UIMC1_MOUSE
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 03-AUG-2022, entry version 144.
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.ENSMUSP00000122196; -.
DR iPTMnet; Q5U5Q9; -.
DR PhosphoSitePlus; Q5U5Q9; -.
DR EPD; Q5U5Q9; -.
DR jPOST; Q5U5Q9; -.
DR MaxQB; Q5U5Q9; -.
DR PaxDb; Q5U5Q9; -.
DR PeptideAtlas; Q5U5Q9; -.
DR PRIDE; Q5U5Q9; -.
DR ProteomicsDB; 298381; -. [Q5U5Q9-1]
DR ProteomicsDB; 298382; -. [Q5U5Q9-2]
DR ProteomicsDB; 298383; -. [Q5U5Q9-3]
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 CTD; 51720; -.
DR MGI; MGI:103185; Uimc1.
DR eggNOG; ENOG502QQGN; Eukaryota.
DR InParanoid; Q5U5Q9; -.
DR OrthoDB; 554207at2759; -.
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-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 111 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: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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; 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; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:HGNC-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR038868; RAP80.
DR InterPro; IPR040714; RAP80_UIM.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR15932; PTHR15932; 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
