ID   UIMC1_MOUSE             Reviewed;         727 AA.
AC   Q5U5Q9; Q3TU77; Q60811; Q8C3Z8; Q8C719; Q8K1X7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=BRCA1-A complex subunit RAP80;
DE   AltName: Full=Receptor-associated protein 80;
DE   AltName: Full=Ubiquitin interaction motif-containing protein 1;
GN   Name=Uimc1; Synonyms=Rap80, Rip110, Rxrip110;
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] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Extraembryonic tissue, Kidney, Placenta, 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 MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary cancer, and 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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 148-727 (ISOFORM 1), AND INTERACTION WITH
RP   NR6A1.
RC   TISSUE=Liver;
RX   PubMed=7760852; DOI=10.1210/mend.9.1.7760852;
RA   Seol W., Choi H.S., Moore D.D.;
RT   "Isolation of proteins that interact specifically with the retinoid X
RT   receptor: two novel orphan receptors.";
RL   Mol. Endocrinol. 9:72-85(1995).
RN   [4]
RP   INTERACTION WITH TSP57.
RX   PubMed=12954732; DOI=10.1095/biolreprod.103.018465;
RA   Kim Y.-S., Nakanishi G., Oudes A.J., Kim K.H., Wang H., Kilpatrick D.L.,
RA   Jetten A.M.;
RT   "Tsp57: a novel gene induced during a specific stage of spermatogenesis.";
RL   Biol. Reprod. 70:106-113(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-46; THR-51; SER-665
RP   AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 80-120 IN COMPLEX WITH
RP   DI-UBIQUITIN, FUNCTION IN UBIQUITIN BINDING, AND UIM DOMAINS.
RX   PubMed=19536136; DOI=10.1038/emboj.2009.160;
RA   Sato Y., Yoshikawa A., Mimura H., Yamashita M., Yamagata A., Fukai S.;
RT   "Structural basis for specific recognition of Lys 63-linked polyubiquitin
RT   chains by tandem UIMs of RAP80.";
RL   EMBO J. 28:2461-2468(2009).
CC   -!- FUNCTION: Ubiquitin-binding protein. Specifically recognizes and binds
CC       'Lys-63'-linked ubiquitin (PubMed:19536136). Plays a central role in
CC       the BRCA1-A complex by specifically binding 'Lys-63'-linked
CC       ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to
CC       target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-
CC       strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase
CC       activity that specifically removes 'Lys-63'-linked ubiquitin on
CC       histones H2A and H2AX. Also weakly binds monoubiquitin but with much
CC       less affinity than 'Lys-63'-linked ubiquitin. May interact with
CC       monoubiquitinated histones H2A and H2B; the relevance of such results
CC       is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May
CC       indirectly act as a transcriptional repressor by inhibiting the
CC       interaction of NR6A1 with the corepressor NCOR1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96RL1, ECO:0000269|PubMed:19536136}.
CC   -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC       UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By
CC       similarity). Component of the BRCA1-A complex, at least composed of the
CC       BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and
CC       BABAM1/NBA1 (By similarity). In the BRCA1-A complex, interacts directly
CC       with ABRAXAS1 (By similarity). Interacts with ESR1 (By similarity).
CC       Interacts with UBE2I (By similarity). Interacts with NR6A1
CC       (PubMed:7760852). Interacts with TSP57 (PubMed:12954732). Interacts
CC       with TRAIP (By similarity). {ECO:0000250|UniProtKB:Q96RL1,
CC       ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:7760852}.
CC   -!- INTERACTION:
CC       Q5U5Q9; P62991: Ubc; NbExp=2; IntAct=EBI-7068640, EBI-413074;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RL1}.
CC       Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC       {ECO:0000250|UniProtKB:Q96RL1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5U5Q9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U5Q9-2; Sequence=VSP_037267, VSP_037268;
CC       Name=3;
CC         IsoId=Q5U5Q9-3; Sequence=VSP_037266;
CC   -!- DOMAIN: The tandem UIM domains form a continuous 60 Angstrom-long
CC       alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and
CC       UIM2 bind to the proximal and distal ubiquitin moieties and recognize
CC       an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with
CC       the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM
CC       domains determines the selectivity for 'Lys-63'-linkage, and its length
CC       is very important for specificity. {ECO:0000269|PubMed:19536136}.
