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BRCA1_PANTR
ID   BRCA1_PANTR             Reviewed;        1863 AA.
AC   Q9GKK8; O46484;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-MAY-2022, entry version 154.
DE   RecName: Full=Breast cancer type 1 susceptibility protein homolog;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398};
DE   AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
GN   Name=BRCA1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-309; GLY-590; GLU-731 AND
RP   GLU-1100.
RC   TISSUE=Blood;
RA   Takeda R., Hink R.L., Jogodka C., Walter N.A.R., Messier W.;
RT   "Positive selection on the human BRCA1 gene may have resulted from pressure
RT   for prolonged care for infants.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15385441; DOI=10.1093/hmg/ddh301;
RA   Pavlicek A., Noskov V.N., Kouprina N., Barrett J.C., Jurka J., Larionov V.;
RT   "Evolution of the tumor suppressor BRCA1 locus in primates: implications
RT   for cancer predisposition.";
RL   Hum. Mol. Genet. 13:2737-2751(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-1365, AND VARIANTS GLU-731 AND
RP   GLU-1100.
RX   PubMed=9462745; DOI=10.1038/ng0298-155;
RA   Hacia J.G., Makalowski W., Edgemon K., Erdos M.R., Robbins C.M.,
RA   Fodor S.P.A., Brody L.C., Collins F.S.;
RT   "Evolutionary sequence comparisons using high-density oligonucleotide
RT   arrays.";
RL   Nat. Genet. 18:155-158(1998).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the
CC       formation of 'Lys-6'-linked polyubiquitin chains and plays a central
CC       role in DNA repair by facilitating cellular responses to DNA damage. It
CC       is unclear whether it also mediates the formation of other types of
CC       polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse
CC       range of cellular pathways such as DNA damage repair, ubiquitination
CC       and transcriptional regulation to maintain genomic stability. Regulates
CC       centrosomal microtubule nucleation. Required for appropriate cell cycle
CC       arrests after ionizing irradiation in both the S-phase and the G2 phase
CC       of the cell cycle. Required for FANCD2 targeting to sites of DNA
CC       damage. Inhibits lipid synthesis by binding to inactive phosphorylated
CC       ACACA and preventing its dephosphorylation. Contributes to homologous
CC       recombination repair (HRR) via its direct interaction with PALB2, fine-
CC       tunes recombinational repair partly through its modulatory role in the
CC       PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks.
CC       Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation
CC       and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-
CC       mediated ubiquitination of RBBP8. Acts as a transcriptional activator.
CC       {ECO:0000250|UniProtKB:P38398}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P38398};
CC   -!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome
CC       surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1,
CC       ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This
CC       association could be a dynamic process changing throughout the cell
CC       cycle and within subnuclear domains. Component of the BRCA1-A complex,
CC       at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
CC       BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1
CC       (phosphorylated form); this is important for recruitment to sites of
CC       DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1
CC       (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts
CC       (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the
CC       interaction ubiquitinates RBBP8, regulates CHEK1 activation, and
CC       involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC       damage. Associates with RNA polymerase II holoenzyme. Interacts with
CC       SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and
CC       PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
CC       Interacts with FANCD2 (ubiquitinated form). Interacts with H2AX
CC       (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with
CC       ACACA (phosphorylated form); the interaction prevents dephosphorylation
CC       of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2.
CC       Interacts directly with PALB2; the interaction is essential for its
CC       function in HRR. Interacts directly with BRCA2; the interaction occurs
CC       only in the presence of PALB2 which serves as the bridging protein.
CC       Interacts (via the BRCT domains) with LMO4; the interaction represses
CC       the transcriptional activity of BRCA1. Interacts (via the BRCT domains)
CC       with CCAR2 (via N-terminus); the interaction represses the
CC       transcriptional activator activity of BRCA1 (By similarity). Interacts
CC       with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this
CC       interaction is direct and links BRCA1 to the RNA polymerase II
CC       holoenzyme (By similarity). {ECO:0000250|UniProtKB:P38398}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}.
CC       Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage
CC       at double-strand breaks (DSBs); recruitment to DNA damage sites is
CC       mediated by the BRCA1-A complex. Translocated to the cytoplasm during
CC       UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}.
CC   -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif
CC       on proteins. The interaction with the phosphorylated pSXXF motif of
CC       ABRAXAS1, recruits BRCA1 at DNA damage sites.
CC       {ECO:0000250|UniProtKB:P38398}.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
CC       {ECO:0000250|UniProtKB:P38398}.
CC   -!- PTM: Phosphorylated in response to IR, UV, and various stimuli that
CC       cause checkpoint activation, probably by ATM or ATR. Phosphorylation at
CC       Ser-988 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by
CC       AURKA regulates centrosomal microtubule nucleation.
CC       {ECO:0000250|UniProtKB:P38398}.
