ID Q2VJ45_HUMAN Unreviewed; 776 AA.
AC Q2VJ45;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=HOOK3-RET fusion protein {ECO:0000313|EMBL:AAZ57203.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAZ57203.1};
RN [1] {ECO:0000313|EMBL:AAZ57203.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17639057; DOI=10.1677/ERC-07-0039;
RA Ciampi R., Giordano T.J., Wikenheiser-Brokamp K., Koenig R.J.,
RA Nikiforov Y.E.;
RT "HOOK3-RET: a novel type of RET/PTC rearrangement in papillary thyroid
RT carcinoma.";
RL Endocr. Relat. Cancer 14:445-452(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the hook family.
CC {ECO:0000256|ARBA:ARBA00006946}.
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; DQ104207; AAZ57203.1; -; mRNA.
DR AlphaFoldDB; Q2VJ45; -.
DR PeptideAtlas; Q2VJ45; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
DR CDD; cd22226; HkD_Hook3; 1.
DR CDD; cd05045; PTKc_RET; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR008636; Hook_C.
DR InterPro; IPR043936; HOOK_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR18947; HOOK PROTEINS; 1.
DR PANTHER; PTHR18947:SF38; PROTEIN HOOK HOMOLOG 3; 1.
DR Pfam; PF05622; HOOK; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF116907; Hook domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 10..126
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 386..678
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 171..374
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 776 AA; 88399 MW; 694B9D66B46D7080 CRC64;
MFSVESLERA ELCESLLTWI QTFNVDAPCQ TVEDLTNGVV MAQVLQKIDP AYFDENWLNR
IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ
LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGNDA YVDLDRQLKK
TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QVLMERLNQS DSIEDPNSPA
GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK
ANAARSQLET YKRQEDPKWE FPRKNLVLGK TLGEGEFGKV VKATAFHLKG RAGYTTVAVK
MLKENASPSE LRDLLSEFNV LKQVNHPHVI KLYGACSQDG PLLLIVEYAK YGSLRGFLRE
SRKVGPGYLG SGGSRNSSSL DHPDERALTM GDLISFAWQI SQGMQYLAEM KLVHRDLAAR
NILVAEGRKM KISDFGLSRD VYEEDSYVKR SQGRIPVKWM AIESLFDHIY TTQSDVWSFG
VLLWEIVTLG GNPYPGIPPE RLFNLLKTGH RMERPDNCSE EMYRLMLQCW KQEPDKRPVF
ADISKDLEKM MVKRRDYLDL AASTPSDSLI YDDGLSEEET PLVDCNNAPL PRALPSTWIE
NKLYGMSDPN WPGESPVPLT RADGTNTGFP RYPNDSVYAN WMLSPSAAKL MDTFDS
//
