ID U3JJ06_FICAL Unreviewed; 1879 AA.
AC U3JJ06;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Pleckstrin homology domain interacting protein {ECO:0000313|Ensembl:ENSFALP00000002760.1};
GN Name=PHIP {ECO:0000313|Ensembl:ENSFALP00000002760.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002760.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002760.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002760.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 59894.ENSFALP00000002760; -.
DR Ensembl; ENSFALT00000002772.2; ENSFALP00000002760.1; ENSFALG00000002652.2.
DR eggNOG; KOG0644; Eukaryota.
DR GeneTree; ENSGT00950000183107; -.
DR HOGENOM; CLU_001108_0_0_1; -.
DR OMA; XRLAVGE; -.
DR Proteomes; UP000016665; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR CDD; cd05529; Bromo_WDR9_I_like; 1.
DR CDD; cd05496; Bromo_WDR9_II; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR16266:SF17; BRWD3; 1.
DR PANTHER; PTHR16266; WD REPEAT DOMAIN 9; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 236..277
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 278..319
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 320..355
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 418..452
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 519..561
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1235..1305
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1393..1463
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1879 AA; 212159 MW; D611777A67D167E0 CRC64;
MDGWRDGGMD GWRRRAWRGG GGRAGPPPPP PPPPPPPPPP PPPPPPPPPA GRGRPGRAAD
RAARWPLRPP SPIFSLFETF SHAPLLLLLQ VLIREVAEKE LLPKRTDWTG KEHPRSYENL
VKYYRHLAPD HLLQICHRLG PLLEQEIPQS VPGVQTLLGA GRQSLLRTNK SCKHVVWKGS
ALAALHCGRP PESPVNYGSP PSIVDTLFSR KLNGKYRLER LVPTAVYQHM KMHKRILGHL
SSVYCVTFDR TGRRIFTGSD DCLVKIWATD DGRLLATLRG HAAEISDMAV NYENTMIAAG
SCDKMIRVWC LRTCAPLAVL QGHSASITSL QFSPLCSGSK RYLSSTGADG TICFWLWDAG
TLKINPRPTK FTERPRPGVQ MICSSFSAGG MFLATGSTDH IIRVYFFGSG QPEKISELEF
HTDKVDSIQF SNSSSRFVSG SRDGTARIWQ FKRREWKSIL LDMATRPAGQ SFQGVEDKIT
KLKVTMVAWD RHDNSVITAV NNMTLKVWNS FTGQLIHILM GHEDEVFVLE PHPFDPRVLF
SAGHDGNVIV WDLARGVKIR SYFNMIEGQG HGAVFDCKCS PDGQHFACTD SHGHLLIFGF
GSSSKYDKIA DQMFFHSDYR PLIRDANNFV LDEQTQQAPH LMPPPFLVDV DGNPHPARYQ
RLVPGRENCR EEQLIPQMGV TSSGLNQVLS QQVNQEISPL DSMIQRLQQE QDQRRSGEAG
TSSTSRISRG SVSSTSEVHS PPNIGLRRSG QIEGVRQMHS NAPRSEIATE RDLVAWSRRV
VVPELSSGVA SRQEEWRTAK GEEEIRVYRS EEKRKHVISH IPRENKIPTF SKNHSHDNLL
DASDSKKQAA NQHNYRTRYA AEETARPAEE LENGHSSSDE GEVVVASGGT SEDDERAWHS
DGSSSDYSSD YSDWTADAGI NLQPPKKIPK IKTKKAESSS EDEEGPEKQR KQIKKERKKG
IEEKDGPSTS PKKRKPKERK QKRLAVGVLA ENGLTLEEWL PSAWITDTVP RRCPFVPQMG
DEVYYFRQGH EAYVVMAKKN KIYNINPKKQ PWHKMELREQ ELMKIVGIKY EVGLPTLCCL
KLAFLDPDTG KLTGGAFTMK YHDMPDVIDF LVLRQQFDDA KHRRWNIGDR FRSVIDDAWW
FGTIESQEPL QPDYPDSLFQ CYNVCWDNGD TEKMSPWDME LIPSNAVFPE ELGTSVPLTD
DERRTLLYKP LDGEWGSRTR EEECDRIIAG INQLMTLDIA SAFVAPVDLQ AYPMYCTVVA
YPTDLSTIKQ RLESRFYRRL SSLMWEVRYI EHNTRTFNEP GSPIVKAAKF VTDLLLHFIK
DQSCYDIIPL YNAMKKKVLS DSDEEEEKDT NVPGTSTRKR KDHQPKRRLR NRAQSYDIQS
WKKQCQELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME
LCKDVRLIFS NSKAYTPSKR SRIYSMSLRL SAFFEEHISS ILSDYKSALR FHKRNTIKKR
RKKRSRSSSV SSSVASSPER KRRLIKPQLK AETSATSSSS APARSTALRH TPPQMNGKAA
EASSLVRTRS NRGTTDVAVT EQPSTSSGAK PLTIKPLITK PNTTAGSGKS VLENSTKHSK
NQNIVSNPTP SDYSHNTRNN STRENPEKEK QIKRKVKSST VNPQADCKNN ALASGSIQVN
GHGGQPLKPP VKRGPGRKPK VETNNSSCEV VVHKKRGRKP KKLQIVEQQK VAEQNTIQTT
RDVPEEASVS TACNSLSENN VKEDLLQKKG RGGRKPKRKI KSRQPGSDLL VPANVKMQTR
SRRKKTHEPM EESSEELKDS EPHMRTRNQG RRTAFYNEDD SEEEQRQLLF EDTSLTFGTS
SRGRVRKLTE KAKANLIGW
//
