ID RIP_HUMAN Reviewed; 219 AA. AC Q86UA6; A0A0B4J1T3; B4DI36; B4DTX7; E9PDG9; E9PES3; J3KNH8; Q4G2Y0; Q4G2Y5; AC Q4G2Y8; Q6B4V9; Q6B4W0; Q6B4W1; Q6B4W4; Q86X49; Q9BT00; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 2. DT 27-MAR-2024, entry version 154. DE RecName: Full=RPA-interacting protein; DE Short=hRIP; GN Name=RPAIN; Synonyms=RIP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND VARIANT LYS-103. RX PubMed=16008515; DOI=10.1089/dna.2005.24.464; RA Chen J.-Z., Huang S.-D., Ji C.-N., Pang R.-Y., Xie Y., Xue J.-L.; RT "Identification, expression pattern, and subcellular location of human RIP RT isoforms."; RL DNA Cell Biol. 24:464-469(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6 AND 7), FUNCTION, RP SUBCELLULAR LOCATION, SUMOYLATION AT LYS-121, INTERACTION WITH RPA1, RP MUTAGENESIS OF LYS-114; LYS-121 AND LYS-142, AND VARIANT LYS-103. RX PubMed=16135809; DOI=10.1128/mcb.25.18.8202-8214.2005; RA Park J., Seo T., Kim H., Choe J.; RT "Sumoylation of the novel protein hRIPbeta is involved in replication RT protein A deposition in PML nuclear bodies."; RL Mol. Cell. Biol. 25:8202-8214(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 8), AND VARIANT RP LYS-103. RC TISSUE=Corpus callosum, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 6), AND VARIANT RP LYS-103. RC TISSUE=Eye; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Mediates the import of RPA complex into the nucleus, possibly CC via some interaction with importin beta. Isoform 2 is sumoylated and CC mediates the localization of RPA complex into the PML body of the CC nucleus, thereby participating in RPA function in DNA metabolism. CC {ECO:0000269|PubMed:16135809}. CC -!- SUBUNIT: Interacts with the RPA1 subunit of RPA complex. CC {ECO:0000269|PubMed:16135809}. CC -!- INTERACTION: CC Q86UA6; O15315: RAD51B; NbExp=3; IntAct=EBI-3907663, EBI-2824089; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, PML body. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=Alpha, hRIPalpha; CC IsoId=Q86UA6-1; Sequence=Displayed; CC Name=2; Synonyms=Beta, hRIPbeta; CC IsoId=Q86UA6-2; Sequence=VSP_016410; CC Name=3; Synonyms=Gamma2; CC IsoId=Q86UA6-3; Sequence=VSP_016408; CC Name=4; Synonyms=Gamma1; CC IsoId=Q86UA6-4; Sequence=VSP_016407, VSP_016409; CC Name=5; Synonyms=Delta2; CC IsoId=Q86UA6-5; Sequence=VSP_016403, VSP_016405; CC Name=6; Synonyms=Delta3; CC IsoId=Q86UA6-6; Sequence=VSP_016404, VSP_016405; CC Name=7; Synonyms=Delta1, Delta 4; CC IsoId=Q86UA6-7; Sequence=VSP_016402, VSP_016406; CC Name=8; CC IsoId=Q86UA6-8; Sequence=VSP_045356; CC Name=9; CC IsoId=Q86UA6-9; Sequence=VSP_046795; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney, CC muscle, liver, lung, placenta, brain, heart, leukocytes, colon, CC intestine, ovary, testis, prostate, thymus and spleen. CC {ECO:0000269|PubMed:16008515}. CC -!- PTM: [Isoform 2]: Sumoylated. Sumoylation is required for localization CC in the nuclear PML body and transport of RPA complex in PML body. Upon CC UV irradiation and during S phase, it is desumoylated, releasing RPA CC complex that is translocated to sites of DNA damage. Sumoylation takes CC place at different Lys residues. Variant 'Lys-103' adds a sumoylation CC site and increases total sumoylation levels. CC {ECO:0000269|PubMed:16135809}. CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform with isoform 2. CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform with isoform 1. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. May be due to an intron retention. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {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; AY775314; AAX14368.1; -; mRNA. DR EMBL; AY775315; AAX14369.1; -; mRNA. DR EMBL; AY775316; AAX14370.1; -; mRNA. DR EMBL; AY775317; AAX14371.1; -; mRNA. DR EMBL; AY775318; AAX14372.1; -; mRNA. DR EMBL; AY775319; AAX14373.1; -; mRNA. DR EMBL; AY775320; AAX14374.1; -; mRNA. DR EMBL; AY775321; AAX14375.1; -; mRNA. DR EMBL; AY775323; AAX14377.1; -; mRNA. DR EMBL; AY680654; AAT80872.1; -; mRNA. DR EMBL; AY680655; AAT80873.1; -; mRNA. DR EMBL; AY680656; AAT80874.1; -; mRNA. DR EMBL; AY680657; AAT80875.1; -; mRNA. DR EMBL; AY680658; AAT80876.1; -; mRNA. DR EMBL; AY680659; AAT80877.1; -; mRNA. DR EMBL; AY680660; AAT80878.1; -; mRNA. DR EMBL; AK295394; BAG58348.1; -; mRNA. DR EMBL; AK300409; BAG62139.1; -; mRNA. DR EMBL; CH471108; EAW90338.1; -; Genomic_DNA. DR EMBL; AC004148; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004451; AAH04451.1; -; mRNA. DR EMBL; BC046349; AAH46349.1; -; mRNA. DR EMBL; BC051849; AAH51849.1; -; mRNA. DR CCDS; CCDS32536.1; -. [Q86UA6-1] DR CCDS; CCDS54075.1; -. [Q86UA6-8] DR CCDS; CCDS54076.1; -. [Q86UA6-2] DR CCDS; CCDS54077.1; -. [Q86UA6-9] DR CCDS; CCDS54079.1; -. [Q86UA6-6] DR RefSeq; NP_001028174.2; NM_001033002.3. [Q86UA6-1] DR RefSeq; NP_001153715.1; NM_001160243.1. [Q86UA6-8] DR RefSeq; NP_001153716.1; NM_001160244.1. [Q86UA6-2] DR RefSeq; NP_001153718.1; NM_001160246.1. [Q86UA6-6] DR RefSeq; NP_001153738.1; NM_001160266.1. [Q86UA6-9] DR AlphaFoldDB; Q86UA6; -. DR BioGRID; 123995; 22. DR IntAct; Q86UA6; 9. DR STRING; 9606.ENSP00000385814; -. DR GlyGen; Q86UA6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86UA6; -. DR PhosphoSitePlus; Q86UA6; -. DR BioMuta; RPAIN; -. DR DMDM; 74727468; -. DR EPD; Q86UA6; -. DR jPOST; Q86UA6; -. DR MassIVE; Q86UA6; -. DR MaxQB; Q86UA6; -. DR PaxDb; 9606-ENSP00000385814; -. DR PeptideAtlas; Q86UA6; -. DR ProteomicsDB; 19663; -. DR ProteomicsDB; 19952; -. DR ProteomicsDB; 69786; -. [Q86UA6-1] DR ProteomicsDB; 69787; -. [Q86UA6-2] DR ProteomicsDB; 69788; -. [Q86UA6-3] DR ProteomicsDB; 69789; -. [Q86UA6-4] DR ProteomicsDB; 69790; -. [Q86UA6-5] DR ProteomicsDB; 69791; -. [Q86UA6-6] DR ProteomicsDB; 69792; -. [Q86UA6-7] DR Pumba; Q86UA6; -. DR Antibodypedia; 23662; 221 antibodies from 28 providers. DR DNASU; 84268; -. DR Ensembl; ENST00000327154.10; ENSP00000315069.6; ENSG00000129197.15. [Q86UA6-9] DR Ensembl; ENST00000381208.9; ENSP00000370605.5; ENSG00000129197.15. [Q86UA6-2] DR Ensembl; ENST00000381209.8; ENSP00000370606.3; ENSG00000129197.15. [Q86UA6-1] DR Ensembl; ENST00000405578.8; ENSP00000385814.4; ENSG00000129197.15. [Q86UA6-8] DR Ensembl; ENST00000536255.6; ENSP00000439939.2; ENSG00000129197.15. [Q86UA6-6] DR Ensembl; ENST00000539417.6; ENSP00000446453.2; ENSG00000129197.15. [Q86UA6-4] DR Ensembl; ENST00000571558.5; ENSP00000458699.1; ENSG00000129197.15. [Q86UA6-7] DR Ensembl; ENST00000573577.5; ENSP00000460162.1; ENSG00000129197.15. [Q86UA6-7] DR Ensembl; ENST00000574003.1; ENSP00000467178.1; ENSG00000129197.15. [Q86UA6-5] DR Ensembl; ENST00000575112.5; ENSP00000460354.1; ENSG00000129197.15. [Q86UA6-7] DR Ensembl; ENST00000575599.5; ENSP00000458218.1; ENSG00000129197.15. [Q86UA6-5] DR GeneID; 84268; -. DR KEGG; hsa:84268; -. DR MANE-Select; ENST00000381209.8; ENSP00000370606.3; NM_001033002.4; NP_001028174.2. DR UCSC; uc002gbw.3; human. [Q86UA6-1] DR AGR; HGNC:28641; -. DR DisGeNET; 84268; -. DR GeneCards; RPAIN; -. DR HGNC; HGNC:28641; RPAIN. DR HPA; ENSG00000129197; Low tissue specificity. DR MIM; 617299; gene. DR neXtProt; NX_Q86UA6; -. DR OpenTargets; ENSG00000129197; -. DR PharmGKB; PA145007849; -. DR VEuPathDB; HostDB:ENSG00000129197; -. DR eggNOG; ENOG502R0QT; Eukaryota. DR GeneTree; ENSGT00390000006416; -. DR InParanoid; Q86UA6; -. DR OMA; HGVAQMF; -. DR OrthoDB; 3032190at2759; -. DR PhylomeDB; Q86UA6; -. DR TreeFam; TF326215; -. DR PathwayCommons; Q86UA6; -. DR SignaLink; Q86UA6; -. DR BioGRID-ORCS; 84268; 573 hits in 1154 CRISPR screens. DR ChiTaRS; RPAIN; human. DR