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Magnesium-chelatase subunit ChlH, chloroplastic (Mg-chelatase subunit H) (EC 6.6.1.1) (ABA-binding protein) (Mg-protoporphyrin IX chelatase subunit ChlH) (Protein CONDITIONAL CHLORINA) (Protein GENOMES UNCOUPLED 5) (Protein RAPID TRANSPIRATION IN DETACHED LEAVES 1)

 CHLH_ARATH              Reviewed;        1381 AA.
Q9FNB0; B9DI09; B9DI10; Q39049; Q8RY14;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 105.
RecName: Full=Magnesium-chelatase subunit ChlH, chloroplastic;
Short=Mg-chelatase subunit H;
EC=6.6.1.1;
AltName: Full=ABA-binding protein;
AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlH;
AltName: Full=Protein CONDITIONAL CHLORINA;
AltName: Full=Protein GENOMES UNCOUPLED 5;
AltName: Full=Protein RAPID TRANSPIRATION IN DETACHED LEAVES 1;
Flags: Precursor;
Name=CHLH; Synonyms=ABAR, CCH, GUN5, RTL1;
OrderedLocusNames=At5g13630; ORFNames=MSH12.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. C24;
PubMed=8685276; DOI=10.1104/pp.111.1.61;
Gibson L., Marrison J., Leech R., Jensen P., Bassham D., Gibson M.,
Hunter C.;
"A putative Mg chelatase subunit from Arabidopsis thaliana cv. C24:
sequence and transcript analysis of the gene, import of the protein
into chloroplasts and in situ localisation of the transcript.";
Plant Physiol. 111:61-71(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1381.
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-642 AND
ALA-990.
PubMed=11172074; DOI=10.1073/pnas.98.4.2053;
Mochizuki N., Brusslan J.A., Larkin R., Nagatani A., Chory J.;
"Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement
of Mg-chelatase H subunit in plastid-to-nucleus signal transduction.";
Proc. Natl. Acad. Sci. U.S.A. 98:2053-2058(2001).
[7]
INTERACTION WITH GUN4.
PubMed=12574634; DOI=10.1126/science.1079978;
Larkin R.M., Alonso J.M., Ecker J.R., Chory J.;
"GUN4, a regulator of chlorophyll synthesis and intracellular
signaling.";
Science 299:902-906(2003).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17051210; DOI=10.1038/nature05176;
Shen Y.Y., Wang X.F., Wu F.Q., Du S.Y., Cao Z., Shang Y., Wang X.L.,
Peng C.C., Yu X.C., Zhu S.Y., Fan R.C., Xu Y.H., Zhang D.P.;
"The Mg-chelatase H subunit is an abscisic acid receptor.";
Nature 443:823-826(2006).
[9]
INDUCTION BY LIGHT.
PubMed=18846290; DOI=10.1039/b802596g;
Stephenson P.G., Terry M.J.;
"Light signalling pathways regulating the Mg-chelatase branchpoint of
chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
Photochem. Photobiol. Sci. 7:1243-1252(2008).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19363094; DOI=10.1104/pp.109.135368;
Huang Y.S., Li H.M.;
"Arabidopsis CHLI2 can substitute for CHLI1.";
Plant Physiol. 150:636-645(2009).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19535472; DOI=10.1104/pp.109.140731;
Wu F.Q., Xin Q., Cao Z., Liu Z.Q., Du S.Y., Mei C., Zhao C.X.,
Wang X.F., Shang Y., Jiang T., Zhang X.F., Yan L., Zhao R., Cui Z.N.,
Liu R., Sun H.L., Yang X.L., Su Z., Zhang D.P.;
"The magnesium-chelatase H subunit binds abscisic acid and functions
in abscisic acid signaling: new evidence in Arabidopsis.";
Plant Physiol. 150:1940-1954(2009).
[12]
FUNCTION, INTERACTION WITH WRKY40, AND SUBCELLULAR LOCATION.
PubMed=20543028; DOI=10.1105/tpc.110.073874;
Shang Y., Yan L., Liu Z.Q., Cao Z., Mei C., Xin Q., Wu F.Q.,
Wang X.F., Du S.Y., Jiang T., Zhang X.F., Zhao R., Sun H.L., Liu R.,
Yu Y.T., Zhang D.P.;
"The Mg-chelatase H subunit of Arabidopsis antagonizes a group of WRKY
transcription repressors to relieve ABA-responsive genes of
inhibition.";
Plant Cell 22:1909-1935(2010).
