ID G1TDI1_RABIT Unreviewed; 1902 AA.
AC G1TDI1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Tumor protein p53 binding protein 1 {ECO:0000313|Ensembl:ENSOCUP00000014902.3};
GN Name=TP53BP1 {ECO:0000313|Ensembl:ENSOCUP00000014902.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000014902.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000014902.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000014902.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000014902.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000014902.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AAGW02024592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02024593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02024594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02024595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02024596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSOCUT00000017341.3; ENSOCUP00000014902.3; ENSOCUG00000017337.4.
DR eggNOG; KOG3548; Eukaryota.
DR GeneTree; ENSGT00390000011891; -.
DR HOGENOM; CLU_002167_0_0_1; -.
DR TreeFam; TF350227; -.
DR Proteomes; UP000001811; Chromosome 17.
DR Bgee; ENSOCUG00000017337; Expressed in embryo and 15 other cell types or tissues.
DR ExpressionAtlas; G1TDI1; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR CDD; cd17745; BRCT_p53bp1_rpt1; 1.
DR CDD; cd17724; BRCT_p53bp1_rpt2; 1.
DR CDD; cd20383; Tudor_53BP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR InterPro; IPR015125; 53-BP1_Tudor.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR047249; BRCT_p53bp1-like_rpt1.
DR InterPro; IPR047250; BRCT_p53bp1-like_rpt2.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR047252; TP53BP1-like.
DR PANTHER; PTHR15321:SF3; TP53-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR15321; TUMOR SUPPRESSOR P53-BINDING PROTEIN 1; 1.
DR Pfam; PF09038; 53-BP1_Tudor; 1.
DR Pfam; PF18428; BRCT_3; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 1654..1778
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1794..1894
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1902 AA; 206731 MW; 65456056E17AE45C CRC64;
IPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE
NPVLDVVSNP EQTAGEEPRD TNSGFTGHVK ENKAADSTDS PHLDTCGSIS QVIEQLPQPN
RTSSILGMPV GSAPTMGEEK EDLEEEKGEK EDSPDDVVHS FGAEEPASSQ LGFGVLELSQ
SQDVEELPVP CEVDREHLQS VTTNSYTRLS DADANTAIKH EEQSNEDIPV AEQSSKDTLE
TAQPSKNVHV VEEQNSPPTR SEDITSSPKV CLAAMEAKEQ MSTQELLEGG LQIQKSLEPE
ILSTQEDLFD QSNKTDEPMD MSVLAEEGGA PFQKQLQDDE PMEIENPPLP PKPAVSPQAS
TPVSQSTPVF TPASLPIPSQ PEFSHDIFIP SPSLEDQSND GKKGGDLNSS SLTVECSKTS
ESEPKNSTED LGLSLTGDSC KLMLSTSEYS QSPKMESLGS QRIDEDGENT QIEDTEPMSP
VLNSKLVAAE NDSILLNPAQ DGQVELSHND DKTKGEDTET RDDISVLATG CKVREETVAE
DVCIDLTCDS GSQAVPSPAT RSEALSSVLD QEEAMEIKEH HPEEGSSGSE VEEIPETPCE
SQGEEPKEEN MENVQLHLSL TETQSQGLCL QKEVPKQECS EAMEVETSVI SIDSPPKLPV
IDQELEHKDQ EAWEEATSED SSVVIVDVKE PSPRVDVSCE PLEGVEKCSD SQSWEDVAPE
IEPCAETRLD TQEEKNIKYR EEVKAVPAEK EPVGEDCAQP PLPLEAKNEP PRPDQEKQEP
QPQEKTDNVL TEVSKVANAK QLDSGREAQQ LEKASAHASQ SFCENSSETP FHFTLPKEGD
IIPPLAGATP PLIGHLKLEP KRHSTPIGIS NYPESTIATS DVMSESMVET NDPLLGSGKR
DSGAAPEMDD KLCLRMKLVS PETEASEESL QFSLEKPATS ERKNGSTAVA ETVASPQKTM
TVFSCICEGR QEDEVRSEDS PSAPIRGNLL HFPSTQAEEE KEKLEGDQRI RQSEQSVKPV
SPHRDPASPL SQQVATQRPS SPQEEAMETD VLEGQRGRQN TDREKPSKTL VERPTQNNIG
IQTMERSLWV PETVSAGTQT VKNVCEQGTS TVDHSSGKQD AVVQTEKGSG EKPGGAPGDD
TESLHSQGEE EFEMPQPPHG HVLHRHMRTI REVRTLVTRV ITDVYYVDGT EVERKVTEET
EEPIVECQEC ETEVSLPSRK GGSPQGPGGK NNPLPPPRNP ALHRTSSGTS LSAMHSSGSS
GRGAAPPKGK TSGTEPADFA LPSSRGGPGK LSPRKGVSQT GAPVCEEDGD AGLGIRQGGK
APVTPRGRGR RGRPPSRTTG TRETAVPGPL GIEDISPSMS PDDKSFTRIM PRVPDSSRRA
DVGTGALRRS DSPEIPFQAA AGSSDGLDTS SPGNSFVGLR VVAKWSSNGY FYSGKITRDV
GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED EYFSAGVVKG HRKESGELYY
SIEKEGQRKW YKRMAVILSL EQGNRLREQY GLGPYEAVTP LTKAADISLD NLVEGKRKRR
SNISSPATPT ASSSSSTTPA RKITESPRAS VGVPAGKRKL IASEEERSPA KRGRKSAAAK
PGAVGAGECV SPCESGDHTT EPSTMEEQRG PLPLNKTLFL GYAFLLTMAT TSDKLASRSK
LSDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY QCLLIADQHC
RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA GYSLEEQRIL DWQPRENPFQ
NLKVLLVSDQ QQNFLELWSE ILMTGGAASV KQHHSSAHNK DIALGVFDVV VTDPSCPASV
LKCAEALQLP VVSQEWVIQC LIVGERIGFK QHPKYKHDYV SH
//
