Full text data of SCYL1
SCYL1
(CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP)
[Confidence: low (only semi-automatic identification from reviews)]
N-terminal kinase-like protein (Coated vesicle-associated kinase of 90 kDa; SCY1-like protein 1; Telomerase regulation-associated protein; Telomerase transcriptional element-interacting factor; Teratoma-associated tyrosine kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-terminal kinase-like protein (Coated vesicle-associated kinase of 90 kDa; SCY1-like protein 1; Telomerase regulation-associated protein; Telomerase transcriptional element-interacting factor; Teratoma-associated tyrosine kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96KG9
ID NTKL_HUMAN Reviewed; 808 AA.
AC Q96KG9; A6NJF1; Q96G50; Q96KG8; Q96KH1; Q9HAW5; Q9HBL3; Q9NR53;
read moreDT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=N-terminal kinase-like protein;
DE AltName: Full=Coated vesicle-associated kinase of 90 kDa;
DE AltName: Full=SCY1-like protein 1;
DE AltName: Full=Telomerase regulation-associated protein;
DE AltName: Full=Telomerase transcriptional element-interacting factor;
DE AltName: Full=Teratoma-associated tyrosine kinase;
GN Name=SCYL1; Synonyms=CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP;
GN ORFNames=HT019;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12036289; DOI=10.1006/geno.2002.6774;
RA Kato M., Yano K., Morotomi-Yano K., Saito H., Miki Y.;
RT "Identification and characterization of the human protein kinase-like
RT gene NTKL: mitosis-specific centrosomal localization of an
RT alternatively spliced isoform.";
RL Genomics 79:760-767(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), DNA-BINDING (ISOFORM 6), AND
RP SUBCELLULAR LOCATION (ISOFORM 6).
RC TISSUE=Cervix carcinoma;
RX PubMed=15504359; DOI=10.1016/j.bbrc.2004.09.201;
RA Tang Z., Zhao Y., Mei F., Yang S., Li X., Lv J., Hou L., Zhang B.;
RT "Molecular cloning and characterization of a human gene involved in
RT transcriptional regulation of hTERT.";
RL Biochem. Biophys. Res. Commun. 324:1324-1332(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 310-808 (ISOFORM 4).
RC TISSUE=Eye, and Teratocarcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-283.
RX PubMed=10843802; DOI=10.1006/geno.2000.6194;
RA van Asseldonk M., Schepens M., de Bruijn D., Janssen B., Merkx G.,
RA Geurts van Kessel A.;
RT "Construction of a 350-kb sequence-ready 11q13 cosmid contig
RT encompassing the markers D11S4933 and D11S546: mapping of 11 genes and
RT 3 tumor-associated translocation breakpoints.";
RL Genomics 66:35-42(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-808 (ISOFORM 5).
RC TISSUE=Hypothalamus;
RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION (ISOFORM 6), AND DNA-BINDING (ISOFORM 6).
RX PubMed=15963946; DOI=10.1016/j.bbrc.2005.05.172;
RA Zhao Y., Zheng J., Ling Y., Hou L., Zhang B.;
RT "Transcriptional upregulation of DNA polymerase beta by TEIF.";
RL Biochem. Biophys. Res. Commun. 333:908-916(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18556652; DOI=10.1074/jbc.M801869200;
RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
RA Presley J.F., McPherson P.S.;
RT "Scyl1, mutated in a recessive form of spinocerebellar
RT neurodegeneration, regulates COPI-mediated retrograde traffic.";
RL J. Biol. Chem. 283:22774-22786(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-479; TYR-495; HIS-663 AND SER-755.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Regulates COPI-mediated retrograde traffic. Has no
CC detectable kinase activity in vitro.
CC -!- FUNCTION: Isoform 6 acts as transcriptional activator. It binds to
CC three different types of GC-rich DNA binding sites (box-A, -B and
CC -C) in the beta-polymerase promoter region. It also binds to the
CC TERT promoter region.
CC -!- SUBUNIT: Interacts with GORAB. Interacts with COPA, COPB1 and
CC COPB2 (By similarity). Homooligomer. Interacts with AP2B1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Endoplasmic reticulum-Golgi
CC intermediate compartment. Golgi apparatus, cis-Golgi network.
CC Note=Localized to the Endoplasmic reticulum-Golgi intermediate and
CC cis-Golgi in an ARF1-independent manner.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Cytoplasmic
CC throughout the cell cycle.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Cytoplasmic
CC throughout the cell cycle.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC Note=Cytoplasmic during interphase and centrosomal during mitosis,
CC it localizes to the centrosomes in a microtubule-independent
CC manner.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96KG9-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 1;
CC IsoId=Q96KG9-2; Sequence=VSP_020504;
CC Name=3; Synonyms=Variant 2;
CC IsoId=Q96KG9-3; Sequence=VSP_020504, VSP_020506;
CC Note=Non-canonical splice junctions;
CC Name=4;
CC IsoId=Q96KG9-4; Sequence=VSP_020508;
CC Name=5;
CC IsoId=Q96KG9-5; Sequence=VSP_020503, VSP_020505;
CC Name=6;
CC IsoId=Q96KG9-6; Sequence=VSP_020507;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC -!- SIMILARITY: Contains 3 HEAT repeats.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09726.1; Type=Frameshift; Positions=289, 307;
CC Sequence=AAG17902.1; Type=Frameshift; Positions=Several;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB047077; BAB55454.1; -; mRNA.
