ID   RAD21_MOUSE             Reviewed;         635 AA.
AC   Q61550; P70219; Q3TQ09; Q810A8; Q91VB9; Q9DBU4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Double-strand-break repair protein rad21 homolog;
DE            Short=mHR21 {ECO:0000303|PubMed:8812457};
DE   AltName: Full=Pokeweed agglutinin-binding protein 29;
DE            Short=PW29 {ECO:0000303|PubMed:8521526};
DE   AltName: Full=SCC1 homolog;
DE   Contains:
DE     RecName: Full=64-kDa C-terminal product;
DE     AltName: Full=64-kDa carboxy-terminal product {ECO:0000250|UniProtKB:O60216};
GN   Name=Rad21;
GN   Synonyms=Hr21 {ECO:0000303|PubMed:8812457}, Scc1
GN   {ECO:0000250|UniProtKB:O60216};
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=8521526; DOI=10.1247/csf.20.263;
RA   Yu S., Ozawa M., Naved A.F., Miyauchi T., Muramatsu H., Muramatsu T.;
RT   "cDNA cloning and sequence analysis of a novel calcium binding protein with
RT   oligoproline motif.";
RL   Cell Struct. Funct. 20:263-268(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=8812457; DOI=10.1006/geno.1996.0466;
RA   McKay M.J., Troelstra C., van der Spek P., Kanaar R., Smit B.,
RA   Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.;
RT   "Sequence conservation of the rad21 Schizosaccharomyces pombe DNA double-
RT   strand break repair gene in human and mouse.";
RL   Genomics 36:305-315(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants within
RT   alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [6]
RP   IDENTIFICATION IN THE COHESIN COMPLEX, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10375619; DOI=10.1016/s0378-1119(99)00160-2;
RA   Darwiche N., Freeman L.A., Strunnikov A.;
RT   "Characterization of the components of the putative mammalian sister
RT   chromatid cohesion complex.";
RL   Gene 233:39-47(1999).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH SMC1; SMC3 AND STAG1.
RX   PubMed=18237772; DOI=10.1016/j.cell.2008.01.011;
RA   Parelho V., Hadjur S., Spivakov M., Leleu M., Sauer S., Gregson H.C.,
RA   Jarmuz A., Canzonetta C., Webster Z., Nesterova T., Cobb B.S., Yokomori K.,
RA   Dillon N., Aragon L., Fisher A.G., Merkenschlager M.;
RT   "Cohesins functionally associate with CTCF on mammalian chromosome arms.";
RL   Cell 132:422-433(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-175, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, and Spleen;
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).
CC   -!- FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a
CC       member of the cohesin complex, involved in sister chromatid cohesion
CC       from the time of DNA replication in S phase to their segregation in
CC       mitosis, a function that is essential for proper chromosome
CC       segregation, post-replicative DNA repair, and the prevention of
CC       inappropriate recombination between repetitive regions. The cohesin
CC       complex may also play a role in spindle pole assembly during mitosis
CC       (By similarity). In interphase, cohesins may function in the control of
CC       gene expression by binding to numerous sites within the genome
CC       (PubMed:18237772). May control RUNX1 gene expression. Binds to and
CC       represses APOB gene promoter (By similarity). May play a role in
CC       embryonic gut development, possibly through the regulation of enteric
CC       neuron development (By similarity). {ECO:0000250|UniProtKB:O60216,
CC       ECO:0000250|UniProtKB:Q6TEL1, ECO:0000269|PubMed:18237772}.
CC   -!- FUNCTION: [64-kDa C-terminal product]: May promote apoptosis.
CC       {ECO:0000250|UniProtKB:O60216}.
CC   -!- SUBUNIT: Component of the cohesin complex, which consists of an SMC1A/B
CC       and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1,
CC       STAG2/SA2 or STAG3/SA3 (PubMed:10375619, PubMed:18237772). Interacts
CC       (via C-terminus) with SMC1A and (via N-terminus) with SMC3; these
CC       interactions are direct (By similarity). The cohesin complex interacts
CC       with NUMA1. The cohesin complex also interacts with CDCA5, PDS5A and
CC       PDS5B; this interaction might regulate the ability of the cohesin
CC       complex to mediate sister chromatid cohesion. The interaction with
CC       PDS5B is direct and is stimulated by STAG1/SA1. The cohesin complex
CC       interacts with the cohesin loading complex subunits NIPBL/Scc2 (via
CC       HEAT repeats) and MAU2/Scc4. NIPBL directly contacts all members of the
CC       complex, RAD21, SMC1A/B, SMC3 and STAG1 (By similarity). The cohesin
CC       complex interacts with DDX11/ChIR1. Directly interacts with WAPL; this
CC       interaction is stimulated by STAG1/SA1 (By similarity). Interacts with
CC       the ISWI chromatin remodeling complex component SMARCA5; the
CC       interaction is direct (By similarity). Interacts with the NuRD complex
CC       component CHD4; the interaction is direct (By similarity).
