ID HELZ2_HUMAN Reviewed; 2649 AA.
AC Q9BYK8; Q3C2G2; Q4VXQ1; Q8TEF3; Q96ND3; Q9C094;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 02-NOV-2016, entry version 159.
DE RecName: Full=Helicase with zinc finger domain 2;
DE AltName: Full=ATP-dependent helicase PRIC285;
DE AltName: Full=Helicase with zinc finger 2, transcriptional coactivator;
DE AltName: Full=PPAR-alpha-interacting complex protein 285;
DE AltName: Full=PPAR-gamma DNA-binding domain-interacting protein 1;
DE Short=PDIP1;
DE Short=PPAR-gamma DBD-interacting protein 1;
DE AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 285 kDa protein;
DE EC=3.6.4.-;
GN Name=HELZ2; Synonyms=KIAA1769, PRIC285;
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 2), AND VARIANTS ASN-788;
RP ARG-1123; LEU-2016 AND GLU-2049.
RX PubMed=12189208; DOI=10.1073/pnas.182426699;
RA Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V.,
RA Kashireddy P., Cherkaoui-Malki M., Qi C., Zhu Y.-J., Rao M.S.,
RA Reddy J.K.;
RT "Identification of a transcriptionally active peroxisome proliferator-
RT activated receptor alpha-interacting cofactor complex in rat liver and
RT characterization of PRIC285 as a coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11836-11841(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION
RP WITH PPARG, TISSUE SPECIFICITY, DOMAIN, AND VARIANTS ASN-788;
RP ARG-1123; LEU-2016 AND GLU-2049.
RX PubMed=16239304; DOI=10.1210/en.2005-0450;
RA Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T.,
RA Yamada M., Mori M.;
RT "Isolation and characterization of a transcriptional cofactor and its
RT novel isoform that bind the DNA-binding domain of peroxisome
RT proliferator-activated receptor gamma.";
RL Endocrinology 147:377-388(2006).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND
RP VARIANTS VARIANTS ASN-788; ARG-1123; LEU-2016 AND GLU-2049.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1526-2649 (ISOFORMS 1/2/3).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2194-2649 (ISOFORMS 1/2/3).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP FUNCTION, INTERACTION WITH PPARG AND THRAP3, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T.,
RA Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H.,
RA Hashimoto K., Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA Vemulapalli V., Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Helicase that acts as a transcriptional coactivator for
CC a number of nuclear receptors including PPARA, PPARG, THRA, THRB
CC and RXRA. {ECO:0000269|PubMed:16239304,
CC ECO:0000269|PubMed:23525231}.
CC -!- SUBUNIT: Interacts with PPARA (via DNA-binding domain) and PPARG;
CC the interaction stimulates the transcriptional activity of PPARA
CC and PPARG. Interacts with THRAP3; the interaction is direct and
CC HELZ2 and THRAP3 synergistically enhance the transcriptional
CC activity of PPARG. It is probably part of the peroxisome
CC proliferator activated receptor alpha interacting complex (PRIC).
CC {ECO:0000269|PubMed:16239304, ECO:0000269|PubMed:23525231}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=PDIP1-beta;
CC IsoId=Q9BYK8-1; Sequence=Displayed;
CC Note=More abundantly expressed than isoform 2.;
CC Name=2; Synonyms=PDIP1-alpha;
CC IsoId=Q9BYK8-2; Sequence=VSP_007297, VSP_007298;
CC Name=3;
CC IsoId=Q9BYK8-4; Sequence=VSP_017377, VSP_017378;
CC Note=Incomplete sequence. No experimental confirmation
CC available.;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues including heart,
CC pancreas, skeletal muscle, colon, spleen, liver, kidney, lung,
CC peripheral blood and placenta. {ECO:0000269|PubMed:16239304}.
CC -!- DOMAIN: Contains 5 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. These
CC motifs are not required for interaction with PPARG.
CC {ECO:0000269|PubMed:16239304}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}.
CC -!- CAUTION: PubMed:12189208 experiments have been carried out partly
CC in rat and partly in human. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70969.1; Type=Frameshift; Positions=2206; Evidence={ECO:0000305};
DR EMBL; AF517673; AAM74197.1; -; mRNA.
DR EMBL; AB201715; BAE46995.1; -; mRNA.
DR EMBL; AB051556; BAB21860.2; -; mRNA.
DR EMBL; AL121829; CAI95749.1; -; Genomic_DNA.
DR EMBL; AK074171; BAB84997.1; -; mRNA.
DR EMBL; AK055611; BAB70969.1; ALT_FRAME; mRNA.
DR CCDS; CCDS13527.1; -. [Q9BYK8-2]
DR CCDS; CCDS33508.1; -. [Q9BYK8-1]
DR RefSeq; NP_001032412.2; NM_001037335.2. [Q9BYK8-1]
DR RefSeq; NP_208384.3; NM_033405.3. [Q9BYK8-2]
DR UniGene; Hs.517180; -.
DR ProteinModelPortal; Q9BYK8; -.
DR BioGrid; 124528; 10.
DR IntAct; Q9BYK8; 1.
DR STRING; 9606.ENSP00000417401; -.
DR iPTMnet; Q9BYK8; -.
DR PhosphoSitePlus; Q9BYK8; -.
DR BioMuta; HELZ2; -.
DR DMDM; 317373591; -.
DR EPD; Q9BYK8; -.
DR MaxQB; Q9BYK8; -.
DR PaxDb; Q9BYK8; -.
DR PeptideAtlas; Q9BYK8; -.
DR PRIDE; Q9BYK8; -.
DR Ensembl; ENST00000427522; ENSP00000393257; ENSG00000130589. [Q9BYK8-2]
DR Ensembl; ENST00000467148; ENSP00000417401; ENSG00000130589. [Q9BYK8-1]
DR GeneID; 85441; -.
DR KEGG; hsa:85441; -.
DR UCSC; uc002yfl.2; human. [Q9BYK8-1]
DR CTD; 85441; -.
DR DisGeNET; 85441; -.
DR GeneCards; HELZ2; -.
DR HGNC; HGNC:30021; HELZ2.
DR HPA; HPA051267; -.
DR MIM; 611265; gene.
DR neXtProt; NX_Q9BYK8; -.
DR OpenTargets; ENSG00000130589; -.
DR eggNOG; KOG1804; Eukaryota.
DR eggNOG; KOG2102; Eukaryota.
DR eggNOG; COG0557; LUCA.
DR eggNOG; COG1112; LUCA.
DR GeneTree; ENSGT00800000124068; -.
DR HOGENOM; HOG000231856; -.
DR HOVERGEN; HBG080465; -.
DR InParanoid; Q9BYK8; -.
DR OMA; PRHPQHY; -.
DR OrthoDB; EOG091G01CH; -.
DR PhylomeDB; Q9BYK8; -.
DR BioCyc; ZFISH:ENSG00000130589-MONOMER; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
DR Reactome; R-HSA-400253; Circadian Clock.
DR GeneWiki; PRIC285; -.
DR GenomeRNAi; 85441; -.
DR PRO; PR:Q9BYK8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000130589; -.
DR Genevisible; Q9BYK8; HS.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR031191; HELZ2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022966; RNase_II/R_CS.
DR PANTHER; PTHR10887:SF376; PTHR10887:SF376; 3.
DR SUPFAM; SSF50249; SSF50249; 4.
DR SUPFAM; SSF52540; SSF52540; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Complete proteome;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 2649 Helicase with zinc finger domain 2.
FT /FTId=PRO_0000058561.
FT ZN_FING 40 64 C2H2-type; atypical.
FT NP_BIND 544 551 ATP. {ECO:0000255}.
FT NP_BIND 2174 2181 ATP. {ECO:0000255}.
FT REGION 563 1059 Interaction with THRAP3.
FT {ECO:0000269|PubMed:23525231}.
FT REGION 2135 2649 Interaction with THRAP3.
FT {ECO:0000269|PubMed:23525231}.
FT MOTIF 667 670 DEAA box.
FT MOTIF 1075 1079 LXXLL motif 1.
FT MOTIF 1118 1122 LXXLL motif 2.
FT MOTIF 1173 1177 LXXLL motif 3.
FT MOTIF 2012 2016 LXXLL motif 4.
FT MOTIF 2229 2233 LXXLL motif 5.
FT COMPBIAS 968 1059 Ala-rich.
FT MOD_RES 1006 1006 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 1 569 Missing (in isoform 2).
FT {ECO:0000303|PubMed:12189208,
FT ECO:0000303|PubMed:16239304}.
FT /FTId=VSP_007297.
FT VAR_SEQ 1 535 Missing (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_017377.