CC   -!- DOMAIN: The Abraxas-interacting region (AIR) mediates the interaction
CC       with ABRAXAS1. {ECO:0000250|UniProtKB:Q96RL1}.
CC   -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:Q96RL1}.
CC   -!- PTM: Phosphorylated upon DNA damage by ATM or ATR.
CC       {ECO:0000250|UniProtKB:Q96RL1}.
CC   -!- SIMILARITY: Belongs to the RAP80 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37092.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK052704; BAC35106.1; -; mRNA.
DR   EMBL; AK083342; BAC38875.1; -; mRNA.
DR   EMBL; AK160926; BAE36094.1; -; mRNA.
DR   EMBL; BC037092; AAH37092.1; ALT_INIT; mRNA.
DR   EMBL; BC040808; AAH40808.1; -; mRNA.
DR   EMBL; U22015; AAC52167.1; -; mRNA.
DR   CCDS; CCDS36671.1; -. [Q5U5Q9-1]
DR   CCDS; CCDS79189.1; -. [Q5U5Q9-3]
DR   RefSeq; NP_001280589.1; NM_001293660.1.
DR   RefSeq; NP_035437.1; NM_011307.2.
DR   RefSeq; XP_006517229.1; XM_006517166.2.
DR   PDB; 3A1Q; X-ray; 2.20 A; C/F=80-120.
DR   PDB; 6GVW; X-ray; 3.75 A; E/J=275-334.
DR   PDBsum; 3A1Q; -.
DR   PDBsum; 6GVW; -.
DR   AlphaFoldDB; Q5U5Q9; -.
DR   SMR; Q5U5Q9; -.
DR   BioGRID; 203041; 3.
DR   ComplexPortal; CPX-4702; BRCA1-A complex.
DR   IntAct; Q5U5Q9; 1.
DR   MINT; Q5U5Q9; -.
DR   STRING; 10090.ENSMUSP00000026997; -.
DR   GlyGen; Q5U5Q9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5U5Q9; -.
DR   PhosphoSitePlus; Q5U5Q9; -.
DR   EPD; Q5U5Q9; -.
DR   jPOST; Q5U5Q9; -.
DR   MaxQB; Q5U5Q9; -.
DR   PaxDb; 10090-ENSMUSP00000122196; -.
DR   PeptideAtlas; Q5U5Q9; -.
DR   ProteomicsDB; 298381; -. [Q5U5Q9-1]
DR   ProteomicsDB; 298382; -. [Q5U5Q9-2]
DR   ProteomicsDB; 298383; -. [Q5U5Q9-3]
DR   Pumba; Q5U5Q9; -.
DR   DNASU; 20184; -.
DR   GeneID; 20184; -.
DR   KEGG; mmu:20184; -.
DR   UCSC; uc007qpv.2; mouse. [Q5U5Q9-1]
DR   UCSC; uc007qpw.2; mouse. [Q5U5Q9-3]
DR   AGR; MGI:103185; -.
DR   CTD; 51720; -.
DR   MGI; MGI:103185; Uimc1.
DR   eggNOG; ENOG502QQGN; Eukaryota.
DR   InParanoid; Q5U5Q9; -.
DR   OrthoDB; 4616645at2759; -.
DR   PhylomeDB; Q5U5Q9; -.
DR   Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR   Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR   BioGRID-ORCS; 20184; 12 hits in 117 CRISPR screens.
DR   ChiTaRS; Uimc1; mouse.
DR   EvolutionaryTrace; Q5U5Q9; -.
DR   PRO; PR:Q5U5Q9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q5U5Q9; Protein.
DR   GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:MGI.
DR   GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISO:MGI.
DR   GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; ISO:MGI.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0044818; P:mitotic G2/M transition checkpoint; NAS:ComplexPortal.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:HGNC-UCL.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   CDD; cd20912; AIR_RAP80-like; 1.
