophys. Res. Commun. 346:794-801(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1093, AND DNA-BINDING.
RX PubMed=15640446; DOI=10.1093/nar/gki145;
RA Patsialou A., Wilsker D., Moran E.;
RT "DNA-binding properties of ARID family proteins.";
RL Nucleic Acids Res. 33:66-80(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-1835 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-1835 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-1835 (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 976-1835 (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1030-1835 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-635; THR-653;
RP SER-689; THR-692 AND SER-1496, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-689 AND
RP SER-1496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-631; SER-1300;
RP SER-1391 AND SER-1496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [12]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=12672490; DOI=10.1016/S0959-437X(03)00022-4;
RA Martens J.A., Winston F.;
RT "Recent advances in understanding chromatin remodeling by SWI/SNF
RT complexes.";
RL Curr. Opin. Genet. Dev. 13:136-142(2003).
RN [13]
RP IDENTIFICATION IN THE PBAF COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15985610; DOI=10.1101/gad.1323805;
RA Yan Z., Cui K., Murray D.M., Ling C., Xue Y., Gerstein A., Parsons R.,
RA Zhao K., Wang W.;
RT "PBAF chromatin-remodeling complex requires a novel specificity
RT subunit, BAF200, to regulate expression of selective interferon-
RT responsive genes.";
RL Genes Dev. 19:1662-1667(2005).
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Required for the stability of the SWI/SNF chromatin
CC remodeling complex SWI/SNF-B (PBAF). May be involved in targeting
CC the complex to different genes. May be involved in regulating
CC transcriptional activation of cardiac genes.
CC {ECO:0000269|PubMed:16782067}.
CC -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling
CC complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47,
CC ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A,
CC SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155,
CC SMARCC2/BAF170, PB1/BAF180, ARID2/BAF200, ARID1A/BAF250A or
CC ARID1B/BAF250B and actin. Interacts with SRF. Forms complexes with
CC SRF and SRF cofactors MYOCD, NKX2-5 and SRFBP1.
CC {ECO:0000269|PubMed:15985610, ECO:0000269|PubMed:16782067}.
CC -!- INTERACTION:
CC Q86U86:PBRM1; NbExp=5; IntAct=EBI-637818, EBI-637807;
CC P51532:SMARCA4; NbExp=6; IntAct=EBI-637818, EBI-302489;
CC Q12824:SMARCB1; NbExp=3; IntAct=EBI-637818, EBI-358419;
CC Q969G3:SMARCE1; NbExp=4; IntAct=EBI-637818, EBI-455078;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68CP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68CP9-3; Sequence=VSP_015230;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and testis.
CC {ECO:0000269|PubMed:16782067}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in adult heart (at protein
CC level). {ECO:0000269|PubMed:16782067}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU20329.2; Type=Miscellaneous discrepancy; Note=Differs from position 1094 onward for unknown reason.; Evidence={ECO:0000305};
CC Sequence=BAB55320.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=BAC87171.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; DQ096628; AAZ74794.1; -; mRNA.
DR EMBL; AY727870; AAU20329.2; ALT_TERM; mRNA.
DR EMBL; AL832200; CAD91164.1; -; mRNA.
DR EMBL; BX537879; CAD97878.1; -; mRNA.
DR EMBL; CR749833; CAH18689.1; -; mRNA.
DR EMBL; AK027718; BAB55320.1; ALT_INIT; mRNA.
DR EMBL; AK127872; BAC87171.1; ALT_SEQ; mRNA.
DR EMBL; BC090062; AAH90062.1; -; mRNA.
DR EMBL; AB046777; BAB13383.1; -; mRNA.
DR CCDS; CCDS31783.1; -. [Q68CP9-1]
DR RefSeq; NP_001334768.1; NM_001347839.1.
DR RefSeq; NP_689854.2; NM_152641.3. [Q68CP9-1]
DR UniGene; Hs.317304; -.
DR ProteinModelPortal; Q68CP9; -.
DR BioGrid; 128219; 31.
DR DIP; DIP-33391N; -.
DR IntAct; Q68CP9; 22.
DR STRING; 9606.ENSP00000335044; -.
DR iPTMnet; Q68CP9; -.
DR PhosphoSitePlus; Q68CP9; -.
DR BioMuta; ARID2; -.
DR DMDM; 73921721; -.
DR EPD; Q68CP9; -.
DR MaxQB; Q68CP9; -.
DR PaxDb; Q68CP9; -.
DR PeptideAtlas; Q68CP9; -.
DR PRIDE; Q68CP9; -.
DR DNASU; 196528; -.
DR Ensembl; ENST00000334344; ENSP00000335044; ENSG00000189079. [Q68CP9-1]
DR GeneID; 196528; -.
DR KEGG; hsa:196528; -.
