UBR1_SCHPO
ID UBR1_SCHPO Reviewed; 1958 AA.
AC O60152;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase ubr1;
DE EC=2.3.2.27;
DE AltName: Full=N-end-recognizing protein;
DE AltName: Full=N-recognin-1;
DE AltName: Full=RING-type E3 ubiquitin transferase ubr1;
GN Name=ubr1; ORFNames=SPBC19C7.02, SPBC32F12.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11702950; DOI=10.1016/s1534-5807(01)00037-5;
RA Kitamura K., Katayama S., Dhut S., Sato M., Watanabe Y., Yamamoto M.,
RA Toda T.;
RT "Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual
RT differentiation via ubiquitin proteolysis and 14-3-3 protein in fission
RT yeast.";
RL Dev. Cell 1:389-399(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; AB079542; BAB84667.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19375.1; -; Genomic_DNA.
DR PIR; T39808; T39808.
DR PIR; T40238; T40238.
DR RefSeq; NP_596158.2; NM_001022077.3.
DR AlphaFoldDB; O60152; -.
DR SMR; O60152; -.
DR BioGRID; 277284; 41.
DR STRING; 4896.SPBC19C7.02.1; -.
DR MaxQB; O60152; -.
DR PaxDb; O60152; -.
DR PRIDE; O60152; -.
DR EnsemblFungi; SPBC19C7.02.1; SPBC19C7.02.1:pep; SPBC19C7.02.
DR GeneID; 2540764; -.
DR KEGG; spo:SPBC19C7.02; -.
DR PomBase; SPBC19C7.02; ubr1.
DR VEuPathDB; FungiDB:SPBC19C7.02; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR InParanoid; O60152; -.
DR OMA; ATTVYRI; -.
DR PhylomeDB; O60152; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O60152; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; NAS:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1958
FT /note="E3 ubiquitin-protein ligase ubr1"
FT /id="PRO_0000056134"
FT ZN_FING 94..166
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1182..1334
FT /note="RING-type; atypical"
SQ SEQUENCE 1958 AA; 225758 MW; 65ABBB2ADC5911B5 CRC64;
MLQDESSRSL PRSALIRRRL SLFLQSHALM YSFLWSESAK KSLLNEVFSA LLGYDHTLWN
TLLPERPTID ASFLLRRAQG HSEGDEYRHG TCESKCGHIF RKGEVFYRCK TCSVDSNSAL
CVKCFRATSH KDHETSFTVS AGSGGCCDCG NAAAWIGDVS CKIHSHEEDA TISNDMIDEI
PEKLENSIQT TIDCVLDFVL DVFSCSPENL KKMPTLESIL QDEKTSRLSE NKYGDIDDSC
NMYSLVLWND EKHSFKQFYE QITTALELPN NVFGKKMANI INDIGRACIV TETNIKELLK
IGQKLAQINL AVSIRSMRDI FREESCAVLL EWLADIAGSS ICGKRNYFSS VICKELVRPW
NCGLHNSDLT FRLSLRSLAL PEIVAIDSPD IFLNEDHINS SGPSDTSSHM LETDESSIHS
RHWYPSNSLP DVLSYASRVR FDYFFLYDLK LWKSLRYKLQ ELYLGYFITQ PGFKEIMGAR
IAISYRRLAE LFLLLDREPE HSVIFFSMQI FTVADVAKLL VTEYDFLTTI NATLYTFFTY
KKLNTPNYVD QHAMIRTDSA AFHSRRYIHI FHHIQFMLSI PCVAEIVRED LKFLKQYADF
FNLFQGMCPY TRAVSQHVEW ENDSWMYVLN VSLQVAKLCR HVGNVFMELN TNKLANAINY
LISLILYPKA RNESWTNTES LTTGITVDER GNSKLIEYDI ALQPVSFHHP LHWLLVYLLS
FYVERDNYKL LWTQLDLLAV TDHPLRVCAW LSQMRAKLWI RNGTTLRDQA HHYRNLSFHE
YTFDLDVLLL QLTLTYGDPD AILPSFISRF QLEDQMYGRF FVPHKHYDVS QVTIMMEEFL
LLLISIVCNT AVLDHWDITR RIEYGIAHIL CFRPLPYSEI TKRTCEHLLE HKQFESTLKK
VATFRNAEGI NDSGSFTLKD EYFDYVDPFN IHYSRNQREE AENILRRRYS KQHSKHLESV
VYEEYHPILH SNITIPILQS DSFVGILWHT IVYAYIYPYD QGKLEGLVNT ALHACLLVLM
SEKGSEPIFS KKICENRFPV VEGLQEYCNS PDVTLFSVLC QMKNHRNFVY VKEKISLIMK
ILKSEVPLLY EPVYAETLSI SSSKIVQSLS DAEQQEQHLA KVRMAKERQA RIMEQFRMQQ
NKFLENHALF EASDCEMDEA DEFSVTSSVS TKLFLDPPID TCLLCQEELK DKRPYGTLVF
VLRSSVLRLF PADDANYVSE VLDIPDSLDH EIQERPFGLA GKRKKVLDST EAYDYDNYYY
EKKGNELHQL KDSFNGFPPD QLDRGLHATG CGHFMHIDCF KNHIATVTLA TRANPYRNHP
HNLSMKEFLC PLCKALCNTI FPILWRPKEE INFQEAGVLT APLKNWLVSK TFSFNKDLNQ
QLLDIETSPS EHTQSYNLNL LDVLQHTLRD SLKDIYTLNT GADNSSDNVE ENADNLFQSS
VLDHVHFKSV VNNEVPADER LAISDDIFEL YRRLDDVIDL NSSLYSDDFI PVNGKLHNVV
KLFSYSLCQV EASTRGHIKC SSIPADIWVH NLGKNQQVFL RILSESIKTY TLLCAHDSQK
RIGGSIQEFE FISFCQQKRI FGRLLPSLDS PVTKSITDDR VEPLLVKDTF REFAEASVSG
LLSCDESFHY LTQLYYTADI VRNLWILLSQ RNSLLKCMES VEFEAFDYEQ LKGFEHLVIQ
IWKSLRVDGA GLINFDCCTE DDLNNPHLLF TLYKLLERFS LIFLRKCALL WYCRYGVSFE
TQPNLNFQNS ELSRLQTKMH IPGVIELSNH LCLTASSTEW SLIKHWCNFF TETGPLCDFP
RAYYPGIYEL VSLPYELDKV FELLLARRCS KCLTEPMEPA ICLFCGKLLC FQSHCCSFNG
IGECNLHMQQ CASDIGIFLI VKKCAILYLN PPVGSFSVAP FLDAYGETDL GLRRGRSQYL
SQKRYDETVR TMWLNGSIPS YIARQLDANP DTGGWETL
