ID REPI1_MOUSE Reviewed; 545 AA.
AC Q5U4E2; Q8BTQ5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 10-MAY-2017, entry version 110.
DE RecName: Full=Replication initiator 1;
DE AltName: Full=Zinc finger protein 464;
DE Short=Zfp-464;
GN Name=Repin1; Synonyms=Zfp464;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=12466851; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J.,
RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W.,
RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S.,
RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S.,
RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J.,
RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D.,
RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L.,
RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A.,
RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H.,
RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G.,
RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S.,
RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M.,
RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M.,
RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C.,
RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L.,
RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N.,
RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K.,
RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S.,
RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I.,
RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A.,
RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J.,
RA Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Sequence-specific double-stranded DNA-binding protein
CC required for initiation of chromosomal DNA replication. Binds on
CC 5'-ATT-3' reiterated sequences downstream of the origin of
CC bidirectional replication (OBR) and a second, homologous ATT
CC sequence of opposite orientation situated within the OBR zone.
CC Facilitates DNA bending (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimers and homomultimers. Found in a complex with
CC RIP60 and RIP100 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40716.1; Type=Frameshift; Positions=426; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK089041; BAC40716.1; ALT_FRAME; mRNA.
DR EMBL; BC085128; AAH85128.1; -; mRNA.
DR CCDS; CCDS39480.1; -.
DR RefSeq; NP_001073370.2; NM_001079901.1.
DR RefSeq; NP_001073371.2; NM_001079902.1.
DR RefSeq; NP_001073372.2; NM_001079903.1.
DR RefSeq; NP_001073373.2; NM_001079904.1.
DR RefSeq; NP_001073374.1; NM_001079905.1.
DR RefSeq; NP_780308.2; NM_175099.3.
DR UniGene; Mm.219183; -.
DR UniGene; Mm.410678; -.
DR ProteinModelPortal; Q5U4E2; -.
DR SMR; Q5U4E2; -.
DR STRING; 10090.ENSMUSP00000009420; -.
DR iPTMnet; Q5U4E2; -.
DR PhosphoSitePlus; Q5U4E2; -.
DR EPD; Q5U4E2; -.
DR MaxQB; Q5U4E2; -.
DR PaxDb; Q5U4E2; -.
DR PeptideAtlas; Q5U4E2; -.
DR PRIDE; Q5U4E2; -.
DR Ensembl; ENSMUST00000009420; ENSMUSP00000009420; ENSMUSG00000052751.
DR Ensembl; ENSMUST00000163452; ENSMUSP00000132365; ENSMUSG00000052751.
DR GeneID; 58887; -.
DR KEGG; mmu:58887; -.
DR UCSC; uc009buv.1; mouse.
DR CTD; 29803; -.
DR MGI; MGI:1889817; Repin1.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00840000129964; -.
DR HOGENOM; HOG000234617; -.
DR HOVERGEN; HBG018163; -.
DR InParanoid; Q5U4E2; -.
DR OrthoDB; EOG091G02KC; -.
DR PhylomeDB; Q5U4E2; -.
DR TreeFam; TF326846; -.
DR ChiTaRS; Repin1; mouse.
DR PRO; PR:Q5U4E2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000052751; -.
DR CleanEx; MM_REPIN1; -.
DR ExpressionAtlas; Q5U4E2; baseline and differential.
DR Genevisible; Q5U4E2; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:MGI.
DR GO; GO:0005811; C:lipid particle; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:2000191; P:regulation of fatty acid transport; IMP:MGI.
DR GO; GO:2001273; P:regulation of glucose import in response to insulin stimulus; IMP:MGI.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; DNA replication; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1 545 Replication initiator 1.
FT /FTId=PRO_0000274913.
FT ZN_FING 52 74 C2H2-type 1; atypical.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 80 102 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 111 133 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 140 162 C2H2-type 4; atypical.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 172 194 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 229 251 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 257 279 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 285 307 C2H2-type 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 353 375 C2H2-type 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 381 403 C2H2-type 10. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 409 431 C2H2-type 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 437 459 C2H2-type 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 465 487 C2H2-type 13. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 493 515 C2H2-type 14. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 521 543 C2H2-type 15. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT MOD_RES 27 27 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9BWE0}.
FT MOD_RES 39 39 N6-acetyllysine.
FT {ECO:0000244|PubMed:23806337}.
FT MOD_RES 269 269 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:Q9BWE0}.
FT CONFLICT 33 33 G -> R (in Ref. 1; BAC40716).
FT {ECO:0000305}.
FT CONFLICT 339 339 L -> Q (in Ref. 1; BAC40716).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 465 487 ismart:ZnF_C2H2 [T]
FT MYHIT 521 545 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 411 431 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 493 520 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 285 307 ismart:ZnF_C2H2 [T]
FT MYHIT 409 436 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 259 279 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 353 375 ismart:ZnF_C2H2 [T]
FT MYHIT 437 464 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 257 284 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 493 515 ismart:ZnF_C2H2 [T]
FT MYHIT 465 492 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 285 307 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 439 459 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 495 515 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 140 167 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 257 279 ismart:ZnF_C2H2 [T]
FT MYHIT 172 199 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 140 160 ismart:ZnF_C2H2 [T]
FT MYHIT 80 102 ismart:ZnF_C2H2 [T]
FT MYHIT 231 251 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 174 194 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 353 380 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 52 72 ismart:ZnF_C2H2 [T]
FT MYHIT 287 307 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 82 102 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 80 107 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 172 194 ismart:ZnF_C2H2 [T]
FT MYHIT 521 543 ismart:ZnF_C2H2 [T]
FT MYHIT 381 408 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 381 403 ismart:ZnF_C2H2 [T]
FT MYHIT 437 459 ismart:ZnF_C2H2 [T]
FT MYHIT 229 256 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 111 138 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 113 133 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 522 543 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 467 487 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 409 431 ismart:ZnF_C2H2 [T]
FT MYHIT 111 133 ismart:ZnF_C2H2 [T]
FT MYHIT 229 251 ismart:ZnF_C2H2 [T]
FT MYHIT 383 403 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 355 375 ipat:ZINC_FINGER_C2H2_1 [T]
SQ SEQUENCE 545 AA; 61830 MW; CC62C2AA5501C989 CRC64;
MLEQRCRGPT AMGPAQPWLF SGPSQESSQP DRGLRYQGKS AQPRGQTPGK VHRCAHCRKR
FPGWVALWLH ARRCQARLPL PCHECNQRFR HAPFLALHLQ VHASAVPDLG FICHLCGHSF
RGWVALVLHL RAHSASKRPI TCPECDRRFW RQKQLRAHLR RCQPPVPEAR PFICGNCGRS
FAQWDQLVVH KRVHVAEALE EAAAKALGPR PRGRPAAPRP GGDAVDRPFQ CACCGKRFRH
KPNLIAHRRV HTGERPHQCP ECGKRFTNKP YLTSHRRIHT GEKPYPCTEC GRRFRHKPNL
LSHSKIHKRL EVSAQAAPHP ESHQIAAEPM AQPALGVPLG SPRTPAEAPA LLHSCSDCGR
SFRLERFLRL HQRQHTGERP FACTECGKNF GKKTHLVAHS RVHSGERPFA CEECGRRFSQ
GSHLAAHRRD HAPERPFVCP DCGKAFRHKP YLAAHRRIHT GEKPYVCPDC GKAFSQKSNL
VSHRRIHTGE RPYACPDCDR SFSQKSNLIT HRKSHIRDGA FCCAICGQTF DDEDRLLMHQ
KKHDA
//
|