DR UCSC; uc001ros.2; human. [Q68CP9-1]
DR CTD; 196528; -.
DR DisGeNET; 196528; -.
DR GeneCards; ARID2; -.
DR HGNC; HGNC:18037; ARID2.
DR HPA; HPA063044; -.
DR MIM; 609539; gene.
DR neXtProt; NX_Q68CP9; -.
DR OpenTargets; ENSG00000189079; -.
DR PharmGKB; PA134916396; -.
DR eggNOG; KOG2312; Eukaryota.
DR eggNOG; KOG2744; Eukaryota.
DR eggNOG; ENOG410XT3H; LUCA.
DR GeneTree; ENSGT00390000016138; -.
DR HOVERGEN; HBG068777; -.
DR InParanoid; Q68CP9; -.
DR KO; K11765; -.
DR OMA; LKQYYLR; -.
DR OrthoDB; EOG091G169Y; -.
DR PhylomeDB; Q68CP9; -.
DR TreeFam; TF106406; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR SIGNOR; Q68CP9; -.
DR ChiTaRS; ARID2; human.
DR GeneWiki; ARID2; -.
DR GenomeRNAi; 196528; -.
DR PMAP-CutDB; Q68CP9; -.
DR PRO; PR:Q68CP9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000189079; -.
DR ExpressionAtlas; Q68CP9; baseline and differential.
DR Genevisible; Q68CP9; HS.
DR GO; GO:0090544; C:BAF-type complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0042592; P:homeostatic process; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator;
KW Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
FT CHAIN 2 1835 AT-rich interactive domain-containing
FT protein 2.
FT /FTId=PRO_0000200577.
FT DOMAIN 13 105 ARID. {ECO:0000255|PROSITE-
FT ProRule:PRU00355}.
FT DNA_BIND 524 603 RFX-type winged-helix.
FT {ECO:0000255|PROSITE-ProRule:PRU00858}.
FT ZN_FING 1632 1657 C2H2-type.
FT MOTIF 313 317 LXXLL.
FT COMPBIAS 793 1128 Gln-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:22814378}.
FT MOD_RES 4 4 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 635 635 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231}.
FT MOD_RES 653 653 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 689 689 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231}.
FT MOD_RES 692 692 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 1300 1300 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 1391 1391 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 1496 1496 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 1784 1835 Missing (in isoform 2).
FT {ECO:0000303|PubMed:17974005}.
FT /FTId=VSP_015230.
FT CONFLICT 169 169 L -> P (in Ref. 3; CAH18689).
FT {ECO:0000305}.
FT CONFLICT 217 217 F -> L (in Ref. 3; CAD91164).
FT {ECO:0000305}.
FT CONFLICT 665 665 T -> I (in Ref. 3; CAD91164).
FT {ECO:0000305}.
FT CONFLICT 801 801 M -> T (in Ref. 1; AAZ74794).
FT {ECO:0000305}.
FT CONFLICT 825 825 S -> P (in Ref. 3; CAH18689).
FT {ECO:0000305}.
FT CONFLICT 906 906 V -> F (in Ref. 3; CAD91164).
FT {ECO:0000305}.
FT CONFLICT 956 956 A -> V (in Ref. 3; CAD91164).
FT {ECO:0000305}.
FT CONFLICT 988 988 M -> T (in Ref. 3; CAH18689).
FT {ECO:0000305}.
FT CONFLICT 989 989 S -> P (in Ref. 3; CAD97878).
FT {ECO:0000305}.
FT CONFLICT 1035 1035 Q -> R (in Ref. 4; BAB55320).
FT {ECO:0000305}.
FT CONFLICT 1062 1062 Q -> R (in Ref. 3; CAH18689).
FT {ECO:0000305}.
FT CONFLICT 1204 1204 S -> G (in Ref. 3; CAD97878).
FT {ECO:0000305}.
FT CONFLICT 1292 1292 S -> N (in Ref. 3; CAD97878).
FT {ECO:0000305}.
FT CONFLICT 1460 1460 V -> A (in Ref. 3; CAD97878).
FT {ECO:0000305}.
FT CONFLICT 1543 1543 D -> G (in Ref. 3; CAD91164).
FT {ECO:0000305}.
FT CONFLICT 1543 1543 D -> N (in Ref. 4; BAC87171).
FT {ECO:0000305}.
FT CONFLICT 1647 1647 S -> P (in Ref. 3; CAD97878).
FT {ECO:0000305}.
