TE2IP_MOUSE
ID TE2IP_MOUSE Reviewed; 393 AA.
AC Q91VL8; D3YWE8; Q543F4; Q8C2Y1; Q9JJE8; Q9JJE9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1;
DE Short=TERF2-interacting telomeric protein 1;
DE Short=TRF2-interacting telomeric protein 1;
DE AltName: Full=Repressor/activator protein 1 homolog;
DE Short=RAP1 homolog;
GN Name=Terf2ip; Synonyms=Rap1; ORFNames=MNCb-0448, MNCb-0628;
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].
RC STRAIN=C57BL/6J;
RC TISSUE=Eye, Head, Heart, Ovary, Oviduct, Pancreas, Testis, 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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-286.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP BIDIRECTIONAL PROMOTER WITH KARS1.
RX PubMed=14659874; DOI=10.1016/j.gene.2003.08.026;
RA Tan M., Wei C., Price C.M.;
RT "The telomeric protein Rap1 is conserved in vertebrates and is expressed
RT from a bidirectional promoter positioned between the Rap1 and KARS genes.";
RL Gene 323:1-10(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20622869; DOI=10.1038/ncb2081;
RA Martinez P., Thanasoula M., Carlos A.R., Gomez-Lopez G., Tejera A.M.,
RA Schoeftner S., Dominguez O., Pisano D.G., Tarsounas M., Blasco M.A.;
RT "Mammalian Rap1 controls telomere function and gene expression through
RT binding to telomeric and extratelomeric sites.";
RL Nat. Cell Biol. 12:768-780(2010).
RN [10]
RP FUNCTION IN NF-KAPPA-B PATHWAY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TERF2; CHUK; IKBKB AND IKBKG.
RX PubMed=20622870; DOI=10.1038/ncb2080;
RA Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
RA de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J., Wong M.,
RA Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
RT "Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
RT dependent gene expression.";
RL Nat. Cell Biol. 12:758-767(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP TERF2.
RX PubMed=20339076; DOI=10.1126/science.1185100;
RA Sfeir A., Kabir S., van Overbeek M., Celli G.B., de Lange T.;
RT "Loss of Rap1 induces telomere recombination in the absence of NHEJ or a
RT DNA damage signal.";
RL Science 327:1657-1661(2010).
CC -!- FUNCTION: Acts both as a regulator of telomere function and as a
CC transcription regulator. Involved in the regulation of telomere length
CC and protection as a component of the shelterin complex (telosome). In
CC contrast to other components of the shelterin complex, it is
CC dispensible for telomere capping and does not participate in the
CC protection of telomeres against non-homologous end-joining (NHEJ)-
CC mediated repair. Instead, it is required to negatively regulate
CC telomere recombination and is essential for repressing homology-
CC directed repair (HDR), which can affect telomere length. Does not bind
CC DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3'
CC repeats via its interaction with TERF2. Independently of its function
CC in telomeres, also acts as a transcription regulator: recruited to
CC extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or
CC other factors, and regulates gene expression. When cytoplasmic,
CC associates with the I-kappa-B-kinase (IKK) complex and acts as a
CC regulator of the NF-kappa-B signaling by promoting IKK-mediated
CC phosphorylation of RELA/p65, leading to activate expression of NF-
CC kappa-B target genes. {ECO:0000269|PubMed:20339076,
CC ECO:0000269|PubMed:20622869, ECO:0000269|PubMed:20622870}.
CC -!- SUBUNIT: Homodimer. Component of the shelterin complex (telosome)
CC composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Binds to TERF2
CC (but not TERF1) with its C-terminus. Interacts with SLX4/BTBD12 (By
CC similarity). Interacts with TERF2; the interaction is direct. Does not
CC interact with TERF1. Associates with the I-kappa-B-kinase (IKK) core
CC complex, composed of CHUK, IKBKB and IKBKG. {ECO:0000250,
CC ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20622870}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20622870}. Cytoplasm
CC {ECO:0000269|PubMed:20622870}. Chromosome
CC {ECO:0000269|PubMed:20622869}. Chromosome, telomere
CC {ECO:0000269|PubMed:20622869}. Note=Associates with chromosomes, both
CC at telomeres and in extratelomeric sites (PubMed:20622869). Also exists
CC as a cytoplasmic form, where it associates with the IKK complex
CC (PubMed:20622870). {ECO:0000269|PubMed:20622869,
CC ECO:0000269|PubMed:20622870}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. No major telomere
CC dysfunction such as telomere fusions are observed. An increased
CC telomere fragility and recombination due to defects in HDR are however
CC present. Mice with conditional deletion in stratified epithelia display
CC shorter telomeres and developed skin hyperpigmentation in adulthood.
CC {ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20622869}.
CC -!- MISCELLANEOUS: Shares a bidirectional promoter with KARS1
CC (PubMed:14659874). This shared promoter with an essential gene
CC complicated the task when generating knockout mice; the problem was
CC overcome by generating conditional knockout strategies (PubMed:20339076
CC and PubMed:20622869;). {ECO:0000305|PubMed:14659874}.