DR EMBL; AB051427; BAB55458.1; -; mRNA.
DR EMBL; AB051428; BAB55459.1; -; mRNA.
DR EMBL; AF297709; AAG17902.1; ALT_FRAME; mRNA.
DR EMBL; AP000769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74399.1; -; Genomic_DNA.
DR EMBL; BC009967; AAH09967.2; -; mRNA.
DR EMBL; BC069233; AAH69233.1; -; mRNA.
DR EMBL; AF255613; AAF81422.1; -; Genomic_DNA.
DR EMBL; AF225424; AAG09726.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001041683.1; NM_001048218.1.
DR RefSeq; NP_065731.3; NM_020680.3.
DR RefSeq; XP_005274176.1; XM_005274119.1.
DR RefSeq; XP_005274177.1; XM_005274120.1.
DR UniGene; Hs.238839; -.
DR ProteinModelPortal; Q96KG9; -.
DR SMR; Q96KG9; 29-526.
DR IntAct; Q96KG9; 9.
DR MINT; MINT-3055065; -.
DR STRING; 9606.ENSP00000270176; -.
DR PhosphoSite; Q96KG9; -.
DR DMDM; 74762671; -.
DR PaxDb; Q96KG9; -.
DR PRIDE; Q96KG9; -.
DR DNASU; 57410; -.
DR Ensembl; ENST00000270176; ENSP00000270176; ENSG00000142186.
DR Ensembl; ENST00000279270; ENSP00000279270; ENSG00000142186.
DR Ensembl; ENST00000420247; ENSP00000408192; ENSG00000142186.
DR Ensembl; ENST00000527630; ENSP00000433450; ENSG00000142186.
DR Ensembl; ENST00000533862; ENSP00000437254; ENSG00000142186.
DR GeneID; 57410; -.
DR KEGG; hsa:57410; -.
DR UCSC; uc001oea.1; human.
DR CTD; 57410; -.
DR GeneCards; GC11P065292; -.
DR HGNC; HGNC:14372; SCYL1.
DR HPA; HPA015015; -.
DR MIM; 607982; gene.
DR neXtProt; NX_Q96KG9; -.
DR PharmGKB; PA31812; -.
DR eggNOG; NOG293900; -.
DR HOVERGEN; HBG082065; -.
DR InParanoid; Q96KG9; -.
DR KO; K08876; -.
DR OMA; GANPRVR; -.
DR OrthoDB; EOG7RJPQX; -.
DR PhylomeDB; Q96KG9; -.
DR SignaLink; Q96KG9; -.
DR ChiTaRS; SCYL1; human.
DR GeneWiki; SCYL1; -.
DR GenomeRNAi; 57410; -.
DR NextBio; 63536; -.
DR PRO; PR:Q96KG9; -.
DR ArrayExpress; Q96KG9; -.
DR Bgee; Q96KG9; -.
DR CleanEx; HS_SCYL1; -.
DR Genevestigator; Q96KG9; -.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; DNA-binding; ER-Golgi transport;
KW Golgi apparatus; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1 808 N-terminal kinase-like protein.
FT /FTId=PRO_0000249541.
FT DOMAIN 14 314 Protein kinase.
FT REPEAT 350 388 HEAT 1.
FT REPEAT 389 427 HEAT 2.
FT REPEAT 507 545 HEAT 3.
FT REGION 793 808 Interaction with COPB1 (By similarity).
FT COILED 761 797 Potential.
FT COMPBIAS 589 619 Pro-rich.
FT MOD_RES 754 754 Phosphoserine.
FT VAR_SEQ 603 626 TPEGVPAPAPTPVPATPTTSGHWE -> SRPARRPLGDAGG
FT GQGHSRGQQHC (in isoform 5).
FT /FTId=VSP_020503.
FT VAR_SEQ 606 622 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_020504.
FT VAR_SEQ 627 808 Missing (in isoform 5).
FT /FTId=VSP_020505.
FT VAR_SEQ 628 711 Missing (in isoform 3).
FT /FTId=VSP_020506.
FT VAR_SEQ 678 808 VSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDG
FT TRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDN
FT WEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPM
FT KLGARKLD -> SPTGAAGKLRAPGNRAGRSQAPRSHLLTV
FT HGWPASITGVAQSPATRATPSLPCLHVPAPSRGQTLGVRTT
FT GRASRLTVDRSRLSWPGRSARSGGGRWRPNAPRGRWPRAP
FT (in isoform 6).
