SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0CG63

- UBI4P_YEAST

UniProt

P0CG63 - UBI4P_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Polyubiquitin
Gene
UBI4, SCD2, YLL039C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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-6-linked may be involved in DNA repair; 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.

GO - Molecular functioni

  1. ATP-dependent protein binding Source: SGD
  2. protein binding Source: IntAct
  3. protein tag Source: FlyBase
Complete GO annotation...

GO - Biological processi

  1. ascospore formation Source: SGD
  2. protein deubiquitination Source: SGD
  3. protein monoubiquitination Source: SGD
  4. protein polyubiquitination Source: SGD
  5. protein ubiquitination Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-32141-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin
Cleaved into the following chain:
Gene namesi
Name:UBI4
Synonyms:SCD2
Ordered Locus Names:YLL039C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000003962. UBI4.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291K → R: Deficiency in ubiquitin-protein conjugate formation. 2 Publications
Mutagenesisi48 – 481K → R: Deficiency in ubiquitin-protein conjugate formation. 2 Publications
Mutagenesisi63 – 631K → R: Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676Ubiquitin
PRO_0000396306Add
BLAST
Chaini77 – 15276Ubiquitin
PRO_0000396307Add
BLAST
Chaini153 – 22876Ubiquitin
PRO_0000396308Add
BLAST
Chaini229 – 30476Ubiquitin
PRO_0000396309Add
BLAST
Chaini305 – 38076Ubiquitin
PRO_0000396310Add
BLAST
Propeptidei381 – 3811
PRO_0000396311

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRIDEiP0CG63.

2D gel databases

SWISS-2DPAGEP61864.

Expressioni

Gene expression databases

GenevestigatoriP61864.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DDI1P400873EBI-7000452,EBI-5717
DSK2P485103EBI-7000452,EBI-6174
GYP7P483652EBI-7000452,EBI-8018
RAD23P326284EBI-7000452,EBI-14668
TDH2P003582EBI-7000452,EBI-7212

Protein-protein interaction databases

BioGridi31215. 3472 interactions.
IntActiP0CG63. 151 interactions.
MINTiMINT-545233.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76
Beta strandi12 – 165
Helixi23 – 3412
Turni38 – 403
Beta strandi41 – 455
Beta strandi52 – 554
Helixi56 – 594
Beta strandi66 – 716
Beta strandi88 – 947
Beta strandi101 – 1066
Beta strandi143 – 1497
Beta strandi157 – 1626
Helixi163 – 1697
Helixi170 – 1723
Helixi180 – 1823
Beta strandi184 – 1907
Beta strandi207 – 2137
Beta strandi227 – 2326
Beta strandi236 – 2383
Beta strandi241 – 2433
Helixi251 – 2566
Helixi266 – 2683
Beta strandi270 – 2723
Beta strandi274 – 2774
Helixi285 – 2873
Beta strandi294 – 2985
Beta strandi305 – 3117
Turni312 – 3143
Beta strandi316 – 3227
Beta strandi323 – 3264
Helixi327 – 33812
Helixi342 – 3443
Beta strandi346 – 3494
Beta strandi351 – 3533
Beta strandi358 – 3603
Helixi361 – 3633
Beta strandi370 – 3745
Helixi377 – 3793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTRNMR-B1-76[»]
1Q0WNMR-B1-76[»]
1WR1NMR-A1-76[»]
1ZW7NMR-A1-76[»]
2G3QNMR-B1-76[»]
2JT4NMR-B1-76[»]
2JWZNMR-A1-76[»]
2KDINMR-A2-76[»]
2L00NMR-B1-76[»]
3CMMX-ray2.70B/D1-76[»]
3L0WX-ray2.80B1-76[»]
3L10X-ray2.80B1-76[»]
3OLMX-ray2.50D1-76[»]
4HCNX-ray2.60B1-76[»]
4NNJX-ray2.40B/D/E305-380[»]
ProteinModelPortaliP0CG63.
SMRiP0CG63. Positions 1-379.

Miscellaneous databases

EvolutionaryTraceiP0CG63.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1
Add
BLAST
Domaini77 – 15276Ubiquitin-like 2
Add
BLAST
Domaini153 – 22876Ubiquitin-like 3
Add
BLAST
Domaini229 – 30476Ubiquitin-like 4
Add
BLAST
Domaini305 – 38076Ubiquitin-like 5
Add
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00750000117776.
KOiK08770.
OMAiEKNISAW.
OrthoDBiEOG7D5B06.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 5 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 5 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 5 hits.
PROSITEiPS00299. UBIQUITIN_1. 5 hits.
PS50053. UBIQUITIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CG63-1 [UniParc]FASTAAdd to Basket

« Hide

MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL    50
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID 100
NVKSKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR 150
GGMQIFVKTL TGKTITLEVE SSDTIDNVKS KIQDKEGIPP DQQRLIFAGK 200
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVESSDT 250
IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 300
LRGGMQIFVK TLTGKTITLE VESSDTIDNV KSKIQDKEGI PPDQQRLIFA 350
GKQLEDGRTL SDYNIQKEST LHLVLRLRGG N 381
Length:381
Mass (Da):42,826
Last modified:August 10, 2010 - v1
Checksum:i68C6235F9909A2AE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti352 – 3521K → N in CAA25706. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05731 Genomic DNA. Translation: CAA29198.1.
Z73144 Genomic DNA. Translation: CAA97489.1.
X01473 Genomic DNA. Translation: CAA25704.1.
X01474 Genomic DNA. Translation: CAA25706.1.
BK006945 Genomic DNA. Translation: DAA09283.1.
PIRiD29456. UQBY.
RefSeqiNP_013061.1. NM_001181859.1.

