ID F1S9X3_PIG Unreviewed; 1092 AA.
AC F1S9X3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Protein phosphatase 1 regulatory subunit 13B {ECO:0000313|Ensembl:ENSSSCP00000002753.3};
GN Name=PPP1R13B {ECO:0000313|Ensembl:ENSSSCP00000002753.3,
GN ECO:0000313|VGNC:VGNC:91721};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000002753.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000002753.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000002753.3};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000002753.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F1S9X3; -.
DR PeptideAtlas; F1S9X3; -.
DR Ensembl; ENSSSCT00000002825.5; ENSSSCP00000002753.3; ENSSSCG00000002544.5.
DR VGNC; VGNC:91721; PPP1R13B.
DR GeneTree; ENSGT00940000153463; -.
DR HOGENOM; CLU_008234_0_0_1; -.
DR TreeFam; TF105545; -.
DR Proteomes; UP000008227; Unplaced.
DR Bgee; ENSSSCG00000002544; Expressed in oocyte and 44 other cell types or tissues.
DR ExpressionAtlas; F1S9X3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd17224; RA_ASPP1; 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; IPR028319; ASPP1_RA.
DR InterPro; IPR048942; ASPP2-like_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:SF5; APOPTOSIS-STIMULATING OF P53 PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF21801; ASPP2-like_RA; 1.
DR Pfam; PF00018; SH3_1; 1.
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 1: Evidence at protein level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S9X3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT REPEAT 922..954
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 955..987
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1021..1083
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 82..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..196
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 221..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 90..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 118978 MW; CC934E7DF73D88F7 CRC64;
MMPMILTVFL SNNEQILTEV PVTPETTCRD VVEFCKEPGE GSCHLAEVWR GNERPIPFDY
MMYEHLQKWG PRREEVKFFL RHEDSPTESS EQGGRQTQEQ RTQRNVINVP GEKRAENGVG
NPRVELTLSE LQDMAARQQQ QIENQQQMLV AKEQRLHFLK QQERRQQQSV SENEKLQKLK
ERVEAQENKL KKIRAMRGQV DYSKIMNGNL SAEIERFSAM FQEKKQEVQT AILRVDQLSQ
QLEDLKKGKL NGFQSYTGKL TGPAAVELKR LYQELQIRNQ LNQEQNSKLQ QQKELLSKRN
MEVAVMDKRI SELRERLYGK KIQLSRVNGT SSPQSPLSTP GRVAAVGPYI QVPSSGSYSV
PGDPVKPQSL TVAPSAAHGR SKSANDGNWP TLKQNSGSSV KGTQIASVDW RDSSTEGPLK
QGAVSSQPVP LPALGATEKL GLEMGKVPPP IPGVGKQPPP SYGTYPSPAP VGPGSTNSLE
RRKEGSLPRP STGLPSRQKP APLPPAGSPH PPGSSQQIQQ RISVPPSPTY PPAGLPAFPA
GDGKPELPLT VAIRPFLADK GSRPQSPRKG PQTVNSSSIY SMYLQQATPP KNYQPAAHGT
LNKSVKAVYG KPVLPSGSTS PSPLPFLHGS LATSTSQPQP PSESAEKEPE QDSPAPPGDG
GGASTVESLP RPLSPTKLTP IVHSPLRYQS DADLEALRRK LANAPRPLKK RSSITEPEGP
GGPNIQKLLY QRFNTLAGGM EGTPFYQPSP SQDFLGTLAD VDNGNTTANG NLGEASPAPP
TAPHPAEPAP ASDANDNQLP SPEPEGLTCP PDTHQTAEPA EDDNNNVATA PSTEQVPSPG
AEAPSPGEEQ VLLSLPPAVP PPAVSTSKRT NLKKPNSERT GHGLRVRFNP LALLLDASLE
GEFDLVQRVI YEVEDPSKPN DEGITPLHNA VCAGHHHIVR FLLDFGVNVN AADSDGWTPL
HCAASCNSVH LCKQLVESGA AIFASTVSDI ETAADKCEEM EEGYIQCSQF LYGVQEKLGV
MNKGVVYALW AYDAQNSDEL SFHEGDALTI LRRKDESETD WWWARLGDRE GYVPKNLLGL
YPRIKPRQRT LA
//
