(data stored in ACNUC13479 zone)

SWISSPROT: ATL56_ARATH

ID   ATL56_ARATH             Reviewed;         181 AA.
AC   Q9ZV51; Q8L900;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   30-AUG-2017, entry version 124.
DE   RecName: Full=RING-H2 finger protein ATL56;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL56 {ECO:0000305};
GN   Name=ATL56; OrderedLocusNames=At2g18670; ORFNames=MSF3.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=15644464; DOI=10.1104/pp.104.052423;
RA   Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E.,
RA   Callis J.;
RT   "Functional analysis of the RING-type ubiquitin ligase family of
RT   Arabidopsis.";
RL   Plant Physiol. 137:13-30(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA   Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT   "Evaluation and classification of RING-finger domains encoded by the
RT   Arabidopsis genome.";
RL   Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN   [7]
RP   NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX   PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA   Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT   "The ATL gene family from Arabidopsis thaliana and Oryza sativa
RT   comprises a large number of putative ubiquitin ligases of the RING-H2
RT   type.";
RL   J. Mol. Evol. 62:434-445(2006).
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine. {ECO:0000305}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL
CC       subfamily. {ECO:0000305}.
DR   EMBL; DQ059107; AAY57593.1; -; mRNA.
DR   EMBL; AC005724; AAD08936.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06791.1; -; Genomic_DNA.
DR   EMBL; AY052699; AAK96603.1; -; mRNA.
DR   EMBL; AY098955; AAM19965.1; -; mRNA.
DR   EMBL; AY088712; AAM67030.1; -; mRNA.
DR   PIR; B84567; B84567.
DR   RefSeq; NP_179457.1; NM_127423.4.
DR   UniGene; At.13211; -.
DR   UniGene; At.69600; -.
DR   UniGene; At.73918; -.
DR   ProteinModelPortal; Q9ZV51; -.
DR   SMR; Q9ZV51; -.
DR   STRING; 3702.AT2G18670.1; -.
DR   PaxDb; Q9ZV51; -.
DR   EnsemblPlants; AT2G18670.1; AT2G18670.1; AT2G18670.
DR   GeneID; 816382; -.
DR   Gramene; AT2G18670.1; AT2G18670.1; AT2G18670.
DR   KEGG; ath:AT2G18670; -.
DR   Araport; AT2G18670; -.
DR   TAIR; locus:2053994; AT2G18670.
DR   eggNOG; KOG0800; Eukaryota.
DR   eggNOG; ENOG41121N2; LUCA.
DR   HOGENOM; HOG000237642; -.
DR   InParanoid; Q9ZV51; -.
DR   OMA; TRYESDC; -.
DR   OrthoDB; EOG09360ROW; -.
DR   PhylomeDB; Q9ZV51; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9ZV51; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q9ZV51; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9ZV51.
DR   SWISS-2DPAGE; Q9ZV51.
KW   Complete proteome; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    181       RING-H2 finger protein ATL56.
FT                                /FTId=PRO_0000396124.
FT   TRANSMEM     32     52       Helical. {ECO:0000255}.
FT   ZN_FING     110    152       RING-type; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   COMPBIAS     70     77       Poly-Arg.
FT   CONFLICT     20     20       H -> P (in Ref. 5; AAM67030).
FT                                {ECO:0000305}.
SQ   SEQUENCE   181 AA;  21067 MW;  F72C6A93374BD14E CRC64;
     MPPTNNYRIS GEPPSTTPSH PPPKPKTRIL SLFLVGVIMF SIFFLFLVLI GIASVLILPL
     LLSSLHRHHR RRRRNRRQES SDGLSSRFVK KLPQFKFSEP STYTRYESDC VVCFDGFRQG
     QWCRNLPGCG HVFHRKCVDT WLLKASTCPI CRARVRLWEE DPQEGELWRC FGHRRSSLLD
     L
//

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