RIP_HUMAN
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 03-AUG-2022, entry version 145.
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}.
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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; 18.
DR IntAct; Q86UA6; 9.
DR STRING; 9606.ENSP00000385814; -.
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; Q86UA6; -.
DR PeptideAtlas; Q86UA6; -.
DR PRIDE; 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 Antibodypedia; 23662; 198 antibodies from 27 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 CTD; 84268; -.
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; EHSTHCP; -.
DR PhylomeDB; Q86UA6; -.
DR TreeFam; TF326215; -.
DR PathwayCommons; Q86UA6; -.
DR SignaLink; Q86UA6; -.
DR BioGRID-ORCS; 84268; 557 hits in 1076 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 182 other tissues.
DR ExpressionAtlas; Q86UA6; baseline and differential.
DR Genevisible; Q86UA6; HS.
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:0044877; F:protein-containing complex binding; IPI:MGI.
DR GO; GO:0006310; P:DNA recombination; IPI:MGI.
DR GO; GO:0006281; P:DNA repair; IPI:MGI.
DR GO; GO:0006261; P:DNA-templated DNA replication; IPI:MGI.
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; PTHR31742; 1.
DR Pfam; PF14768; RPA_interact_C; 1.
DR Pfam; PF14767; RPA_interact_M; 1.
DR Pfam; PF14766; RPA_interact_N; 1.
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 R-
FT 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 R-
FT 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