[13]
FUNCTION, AND MUTAGENESIS OF LEU-690.
PubMed=21562844; DOI=10.1007/s10265-011-0426-x;
Tsuzuki T., Takahashi K., Inoue S., Okigaki Y., Tomiyama M.,
Hossain M.A., Shimazaki K., Murata Y., Kinoshita T.;
"Mg-chelatase H subunit affects ABA signaling in stomatal guard cells,
but is not an ABA receptor in Arabidopsis thaliana.";
J. Plant Res. 124:527-538(2011).
[14]
SUBCELLULAR LOCATION.
PubMed=21467578; DOI=10.1105/tpc.110.082503;
Adhikari N.D., Froehlich J.E., Strand D.D., Buck S.M., Kramer D.M.,
Larkin R.M.;
"GUN4-porphyrin complexes bind the ChlH/GUN5 subunit of Mg-Chelatase
and promote chlorophyll biosynthesis in Arabidopsis.";
Plant Cell 23:1449-1467(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-50, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
INTERACTION WITH CHLI1 AND CHLD, FUNCTION, AND MUTAGENESIS OF PRO-642
AND LEU-690.
PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
Zhang D.P.;
"Roles of the different components of magnesium chelatase in abscisic
acid signal transduction.";
Plant Mol. Biol. 80:519-537(2012).
-!- FUNCTION: Multifunctional protein involved in chlorophyll
synthesis, plastid-to-nucleus retrograde signaling and abscisic
acid (ABA) perception. In chlorophyll synthesis, catalyzes the
insertion of magnesium ion into protoporphyrin IX to yield Mg-
protoporphyrin IX. The reaction takes place in two steps, with an
ATP-dependent activation followed by an ATP-dependent chelation
step. In addition to its function in the Mg-chelatase enzyme, is
required for the plastid-to-nucleus retrograde signaling. The
plastid-to-nucleus signal plays an important role in the
coordinated expression of both nuclear- and chloroplast-localized
genes that encode photosynthesis-related proteins. Has a role in
mediating ABA signaling in stomatal guard cells and during seed
germination. Binds ABA and is a positive regulator of ABA
signaling. {ECO:0000269|PubMed:11172074,
ECO:0000269|PubMed:17051210, ECO:0000269|PubMed:19363094,
ECO:0000269|PubMed:19535472, ECO:0000269|PubMed:20543028,
ECO:0000269|PubMed:21562844, ECO:0000269|PubMed:23011401}.
-!- CATALYTIC ACTIVITY: ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP
+ phosphate + Mg-protoporphyrin IX + 2 H(+).
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis.
-!- SUBUNIT: The magnesium chelatase complex is a heterotrimer
consisting of subunits CHLI, CHLD, AND CHLH. Interacts with GUN4,
WRKY18, WRKY40, WRKY60, CHLI1 and CHLD.
{ECO:0000269|PubMed:12574634, ECO:0000269|PubMed:20543028,
ECO:0000269|PubMed:23011401}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid,
chloroplast membrane; Peripheral membrane protein; Stromal side.
Plastid, chloroplast membrane; Peripheral membrane protein;
Cytoplasmic side. Note=Predominantly associated with the
chloroplast envelope. Spans the chloroplast envelope and is its
N- and C-termini are exposed to the cytosol (PubMed:20543028).
{ECO:0000269|PubMed:20543028}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9FNB0-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:17051210}.
-!- INDUCTION: By red, far-red and blue light. Down-regulated by white
light. {ECO:0000269|PubMed:18846290}.
-!- DISRUPTION PHENOTYPE: Pale-green phenotype with low survival rates
during de-etiolation and severe embryonic lethality when
homozygous. Chli1 and chli2 double mutants are albino.
{ECO:0000269|PubMed:11172074, ECO:0000269|PubMed:19363094}.
