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Database: UniProt
Entry: H2NN04_PONAB
LinkDB: H2NN04_PONAB
Original site: H2NN04_PONAB 
ID   H2NN04_PONAB            Unreviewed;      1244 AA.
AC   H2NN04; A0A2J8S5H2; A0A6D2X5I2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=TTBK2 isoform 6 {ECO:0000313|EMBL:PNJ16016.1};
DE   SubName: Full=Tau tubulin kinase 2 {ECO:0000313|Ensembl:ENSPPYP00000007256.1};
GN   Name=TTBK2 {ECO:0000313|Ensembl:ENSPPYP00000007256.1};
GN   ORFNames=CR201_G0046001 {ECO:0000313|EMBL:PNJ16016.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007256.1, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000007256.1, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ16016.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ16016.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000007256.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; NDHI03003606; PNJ16016.1; -; Genomic_DNA.
DR   RefSeq; XP_009248027.1; XM_009249752.1.
DR   STRING; 9601.ENSPPYP00000007256; -.
DR   Ensembl; ENSPPYT00000007557.2; ENSPPYP00000007256.1; ENSPPYG00000006404.2.
DR   eggNOG; KOG1164; Eukaryota.
DR   GeneTree; ENSGT00940000160367; -.
DR   HOGENOM; CLU_003410_0_0_1; -.
DR   OMA; EEDWGWG; -.
DR   OrthoDB; 163007at2759; -.
DR   TreeFam; TF351646; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005814; C:centriole; IEA:Ensembl.
DR   GO; GO:0035869; C:ciliary transition zone; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR   GO; GO:1902817; P:negative regulation of protein localization to microtubule; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR   CDD; cd14129; STKc_TTBK2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR047915; TTBK2_STKc.
DR   PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR11909:SF451; TAU-TUBULIN KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT   DOMAIN          21..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          514..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1244 AA;  137319 MW;  1BECA635BD27248A CRC64;
     MSGGGEQPDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV
     LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR
     LGRQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCY MLDFGLARQF TNSCGDVRPP
     RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE
     RYDHRLMLKH LPPEFSIFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKT
     GNDGSLTTTT TSTTPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP
     VGVSPDKLPG SLGHPRPQEK DVWEEMDANK NKIKLGICKA ATEEENSHGQ ANGLLNAPSL
     GSPIRVRSEI TQPDRDIPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETC LEKMQKGTSA
     GKESILPALL HKPCVPAVSR TDHIWHYDEE YLPDASKPAS ANTPEQADGG GSNGFIAVNL
     SSCKQEIDSK EWVIVDKEQD LQDFRTNEAV GHKTTGSPSD EEPEVLQVLE ASPQDEKLQL
     GPWAENDHLK KETSGVVLAL SAEGPPTAAS EQYTDRLELQ PGAASQFIAA TPTSLMEAQA
     EGPLTAITIP RPSVASTQST SGSFHYGQQP EKKDLQPMEP TVELYSPREN FSGLVVTEGE
     PPSGGSRTDL GLQIDHIGHD MLPNIRESNK SQDLGPKELP DNNRLVVREF ENLPGETEEK
     SILLESDNED EKLSRGQHCI EISSFPGDLV IVEKDHSATT EPLDVTKTQT FSVVPNQDKN
     DEIMKLLTVG TSEISSRDID PHVEGQLGQA AEMQKNKISK DDDIMSEDLP GHQGDLSTFL
     HQEGKREKIT PRNGELFHCV SENEHGAPTR KDMVRSSFVT RHSRIPVLAQ EIDSTLESSS
     PVSAKEKLLQ KKAYQPDLVK LLVEKRQFKS FLGDLSSASD KLLEEKLATV PAPFCEEEAL
     TPLSRLTVDS HLSRSTEDSF LSPIISQSRK SKIPRPVSWV NTDQVNSSTS SQFFPRPPPG
     KPPTRPGVEA RLRRYKVLGS SNSDSDLFSR LAQILQNGSQ KPRSTTQCKS PGSPHNPKTP
     PKSPVVPRRS PSASPRSSSL PRTSSSSPSR AGRPHHDQRS SSPHLGRSKS PPSHSGSSSS
     RRSCQQEHCK PSKNGLKGSG SLHHHSASTK TPPGKSKPAS KLSR
//
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