CC       {ECO:0000250|UniProtKB:O60216, ECO:0000269|PubMed:10375619,
CC       ECO:0000269|PubMed:18237772}.
CC   -!- SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21
CC       homolog]: Nucleus {ECO:0000269|PubMed:10375619}. Chromosome
CC       {ECO:0000269|PubMed:10375619}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before
CC       prophase, scattered along chromosome arms. During prophase and
CC       prometaphase, most cohesins dissociate from the arms of condensing
CC       chromosome, possibly through PLK1-mediated phosphorylation (By
CC       similarity). A small amount of cohesin remains in centromeric regions
CC       and is removed from chromosomes only at the onset of anaphase. At
CC       anaphase, cleavage by separase/ESPL1 leads to the dissociation of
CC       cohesin from chromosomes and chromosome separation (By similarity).
CC       {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:O93310}.
CC   -!- SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:O60216}. Nucleus {ECO:0000250|UniProtKB:O60216}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis,
CC       brain, kidney, heart and thymus. Lowest levels in skeletal muscle.
CC       {ECO:0000269|PubMed:8521526, ECO:0000269|PubMed:8812457}.
CC   -!- DEVELOPMENTAL STAGE: Not regulated during the cell cycle (at protein
CC       level). {ECO:0000269|PubMed:10375619}.
CC   -!- DOMAIN: The C-terminal part associates with the ATPase head of SMC1A,
CC       while the N-terminal part binds to the ATPase head of SMC3.
CC       {ECO:0000250|UniProtKB:O60216}.
CC   -!- PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage
CC       is required for sister chromatid separation and cytokinesis. Cleaved by
CC       caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis.
CC       {ECO:0000250|UniProtKB:O60216}.
CC   -!- PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell
CC       cycle. The large dissociation of cohesin from chromosome arms during
CC       prophase may be partly due to its phosphorylation by PLK1.
CC       {ECO:0000250|UniProtKB:O60216}.
CC   -!- MISCELLANEOUS: Seems to bind calcium.
CC   -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR   EMBL; D49429; BAA08408.1; -; mRNA.
DR   EMBL; X98293; CAA66939.1; -; mRNA.
DR   EMBL; AF332086; AAK56114.1; -; mRNA.
DR   EMBL; AF332085; AAK56113.1; -; mRNA.
DR   EMBL; AK004746; BAB23527.1; -; mRNA.
DR   EMBL; AK163992; BAE37576.1; -; mRNA.
DR   EMBL; BC043032; AAH43032.2; -; mRNA.
DR   CCDS; CCDS27463.1; -.
DR   PIR; JC4248; JC4248.
DR   RefSeq; NP_033035.3; NM_009009.4.
DR   RefSeq; XP_006520707.1; XM_006520644.1.
DR   RefSeq; XP_006520708.1; XM_006520645.1.
DR   AlphaFoldDB; Q61550; -.
DR   SMR; Q61550; -.
DR   BioGRID; 202560; 25.
DR   CORUM; Q61550; -.
DR   DIP; DIP-56655N; -.
DR   IntAct; Q61550; 19.
DR   MINT; Q61550; -.
DR   STRING; 10090.ENSMUSP00000022927; -.
DR   iPTMnet; Q61550; -.
DR   PhosphoSitePlus; Q61550; -.
DR   EPD; Q61550; -.
DR   jPOST; Q61550; -.
DR   MaxQB; Q61550; -.
DR   PaxDb; 10090-ENSMUSP00000022927; -.
DR   PeptideAtlas; Q61550; -.
DR   ProteomicsDB; 300304; -.
DR   Pumba; Q61550; -.
DR   Antibodypedia; 13592; 398 antibodies from 35 providers.
DR   DNASU; 19357; -.
DR   Ensembl; ENSMUST00000022927.11; ENSMUSP00000022927.10; ENSMUSG00000022314.11.
DR   GeneID; 19357; -.
DR   KEGG; mmu:19357; -.
DR   UCSC; uc007vrd.2; mouse.
DR   AGR; MGI:108016; -.
DR   CTD; 5885; -.
DR   MGI; MGI:108016; Rad21.
DR   VEuPathDB; HostDB:ENSMUSG00000022314; -.
DR   eggNOG; KOG1213; Eukaryota.
