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UBQ10_ARATH
ID   UBQ10_ARATH             Reviewed;         457 AA.
AC   Q8H159; O80715; P59263; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9; Q9S7X3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Polyubiquitin 10;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor;
GN   Name=UBQ10; OrderedLocusNames=At4g05320; ORFNames=C17L7.240;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7713442; DOI=10.1093/genetics/139.2.921;
RA   Callis J., Carpenter T., Sun C.W., Vierstra R.D.;
RT   "Structure and evolution of genes encoding polyubiquitin and ubiquitin-like
RT   proteins in Arabidopsis thaliana ecotype Columbia.";
RL   Genetics 139:921-939(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated
CC       degradation) and in cell-cycle regulation; Lys-29-linked is involved in
CC       lysosomal degradation; Lys-33-linked is involved in kinase
CC       modification; Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage
CC       responses. Linear polymer chains formed via attachment by the initiator
CC       Met lead to cell signaling. Ubiquitin is usually conjugated to Lys
CC       residues of target proteins, however, in rare cases, conjugation to Cys
CC       or Ser residues has been observed. When polyubiquitin is free
CC       (unanchored-polyubiquitin), it also has distinct roles, such as in
CC       activation of protein kinases, and in signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8H159-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8H159-2; Sequence=VSP_041600;
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes. Ubiquitin is
CC       generally synthesized as a polyubiquitin precursor with tandem head to
CC       tail repeats. Often, there is one to three additional amino acids after
CC       the last repeat, removed in the mature protein. Alternatively,
CC       ubiquitin extension protein is synthesized as a single copy of
CC       ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a
CC       ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC       extension protein is cleaved from ubiquitin.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC       only for the first chain, and are not repeated for each of the
CC       following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN31845.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB81074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; L05361; AAA68878.1; -; mRNA.
DR   EMBL; AC012392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161503; CAB81074.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82500.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82502.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82503.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67151.1; -; Genomic_DNA.
DR   EMBL; AY139999; AAM98141.1; -; mRNA.
DR   EMBL; BT000701; AAN31845.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001118922.1; NM_001125450.2. [Q8H159-2]
DR   RefSeq; NP_001328998.1; NM_001340547.1. [Q8H159-2]
DR   RefSeq; NP_849292.1; NM_178961.1. [Q8H159-2]
DR   RefSeq; NP_849299.4; NM_178968.5. [Q8H159-1]
DR   RefSeq; NP_849301.4; NM_178970.5. [Q8H159-1]
DR   RefSeq; NP_974516.4; NM_202787.4. [Q8H159-2]
DR   AlphaFoldDB; Q8H159; -.
DR   SMR; Q8H159; -.
DR   BioGRID; 11191; 13.
DR   BioGRID; 13437; 3.
DR   IntAct; Q8H159; 1.
DR   STRING; 3702.AT4G05320.2; -.
DR   PaxDb; Q8H159; -.
DR   EnsemblPlants; AT4G02890.3; AT4G02890.3; AT4G02890.
DR   EnsemblPlants; AT4G02890.4; AT4G02890.4; AT4G02890.
DR   EnsemblPlants; AT4G05320.2; AT4G05320.2; AT4G05320. [Q8H159-1]
DR   EnsemblPlants; AT4G05320.4; AT4G05320.4; AT4G05320. [Q8H159-1]
DR   EnsemblPlants; AT4G05320.5; AT4G05320.5; AT4G05320.
DR   EnsemblPlants; AT4G05320.8; AT4G05320.8; AT4G05320.
DR   GeneID; 825880; -.
DR   GeneID; 828148; -.
DR   Gramene; AT4G02890.3; AT4G02890.3; AT4G02890.
DR   Gramene; AT4G02890.4; AT4G02890.4; AT4G02890.
DR   Gramene; AT4G05320.2; AT4G05320.2; AT4G05320. [Q8H159-1]
DR   Gramene; AT4G05320.4; AT4G05320.4; AT4G05320. [Q8H159-1]
DR   Gramene; AT4G05320.5; AT4G05320.5; AT4G05320.
DR   Gramene; AT4G05320.8; AT4G05320.8; AT4G05320.
DR   KEGG; ath:AT4G02890; -.
DR   KEGG; ath:AT4G05320; -.
DR   Araport; AT4G05320; -.
DR   TAIR; locus:2115663; AT4G05320.
DR   eggNOG; KOG0001; Eukaryota.
DR   HOGENOM; CLU_010412_7_1_1; -.
DR   InParanoid; Q8H159; -.
DR   PhylomeDB; Q8H159; -.
DR   PRO; PR:Q8H159; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8H159; baseline and differential.
DR   Genevisible; Q8H159; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 6.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 6.
DR   SUPFAM; SSF54236; SSF54236; 6.
DR   PROSITE; PS00299; UBIQUITIN_1; 6.
DR   PROSITE; PS50053; UBIQUITIN_2; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396888"
FT   CHAIN           77..152
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396889"
FT   CHAIN           153..228
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396890"
FT   CHAIN           229..304
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396891"
FT   CHAIN           305..380
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396892"
FT   CHAIN           381..456
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396893"
FT   PROPEP          457
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000396894"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          77..152
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          229..304
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          305..380
FT                   /note="Ubiquitin-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          381..456
FT                   /note="Ubiquitin-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   VAR_SEQ         1..152
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041600"
SQ   SEQUENCE   457 AA;  51206 MW;  A1BF346A29F15F43 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVESSDT IDNVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VESSDTIDNV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     ADYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ
     QRLIFAGKQL EDGRTLADYN IQKESTLHLV LRLRGGF
 
 
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