OBI1_MOUSE
ID OBI1_MOUSE Reviewed; 722 AA.
AC Q8K2Y0; Q9CYU1; Q9D1Y0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ORC ubiquitin ligase 1 {ECO:0000305};
DE Short=OBI1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5W0B1};
DE AltName: Full=RING finger protein 219;
GN Name=Obi1 {ECO:0000312|MGI:MGI:1919736};
GN Synonyms=Rnf219 {ECO:0000312|MGI:MGI:1919736};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-564 AND SER-566, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin ligase essential for DNA replication origin
CC activation during S phase. Acts as a replication origin selector which
CC selects the origins to be fired and catalyzes the multi-mono-
CC ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-
CC phase. {ECO:0000250|UniProtKB:Q5W0B1}.
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; Evidence={ECO:0000250|UniProtKB:Q5W0B1};
CC -!- SUBUNIT: Associates with ORC complex. Binds to chromatin; association
CC is cell cycle-regulated, absent from mitotic chromosomes, is associated
CC with chromatin from G1 and partially released from chromatin from mid
CC S-phase. {ECO:0000250|UniProtKB:Q5W0B1}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q5W0B1}.
CC Note=Association to chromatin is cell cycle-regulated, absent from
CC mitotic chromosomes, is associated with chromatin from G1 and partially
CC released from chromatin from mid S-phase.
CC {ECO:0000250|UniProtKB:Q5W0B1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K2Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2Y0-2; Sequence=VSP_015335, VSP_015336;
CC Name=3;
CC IsoId=Q8K2Y0-3; Sequence=VSP_015337, VSP_015338;
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q5W0B1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK013314; BAB28786.1; -; mRNA.
DR EMBL; AK020974; BAB32265.1; -; mRNA.
DR EMBL; BC029231; AAH29231.1; ALT_INIT; mRNA.
DR CCDS; CCDS27320.1; -. [Q8K2Y0-1]
DR RefSeq; XP_011243508.1; XM_011245206.2. [Q8K2Y0-2]
DR AlphaFoldDB; Q8K2Y0; -.
DR SMR; Q8K2Y0; -.
DR IntAct; Q8K2Y0; 1.
DR STRING; 10090.ENSMUSP00000022716; -.
DR iPTMnet; Q8K2Y0; -.
DR PhosphoSitePlus; Q8K2Y0; -.
DR EPD; Q8K2Y0; -.
DR jPOST; Q8K2Y0; -.
DR MaxQB; Q8K2Y0; -.
DR PaxDb; Q8K2Y0; -.
DR PRIDE; Q8K2Y0; -.
DR ProteomicsDB; 300544; -. [Q8K2Y0-1]
DR ProteomicsDB; 300545; -. [Q8K2Y0-2]
DR ProteomicsDB; 300546; -. [Q8K2Y0-3]
DR Antibodypedia; 24695; 162 antibodies from 23 providers.
DR DNASU; 72486; -.
DR Ensembl; ENSMUST00000228448; ENSMUSP00000154655; ENSMUSG00000022120. [Q8K2Y0-2]
DR GeneID; 72486; -.
DR UCSC; uc007uxd.1; mouse. [Q8K2Y0-3]
DR UCSC; uc007uxe.1; mouse. [Q8K2Y0-2]
DR CTD; 79596; -.
DR MGI; MGI:1919736; Obi1.
DR VEuPathDB; HostDB:ENSMUSG00000022120; -.
DR eggNOG; ENOG502QTFT; Eukaryota.
DR GeneTree; ENSGT00390000013512; -.
DR InParanoid; Q8K2Y0; -.
DR PhylomeDB; Q8K2Y0; -.
DR BioGRID-ORCS; 72486; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8K2Y0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8K2Y0; protein.
DR Bgee; ENSMUSG00000022120; Expressed in lumbar dorsal root ganglion and 215 other tissues.
DR ExpressionAtlas; Q8K2Y0; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR CDD; cd16562; RING-HC_RNF219; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039209; OBI1.
DR InterPro; IPR035691; RNF219_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14609; PTHR14609; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..722
FT /note="ORC ubiquitin ligase 1"
FT /id="PRO_0000055877"
FT ZN_FING 18..56
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 273..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..129
FT /evidence="ECO:0000255"
FT COILED 157..267
FT /evidence="ECO:0000255"
FT COMPBIAS 288..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT VAR_SEQ 213..214
FT /note="KF -> NL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015335"
FT VAR_SEQ 214..232
FT /note="FGRFTVAALQSKVEQYERE -> YVPHTQSEAIATPMGCGSL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015337"
FT VAR_SEQ 215..722
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015336"
FT VAR_SEQ 233..722
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015338"
SQ SEQUENCE 722 AA; 79958 MW; A7120DE6561FEC95 CRC64;
MAQTVQNVTL SLTLPITCHI CLGKVRQPVV CTNNHVFCSI CIDLWLKNNS QCPACRVPIT
PENPCKEIIG GTSESEPMLS HTVRKHLRKT RLELLHREYE DEIDCLQKEV EELKSKNLSL
ESQIKTILDP LALMQGSQNE DKHPLADNPS KMDPDSVVEW KKKLRTANEI YEKVKDDVDK
LKEANKKLKL ENGGLLRENL RLKAEVDNRS PQKFGRFTVA ALQSKVEQYE RETNRLKKAL
ERSDKYIEEL ESQVAHLKHS EEAKEDVDAL CQRAPSADSK GPNGSDELGP PKNQSDSARK
QAGSASASHL ASPSSSRLAD SGSVRQESTS RTEPNCPQNK DRYPKPTEPR LGARETPMDT
YLEREWGSKP SDCAPYKEDE LYGIPASCTP LSLSCLQLNT PENRENPVIK AGSSKKHANH
LRKLVFDDFC DSPNACNNNS SEDDRRENEK KSDCFASSKT GFWDCCSTSY AQSLEFDGSE
GNAIANSVGE IPSKLSEKSG SCLSKRLSCI RSLEMNRTRT SSEASMDAAY LDKISELDSM
MSESDNSKSP CNNGFKSVEV EGPSKSPQGR EFLEEPDKLQ EGSKLNLSKP ALTADGLESG
GEWKPSSFFL LSPADHEMSE DFSLHSTSHS GTSEVKPPNC LFQTEFSQGA LLSSSQGLFE
DQRFGSSLFK ISSEMQSLHS PLQSPWSAAF VPEKRSKNGN QSTKRKIQSS LANASPSKAT
KS