-!- MISCELLANEOUS: Plants silencing CHLH show significant ABA-
insensitive phenotypes in seed germination, post-germination
growth arrest by ABA and ABA-induced promotion of stomatal closure
and inhibition of stomatal opening. In contrast, plants over-
expressing ABAR display ABA-hypersensitive phenotypes
(PubMed:17051210). {ECO:0000305|PubMed:17051210}.
-!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
{ECO:0000305}.
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EMBL; Z68495; CAA92802.1; -; mRNA.
EMBL; AB006704; BAB08689.1; -; Genomic_DNA.
EMBL; CP002688; AED91919.1; -; Genomic_DNA.
EMBL; AY070133; AAL47483.1; -; mRNA.
EMBL; AY078971; AAL79577.1; -; mRNA.
EMBL; BT002311; AAN73308.1; -; mRNA.
EMBL; AK317719; BAH20377.1; -; mRNA.
EMBL; AK317718; BAH20376.1; -; mRNA.
PIR; S71288; S71288.
RefSeq; NP_196867.1; NM_121366.4. [Q9FNB0-1]
UniGene; At.23621; -.
PDB; 5EWU; X-ray; 1.25 A; A/B=994-1381.
PDBsum; 5EWU; -.
ProteinModelPortal; Q9FNB0; -.
SMR; Q9FNB0; -.
BioGrid; 16485; 6.
STRING; 3702.AT5G13630.1; -.
iPTMnet; Q9FNB0; -.
PaxDb; Q9FNB0; -.
PRIDE; Q9FNB0; -.
EnsemblPlants; AT5G13630.1; AT5G13630.1; AT5G13630. [Q9FNB0-1]
GeneID; 831207; -.
Gramene; AT5G13630.1; AT5G13630.1; AT5G13630. [Q9FNB0-1]
KEGG; ath:AT5G13630; -.
Araport; AT5G13630; -.
TAIR; locus:2173234; AT5G13630.
eggNOG; ENOG410IHVQ; Eukaryota.
eggNOG; COG1429; LUCA.
HOGENOM; HOG000152424; -.
InParanoid; Q9FNB0; -.
KO; K03403; -.
OMA; ELQEMYL; -.
OrthoDB; EOG0936008K; -.
PhylomeDB; Q9FNB0; -.
BioCyc; MetaCyc:AT5G13630-MONOMER; -.
UniPathway; UPA00668; -.
PRO; PR:Q9FNB0; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FNB0; baseline and differential.
Genevisible; Q9FNB0; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009706; C:chloroplast inner membrane; NAS:TAIR.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016851; F:magnesium chelatase activity; ISS:TAIR.
GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
InterPro; IPR011771; BchH.
InterPro; IPR003672; CobN/Mg_chltase.
InterPro; IPR022571; Mg_chelatase_H_N.
Pfam; PF02514; CobN-Mg_chel; 1.
Pfam; PF11965; DUF3479; 1.
TIGRFAMs; TIGR02025; BchH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Chlorophyll biosynthesis; Chloroplast; Complete proteome; Ligase;
Membrane; Nucleotide-binding; Photosynthesis; Plastid;
Reference proteome; Transit peptide.
TRANSIT 1 49 Chloroplast.
{ECO:0000244|PubMed:22223895}.
CHAIN 50 1381 Magnesium-chelatase subunit ChlH,
chloroplastic.
/FTId=PRO_0000418765.
MOD_RES 50 50 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 642 642 P->L: In cch; semi-dwarf plants with pale
green leaves and ABA-insensitive stomatal
movment. {ECO:0000269|PubMed:11172074,
ECO:0000269|PubMed:23011401}.
MUTAGEN 690 690 L->F: In rtl1; semi-dwarf plants with
pale green leaves and ABA-insensitive
stomatal movment.
{ECO:0000269|PubMed:21562844,
ECO:0000269|PubMed:23011401}.
MUTAGEN 990 990 A->V: In gun5; semi-dwarf plants with
pale green leaves.
{ECO:0000269|PubMed:11172074}.
CONFLICT 224 224 V -> G (in Ref. 4; AAL79577).
{ECO:0000305}.
CONFLICT 433 433 N -> K (in Ref. 1; CAA92802).
{ECO:0000305}.
CONFLICT 588 588 A -> P (in Ref. 1; CAA92802).
{ECO:0000305}.
CONFLICT 739 739 L -> V (in Ref. 1; CAA92802).
