Q8RUC6 (RUB2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-NEDD8-like protein RUB2

Cleaved into the following 2 chains:

1. Ubiquitin
2. NEDD8-like protein RUB2
   Alternative name(s):
   Ubiquitin-related protein 2
   Short name=AtRUB2

Gene names

Name:	RUB2
Synonyms:	UBQ7
Ordered Locus Names:	At2g35635
ORF Names:	T20F21.24

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	154 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. NEDD8-like protein RUB2: Appears to function as a stable post-translational protein modifier.
Subunit structure	NEDD8-like protein RUB2: Forms a thiol ester with the heterodimer AXR1/ECR1 By similarity.
Subcellular location	Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Expressed in leaves, stems and flowers. Ref.5
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	Belongs to the ubiquitin family. Contains 2 ubiquitin-like domains.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity PubMed 7713442. Source: TAIR
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 76	76	Ubiquitin		PRO_0000396911
	Chain	77 – 152	76	NEDD8-like protein RUB2		PRO_0000035967
	Propeptide	153 – 154	2	Probable		PRO_0000035968
Regions
	Domain	1 – 76	76	Ubiquitin-like 1
	Domain	77 – 152	76	Ubiquitin-like 2
Amino acid modifications
	Cross-link	11		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
	Cross-link	29		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
	Cross-link	33		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
	Cross-link	48		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
	Cross-link	63		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
	Cross-link	76		Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity
	Cross-link	152		Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RUC6 [UniParc]. Last modified August 10, 2010. Version 3. Checksum: DF75521A63AEF7CA	FASTA	154	17,150
	10 20 30 40 50 60 MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN 70 80 90 100 110 120 IQKESTLHLV LRLRGGTMIK VKTLTGKEIE IDIEPTDTID RIKERVEEKE GIPPVQQRLI 130 140 150 YAGKQLADDK TAKDYAIEGG SVLHLVLALR GGLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]	"The rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in Arabidopsis." Rao-Naik C., delaCruz W., Laplaza J.M., Tan S., Callis J., Fisher A.J. J. Biol. Chem. 273:34976-34982(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"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	AC006068 Genomic DNA. Translation: AAM15116.1. CP002685 Genomic DNA. Translation: AEC09134.1. AK118678 mRNA. Translation: BAC43273.1. AY074850 mRNA. Translation: AAL75902.1. AY093802 mRNA. Translation: AAM10418.1.
IPI	IPI00531002.
PIR	S55242.
RefSeq	NP_565812.1. NM_129118.4.
UniGene	At.37643.
3D structure databases
ProteinModelPortal	Q8RUC6.
SMR	Q8RUC6. Positions 1-152.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G35635.1-P.
Proteomic databases
PaxDb	Q8RUC6.
PRIDE	Q8RUC6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G35635.1; AT2G35635.1; AT2G35635.
GeneID	818132.
KEGG	ath:AT2G35635.
Organism-specific databases
TAIR	At2g35635.
Phylogenomic databases
eggNOG	COG5272.
KO	K12158.
OMA	YRIKERV.
ProtClustDB	CLSN2688712.
Gene expression databases
Genevestigator	Q8RUC6.
GermOnline	AT2G35635. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000626. Ubiquitin. IPR019954. Ubiquitin_CS. IPR019956. Ubiquitin_subgr. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF00240. ubiquitin. 2 hits. [Graphical view]
PRINTS	PR00348. UBIQUITIN.
SMART	SM00213. UBQ. 2 hits. [Graphical view]
PROSITE	PS00299. UBIQUITIN_1. 2 hits. PS50053. UBIQUITIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RUB2_ARATH

Accession

Primary (citable) accession number: Q8RUC6
Secondary accession number(s): O80715 , P59263, Q38875, Q9LDJ2, Q9LYW1, Q9M0W3, Q9M1P9, Q9S7X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	August 10, 2010
Last modified:	May 1, 2013
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program