FT CONFLICT 1700 1700 L -> S (in Ref. 3; CAD91164).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 13 105 iprf:ARID [T]
FT MYHIT 522 602 ipfam:RFX_DNA_binding [T]
FT MYHIT 524 603 iprf:RFX_DBD [T]
FT MYHIT 14 106 ismart:BRIGHT [T]
FT MYHIT 18 101 ipfam:ARID [T]
FT MYHIT 1634 1657 ipat:ZINC_FINGER_C2H2_1 [T]
SQ SEQUENCE 1835 AA; 197391 MW; F540A029FA2264D4 CRC64;
MANSTGKAPP DERRKGLAFL DELRQFHHSR GSPFKKIPAV GGKELDLHGL YTRVTTLGGF
AKVSEKNQWG EIVEEFNFPR SCSNAAFALK QYYLRYLEKY EKVHHFGEDD DEVPPGNPKP
QLPIGAIPSS YNYQQHSVSD YLRQSYGLSM DFNSPNDYNK LVLSLLSGLP NEVDFAINVC
TLLSNESKHV MQLEKDPKII TLLLANAGVF DDTLGSFSTV FGEEWKEKTD RDFVKFWKDI
VDDNEVRDLI SDRNKSHEGT SGEWIWESLF HPPRKLGIND IEGQRVLQIA VILRNLSFEE
GNVKLLAANR TCLRFLLLSA HSHFISLRQL GLDTLGNIAA ELLLDPVDFK TTHLMFHTVT
KCLMSRDRFL KMRGMEILGN LCKAEDNGVL ICEYVDQDSY REIICHLTLP DVLLVISTLE
VLYMLTEMGD VACTKIAKVE KSIDMLVCLV SMDIQMFGPD ALAAVKLIEH PSSSHQMLSE
IRPQAIEQVQ TQTHVASAPA SRAVVAQHVA PPPGIVEIDS EKFACQWLNA HFEVNPDCSV
SRAEMYSEYL STCSKLARGG ILTSTGFYKC LRTVFPNHTV KRVEDSSSNG QAHIHVVGVK
RRAIPLPIQM YYQQQPVSTS VVRVDSVPDV SPAPSPAGIP HGSQTIGNHF QRTPVANQSS
NLTATQMSFP VQGVHTVAQT VSRIPQNPSP HTHQQQNAPV TVIQSKAPIP CEVVKATVIQ
NSIPQTGVPV SIAVGGGPPQ SSVVQNHSTG PQPVTVVNSQ TLLHHPSVIP QQSPLHTVVP
GQIPSGTPVT VIQQAVPQSH MFGRVQNIPA CTSTVSQGQQ LITTSPQPVQ TSSQQTSAGS
QSQDTVIIAP PQYVTTSASN IVSATSVQNF QVATGQMVTI AGVPSPQASR VGFQNIAPKP
LPSQQVSSTV VQQPIQQPQQ PTQQSVVIVS QPAQQGQTYA PAIHQIVLAN PAALPAGQTV
QLTGQPNITP SSSPSPVPAT NNQVPTAMSS SSTPQSQGPP PTVSQMLSVK RQQQQQHSPA
PPPQQVQVQV QQPQQVQMQV QPQQSNAGVG QPASGESSLI KQLLLPKRGP STPGGKLILP
APQIPPPNNA RAPSPQVVYQ VASNQAAGFG VQGQTPAQQL LVGQQNVQLV PSAMPPSGGV
QTVPISNLQI LPGPLISNSP ATIFQGTSGN QVTITVVPNT SFAPATVSQG NATQLIAPAG
ITMSGTQTGV GLPVQTLPAT QASPAGQSSC TTATPPFKGD KIICQKEEEA KEATGLHVHE
RKIEVMENPS CRRGATNTSN GDTKENEMHV GSLLNGRKYS DSSLPPSNSG KIQSETNQCS
LISNGPSLEL GENGASGKQN SEQIDMQDIK SDLRKPLVNG ICDFDKGDGS HLSKNIPNHK
TSNHVGNGEI SPMEPQGTLD ITQQDTAKGD QLERISNGPV LTLGGSSVSS IQEASNAATQ
QFSGTDLLNG PLASSLNSDV PQQRPSVVVS PHSTTSVIQG HQIIAVPDSG SKVSHSPALS
SDVRSTNGTA ECKTVKRPAE DTDRETVAGI PNKVGVRIVT ISDPNNAGCS ATMVAVPAGA
DPSTVAKVAI ESAVQQKQQH PPTYVQNVVP QNTPMPPSPA VQVQGQPNSS QPSPFSGSSQ
PGDPMRKPGQ NFMCLWQSCK KWFQTPSQVF YHAATEHGGK DVYPGQCLWE GCEPFQRQRF
SFITHLQDKH CSKDALLAGL KQDEPGQAGS QKSSTKQPTV GGTSSTPRAQ KAIVNHPSAA
LMALRRGSRN LVFRDFTDEK EGPITKHIRL TAALILKNIG KYSECGRRLL KRHENNLSVL
AISNMEASST LAKCLYELNF TVQSKEQEKD SEMLQ
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