DR   Gene3D; 6.10.250.1800; -; 1.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR038868; RAP80.
DR   InterPro; IPR040714; RAP80_UIM.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR15932:SF2; BRCA1-A COMPLEX SUBUNIT RAP80; 1.
DR   PANTHER; PTHR15932; UBIQUITIN INTERACTION MOTIF-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF18282; RAP80_UIM; 1.
DR   SMART; SM00726; UIM; 2.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS51908; ZF_UBZ4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; DNA damage;
KW   DNA repair; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..727
FT                   /note="BRCA1-A complex subunit RAP80"
FT                   /id="PRO_0000097548"
FT   DOMAIN          80..99
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          104..124
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         510..537
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   REGION          1..101
FT                   /note="Necessary for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..103
FT                   /note="UIM-linker"
FT   REGION          100..200
FT                   /note="Necessary for interaction with NR6A1 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   REGION          133..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..400
FT                   /note="AIR"
FT   REGION          326..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..508
FT                   /note="Necessary for interaction with NR6A1 C-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   REGION          513..590
FT                   /note="Zinc-finger-like region"
FT   REGION          607..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           60..78
FT                   /note="LR motif"
FT   COMPBIAS        45..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         513
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         516
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         532
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         51
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQK4"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         637
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        31
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        75
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        90
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        245
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        382
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        387
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        436
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        552
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        570
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        595
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        617
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        652
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   CROSSLNK        708
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT   VAR_SEQ         120..400
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_037266"
FT   VAR_SEQ         401..406
FT                   /note="SSQGLF -> HCSFDQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037267"
FT   VAR_SEQ         407..727
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037268"
FT   CONFLICT        377
FT                   /note="Q -> R (in Ref. 1; BAC38875)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="I -> T (in Ref. 1; BAC35106/BAC38875/BAE36094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="D -> G (in Ref. 2; AAH40808)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        722
FT                   /note="G -> E (in Ref. 3; AAC52167)"
FT                   /evidence="ECO:0000305"
FT   HELIX           81..119
FT                   /evidence="ECO:0007829|PDB:3A1Q"
SQ   SEQUENCE   727 AA;  81478 MW;  B753BF61180D63ED CRC64;
     MPRRKKKIKE ASESQNLEKK DLETSSCVSI KKKRRLEDLL IVISDSDGEE TKEENGLQKT
     KTKQSNRSKC LAKRKVAHMS EEEQFALALK MSEQEAREVN NQEEKEEELL RKAIAESLNS
     CWSSAASATR SRPLAAELSS HSHQENTKDS GTTEGVWQLV PPSLCKGSHV SQGNEAEQRK
     EPWDHNENTE EEPVSGSSGS WDQSSQPVFE NENVKCFDRC TGHLAEHTQC GKPQESTGSG
     YAFSKAVQGR GDTSRQCLPI PADTKGLQDT GGTVHYYWGI PFCPAGVDPN QYTNVILCQL
     EVYQKSLKMA QRQLVKKRGF GEPVLPRPPF LIQNECGQED QTSDKNEGIS EDMGDEAKEE
     RQESRASVWH SETKDFQKSP IKSLKQKLLL EEEPTTSRGQ SSQGLFVEET SEEGLKSSEG
     DNSVPTTQSI AALTSKRSLV LMPESSAEEI TVCPETQLSF LEPLDLNRED SPDSRELPIE
     VRMAVGDKQV ANREDCMKEN PPPAVSSSTR VSCPLCNQDF PPTKIEQHAM YCNGLMEQET
     VLTRRRREAK NKSDGRTAAQ PALDANRKEK CYLCKSLVPL GEYQCHVEAC LQLAKVDRED
     GIEGTRRPRV CAPVEGKQQQ RLKKSKDKGH SQGRLLSLLE QSEHRTTGVE KKPKYSEVRT
     FRMPSPEVEE ASCSREMQST LSQLNLNESP IKSFVPVSEA TNCLVDFKEQ FAFRSRTKSG
     RGRRRKS
//