DR   GeneTree; ENSGT00940000154655; -.
DR   HOGENOM; CLU_015775_1_1_1; -.
DR   InParanoid; Q61550; -.
DR   OMA; DDGIDNF; -.
DR   OrthoDB; 5481351at2759; -.
DR   PhylomeDB; Q61550; -.
DR   TreeFam; TF101215; -.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR   BioGRID-ORCS; 19357; 29 hits in 118 CRISPR screens.
DR   ChiTaRS; Rad21; mouse.
DR   PRO; PR:Q61550; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q61550; Protein.
DR   Bgee; ENSMUSG00000022314; Expressed in gonadal ridge and 267 other cell types or tissues.
DR   ExpressionAtlas; Q61550; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:MGI.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0008278; C:cohesin complex; IDA:CAFA.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0030892; C:mitotic cohesin complex; ISO:MGI.
DR   GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:CAFA.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0106222; F:lncRNA binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0140588; P:chromatin looping; IMP:MGI.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISO:MGI.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR   GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IMP:CAFA.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
DR   GO; GO:0045876; P:positive regulation of sister chromatid cohesion; ISO:MGI.
DR   GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR   CDD; cd21792; Rad21_Rec8_M_NXP1-like; 1.
DR   Gene3D; 1.10.10.580; Structural maintenance of chromosome 1. Chain E; 1.
DR   InterPro; IPR049589; NXP1_M-like.
DR   InterPro; IPR039781; Rad21/Rec8-like.
DR   InterPro; IPR006909; Rad21/Rec8_C_eu.
DR   InterPro; IPR006910; Rad21_Rec8_N.
DR   InterPro; IPR023093; ScpA-like_C.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12585:SF20; DOUBLE-STRAND-BREAK REPAIR PROTEIN RAD21 HOMOLOG; 1.
DR   PANTHER; PTHR12585; SCC1 / RAD21 FAMILY MEMBER; 1.
DR   Pfam; PF04824; Rad21_Rec8; 1.
DR   Pfam; PF04825; Rad21_Rec8_N; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   Genevisible; Q61550; MM.
PE   1: Evidence at protein level;
KW   Activator; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW   Chromosome partition; Cytoplasm; Developmental protein; DNA damage;
KW   DNA repair; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..635
FT                   /note="Double-strand-break repair protein rad21 homolog"
FT                   /id="PRO_0000097873"
FT   CHAIN           280..635
FT                   /note="64-kDa C-terminal product"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT                   /id="PRO_0000446318"
FT   REGION          126..282
FT                   /note="Required for interaction with SMARCA5"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   REGION          154..171
FT                   /note="Interaction with NIPBL"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   REGION          258..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..403
FT                   /note="Interaction with WAPL and PDS5B"
FT                   /evidence="ECO:0000250"
FT   REGION          362..403
FT                   /note="Interaction with STAG1"
FT                   /evidence="ECO:0000250"
FT   REGION          423..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..551
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            172..173
FT                   /note="Cleavage; by ESPL1"
FT                   /evidence="ECO:0000250"
FT   SITE            279..280
FT                   /note="Cleavage; by caspase-3 or caspase-7"
FT                   /evidence="ECO:0000250"
FT   SITE            454..455
FT                   /note="Cleavage; by ESPL1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   MOD_RES         627
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   CROSSLNK        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   CROSSLNK        418
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O60216"
FT   CONFLICT        147
FT                   /note="E -> G (in Ref. 4; BAB23527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="K -> E (in Ref. 4; BAB23527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="F -> S (in Ref. 1; BAA08408 and 3;
FT                   AAK56113/AAK56114)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        544
FT                   /note="Missing (in Ref. 1; BAA08408)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  72083 MW;  2EC1AC08E358E9CE CRC64;
     MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL
     LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP
     LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD
     DMLVSTSASN LLLEPEQSTS NLNEKMNHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG
     IFDDPPALSE AGVMLPEQPA HDDMDEDDNG SLGGPDSPDS VDPVEPMPTM TDQTTLVPNE
     EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL
     MMWKETGGVE KLFFLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF
     ENPEVPREEQ QPQQQQPQPQ RDVIDEPIIE EPSRLQDSVM EASRTTIEES AMPPPPPQGV
     KRKAGQIDPE PSIPPQQVEQ MEIPPVELPP EEPPNICQLI PELELLPEKE KEKEKEKEEE
     EEEEDEDASG GDQDQEERRW NKRTQQMLHG LQRALAKTGA ESISLLELCR NTNRKQAAAK
     FYSFLVLKKQ QAIELTQEEP YSDIIATPGP RFHII
//