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Protein

E3 ubiquitin-protein ligase ubr1

Gene

ubr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri94 – 16673UBR-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1182 – 1334153RING-type; atypicalAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: PomBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to hyperoxia Source: PomBase
  • negative regulation of SREBP signaling pathway by positive regulation of transcription factor catabolic process in response to increased oxygen levels Source: PomBase
  • negative regulation of transcription by transcription factor catabolism Source: PomBase
  • proteasome localization to nuclear periphery Source: PomBase
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: PomBase
  • protein polyubiquitination involved in nucleus-associated proteasomal ubiquitin-dependent protein catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ubr1 (EC:6.3.2.-)
Alternative name(s):
N-end-recognizing protein
N-recognin-1
Gene namesi
Name:ubr1
ORF Names:SPBC19C7.02, SPBC32F12.14
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC19C7.02.
PomBaseiSPBC19C7.02. ubr1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19581958E3 ubiquitin-protein ligase ubr1PRO_0000056134Add
BLAST

Proteomic databases

MaxQBiO60152.

Interactioni

Protein-protein interaction databases

BioGridi277284. 40 interactions.

Structurei

3D structure databases

ProteinModelPortaliO60152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.

Sequence similaritiesi

Belongs to the UBR1 family.Curated
Contains 1 RING-type zinc finger.Curated
Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri94 – 16673UBR-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1182 – 1334153RING-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiO60152.
KOiK10625.
OMAiQPVSFHH.
OrthoDBiEOG76X67D.
PhylomeDBiO60152.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR011991. WHTH_DNA-bd_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51157. ZF_UBR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQDESSRSL PRSALIRRRL SLFLQSHALM YSFLWSESAK KSLLNEVFSA
60 70 80 90 100
LLGYDHTLWN TLLPERPTID ASFLLRRAQG HSEGDEYRHG TCESKCGHIF
110 120 130 140 150
RKGEVFYRCK TCSVDSNSAL CVKCFRATSH KDHETSFTVS AGSGGCCDCG
160 170 180 190 200
NAAAWIGDVS CKIHSHEEDA TISNDMIDEI PEKLENSIQT TIDCVLDFVL
210 220 230 240 250
DVFSCSPENL KKMPTLESIL QDEKTSRLSE NKYGDIDDSC NMYSLVLWND
260 270 280 290 300
EKHSFKQFYE QITTALELPN NVFGKKMANI INDIGRACIV TETNIKELLK
310 320 330 340 350
IGQKLAQINL AVSIRSMRDI FREESCAVLL EWLADIAGSS ICGKRNYFSS
360 370 380 390 400
VICKELVRPW NCGLHNSDLT FRLSLRSLAL PEIVAIDSPD IFLNEDHINS
410 420 430 440 450
SGPSDTSSHM LETDESSIHS RHWYPSNSLP DVLSYASRVR FDYFFLYDLK
460 470 480 490 500
LWKSLRYKLQ ELYLGYFITQ PGFKEIMGAR IAISYRRLAE LFLLLDREPE
510 520 530 540 550
HSVIFFSMQI FTVADVAKLL VTEYDFLTTI NATLYTFFTY KKLNTPNYVD
560 570 580 590 600
QHAMIRTDSA AFHSRRYIHI FHHIQFMLSI PCVAEIVRED LKFLKQYADF
610 620 630 640 650
FNLFQGMCPY TRAVSQHVEW ENDSWMYVLN VSLQVAKLCR HVGNVFMELN
660 670 680 690 700
TNKLANAINY LISLILYPKA RNESWTNTES LTTGITVDER GNSKLIEYDI
710 720 730 740 750
ALQPVSFHHP LHWLLVYLLS FYVERDNYKL LWTQLDLLAV TDHPLRVCAW
760 770 780 790 800
LSQMRAKLWI RNGTTLRDQA HHYRNLSFHE YTFDLDVLLL QLTLTYGDPD
810 820 830 840 850
AILPSFISRF QLEDQMYGRF FVPHKHYDVS QVTIMMEEFL LLLISIVCNT
860 870 880 890 900
AVLDHWDITR RIEYGIAHIL CFRPLPYSEI TKRTCEHLLE HKQFESTLKK
910 920 930 940 950
VATFRNAEGI NDSGSFTLKD EYFDYVDPFN IHYSRNQREE AENILRRRYS
960 970 980 990 1000
KQHSKHLESV VYEEYHPILH SNITIPILQS DSFVGILWHT IVYAYIYPYD
1010 1020 1030 1040 1050
QGKLEGLVNT ALHACLLVLM SEKGSEPIFS KKICENRFPV VEGLQEYCNS
1060 1070 1080 1090 1100
PDVTLFSVLC QMKNHRNFVY VKEKISLIMK ILKSEVPLLY EPVYAETLSI
1110 1120 1130 1140 1150
SSSKIVQSLS DAEQQEQHLA KVRMAKERQA RIMEQFRMQQ NKFLENHALF
1160 1170 1180 1190 1200
EASDCEMDEA DEFSVTSSVS TKLFLDPPID TCLLCQEELK DKRPYGTLVF
1210 1220 1230 1240 1250
VLRSSVLRLF PADDANYVSE VLDIPDSLDH EIQERPFGLA GKRKKVLDST
1260 1270 1280 1290 1300
EAYDYDNYYY EKKGNELHQL KDSFNGFPPD QLDRGLHATG CGHFMHIDCF
1310 1320 1330 1340 1350
KNHIATVTLA TRANPYRNHP HNLSMKEFLC PLCKALCNTI FPILWRPKEE
1360 1370 1380 1390 1400
INFQEAGVLT APLKNWLVSK TFSFNKDLNQ QLLDIETSPS EHTQSYNLNL
1410 1420 1430 1440 1450
LDVLQHTLRD SLKDIYTLNT GADNSSDNVE ENADNLFQSS VLDHVHFKSV
1460 1470 1480 1490 1500
VNNEVPADER LAISDDIFEL YRRLDDVIDL NSSLYSDDFI PVNGKLHNVV
1510 1520 1530 1540 1550
KLFSYSLCQV EASTRGHIKC SSIPADIWVH NLGKNQQVFL RILSESIKTY
1560 1570 1580 1590 1600
TLLCAHDSQK RIGGSIQEFE FISFCQQKRI FGRLLPSLDS PVTKSITDDR
1610 1620 1630 1640 1650
VEPLLVKDTF REFAEASVSG LLSCDESFHY LTQLYYTADI VRNLWILLSQ
1660 1670 1680 1690 1700
RNSLLKCMES VEFEAFDYEQ LKGFEHLVIQ IWKSLRVDGA GLINFDCCTE
1710 1720 1730 1740 1750
DDLNNPHLLF TLYKLLERFS LIFLRKCALL WYCRYGVSFE TQPNLNFQNS
1760 1770 1780 1790 1800
ELSRLQTKMH IPGVIELSNH LCLTASSTEW SLIKHWCNFF TETGPLCDFP
1810 1820 1830 1840 1850
RAYYPGIYEL VSLPYELDKV FELLLARRCS KCLTEPMEPA ICLFCGKLLC
1860 1870 1880 1890 1900
FQSHCCSFNG IGECNLHMQQ CASDIGIFLI VKKCAILYLN PPVGSFSVAP
1910 1920 1930 1940 1950
FLDAYGETDL GLRRGRSQYL SQKRYDETVR TMWLNGSIPS YIARQLDANP

