Skip Header

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

Polyubiquitin-B

Gene

Ubb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Activating enzyme
Sitei68 – 681Essential for function
Binding sitei72 – 721Activating enzyme

GO - Biological processi

  • adipose tissue development Source: MGI
  • circadian rhythm Source: Reactome
  • energy homeostasis Source: MGI
  • fat pad development Source: MGI
  • female gonad development Source: MGI
  • female meiosis I Source: MGI
  • hypothalamus gonadotrophin-releasing hormone neuron development Source: MGI
  • male gonad development Source: MGI
  • male meiosis I Source: MGI
  • mitochondrion transport along microtubule Source: MGI
  • neuron projection morphogenesis Source: MGI
  • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • regulation of mitochondrial membrane potential Source: MGI
  • regulation of neuron death Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • seminiferous tubule development Source: MGI
  • ubiquitin homeostasis Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_24972. Circadian Clock.
REACT_286692. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_351159. Circadian Clock.
REACT_351311. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
Gene namesi
Name:Ubb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98888. Ubb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000114801Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396188Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396189Add
BLAST
Chaini229 – 30476UbiquitinPRO_0000396190Add
BLAST
Propeptidei305 – 3051PRO_0000396191

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65 – 651Phosphoserine; by PINK1By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Modified residuei141 – 1411PhosphoserineBy similarity

Post-translational modificationi

Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PARK2), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP0CG49.
PRIDEiP0CG49.

2D gel databases

REPRODUCTION-2DPAGEP62991.

PTM databases

PhosphoSiteiP0CG49.

Expressioni

Gene expression databases

BgeeiP0CG49.
ExpressionAtlasiP0CG49. baseline.
GenevestigatoriP62991.

Interactioni

Protein-protein interaction databases

BioGridi204402. 13 interactions.
IntActiP0CG49. 2 interactions.
MINTiMINT-8372791.

Structurei

3D structure databases

ProteinModelPortaliP0CG49.
SMRiP0CG49. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 15276Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 22876Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 30476Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 4 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoidiP0CG49.
KOiK04551.
OMAiEKNISAW.
OrthoDBiEOG7JDR1W.
PhylomeDBiP0CG49.
TreeFamiTF300820.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CG49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT
260 270 280 290 300
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR

LRGGY
Length:305
Mass (Da):34,369
Last modified:August 10, 2010 - v1
Checksum:i0B8C7878AE958E68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311Q → R in BAB29028 (PubMed:16141072).Curated
Sequence conflicti54 – 541R → S in BAB29028 (PubMed:16141072).Curated
Sequence conflicti61 – 611I → N in BAB29028 (PubMed:16141072).Curated
Sequence conflicti92 – 921E → G in BAB29028 (PubMed:16141072).Curated
Sequence conflicti117 – 1171Q → H in AAH19850 (PubMed:15489334).Curated
Sequence conflicti147 – 1471L → F in BAB28242 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51703 mRNA. Translation: CAA35999.1.
AK012443 mRNA. Translation: BAB28242.1.
AK003190 mRNA. Translation: BAB22630.1.
AK013873 mRNA. Translation: BAB29028.1.
BC019850 mRNA. Translation: AAH19850.1.
CCDSiCCDS24826.1.
PIRiS12583.
RefSeqiNP_035794.1. NM_011664.3.
XP_006533222.1. XM_006533159.1.
UniGeneiMm.282093.
Mm.371592.

Genome annotation databases

EnsembliENSMUST00000019649; ENSMUSP00000019649; ENSMUSG00000019505.
GeneIDi22187.
KEGGimmu:22187.
UCSCiuc007jjg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51703 mRNA. Translation: CAA35999.1.
AK012443 mRNA. Translation: BAB28242.1.
AK003190 mRNA. Translation: BAB22630.1.
AK013873 mRNA. Translation: BAB29028.1.
BC019850 mRNA. Translation: AAH19850.1.
CCDSiCCDS24826.1.
PIRiS12583.
RefSeqiNP_035794.1. NM_011664.3.
XP_006533222.1. XM_006533159.1.
UniGeneiMm.282093.
Mm.371592.

3D structure databases

ProteinModelPortaliP0CG49.
SMRiP0CG49. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204402. 13 interactions.
IntActiP0CG49. 2 interactions.
MINTiMINT-8372791.

PTM databases

PhosphoSiteiP0CG49.

2D gel databases

REPRODUCTION-2DPAGEP62991.

Proteomic databases

MaxQBiP0CG49.
PRIDEiP0CG49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019649; ENSMUSP00000019649; ENSMUSG00000019505.
GeneIDi22187.
KEGGimmu:22187.
UCSCiuc007jjg.1. mouse.

Organism-specific databases

CTDi7314.
MGIiMGI:98888. Ubb.

Phylogenomic databases

InParanoidiP0CG49.
KOiK04551.
OMAiEKNISAW.
OrthoDBiEOG7JDR1W.
PhylomeDBiP0CG49.
TreeFamiTF300820.

Enzyme and pathway databases

ReactomeiREACT_24972. Circadian Clock.
REACT_286692. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_351159. Circadian Clock.
REACT_351311. Hedgehog 'on' state.

Miscellaneous databases

NextBioi302157.
PROiP0CG49.
SOURCEiSearch...

Gene expression databases

BgeeiP0CG49.
ExpressionAtlasiP0CG49. baseline.
GenevestigatoriP62991.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Liver and Mammary tumor.
  4. "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.

Entry informationi

Entry nameiUBB_MOUSE
AccessioniPrimary (citable) accession number: P0CG49
Secondary accession number(s): P02248
, P02249, P02250, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: May 27, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.