FT VAR_SEQ 536 576 RVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTN
FT -> LTSDSQTRAVLRGSSAGHTVGALADSTEAPSKKPMSSS
FT PSR (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_017378.
FT VAR_SEQ 570 576 LICTHTN -> MSSSPSR (in isoform 2).
FT {ECO:0000303|PubMed:12189208,
FT ECO:0000303|PubMed:16239304}.
FT /FTId=VSP_007298.
FT VARIANT 788 788 S -> N (in dbSNP:rs438363).
FT {ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208,
FT ECO:0000269|PubMed:16239304}.
FT /FTId=VAR_015597.
FT VARIANT 1123 1123 H -> R (in dbSNP:rs310632).
FT {ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208,
FT ECO:0000269|PubMed:16239304}.
FT /FTId=VAR_015598.
FT VARIANT 1152 1152 S -> L (in dbSNP:rs35817585).
FT /FTId=VAR_047038.
FT VARIANT 1308 1308 V -> L (in dbSNP:rs310631).
FT /FTId=VAR_047039.
FT VARIANT 1381 1381 R -> K (in dbSNP:rs3810487).
FT /FTId=VAR_047040.
FT VARIANT 1821 1821 L -> R (in dbSNP:rs3810486).
FT /FTId=VAR_047041.
FT VARIANT 1889 1889 T -> A (in dbSNP:rs34980032).
FT /FTId=VAR_047042.
FT VARIANT 2016 2016 P -> L (in dbSNP:rs3810485).
FT {ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208,
FT ECO:0000269|PubMed:16239304}.
FT /FTId=VAR_015599.
FT VARIANT 2049 2049 Q -> E (in dbSNP:rs3810483).
FT {ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208,
FT ECO:0000269|PubMed:16239304}.
FT /FTId=VAR_015600.
FT VARIANT 2170 2170 T -> M (in dbSNP:rs3810481).
FT /FTId=VAR_047043.
FT CONFLICT 196 196 V -> A (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 327 329 FNR -> SNH (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 442 442 E -> G (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 836 836 G -> D (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 1873 1873 V -> A (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 2203 2203 G -> S (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 2383 2383 V -> A (in Ref. 2; BAE46995).
FT {ECO:0000305}.
FT CONFLICT 2626 2626 F -> L (in Ref. 2; BAE46995).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1660 1684 ipat:RIBONUCLEASE_II [T]
SQ SEQUENCE 2649 AA; 294651 MW; 419573D5AEE700D7 CRC64;
MAVWEAEQLG GLQRGDLLTP PAPDGDGRTA PLGQPPGAQL YCPACLVTCH SQEAFENHCA
SSEHAQMVAF DQALPWEHRS PPPGLSKFEL CPKPDLCEYG DACTKAHSAQ ELQEWVRRTQ
AVELRGQAAW QDGLVPYQER LLAEYQRSSS EVLVLAETLD GVRVTCNQPL MYQAQERKTQ
YSWTFAVHSE EPLLHVALLK QEPGADFSLV APGLPPGRLY ARGERFRVPS STADFQVGVR
VQAASFGTFE QWVVFDFGRR PVLLQKLGLQ LGQGRRPGPC RNLALGHPEE MERWHTGNRH
VVPGVERTAE QTALMAKYKG PALALEFNRS SVASGPISPT NYRQRMHQFL YEEEAAQQQL
