ID A0A1S3P2Y4_SALSA Unreviewed; 1213 AA.
AC A0A1S3P2Y4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein kinase C-binding protein 1-like isoform X4 {ECO:0000313|RefSeq:XP_014021993.1};
GN Name=LOC106582906 {ECO:0000313|RefSeq:XP_014021993.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014021993.1};
RN [1] {ECO:0000313|RefSeq:XP_014021993.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014021993.1; XM_014166518.1.
DR AlphaFoldDB; A0A1S3P2Y4; -.
DR GeneID; 106582906; -.
DR OrthoDB; 764287at2759; -.
DR Proteomes; UP000087266; Chromosome ssa22.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05508; Bromo_RACK7; 1.
DR CDD; cd15538; PHD_PRKCBP1; 1.
DR CDD; cd20160; PWWP_PRKCBP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR044075; PRKCBP1_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR021931; ZMYND8.
DR InterPro; IPR037967; ZMYND8_Bromo_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46453; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR46453:SF5; PROTEIN KINASE C-BINDING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12064; DUF3544; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_014021993.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|RefSeq:XP_014021993.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 84..129
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 183..253
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 295..345
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1116..1150
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1063..1112
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 132703 MW; BCD2A1DC152F20D2 CRC64;
MHPQSVAEEE VKTESDAVEG MEISTRSKVS VPGSVERAAQ KRKVPSPPHS SNGHSPAETS
SSPVKKKKKP GAVSSSKDQD GRNDFYCWLC HREGQVLCCE LCPRVYHAKC LKLPAEPEGD
WFCPECEKIT VAECIETQSK AMTMLTLDQL SYLLKFALQK MKQPGDQPRS SSHSPHAAAT
QRKAFNWTEP FQKPVSLEQH PDYAEYIFHA MDLCTLEKNT KKKMYGCTEA FLADVKWILH
NCIIYNGGNH KLTATAKVIV KICEHEMNEI EVCPECYLSA CQKRDNWFCE PCSDPHPLVW
AKLKGFPFWP AKALRDKDGQ VDARFFGQHD RAWVPLNNCY LMSKEIPFSV KKTKSIFNSA
MQEMEVYVEN MRKKFGVFTY APFRTPYTPD NQYQMLLDPA NPSSGSVRPE KHEKIKFNFD
MTASPKMPLS RSVLSGGGGC MGGVGGSTGR RISLTDMPRS PMSTNSSGHT GSDGEQETPD
KGQARAPASH YSAGEESMDC TASPASTRPD PVSGAKDSPK PFHSQGPALP LVPKQEKATP
TGSILNLNLD RSKAEMDLKE LSETVQQQQQ QQQGVPPVLT SPKRQIRSRF QLNLDRTIKS
CKAQLGIDEI SEDVYKGVEH SDSEDSDKSD SSDSEYASDE EQKPKVGQHT EANDKGEKDP
SKRGSKDPLP SIQNKEGKTE GPGPATATMG DAGVASTLSE SLSKEKQGVE SDKEPPEKAK
AVPASPAPRE KPQVKQEAKQ TSLVDDSDSE RELVIDLGED QGGRDRKRTR KDAHATKDPP
TNKTEGKAPT PSSALTPSQN NTAPSLTPSV KDSSQSPLAI PLNMVPFTTA APTTIGPTTL
ASATSTAPIT ASSATTAVKK QRPLLPRETV PVVQRAVVWN PTNKFQTSSQ KWHMQKVQRQ
QQNPQPDTPQ LQTASPGQPQ TQKLPQTPTS ATSSSSLSPE QPSQSTRYQT RQSVKAVQQK
DPPLSTSTSA VTLVTSIPAS VAMMAAPGVG SGPSTSMAGD FQIPTASADV AADIAKYTNK
IVDAIKGTMT ELYTELSKST SGNTIAEIRR LRIEIEKLQW LHQQELSEMK HNLELTMAEM
RQSLEQERER LMAEVKKQME VEKQQAVDET KKKQWCANCK KEAIFYCCWN TSYCDYPCQQ
AHWPEHMKSC TQSATASQQE PEAESTADPS AKPPGHSSSA QTPSGTGSAA TDKGPSPTCG
VDKSKDSASV TVP
//
