GenomeNet

Database: UniProt
Entry: A0A2Y9IQH8_ENHLU
LinkDB: A0A2Y9IQH8_ENHLU
Original site: A0A2Y9IQH8_ENHLU 
ID   A0A2Y9IQH8_ENHLU        Unreviewed;      1111 AA.
AC   A0A2Y9IQH8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Protein kinase C-binding protein 1 isoform X7 {ECO:0000313|RefSeq:XP_022350511.1};
GN   Name=LOC111141930 {ECO:0000313|RefSeq:XP_022350511.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350511.1};
RN   [1] {ECO:0000313|RefSeq:XP_022350511.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022350511.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_022350511.1; XM_022494803.1.
DR   AlphaFoldDB; A0A2Y9IQH8; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; 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:SF3; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF12064; DUF3544; 2.
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_022350511.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Transferase {ECO:0000313|RefSeq:XP_022350511.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          83..128
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          160..230
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          272..322
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          952..986
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          899..948
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1111 AA;  122394 MW;  A50FAE38D5CAED34 CRC64;
     MHPQSLAEEE IKTEQEVVEG MDISTRSKDP GSTERTAQKR KFPSPPHSSN GHSPQDTSTS
     PIKKKKKPGL LNNNNKEQDG RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW
     FCPECEKITV AECIETQSKA MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY
     AEYIFHPMDL CTLEKNAKKK MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC
     EHEMNEIEVC PECYLAACQK RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA
     RFFGQHDRAW VPINNCYLMS KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF
     RTPYTPNSQY QMLLDPSNPS AGAAKVDKQE KVKLNFDMTA SPKILMSKPM LSGGAGRRIS
     LSDMPRSPMS TNSSVHTGSD VEQDAEKKAT SSHFSASEES MDFLDKSTDR SKAEMDLKEL
     SESVQQQTAP VPLISPKRQI RSRFQLNLDK TIESCKAQLG INEISEDVYT AVEHSDSEDS
     EKSDSSDSEY ISDDEQKSKN EPEDTEDKEG SRVDKEPSAV KKKPKLASPV ETKEELKSTS
     PASEKADPGS VKEKASPPPE KDFSEKAKAS PHSTKDKLKG KDETDSPTVH LGLDSDSESE
     LVIDLGEDHS GREGRKNKKE PKETSPKQDV VGKAPPSTTA GSQSPPETPL LTRSSSQTPT
     AGVTVTTSTT STVTAPATTA TAAAAATAAA AAAAAATAAA AATTTGSPVK KQRPLLPKET
     APAVQRVAWN SSTVQQKEIT QSPSTSTITL VTSTQSSPLV TSSGSTSTLA SSVSADLPIA
     TASADVAADI AKYTSKMMDA IKGTMTEIYN DLSKNTTGST IAEIRRLRIE IEKLQWLHQQ
     ELSEMKHNLE LTMAEMRQSL EQERDRLMAE VKKQLELEKQ QAVDETKKKQ WCANCKKEAI
     FYCCWNTSYC DYPCQQAHWP EHMKSCTQSA TAPQQEADAE VNSETLNKPS QGSSSSTQAA
     PTETASTSKE KEAPAEKSKD SGSTLDLSGS RETPSSILLG SNQGSDHSRS SKSSCWSSSD
     EKRGPTRSEH NASSSSKSLL PKESRLDTFW D
//
DBGET integrated database retrieval system