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   27-MAR-2024, entry version 188.
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
CC       (PubMed:20339076, 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; 10090-ENSMUSP00000052170; -.
DR   PeptideAtlas; Q91VL8; -.
DR   ProteomicsDB; 263152; -.
DR   Pumba; Q91VL8; -.
DR   Antibodypedia; 1877; 582 antibodies from 42 providers.
DR   DNASU; 57321; -.
DR   Ensembl; ENSMUST00000052138.11; ENSMUSP00000052170.9; ENSMUSG00000033430.11.
DR   GeneID; 57321; -.
DR   KEGG; mmu:57321; -.
DR   UCSC; uc012gla.1; mouse.
DR   AGR; MGI:1929871; -.
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; MEKFAVD; -.
DR   OrthoDB; 2920206at2759; -.
DR   PhylomeDB; Q91VL8; -.
DR   TreeFam; TF332348; -.
DR   BRENDA; 3.6.5.2; 3474.
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   BioGRID-ORCS; 57321; 7 hits in 112 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 248 other cell types or tissues.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0035556; P:intracellular signal transduction; ISO:MGI.
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 canonical NF-kappaB signal transduction; 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 non-canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:0032206; P:positive regulation of telomere maintenance; NAS:ComplexPortal.
DR   GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
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: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   CDD; cd11655; rap1_myb-like; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   Genevisible; Q91VL8; MM.
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
//