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95043.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK041613; BAC31005.1; -; mRNA.
DR EMBL; AK051818; BAC34781.1; -; mRNA.
DR EMBL; AK081557; BAC38258.1; -; mRNA.
DR EMBL; AK087729; BAC39985.1; -; mRNA.
DR EMBL; AK084563; BAC39217.1; -; mRNA.
DR EMBL; AK148508; BAE28592.1; -; mRNA.
DR EMBL; AK148537; BAE28607.1; -; mRNA.
DR EMBL; AK161452; BAE36404.1; -; mRNA.
DR EMBL; AK165074; BAE38026.1; -; mRNA.
DR EMBL; AC114648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012270; AAH12270.1; -; mRNA.
DR EMBL; BC017641; AAH17641.1; -; mRNA.
DR EMBL; AB041557; BAA95042.1; -; mRNA.
DR EMBL; AB041559; BAA95043.1; ALT_INIT; mRNA.
DR CCDS; CCDS52678.1; -.
DR RefSeq; NP_065609.2; NM_020584.2.
DR AlphaFoldDB; Q91VL8; -.
DR SMR; Q91VL8; -.
DR BioGRID; 208258; 4.
DR ComplexPortal; CPX-153; Shelterin complex.
DR IntAct; Q91VL8; 1.
DR STRING; 10090.ENSMUSP00000052170; -.
DR iPTMnet; Q91VL8; -.
DR PhosphoSitePlus; Q91VL8; -.
DR EPD; Q91VL8; -.
DR jPOST; Q91VL8; -.
DR MaxQB; Q91VL8; -.
DR PaxDb; Q91VL8; -.
DR PeptideAtlas; Q91VL8; -.
DR PRIDE; Q91VL8; -.
DR ProteomicsDB; 263152; -.
DR Antibodypedia; 1877; 529 antibodies from 42 providers.
DR DNASU; 57321; -.
DR Ensembl; ENSMUST00000052138; ENSMUSP00000052170; ENSMUSG00000033430.
DR GeneID; 57321; -.
DR KEGG; mmu:57321; -.
DR UCSC; uc012gla.1; mouse.
DR CTD; 54386; -.
DR MGI; MGI:1929871; Terf2ip.
DR VEuPathDB; HostDB:ENSMUSG00000033430; -.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR GeneTree; ENSGT00390000005351; -.
DR HOGENOM; CLU_028192_0_0_1; -.
DR InParanoid; Q91VL8; -.
DR OMA; TQHSWQA; -.
DR OrthoDB; 602157at2759; -.
DR PhylomeDB; Q91VL8; -.
DR TreeFam; TF332348; -.
DR BRENDA; 3.6.5.2; 3474.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-MMU-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 57321; 7 hits in 107 CRISPR screens.
DR ChiTaRS; Terf2ip; mouse.
DR PRO; PR:Q91VL8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91VL8; protein.
DR Bgee; ENSMUSG00000033430; Expressed in ventromedial nucleus of hypothalamus and 245 other tissues.
DR Genevisible; Q91VL8; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000783; C:nuclear telomere cap complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070187; C:shelterin complex; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0048239; P:negative regulation of DNA recombination at telomere; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR021661; Rap1_C.
DR InterPro; IPR015010; Rap1_Myb_dom.
DR InterPro; IPR039595; TE2IP/Rap1.
DR PANTHER; PTHR16466; PTHR16466; 2.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF08914; Myb_DNA-bind_2; 1.
DR Pfam; PF11626; Rap1_C; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Chromosome; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CHAIN 2..393
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000197127"
FT DOMAIN 78..101
FT /note="BRCT"
FT DOMAIN 125..185
FT /note="Myb-like"
FT REGION 104..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..393
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 109..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CONFLICT 281..286
FT /note="PTPEED -> HTHTQS (in Ref. 4; BAA95042/BAA95043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43353 MW; 7A15CFD83733BE2D CRC64;
MAEAMDLGKD PNGPTHSSTL FVREDGSAMS FYVRPSSAKR RLSTLILHGG GTVCRVQEPG
AVLLAQPGEA LAEASGDFIS TQYILDCVDR NEKLDLEAYR LGLTEQASDP KPGASTEGST
EPEPQPLTGR IAYTDAEDVA ILTYVKENAR SPSSVTGNAL WKAMEKSSLT QHSWQSLKDR
YLKHLRGQEH KYLLGNAPVS PSSQKLKRKA EQDPEAADSG EPQNKRAPDL PEEECVKGEI
KENGEADNKL FEEAAPEFGE AVVDESPDFE IHITMCDGDP PTPEEDSETQ PDEEEEEPKV
STQEVGTAIK VIRQLMEKFN LDLSTVTQAL LKNSGELEAT SSFLESGRRP DGYPIWCRQD
DLDLQKDDDD TKNALVKKFG AQNVARRIEF RKK
