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Probable ubiquitin-conjugating enzyme E2 24 (EC 2.3.2.23) (AtPHO2) (E2 ubiquitin-conjugating enzyme 24) (Ubiquitin carrier protein 24) (Ubiquitin-protein ligase 24)

 UBC24_ARATH             Reviewed;         907 AA.
Q8VY10; P93012; Q0WLN6; Q0WM96;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
30-AUG-2017, entry version 121.
RecName: Full=Probable ubiquitin-conjugating enzyme E2 24 {ECO:0000303|PubMed:16339806};
EC=2.3.2.23 {ECO:0000305};
AltName: Full=AtPHO2 {ECO:0000303|PubMed:16679424};
AltName: Full=E2 ubiquitin-conjugating enzyme 24 {ECO:0000303|PubMed:16339806};
AltName: Full=Ubiquitin carrier protein 24 {ECO:0000303|PubMed:16339806};
AltName: Full=Ubiquitin-protein ligase 24 {ECO:0000303|PubMed:16339806};
Name=UBC24 {ECO:0000303|PubMed:16339806};
Synonyms=PHO2 {ECO:0000303|PubMed:16679424};
OrderedLocusNames=At2g33770 {ECO:0000312|Araport:AT2G33770};
ORFNames=T1B8.8 {ECO:0000312|EMBL:AAC69130.1};
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] (ISOFORM 1), GENE FAMILY, AND NOMENCLATURE.
PubMed=16339806; DOI=10.1104/pp.105.067983;
Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
Callis J.;
"Genome analysis and functional characterization of the E2 and RING-
type E3 ligase ubiquitination enzymes of Arabidopsis.";
Plant Physiol. 139:1597-1611(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DEVELOPMENTAL
STAGE, TISSUE SPECIFICITY, AND REGULATION BY MIR399.
PubMed=16679424; DOI=10.1104/pp.106.079707;
Bari R., Datt Pant B., Stitt M., Scheible W.-R.;
"PHO2, microRNA399, and PHR1 define a phosphate-signaling pathway in
plants.";
Plant Physiol. 141:988-999(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, REGULATION BY
MIR399, AND TISSUE SPECIFICITY.
PubMed=16679417; DOI=10.1104/pp.106.078063;
Aung K., Lin S.-I., Wu C.-C., Huang Y.-T., Su C.-L., Chiou T.-J.;
"pho2, a phosphate overaccumulator, is caused by a nonsense mutation
in a microRNA399 target gene.";
Plant Physiol. 141:1000-1011(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
REGULATION BY MIR399.
PubMed=17643101; DOI=10.1038/ng2079;
Franco-Zorrilla J.M., Valli A., Todesco M., Mateos I., Puga M.I.,
Rubio-Somoza I., Leyva A., Weigel D., Garcia J.A., Paz-Ares J.;
"Target mimicry provides a new mechanism for regulation of microRNA
activity.";
Nat. Genet. 39:1033-1037(2007).
[9]
FUNCTION, AND INDUCTION.
PubMed=18390805; DOI=10.1104/pp.108.116269;
Lin S.-I., Chiang S.-F., Lin W.-Y., Chen J.-W., Tseng C.-Y., Wu P.-C.,
Chiou T.-J.;
"Regulatory network of MicroRNA399 and PHO2 by systemic signaling.";
Plant Physiol. 147:732-746(2008).
[10]
FUNCTION, INTERACTION WITH PHO1, MUTAGENESIS OF CYS-748, AND
SUBCELLULAR LOCATION.
PubMed=22634761; DOI=10.1105/tpc.112.096636;
Liu T.Y., Huang T.K., Tseng C.Y., Lai Y.S., Lin S.I., Lin W.Y.,
Chen J.W., Chiou T.J.;
"PHO2-dependent degradation of PHO1 modulates phosphate homeostasis in
Arabidopsis.";
Plant Cell 24:2168-2183(2012).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24122829; DOI=10.1105/tpc.113.115998;
Huang T.K., Han C.L., Lin S.I., Chen Y.J., Tsai Y.C., Chen Y.R.,
Chen J.W., Lin W.Y., Chen P.M., Liu T.Y., Chen Y.S., Sun C.M.,
Chiou T.J.;
"Identification of downstream components of ubiquitin-conjugating
enzyme PHOSPHATE2 by quantitative membrane proteomics in Arabidopsis
roots.";
Plant Cell 25:4044-4060(2013).
-!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes
its covalent attachment to other proteins (By similarity).
Mediates PHO1 degradation through multivesicular body-mediated
vacuolar proteolysis in response to inorganic phosphate (Pi)
availability (PubMed:22634761). Negatively regulates the protein
abundance of PHF1 and PHT1s under Pi-sufficient conditions by
facilitating the degradation of PHT1 proteins at the endomembrane
(PubMed:24122829). {ECO:0000250|UniProtKB:P42743,
ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000305}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with PHO1. {ECO:0000269|PubMed:22634761}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:22634761,
ECO:0000269|PubMed:24122829}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8VY10-1; Sequence=Displayed;
Name=2;
IsoId=Q8VY10-2; Sequence=VSP_034751;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the vascular tissues of
cotyledons, leaves, roots, sepals, filaments, anthers and
junctions between the inflorescence stems and siliques.
{ECO:0000269|PubMed:16679417, ECO:0000269|PubMed:16679424}.
-!- DEVELOPMENTAL STAGE: Up-regulated in senescing leaves and
maturating seeds. {ECO:0000269|PubMed:16679424}.
