ID   PFT1_HUMAN     STANDARD;      PRT;   469 AA.
AC   O94921; Q9UDR0; Q9H3D7;
DT   15-JUN-2002 (Rel. 41, Created)
DT   15-JUN-2002 (Rel. 41, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Serine/threonine-protein kinase PFTAIRE-1 (EC 2.7.1.37).
GN   PFTK1 OR KIAA0834.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A. (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Cervical carcinoma;
RX   MEDLINE=21213900; PubMed=11313143;
RA   Yang T., Chen J.-Y.;
RT   "Identification and cellular localization of human PFTAIRE1.";
RL   Gene 267:165-172(2001).
RN   [2]
RP   SEQUENCE FROM N.A. (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=99156230; PubMed=10048485;
RA   Nagase T., Ishikawa K.-I., Suyama M., Kikuno R., Hirosawa M.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   SEQUENCE OF 165-329 FROM N.A.
RA   Du H., Bauer C., Lehnert L.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in meiosis as well as in neuron
CC       differentiation and/or function (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC   -!- ALTERNATIVE PRODUCTS: 2 isoforms; 1 (shown here) and 2; may be
CC       produced by alternative splicing.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, pancreas, kidney,
CC       heart, testis and ovary. Also detected at lower levels in other
CC       tissues except in spleen and thymus where expression is barely
CC       detected.
CC   -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES.
CC       CDC2/CDKX SUBFAMILY.
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   EMBL; AF119833; AAG43234.1; -.
DR   EMBL; AB020641; BAA74857.1; -.
DR   EMBL; AC006036; AAF19245.1; -.
DR   Genew; HGNC:8883; PFTK1.
DR   HSSP; P24941; 1CKP.
DR   InterPro; IPR000719; Euk_pkinase.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; pkinase; 1.
DR   ProDom; PD000001; Euk_pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
KW   Transferase; Serine/threonine-protein kinase; Nuclear protein;
KW   ATP-binding; Alternative splicing.
FT   DOMAIN      135    419       PROTEIN KINASE.
FT   NP_BIND     141    149       ATP (BY SIMILARITY).
FT   BINDING     164    164       ATP (BY SIMILARITY).
FT   ACT_SITE    256    256       BY SIMILARITY.
FT   VARSPLIC      1     41       MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDE
FT                                -> MHGYFGCNAAAEPGYSAFVGTPQ (IN ISOFORM
FT                                2).
FT   CONFLICT    158    158       W -> G (IN REF. 2).
SQ   SEQUENCE   469 AA;  53186 MW;  769F9FC420D9C502 CRC64;
     MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKDDTTFD EICVTKMSTR NCQGMDSVIK
     PLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC INFKTSSTGK ESPKVRRHSS
     PSSPTSPKFG KADSYEKLEK LGEGSYATVY KGKSKVNWKL VALKVIRLQE EEGTPFTAIR
     EASLLKGLKH ANIVLLHDII HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL
     LRGLSYIHQR YILHRDLKPQ NLLISDTGEL KLADFGLARA KSVPSHTYSN EVVTLWYRPP
     DVLLGSTEYS TCLDMWGVGC IFVEMIQGVA AFPGMKDIQD QLERIFLVLG TPNEDTWPGV
     HSLPHFKPER FTLYSSKNLR QAWNKLSYVN HAEDLASKLL QCSPKNRLSA QAALSHEYFS
     DLPPRLWELT DMSSIFTVPN VRLQPEAGES MRAFGKNNSY GKSLSNSKH
//