{ECO:0000305}.
CONFLICT 987 989 NIH -> TSI (in Ref. 1; CAA92802).
{ECO:0000305}.
CONFLICT 1110 1111 EL -> DV (in Ref. 1; CAA92802).
{ECO:0000305}.
HELIX 999 1019 {ECO:0000244|PDB:5EWU}.
TURN 1020 1022 {ECO:0000244|PDB:5EWU}.
STRAND 1026 1032 {ECO:0000244|PDB:5EWU}.
HELIX 1034 1040 {ECO:0000244|PDB:5EWU}.
HELIX 1043 1052 {ECO:0000244|PDB:5EWU}.
STRAND 1054 1058 {ECO:0000244|PDB:5EWU}.
STRAND 1064 1069 {ECO:0000244|PDB:5EWU}.
HELIX 1072 1075 {ECO:0000244|PDB:5EWU}.
STRAND 1081 1086 {ECO:0000244|PDB:5EWU}.
HELIX 1088 1093 {ECO:0000244|PDB:5EWU}.
HELIX 1095 1109 {ECO:0000244|PDB:5EWU}.
HELIX 1115 1117 {ECO:0000244|PDB:5EWU}.
HELIX 1119 1131 {ECO:0000244|PDB:5EWU}.
HELIX 1135 1138 {ECO:0000244|PDB:5EWU}.
STRAND 1142 1144 {ECO:0000244|PDB:5EWU}.
HELIX 1154 1160 {ECO:0000244|PDB:5EWU}.
HELIX 1166 1177 {ECO:0000244|PDB:5EWU}.
HELIX 1186 1188 {ECO:0000244|PDB:5EWU}.
STRAND 1190 1192 {ECO:0000244|PDB:5EWU}.
HELIX 1194 1202 {ECO:0000244|PDB:5EWU}.
STRAND 1206 1211 {ECO:0000244|PDB:5EWU}.
TURN 1213 1215 {ECO:0000244|PDB:5EWU}.
TURN 1218 1220 {ECO:0000244|PDB:5EWU}.
HELIX 1223 1227 {ECO:0000244|PDB:5EWU}.
HELIX 1230 1236 {ECO:0000244|PDB:5EWU}.
STRAND 1244 1249 {ECO:0000244|PDB:5EWU}.
STRAND 1251 1254 {ECO:0000244|PDB:5EWU}.
STRAND 1256 1259 {ECO:0000244|PDB:5EWU}.
HELIX 1260 1270 {ECO:0000244|PDB:5EWU}.
TURN 1271 1273 {ECO:0000244|PDB:5EWU}.
HELIX 1275 1283 {ECO:0000244|PDB:5EWU}.
HELIX 1285 1306 {ECO:0000244|PDB:5EWU}.
HELIX 1311 1321 {ECO:0000244|PDB:5EWU}.
HELIX 1325 1334 {ECO:0000244|PDB:5EWU}.
HELIX 1336 1351 {ECO:0000244|PDB:5EWU}.
HELIX 1359 1375 {ECO:0000244|PDB:5EWU}.
