ID A0A2K5P8N0_CERAT Unreviewed; 1131 AA.
AC A0A2K5P8N0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Tumor protein p53 binding protein 2 {ECO:0000313|Ensembl:ENSCATP00000046066.1};
GN Name=TP53BP2 {ECO:0000313|Ensembl:ENSCATP00000046066.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000046066.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000046066.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A2K5P8N0; -.
DR Ensembl; ENSCATT00000070517.1; ENSCATP00000046066.1; ENSCATG00000045377.1.
DR GeneTree; ENSGT00940000153463; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000045377; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd17225; RA_ASPP2; 1.
DR CDD; cd11953; SH3_ASPP2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047163; ASPP1/2.
DR InterPro; IPR048942; ASPP2-like_RA.
DR InterPro; IPR047166; ASPP2_RA.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24131; APOPTOSIS-STIMULATING OF P53 PROTEIN; 1.
DR PANTHER; PTHR24131:SF8; APOPTOSIS-STIMULATING OF P53 PROTEIN 2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF21801; ASPP2-like_RA; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT REPEAT 961..993
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 994..1026
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1060..1122
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 87..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 125887 MW; D88BAD529F3CF595 CRC64;
FFFGVKMFLT VYLSNNEQHF TEVPVTPETI CRDVVDLCKE PGESDCHLAE VWCGSERPVA
DNERMFDILQ RFGSQRNEAR FFLRHEHPPG RDIVSGPRSQ DPSLKRNGVK VPGEYRRKEN
GVNSPRMDLT LAELQEMASR QQQQIEAQQQ LLATKEQRLK FLKQQDQRQQ QQVAEQEKLK
RLKEIAENQE AKLKKVRALK GHVEQKRLSN GKLVEEIEQM NSLFQQKQRE LVLAVSKVEE
LTRQLEMLKN GRIDGHHDNQ SAVAELDRLY KELQLRNKLN QEQNAKLQQQ RECLNKRNSE
VAVMDKRVNE LRDRLWKKKA ALQQKENLPV SSDGNLPQQA ASAPSRVAAV GPYIQSSTMP
RMPSRPELLV KPALPDGSLV MQASEGPMKI QTLPNMRSGA ASQTKGSKIH PAGPDWSPSN
ADLFPSQGSA SAPQSTGNAL DQVDDGEVPL REKEKKVRPF SMFDAVDQST APPSFGTLRK
NQSSEDILRD AQAANKSVAK VPPPVPTKPK QINLPYFGQT NQPPSDVKPD GSSQQLSTVV
PSMGTKPKPS GQQPRVLLSP SIPSVGQDQT LSPGSKQESP PAAAVRPFTP QPSKDTLLPP
FRKPQTVAAS SIYSMYTQQQ APGKNFQQAV QSALTKTHTR GPHFSSVYGK PVIAAAQNQQ
QHPENIYSNS QGKPGSPEPE TEPVSSVQEN HENERIPRPL SPTKLLPFLS NPYRNQSDAD
LEALRKKLSN APRPLKKRSS ITEPEGPNGP NIQKLLYQRT TIAAMETISV PSYPSKSASV
TASSERPVEI QNPYLHVEPE KEVVSLVPES LSPEDVGSAS TENSDMPVPS PGLDYEPEGV
PDNSPNLQKN PEEPNPEAPH LLDVYLEEYP PYPPPPYPSG EPEGPGEDSV SMRPPEITGQ
VSLPPGKRTN LRKTGSERIA HGMRVKFNPL ALLLDSSLEG EFDLVQRIIY EVDDPSLPND
EGITALHNAV CAGHTEIVKF LVQFGVNVNA ADSDGWTPLH CAASCNNVQV CKFLVESGAA
VFAMTYSDMQ TAADKCEEME EGYTQCSQFL YGVQEKMGIM NKGVIYALWD YEPQNDDELP
MKEGDCMTII HREDEDEIEW WWARLNDKEG YVPRNLLGLY PRIKPRQRSL A
//
