RFA1_MOUSE
ID RFA1_MOUSE Reviewed; 623 AA.
AC Q8VEE4; Q3TEJ8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit;
DE Short=RP-A p70;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
GN Name=Rpa1;
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], AND VARIANT 134-GLN-GLN-135 DEL.
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Liver, Lung, Spleen, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-176, AND
RP IDENTIFICATION BY 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., Zhang Y.,
RA 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).
RN [6]
RP INTERACTION WITH HROB.
RX PubMed=31467087; DOI=10.1101/gad.329508.119;
RA Hustedt N., Saito Y., Zimmermann M., Alvarez-Quilon A., Setiaputra D.,
RA Adam S., McEwan A., Yuan J.Y., Olivieri M., Zhao Y., Kanemaki M.T.,
RA Jurisicova A., Durocher D.;
RT "Control of homologous recombination by the HROB-MCM8-MCM9 pathway.";
RL Genes Dev. 33:1397-1415(2019).
CC -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC that form during DNA replication or upon DNA stress. It prevents their
CC reannealing and in parallel, recruits and activates different proteins
CC and complexes involved in DNA metabolism. Thereby, it plays an
CC essential role both in DNA replication and the cellular response to DNA
CC damage. In the cellular response to DNA damage, the RPA complex
CC controls DNA repair and DNA damage checkpoint activation. Through
CC recruitment of ATRIP activates the ATR kinase a master regulator of the
CC DNA damage response. It is required for the recruitment of the DNA
CC double-strand break repair factors RAD51 and RAD52 to chromatin in
CC response to DNA damage. Also recruits to sites of DNA damage proteins
CC like XPA and XPG that are involved in nucleotide excision repair and is
CC required for this mechanism of DNA repair. Also plays a role in base
CC excision repair (BER) probably through interaction with UNG. Also
CC recruits SMARCAL1/HARP, which is involved in replication fork restart,
CC to sites of DNA damage. May also play a role in telomere maintenance.
CC {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the canonical replication protein A complex
CC (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. The DNA-binding
CC activity may reside exclusively on the RPA1 subunit. Interacts with
CC PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair
CC where it ubiquitinates the replication protein A complex (RPA).
CC Interacts with RIPK1. Interacts with the polymerase alpha subunit
CC POLA1/p180; this interaction stabilizes the replicative complex and
CC reduces the misincorporation rate of DNA polymerase alpha by acting as
CC a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA
CC repair. Interacts with HELB; this interaction promotes HELB recruitment
CC to chromatin following DNA damage. Interacts with PRIMPOL; leading to
CC recruit PRIMPOL on chromatin and stimulate its DNA primase activity.
CC Interacts with XPA; the interaction is direct and associates XPA with
CC the RPA complex. Interacts with ETAA1; the interaction is direct and
CC promotes ETAA1 recruitment at stalled replication forks. Interacts with
CC RPA1; this interaction associates HROB with the RPA complex
CC (PubMed:31467087). {ECO:0000250|UniProtKB:P27694,
CC ECO:0000269|PubMed:31467087}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:P27694}.
CC -!- PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19
CC mediates ATRIP recruitment to the RPA complex at sites of DNA damage
CC and activation of ATR. Ubiquitinated by RFWD3 at stalled replication
CC forks in response to DNA damage: ubiquitination by RFWD3 does not lead
CC to degradation by the proteasome and promotes removal of the RPA
CC complex from stalled replication forks, promoting homologous
CC recombination. {ECO:0000250|UniProtKB:P27694}.
CC -!- PTM: Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458
CC being the major site. Sumoylation promotes recruitment of RAD51 to the
CC DNA damage foci to initiate DNA repair through homologous
CC recombination. Desumoylated by SENP6 (By similarity).
CC {ECO:0000250|UniProtKB:P27694}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK148035; BAE28302.1; -; mRNA.
DR EMBL; AK150785; BAE29849.1; -; mRNA.
DR EMBL; AK151590; BAE30530.1; -; mRNA.
DR EMBL; AK153144; BAE31755.1; -; mRNA.
DR EMBL; AK165316; BAE38134.1; -; mRNA.
DR EMBL; AK165944; BAE38476.1; -; mRNA.
DR EMBL; AK167598; BAE39655.1; -; mRNA.
DR EMBL; AK169599; BAE41250.1; -; mRNA.
DR EMBL; AL603834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019119; AAH19119.1; -; mRNA.
DR CCDS; CCDS25044.1; -.
DR RefSeq; NP_001157695.1; NM_001164223.1.
DR RefSeq; NP_080929.1; NM_026653.2.
DR AlphaFoldDB; Q8VEE4; -.
DR SMR; Q8VEE4; -.
DR BioGRID; 212778; 42.
DR CORUM; Q8VEE4; -.
DR IntAct; Q8VEE4; 4.
DR STRING; 10090.ENSMUSP00000000767; -.
DR iPTMnet; Q8VEE4; -.
DR PhosphoSitePlus; Q8VEE4; -.
DR SwissPalm; Q8VEE4; -.
DR EPD; Q8VEE4; -.
DR jPOST; Q8VEE4; -.
DR MaxQB; Q8VEE4; -.
DR PaxDb; Q8VEE4; -.
DR PeptideAtlas; Q8VEE4; -.
DR PRIDE; Q8VEE4; -.
DR ProteomicsDB; 255240; -.
DR Antibodypedia; 1868; 491 antibodies from 41 providers.
DR DNASU; 68275; -.
DR Ensembl; ENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
DR GeneID; 68275; -.
DR KEGG; mmu:68275; -.
DR UCSC; uc007kdi.2; mouse.
DR CTD; 6117; -.
DR MGI; MGI:1915525; Rpa1.
DR VEuPathDB; HostDB:ENSMUSG00000000751; -.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; Q8VEE4; -.
DR OMA; VRVTIWG; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q8VEE4; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-MMU-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69166; Removal of the Flap Intermediate.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 68275; 41 hits in 111 CRISPR screens.
DR ChiTaRS; Rpa1; mouse.
DR PRO; PR:Q8VEE4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VEE4; protein.
DR Bgee; ENSMUSG00000000751; Expressed in respiratory primordium and 272 other tissues.
DR ExpressionAtlas; Q8VEE4; baseline and differential.
DR Genevisible; Q8VEE4; MM.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:MGI.
DR GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0034502; P:protein localization to chromosome; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF04057; Rep-A_N; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..623
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000097261"
FT DNA_BIND 206..290
FT /note="OB"
FT REGION 116..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT MOD_RES 172
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 176
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT MOD_RES 268
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 562
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P27694"
FT VARIANT 134..135
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:16141072"
SQ SEQUENCE 623 AA; 69037 MW; 2317F69F1E51B657 CRC64;
MVGHLSEGAI EVMIQQENTS IKPILQVINI RPISTGNRSP RYRLLMSDGL NTLSSFMLAT
QLNTLVEGGQ LASNCVCQVH KFIVNTLKDG RKVVVLMDLE VMKSAEDVGL KIGNPVPYNE
GYGQQQQQQQ QQQQQAVPSP ASAATPPASK PQPQNGSLGM GSTAAKAYGA SKPFGKPAGT
GLLQPSGGTQ SKVVPIASLT PYQSKWTICA RVTNKSQIRT WSNSRGEGKL FSLELVDESG
EIRATAFNEQ VDKFFPLIEV NKVYYFSKGA LKIANKQFSA VKNDYEMTFN NETSVLPCED
GHHLPTVQFD FTGIGDLESK AKDALVDIIG ICKSYEDSIK ITVKSNNREV AKRNIYLMDM
SGKVVTTTLW GEDADKFDGS RQPVMAIKGA RVSDFGGRSL SVLSSSTVIV NPDIPEAYKL
RGWFDSEGQA LDGVSISDHR SGGAGGGNTN WKTLHEAKSE NLGQGDKADY FSTVAAVVFL
RKENCMYQAC PTQDCNKKVI DQQNGLYRCE KCDREFPNFK YRMILSANIA DFQENQWVTC
FQESAEAILG QNTMYLGELK EKNEQAFEEV FQNANFRSFT FRIRVKLETY NDESRIKATV
MDVKPVDFRD YGRRLIANIR KNM