CC   -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination.
CC       'Lys-6'-linked polyubiquitination does not promote degradation.
CC       {ECO:0000250|UniProtKB:P38398}.
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DR   EMBL; AF207822; AAG43492.1; -; mRNA.
DR   EMBL; AY365046; AAR04849.1; -; Genomic_DNA.
DR   EMBL; AF019075; AAC39583.1; -; Genomic_DNA.
DR   RefSeq; NP_001038958.1; NM_001045493.1.
DR   AlphaFoldDB; Q9GKK8; -.
DR   BMRB; Q9GKK8; -.
DR   SMR; Q9GKK8; -.
DR   STRING; 9598.ENSPTRP00000015727; -.
DR   PaxDb; Q9GKK8; -.
DR   GeneID; 449497; -.
DR   KEGG; ptr:449497; -.
DR   CTD; 672; -.
DR   eggNOG; KOG4362; Eukaryota.
DR   InParanoid; Q9GKK8; -.
DR   OrthoDB; 496760at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
DR   GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000931; C:gamma-tubulin large complex; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; NAS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
DR   GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046600; P:negative regulation of centriole replication; NAS:UniProtKB.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0045739; P:positive regulation of DNA repair; NAS:UniProtKB.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR011364; BRCA1.
DR   InterPro; IPR031099; BRCA1-associated.
DR   InterPro; IPR025994; BRCA1_serine_dom.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13763; PTHR13763; 1.
DR   Pfam; PF00533; BRCT; 2.
DR   Pfam; PF12820; BRCT_assoc; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PIRSF; PIRSF001734; BRCA1; 1.
DR   PRINTS; PR00493; BRSTCANCERI.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; Cell cycle; Chromosome; Cytoplasm; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Isopeptide bond; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Tumor suppressor; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1863
FT                   /note="Breast cancer type 1 susceptibility protein homolog"
FT                   /id="PRO_0000055833"
FT   DOMAIN          1642..1736
FT                   /note="BRCT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          1756..1855
FT                   /note="BRCT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ZN_FING         24..65
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          230..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1397..1424
FT                   /note="Interaction with PALB2"
FT                   /evidence="ECO:0000250"
FT   REGION          1440..1505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1565..1642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..911
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1354..1395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1440..1468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1613..1628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         694
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         708
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48754"
FT   MOD_RES         753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         840
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48754"
FT   MOD_RES         988
FT                   /note="Phosphoserine; by CHEK2"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1009
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1457
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   MOD_RES         1542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        301
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        339
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        443
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        459
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        519
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        583
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        654
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        734
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        739
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        918
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        987
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   CROSSLNK        1079
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38398"
FT   VARIANT         309
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_018712"
FT   VARIANT         590
FT                   /note="S -> G"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_018713"
FT   VARIANT         731
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|PubMed:9462745, ECO:0000269|Ref.1"
FT                   /id="VAR_018714"
FT   VARIANT         1100
FT                   /note="G -> E"
FT                   /evidence="ECO:0000269|PubMed:9462745, ECO:0000269|Ref.1"
FT                   /id="VAR_018715"
FT   CONFLICT        427
FT                   /note="E -> K (in Ref. 2; AAR04849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        925
FT                   /note="I -> T (in Ref. 2; AAR04849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1520
FT                   /note="R -> T (in Ref. 1; AAG43492)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1863 AA;  207899 MW;  49673829CCFA756E CRC64;
     MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
     CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD
     EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKKSVYI
     ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ
     PSNNDLNTTE KRATERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE
     KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC
     SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GGSESNAKVA DVLDVLNEVD
     EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNTEDKI FGKTYRRKAS LPNLSHVTEN
     LIIGAFVTEP QIIQERPLTN KLKRKRRATS GLHPEDFIKK ADLAVQKTPE MINQGTNQME
     QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI
     HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV
     RHSRNLQLME DKEPATGVKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT NCSNTSELKE
     FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ
     ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DTRNDTEGFK YPLGHEVNHS
     RETSIEMEES ELDAQYLQNT FKVSKRQSFA LFSNPGNPEE ECATFSAHCR SLKKQSPKVT
     FEREQKEQNQ GKNESNIKPV QTVNITAGFP VVCQKDKPVD YAKCSIKGGS RFCLSSQFRG
     NETGLITPNK HGLLQNPYHI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP
     STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE VGSSDENIQA ELGRNRGPKL
     NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPCLIS DNLEQPMGSS
     HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQRGELSRSP SPFTHTHLAQ
     GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVSNIPSQ STRHSTVATE CLSKNTEENL
     LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS
     SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE
     DCSGLSSQSD ILTTQQRDTM QDNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE
     DLQNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK
     CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG
     TPYLESGISL FSDDPESDPS EDKAPESAHV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT
     NTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI
     TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
     VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL
     GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
     SHY
 
 
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