-!- INDUCTION: Down-regulated by phosphate deprivation
(PubMed:16679424). Systemically regulated by microRNA399 (miR399)
(PubMed:16679424, PubMed:18390805). {ECO:0000269|PubMed:16679424,
ECO:0000269|PubMed:18390805}.
-!- DISRUPTION PHENOTYPE: Plants are unable to regulate the amount of
phosphate accumulated into shoots. {ECO:0000269|PubMed:16679417}.
-!- MISCELLANEOUS: MicroRNA399 (miR399) can be sequestered by IPS1, a
non-protein coding RNA containing a motif with sequence
complementarity to miR399, but with a mismatched loop at the
expected miRNA cleavage site. Thus IPS1 mimics the target of
miR399 to block the cleavage of UBC24/PHO2 under Pi-deficient
conditions. {ECO:0000269|PubMed:17643101}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAC69130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ027037; AAY44863.1; -; mRNA.
EMBL; U78721; AAC69130.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC08882.1; -; Genomic_DNA.
EMBL; AY074292; AAL66989.1; -; mRNA.
EMBL; AY091326; AAM14265.1; -; mRNA.
EMBL; AK229934; BAF01760.1; -; mRNA.
EMBL; AK230162; BAF01971.1; -; mRNA.
PIR; D84749; D84749.
RefSeq; NP_850218.1; NM_179887.3. [Q8VY10-1]
UniGene; At.14693; -.
ProteinModelPortal; Q8VY10; -.
SMR; Q8VY10; -.
BioGrid; 3290; 1.
STRING; 3702.AT2G33770.1; -.
PaxDb; Q8VY10; -.
EnsemblPlants; AT2G33770.1; AT2G33770.1; AT2G33770. [Q8VY10-1]
GeneID; 817943; -.
Gramene; AT2G33770.1; AT2G33770.1; AT2G33770.
KEGG; ath:AT2G33770; -.
Araport; AT2G33770; -.
TAIR; locus:2057589; AT2G33770.
eggNOG; KOG0895; Eukaryota.
eggNOG; ENOG410XQ7W; LUCA.
HOGENOM; HOG000237457; -.
InParanoid; Q8VY10; -.
KO; K10581; -.
OMA; GCKNSST; -.
OrthoDB; EOG0936025V; -.
PhylomeDB; Q8VY10; -.
UniPathway; UPA00143; -.
PRO; PR:Q8VY10; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; Q8VY10; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0044257; P:cellular protein catabolic process; IGI:TAIR.
GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
GO; GO:0055062; P:phosphate ion homeostasis; IMP:TAIR.
GO; GO:0006817; P:phosphate ion transport; IMP:TAIR.
GO; GO:2000185; P:regulation of phosphate transmembrane transport; IGI:TAIR.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Endoplasmic reticulum; Golgi apparatus; Ligase; Membrane;
Nucleotide-binding; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 907 Probable ubiquitin-conjugating enzyme E2
24.
/FTId=PRO_0000344361.
COMPBIAS 480 578 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
ACT_SITE 748 748 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
VAR_SEQ 1 476 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_034751.
MUTAGEN 748 748 C->A: Loss of ubiquitin conjugase
activity and loss of down-regulation of
PHO1. {ECO:0000269|PubMed:22634761}.
SEQUENCE 907 AA; 100484 MW; 6C9CB1D8A3A95359 CRC64;
MEMSLTDSDW DSSSDSGSSE HEEVEFSYGG RAQNIFSNLE ETIGKIDEFL SFERGFMYGD
IVRSATEPSG QSGRVINIDM FVNLESTHGK IMKEVDTKRL QKLRSISLSD YVINGPWVGR
VDKIVERVSV TLDDGTNYEV LVDGQDKLVA IPPNLLEDSQ YSYYPGQRVQ VKLAHAPRST
TWLCGTWRGT QVMGTVCTVE AGLVYVDWVA SIVMEGDRNL TAPQALQNPE SLTLLPCVSH
ASWQLGDWCI LPGSSHCDIA ERQTPNVAAY NLNECHKTFQ KGFNRNMQNS GLDELFVITK
TKMKVAVMWQ DGSCSLGVDS QQLLPVGAVN AHDFWPEQFV VEKETCNSKK WGVVKAVNAK
EQTVKVQWTI QVEKEATGCV DEVMEEIVSA YELLEHPDFG FCFSDVVVKL LPEGKFDPNA
DTIVATEAKH LLTESDYSGA YFLSSIGVVT GFKNGSVKVK WANGSTSKVA PCEIWKMERS
EYSNSSTVSS EGSVQDLSQK ISQSDEASSN HQETGLVKLY SVGESCNENI PECSSFFLPK
AAIGFITNLA SSLFGYQGST SVISSHSRCN DSEDQSDSEV LVQETAESYD NSETNSGEVD
MTTTMVNIPI EGKGINKTLD STLLENSRNQ VRFRQFDMVN DCSDHHFLSS DKGLAQSQVT
KSWVKKVQQE WSNLEANLPN TIYVRVCEER MDLLRAALVG APGTPYHDGL FFFDIMLPPQ
YPHEPPMVHY HSGGMRLNPN LYESGRVCLS LLNTWSGSGT EVWNAGSSSI LQLLLSFQAL
VLNEKPYFNE AGYDKQLGRA EGEKNSVSYN ENAFLITCKS MISMLRKPPK HFEMLVKDHF
THRAQHVLAA CKAYMEGVPV GSSANLQGNS TTNSTGFKIM LSKLYPKLLE AFSEIGVDCV
QEIGPES


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