GeneWiki; RPAIN; -. DR GenomeRNAi; 84268; -. DR Pharos; Q86UA6; Tbio. DR PRO; PR:Q86UA6; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q86UA6; Protein. DR Bgee; ENSG00000129197; Expressed in cortical plate and 184 other cell types or tissues. DR ExpressionAtlas; Q86UA6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0016605; C:PML body; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR GO; GO:0009411; P:response to UV; IDA:MGI. DR InterPro; IPR028156; RIP. DR InterPro; IPR028159; RPA_interact_C_dom. DR InterPro; IPR028155; RPA_interact_central. DR InterPro; IPR028158; RPA_interact_N_dom. DR PANTHER; PTHR31742:SF1; RPA-INTERACTING PROTEIN; 1. DR PANTHER; PTHR31742; RPA-INTERACTING PROTEIN RPAIN; 1. DR Pfam; PF14768; RPA_interact_C; 1. DR Pfam; PF14767; RPA_interact_M; 1. DR Pfam; PF14766; RPA_interact_N; 1. DR Genevisible; Q86UA6; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..219 FT /note="RPA-interacting protein" FT /id="PRO_0000076299" FT ZN_FING 137..212 FT /note="RIP-type" FT REGION 164..180 FT /note="Mediates nuclear export" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); in isoform 2" FT /evidence="ECO:0000269|PubMed:16135809" FT VAR_SEQ 105..107 FT /note="EQS -> GTT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16008515, FT ECO:0000303|PubMed:16135809" FT /id="VSP_016402" FT VAR_SEQ 105..106 FT /note="EQ -> VF (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16008515, FT ECO:0000303|PubMed:16135809" FT /id="VSP_016403" FT VAR_SEQ 105..106 FT /note="EQ -> GL (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16008515, ECO:0000303|PubMed:16135809" FT /id="VSP_016404" FT VAR_SEQ 107..219 FT /note="Missing (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16008515, ECO:0000303|PubMed:16135809" FT /id="VSP_016405" FT VAR_SEQ 108..219 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16008515, FT ECO:0000303|PubMed:16135809" FT /id="VSP_016406" FT VAR_SEQ 142..145 FT /note="KYNL -> NLLS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16008515, ECO:0000303|PubMed:16135809" FT /id="VSP_016407" FT VAR_SEQ 143..219 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:16008515" FT /id="VSP_016408" FT VAR_SEQ 143..219 FT /note="YNLRITSGVVVCQCGLSIPSHSSELTEQKLRACLEGSINEHSAHCPHTPEFS FT VTGGTEEKSSLLMSCLACDTWAVIL -> PVILGL (in isoform 9)" FT /evidence="ECO:0000305" FT /id="VSP_046795" FT VAR_SEQ 146..219 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16008515, ECO:0000303|PubMed:16135809" FT /id="VSP_016409" FT VAR_SEQ 164..210 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16008515, FT ECO:0000303|PubMed:16135809" FT /id="VSP_016410" FT VAR_SEQ 211..219 FT /note="ACDTWAVIL -> VSVSWDPLCGKRDLWLVLFPP (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045356" FT VARIANT 103 FT /note="N -> K (sumoylated and increases total protein FT sumoylation levels; dbSNP:rs12761)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16008515, FT ECO:0000269|PubMed:16135809" FT /id="VAR_023947" FT MUTAGEN 114 FT /note="K->R: Abolishes sumoylation; when associated with FT R-121 and R-142." FT /evidence="ECO:0000269|PubMed:16135809" FT MUTAGEN 121 FT /note="K->R: Induces a strong decrease in sumoylation; when FT associated with N-103. Abolishes sumoylation; when FT associated with R-114 and R-142." FT /evidence="ECO:0000269|PubMed:16135809" FT MUTAGEN 142 FT /note="K->R: Abolishes sumoylation; when associated with FT R-114 and R-121." FT /evidence="ECO:0000269|PubMed:16135809" SQ SEQUENCE 219 AA; 24770 MW; BAF576893B8B1B23 CRC64; MAESLRSPRR SLYKLVGSPP WKEAFRQRCL ERMRNSRDRL LNRYRQAGSS GPGNSQNSFL VQEVMEEEWN ALQSVENCPE DLAQLEELID MAVLEEIQQE LINQEQSIIS EYEKSLQFDE KCLSIMLAEW EANPLICPVC TKYNLRITSG VVVCQCGLSI PSHSSELTEQ KLRACLEGSI NEHSAHCPHT PEFSVTGGTE EKSSLLMSCL ACDTWAVIL //