VAKLTLRGQV FLKTALQTPA LNMLFAPPGA LYAEVPVPSS LMPDTDQGFL LGRAVSTALV
APVPAPDNTV FEVRLERRAS SEQALWLLLP ARCCLALGLQ PEARLVLEVQ FQIDPMTFRL
WHQAVDTLPE EQLVVPDLPT CALPRPWSVP PLRRGNRKQE LAVALIAGWG PGDGRRVPPL
LIYGPFGTGK TYTLAMASLE VIRRPETKVL ICTHTNSAAD IYIREYFHSH VSGGHPEATP
LRVMYTDRPL SQTDPVTLQY CCLTDDRQAF RPPTRAELAR HRVVVTTTSQ ARELRVPVGF
FSHILIDEAA QMLECEALTP LAYASHGTRL VLAGDHMQVT PRLFSVARAR AAEHTLLHRL
FLCYQQETHE VARQSRLVFH ENYRCTDAIV SFISRHFYVA KGNPIHARGK VPPHPRHYPL
MFCHVAGSPD RDMSMASWLN LAEIAQVVEK VQEAYNTWPS CWGGREQRCI CVVSHGAQVS
ALRQELRRRD LGQVSVGSFE ILPGRQFRVV VLSTVHTCQS LLSPGALAPE FFTDARVLNT
VLTRAQSQLV VVGDAVALCS FGACGKLWES FIRECVERHS VCPEGLSMEQ VEQGVAQRRR
WPPRGTQAGA AGNWEAAPEP VGDLAEEQAA VVTAMVKAEP GDEALSPASR DITATTAQTE
AAAAPAGDAV KEDVVPGACA AGAAAAAGVE STEAEDAEAD FWPWDGELNA DDAILRELLD
ESQKVMVTVG EDGLLDTVAR PESLQQARLY ENLPPAALRK LLHAEPERYR HCSFVPETFE
RASAIPLDDA SSGPIQVRGR LDCGMAFAGD EVLVQLLSGD KAPEGRLRGR VLGVLKRKRH
ELAFVCRMDT WDPRIMVPIN GSVTKIFVAE LKDPSQVPIY SLRKGRLQRV GLERLTAEAR
HSRLFWVQIV LWRQGFYYPL GIVREVLPEA STWEQGLRIL GLEYSLRVPP SDQATITKVL
QKYHTELGRV AGRREDCRAF LTFTVDPQGA CNLDDALSVR DLGPRCEVAV HITDVASFVP
RDGVLDVEAR RQGAAFYAPG REPVPMLPAS LCQDVLSLLP GRDRLAISLF LTMEKASGQL
KSLRFAPSVV QSDRQLSYEE AEEVIRQHPG AGRELPARLD SVDACVVAAC YFSRLLRRHR
LRSDCFYEQP DEDGTLGFRA AHIMVKEYMI QFNRLVAEFL VGSECTRTVT PLRWQPAPRS
QQLKALCEKH GDRVPLSLHL GHHLHGGGGS PPDTRLHLLA SLWKQVQFAA RTQDYEQMVD
LVTTDDMHPF LAPAGRDLRK ALERSAFGRC ARGHQQQGGH YSLQVDWYTW ATSPIRRYLD
VVLQRQILLA LGHGGSAYSA RDIDGLCQAF SLQHALAQSY QRRARSLHLA VQLKAQPLDK
LGFVVDVEAG SRCFRLLFPS NRETLPDPCP VPYGSLQLAE HPHALAGRPG LRLLWRRRVY
SAQGSSPPLP LPGTVPDPHT LAVETALWKQ LLELVELQRW PEAAALIQEK GEASQRRELV
QVQRSHCGHF LEVARELGSG DTLQVQLGTS LQHGFLVPSP QLWTVAPGFS LCLEHVERPG
DCFSGRVYRA PRDRYRDVDE YACVWEPFCA LESATGAVAE NDSVTLQHLS VSWEASRTPQ
GQLQGAFRLE AAFLEENCAD INFSCCYLCI RLEGLPAPTA SPRPGPSSLG PGLNVDPGTY
TWVAHGQTQD WDQERRADRQ EAPRRVHLFV HHMGMEKVPE EVLRPGTLFT VELLPKQLPD
LRKEEAVRGL EEASPLVTSI ALGRPVPQPL CRVIPSRFLE RQTYNIPGGR HKLNPSQNVA
VREALEKPFT VIQGPPGTGK TIVGLHIVFW FHKSNQEQVQ PGGPPRGEKR LGGPCILYCG
PSNKSVDVLA GLLLRRMELK PLRVYSEQAE ASEFPVPRVG SRKLLRKSPR EGRPNQSLRS
ITLHHRIRQA PNPYSSEIKA FDTRLQRGEL FSREDLVWYK KVLWEARKFE LDRHEVILCT
CSCAASASLK ILDVRQILVD EAGMATEPET LIPLVQFPQA EKVVLLGDHK QLRPVVKNER
LQNLGLDRSL FERYHEDAHM LDTQYRMHEG ICAFPSVAFY KSKLKTWQGL RRPPSVLGHA
GKESCPVIFG HVQGHERSLL VSTDEGNENS KANLEEVAEV VRITKQLTLG RTVEPQDIAV
LTPYNAQASE ISKALRREGI AGVAVSSITK SQGSEWRYVL VSTVRTCAKS DLDQRPTKSW
LKKFLGFVVD PNQVNVAVTR AQEGLCLIGD HLLLRCCPLW RSLLDFCEAQ QTLVPAGQVR
VCRRPTMPS
//
|