Genome annotation databases

EnsemblFungiiYLL039C; YLL039C; YLL039C.
GeneIDi850620.
KEGGisce:YLL039C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05731 Genomic DNA. Translation: CAA29198.1 .
Z73144 Genomic DNA. Translation: CAA97489.1 .
X01473 Genomic DNA. Translation: CAA25704.1 .
X01474 Genomic DNA. Translation: CAA25706.1 .
BK006945 Genomic DNA. Translation: DAA09283.1 .
PIRi D29456. UQBY.
RefSeqi NP_013061.1. NM_001181859.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OTR NMR - B 1-76 [» ]
1Q0W NMR - B 1-76 [» ]
1WR1 NMR - A 1-76 [» ]
1ZW7 NMR - A 1-76 [» ]
2G3Q NMR - B 1-76 [» ]
2JT4 NMR - B 1-76 [» ]
2JWZ NMR - A 1-76 [» ]
2KDI NMR - A 2-76 [» ]
2L00 NMR - B 1-76 [» ]
3CMM X-ray 2.70 B/D 1-76 [» ]
3L0W X-ray 2.80 B 1-76 [» ]
3L10 X-ray 2.80 B 1-76 [» ]
3OLM X-ray 2.50 D 1-76 [» ]
4HCN X-ray 2.60 B 1-76 [» ]
4NNJ X-ray 2.40 B/D/E 305-380 [» ]
ProteinModelPortali P0CG63.
SMRi P0CG63. Positions 1-379.
ModBasei Search...

Protein-protein interaction databases

BioGridi 31215. 3472 interactions.
IntActi P0CG63. 151 interactions.
MINTi MINT-545233.

2D gel databases

SWISS-2DPAGE P61864.

Proteomic databases

PRIDEi P0CG63.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLL039C ; YLL039C ; YLL039C .
GeneIDi 850620.
KEGGi sce:YLL039C.

Organism-specific databases

SGDi S000003962. UBI4.

Phylogenomic databases

GeneTreei ENSGT00750000117776.
KOi K08770.
OMAi EKNISAW.
OrthoDBi EOG7D5B06.

Enzyme and pathway databases

BioCyci YEAST:G3O-32141-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0CG63.
NextBioi 966520.
PROi P0CG63.

Gene expression databases

Genevestigatori P61864.

Family and domain databases

InterProi IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view ]
Pfami PF00240. ubiquitin. 5 hits.
[Graphical view ]
PRINTSi PR00348. UBIQUITIN.
SMARTi SM00213. UBQ. 5 hits.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 5 hits.
PROSITEi PS00299. UBIQUITIN_1. 5 hits.
PS50053. UBIQUITIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast ubiquitin genes: a family of natural gene fusions."
    Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.
    EMBO J. 6:1429-1439(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein."
    Oezkaynak E., Finley D., Varshavsky A.
    Nature 312:663-666(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-381.
  5. "A proteolytic pathway that recognizes ubiquitin as a degradation signal."
    Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.
    J. Biol. Chem. 270:17442-17456(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63.
  6. "A ubiquitin mutant with specific defects in DNA repair and multiubiquitination."
    Spence J., Sadis S., Haas A.L., Finley D.
    Mol. Cell. Biol. 15:1265-1273(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYSINE RESIDUES.
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33; LYS-48 AND LYS-63.
    Strain: SUB592.
  8. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48 AND LYS-63.
  9. "Structural basis for the specificity of ubiquitin C-terminal hydrolases."
    Johnston S.C., Riddle S.M., Cohen R.E., Hill C.P.
    EMBO J. 18:3877-3887(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH YUH1.
  10. "A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain."
    Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.
    EMBO J. 22:1273-1281(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH VPS9.
  11. "Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail."
    Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T., McKenna S., Ptak C., Glover M., Shaw G.S.
    Structure 9:897-904(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH UBC1.
  12. "Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding."
    Kang R.S., Daniels C.M., Francis S.A., Shih S.C., Salerno W.J., Hicke L., Radhakrishnan I.
    Cell 113:621-630(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF COMPLEX WITH CUE2 N-TERMINAL DOMAIN.

Entry informationi

Entry nameiUBI4P_YEAST
AccessioniPrimary (citable) accession number: P0CG63
Secondary accession number(s): D6VXW7
, P04838, P61864, Q6LA96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: September 3, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Ubiquitin is encoded by 4 different genes. UBI1 and UBI2 genes code for a single copy of ubiquitin fused to the ribosomal proteins L40. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein S37. UBI4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi