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 27-MAR-2024, entry version 176. 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 (By similarity). CC The DNA-binding activity may reside exclusively on the RPA1 subunit (By CC similarity). Interacts with PRPF19; the PRP19-CDC5L complex is CC recruited to the sites of DNA repair where it ubiquitinates the CC replication protein A complex (RPA) (By similarity). Interacts with CC RIPK1 (By similarity). 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 (By similarity). Interacts with RAD51 and SENP6 to CC regulate DNA repair (By similarity). Interacts with HELB; this CC interaction promotes HELB recruitment to chromatin following DNA damage CC (By similarity). Interacts with PRIMPOL; leading to recruit PRIMPOL on CC chromatin and stimulate its DNA primase activity (By similarity). CC Interacts with XPA; the interaction is direct and associates XPA with CC the RPA complex (By similarity). Interacts with ETAA1; the interaction CC is direct and promotes ETAA1 recruitment at stalled replication forks CC (By similarity). Interacts with RPA1; this interaction associates HROB CC with the RPA complex (PubMed:31467087). Interacts (when poly-ADP- CC ribosylated) with HTATSF1 (By similarity). CC {ECO:0000250|UniProtKB:P27694, 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 -!- PTM: Poly-ADP-ribosylated by PARP1; promoting recruitment of HTATSF1. 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 EMDB; EMD-2789; -. DR SMR; Q8VEE4; -. DR BioGRID; 212778; 44. 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; 10090-ENSMUSP00000000767; -. DR PeptideAtlas; Q8VEE4; -. DR ProteomicsDB; 255240; -. DR Pumba; Q8VEE4; -. DR Antibodypedia; 1868; 571 antibodies from 41 providers. DR DNASU; 68275; -. DR Ensembl; ENSMUST00000092907.12; ENSMUSP00000090585.6; ENSMUSG00000000751.14. DR GeneID; 68275; -. DR KEGG; mmu:68275; -. DR UCSC; uc007kdi.2; mouse. DR AGR; MGI:1915525; -. 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; FNDQCDA; -. DR OrthoDB; 1122034at2759; -. 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 115 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 276 other cell types or tissues. DR ExpressionAtlas; Q8VEE4; baseline and differential. 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:0051276; P:chromosome organization; IMP:MGI. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; ISO:MGI. DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB. 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; cd04474; RPA1_DBD_A; 1. DR CDD; cd04475; RPA1_DBD_B; 1. DR CDD; cd04476; RPA1_DBD_C; 1. DR CDD; cd04477; RPA1N; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4. DR InterPro; IPR047192; Euk_RPA1_DBD_C. 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 NCBIfam; TIGR00617; rpa1; 1. DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1. DR PANTHER; PTHR23273:SF4; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT; 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; Nucleic acid-binding proteins; 4. DR Genevisible; Q8VEE4; MM. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; DNA damage; DNA recombination; DNA repair; KW DNA replication; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; 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 ZN_FING 490..512 FT /note="C4-type" FT /evidence="ECO:0000255" 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 //