DTGGWETL
Length:1,958
Mass (Da):225,758
Last modified:August 1, 1998 - v1
Checksum:i65ABBB2ADC5911B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079542 Genomic DNA. Translation: BAB84667.1.
CU329671 Genomic DNA. Translation: CAA19375.1.
PIRiT39808.
T40238.
RefSeqiNP_596158.2. NM_001022077.3.

Genome annotation databases

EnsemblFungiiSPBC19C7.02.1; SPBC19C7.02.1:pep; SPBC19C7.02.
GeneIDi2540764.
KEGGispo:SPBC19C7.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079542 Genomic DNA. Translation: BAB84667.1.
CU329671 Genomic DNA. Translation: CAA19375.1.
PIRiT39808.
T40238.
RefSeqiNP_596158.2. NM_001022077.3.

3D structure databases

ProteinModelPortaliO60152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277284. 40 interactions.

Proteomic databases

MaxQBiO60152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC19C7.02.1; SPBC19C7.02.1:pep; SPBC19C7.02.
GeneIDi2540764.
KEGGispo:SPBC19C7.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC19C7.02.
PomBaseiSPBC19C7.02. ubr1.

Phylogenomic databases

InParanoidiO60152.
KOiK10625.
OMAiQPVSFHH.
OrthoDBiEOG76X67D.
PhylomeDBiO60152.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiO60152.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR011991. WHTH_DNA-bd_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual differentiation via ubiquitin proteolysis and 14-3-3 protein in fission yeast."
    Kitamura K., Katayama S., Dhut S., Sato M., Watanabe Y., Yamamoto M., Toda T.
    Dev. Cell 1:389-399(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiUBR1_SCHPO
AccessioniPrimary (citable) accession number: O60152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.