SEQUENCE 1381 AA; 153574 MW; 8EBAD26670A7B336 CRC64;
MASLVYSPFT LSTSKAEHLS SLTNSTKHSF LRKKHRSTKP AKSFFKVKSA VSGNGLFTQT
NPEVRRIVPI KRDNVPTVKI VYVVLEAQYQ SSLSEAVQSL NKTSRFASYE VVGYLVEELR
DKNTYNNFCE DLKDANIFIG SLIFVEELAI KVKDAVEKER DRMDAVLVFP SMPEVMRLNK
LGSFSMSQLG QSKSPFFQLF KRKKQGSAGF ADSMLKLVRT LPKVLKYLPS DKAQDARLYI
LSLQFWLGGS PDNLQNFVKM ISGSYVPALK GVKIEYSDPV LFLDTGIWHP LAPTMYDDVK
EYWNWYDTRR DTNDSLKRKD ATVVGLVLQR SHIVTGDDSH YVAVIMELEA RGAKVVPIFA
GGLDFSGPVE KYFVDPVSKQ PIVNSAVSLT GFALVGGPAR QDHPRAIEAL KKLDVPYLVA
VPLVFQTTEE WLNSTLGLHP IQVALQVALP ELDGAMEPIV FAGRDPRTGK SHALHKRVEQ
LCIRAIRWGE LKRKTKAEKK LAITVFSFPP DKGNVGTAAY LNVFASIFSV LRDLKRDGYN
VEGLPENAET LIEEIIHDKE AQFSSPNLNV AYKMGVREYQ DLTPYANALE ENWGKPPGNL
NSDGENLLVY GKAYGNVFIG VQPTFGYEGD PMRLLFSKSA SPHHGFAAYY SYVEKIFKAD
AVLHFGTHGS LEFMPGKQVG MSDACFPDSL IGNIPNVYYY AANNPSEATI AKRRSYANTI
SYLTPPAENA GLYKGLKQLS ELISSYQSLK DTGRGPQIVS SIISTAKQCN LDKDVDLPDE
GLELSPKDRD SVVGKVYSKI MEIESRLLPC GLHVIGEPPS AMEAVATLVN IAALDRPEDE
ISALPSILAE CVGREIEDVY RGSDKGILSD VELLKEITDA SRGAVSAFVE KTTNSKGQVV
DVSDKLTSLL GFGINEPWVE YLSNTKFYRA NRDKLRTVFG FLGECLKLVV MDNELGSLMQ
ALEGKYVEPG PGGDPIRNPK VLPTGKNIHA LDPQAIPTTA AMASAKIVVE RLVERQKLEN
EGKYPETIAL VLWGTDNIKT YGESLGQVLW MIGVRPIADT FGRVNRVEPV SLEELGRPRI
DVVVNCSGVF RDLFINQMNL LDRAIKMVAE LDEPVEQNFV RKHALEQAEA LGIDIREAAT
RVFSNASGSY SANISLAVEN SSWNDEKQLQ DMYLSRKSFA FDSDAPGAGM AEKKQVFEMA
LSTAEVTFQN LDSSEISLTD VSHYFDSDPT NLVQSLRKDK KKPSSYIADT TTANAQVRTL
SETVRLDART KLLNPKWYEG MMSSGYEGVR EIEKRLSNTV GWSATSGQVD NWVYEEANST
FIQDEEMLNR LMNTNPNSFR KMLQTFLEAN GRGYWDTSAE NIEKLKELYS QVEDKIEGID
R


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EIAAB29458 Homo sapiens,Human,PP2A subunit B isoform PR48,PPP2R3B,PPP2R3L,Protein phosphatase 2A 48 kDa regulatory subunit,Serine_threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
EIAAB32114 33 kDa glycogen-binding protein,Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 r
EIAAB46625 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Mouse,Msy1,Msy-1,Mus musculus,Nsep1,Nuclease-sensitive element-binding protein 1,Yb1,Y
EIAAB46626 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Homo sapiens,Human,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box t
EIAAB46624 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Msy-1,Nsep1,Nuclease-sensitive element-binding protein 1,Rat,Rattus norvegicus,Yb1,YB-
EIAAB46627 Bos taurus,Bovine,CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box tr
EIAAB46584 86 kDa subunit of Ku antigen,ATP-dependent DNA helicase 2 subunit 2,ATP-dependent DNA helicase II 80 kDa subunit,CTC box-binding factor 85 kDa subunit,CTC85,CTCBF,DNA repair protein XRCC5,G22P2,Homo s
20-272-191788 RFC1 - Mouse monoclonal [1320] to RFC1; Replication factor C large subunit; RF-C 140 kDa subunit; Activator 1 140 kDa subunit; Activator 1 large subunit; A1 140 kDa subunit; DNA-binding protein PO-GA 0.05 mg
EIAAB32659 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,Homo sapiens,Human,MB67-interacting protein,MIP224,MIP224,Proteasome 26S subunit ATPase 4,PSMC4,Tat-binding protein 7,TBP7,TBP
EIAAB32120 Homo sapiens,Human,PP1 subunit R5,PPP1R3C,PPP1R5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
EIAAB32654 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Homo sapiens,Human,Proteasome 26S subunit ATPase 3,Proteasome subunit P50,PSMC3,Tat-binding protein 1,TBP1,TBP-1
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1


 

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