P59232 (R27AB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-40S ribosomal protein S27a-2

Cleaved into the following 2 chains:

1. Ubiquitin
2. 40S ribosomal protein S27a-2

Gene names

Name:	RPS27AB
Synonyms:	UBQ6
Ordered Locus Names:	At2g47110
ORF Names:	F14M4.6

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling By similarity. Ribosomal protein RSP27a-2 is a component of the 40S subunit of the ribosome.
Subunit structure	Ribosomal protein RSP27a-2 is part of the 40S ribosomal subunit By similarity.
Subcellular location	Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.
Miscellaneous	Ubiquitin is encoded by 16 different genes. Ubiquitin is generally synthesized as a polyubiquitin precursor with tandem head to tail repeats. Often, there is one to three additional amino-acids after the last repeat, removed in the mature protein. Alternatively, ubiquitin extension protein is synthesized as a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27A) or to an ubiquitin-related protein (either RUB1 or RUB2). Following translation, extension protein is cleaved from ubiquitin.
Sequence similarities	In the N-terminal section; belongs to the ubiquitin family. In the C-terminal section; belongs to the ribosomal protein S27Ae family. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity Ref.1. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR cytosolic small ribosomal subunit Inferred from direct assay PubMed 17934214. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 76	76	Ubiquitin		PRO_0000396872
	Chain	77 – 157	81	40S ribosomal protein S27a-2		PRO_0000137675
Regions
	Domain	1 – 76	76	Ubiquitin-like
	Zinc finger	121 – 144	24	C4-type
	Compositional bias	77 – 99	23	Lys-rich (highly basic)
Amino acid modifications
	Cross-link	11		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	29		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	33		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	48		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	63		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	76		Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59232 [UniParc]. Last modified August 10, 2010. Version 2. Checksum: AE3B7797763FD558	FASTA	157	17,812
	10 20 30 40 50 60 MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN 70 80 90 100 110 120 IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKHKKVKL AVLQFYKVDG SGKVQRLRKE 130 140 150 CPNATCGAGT FMASHFDRHY CGKCGLTYVY QKEGAQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ubiquitin extension proteins of Arabidopsis thaliana. Structure, localization, and expression of their promoters in transgenic tobacco." Callis J., Raasch J.A., Vierstra R.D. J. Biol. Chem. 265:12486-12493(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." 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. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome." Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R., Delseny M., Bailey-Serres J. Plant Physiol. 127:398-415(2001) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
[7]	"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants." Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K. Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-29; LYS-33; LYS-48 AND LYS-63, MASS SPECTROMETRY. Strain: cv. Landsberg erecta.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05540 Genomic DNA. Translation: AAA32907.1. AC004411 Genomic DNA. Translation: AAC34235.1. CP002685 Genomic DNA. Translation: AEC10801.1. CP002685 Genomic DNA. Translation: AEC10802.1. AF375416 mRNA. Translation: AAK53000.1. AY142033 mRNA. Translation: AAM98297.1. AY143810 mRNA. Translation: AAN28749.1. AY088370 mRNA. Translation: AAM65909.1.
IPI	IPI00534346.
PIR	D36571.
RefSeq	NP_001189768.1. NM_001202839.1. NP_566095.1. NM_130278.3.
UniGene	At.27680. At.75284.
3D structure databases
ProteinModelPortal	P59232.
SMR	P59232. Positions 1-76, 102-150.
ModBase	Search...
Protein-protein interaction databases
IntAct	P59232. 2 interactions.
Proteomic databases
PaxDb	P59232.
PRIDE	P59232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G47110.1; AT2G47110.1; AT2G47110. AT2G47110.2; AT2G47110.2; AT2G47110.
GeneID	819323.
KEGG	ath:AT2G47110.
Organism-specific databases
TAIR	At2g47110.
Phylogenomic databases
eggNOG	COG5272.
KO	K02977.
OMA	KKVYTTP.
ProtClustDB	CLSN2682087.
Gene expression databases
GermOnline	AT2G47110. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002906. Ribosomal_S27a. IPR000626. Ubiquitin. IPR019954. Ubiquitin_CS. IPR019956. Ubiquitin_subgr. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF01599. Ribosomal_S27. 1 hit. PF00240. ubiquitin. 1 hit. [Graphical view]
PRINTS	PR00348. UBIQUITIN.
SMART	SM00213. UBQ. 1 hit. [Graphical view]
PROSITE	PS00299. UBIQUITIN_1. 1 hit. PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

R27AB_ARATH

Accession

Primary (citable) accession number: P59232
Secondary accession number(s): O80715 , P19233, P59263, Q38875, Q9LDJ2, Q9LYW1, Q9M0W3, Q9M1P9, Q9S7X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	August 10, 2010
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program