FT /FTId=VSP_020507.
FT VAR_SEQ 750 808 PRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKR
FT AERKVAKGPMKLGARKLD -> DRSRLSWPGRSARSGGGRW
FT RPNAPRGRWPRAP (in isoform 4).
FT /FTId=VSP_020508.
FT VARIANT 479 479 P -> L (in dbSNP:rs55977709).
FT /FTId=VAR_041364.
FT VARIANT 495 495 H -> Y (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041365.
FT VARIANT 663 663 Q -> H (in dbSNP:rs56076708).
FT /FTId=VAR_041366.
FT VARIANT 755 755 W -> S (in dbSNP:rs56077405).
FT /FTId=VAR_041367.
FT CONFLICT 168 169 GN -> AT (in Ref. 2; AAG17902).
FT CONFLICT 530 530 I -> F (in Ref. 7; AAG09726).
FT CONFLICT 574 574 V -> W (in Ref. 7; AAG09726).
SQ SEQUENCE 808 AA; 89631 MW; E87A2957DDCCE937 CRC64;
MWFFARDPVR DFPFELIPEP PEGGLPGPWA LHRGRKKATG SPVSIFVYDV KPGAEEQTQV
AKAAFKRFKT LRHPNILAYI DGLETEKCLH VVTEAVTPLG IYLKARVEAG GLKELEISWG
LHQIVKALSF LVNDCSLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPRKGIPE
LEQYDPPELA DSSGRVVREK WSADMWRLGC LIWEVFNGPL PRAAALRNPG KIPKTLVPHY
CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
LDAFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKF LSAEEYQQKI IPVVVKMFSS
TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVVHGFLDT NPAIREQTVK SMLLLAPKLN
EANLNVELMK HFARLQAKDE QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATRDPF
APSRVAGVLG FAATHNLYSM NDCAQKILPV LCGLTVDPEK SVRDQAFKAI RSFLSKLESV
SEDPTQLEEV EKDVHAASSP GMGGAAASWA GWAVTGVSSL TSKLIRSHPT TAPTETNIPQ
RPTPEGVPAP APTPVPATPT TSGHWETQEE DKDTAEDSST ADRWDDEDWG SLEQEAESVL
AQQDDWSTGG QVSRASQVSN SDHKSSKSPE SDWSSWEAEG SWEQGWQEPS SQEPPPDGTR
LASEYNWGGP ESSDKGDPFA TLSARPSTQP RPDSWGEDNW EGLETDSRQV KAELARKKRE
ERRREMEAKR AERKVAKGPM KLGARKLD
//
ID NTKL_HUMAN Reviewed; 808 AA.
AC Q96KG9; A6NJF1; Q96G50; Q96KG8; Q96KH1; Q9HAW5; Q9HBL3; Q9NR53;
read moreDT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=N-terminal kinase-like protein;
DE AltName: Full=Coated vesicle-associated kinase of 90 kDa;
DE AltName: Full=SCY1-like protein 1;
DE AltName: Full=Telomerase regulation-associated protein;
DE AltName: Full=Telomerase transcriptional element-interacting factor;
DE AltName: Full=Teratoma-associated tyrosine kinase;
GN Name=SCYL1; Synonyms=CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP;
GN ORFNames=HT019;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12036289; DOI=10.1006/geno.2002.6774;
RA Kato M., Yano K., Morotomi-Yano K., Saito H., Miki Y.;
RT "Identification and characterization of the human protein kinase-like
RT gene NTKL: mitosis-specific centrosomal localization of an
RT alternatively spliced isoform.";
RL Genomics 79:760-767(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), DNA-BINDING (ISOFORM 6), AND
RP SUBCELLULAR LOCATION (ISOFORM 6).
RC TISSUE=Cervix carcinoma;
RX PubMed=15504359; DOI=10.1016/j.bbrc.2004.09.201;
RA Tang Z., Zhao Y., Mei F., Yang S., Li X., Lv J., Hou L., Zhang B.;
RT "Molecular cloning and characterization of a human gene involved in
RT transcriptional regulation of hTERT.";
RL Biochem. Biophys. Res. Commun. 324:1324-1332(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 310-808 (ISOFORM 4).
RC TISSUE=Eye, and Teratocarcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-283.
RX PubMed=10843802; DOI=10.1006/geno.2000.6194;
RA van Asseldonk M., Schepens M., de Bruijn D., Janssen B., Merkx G.,
RA Geurts van Kessel A.;
RT "Construction of a 350-kb sequence-ready 11q13 cosmid contig
RT encompassing the markers D11S4933 and D11S546: mapping of 11 genes and
RT 3 tumor-associated translocation breakpoints.";
RL Genomics 66:35-42(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-808 (ISOFORM 5).
RC TISSUE=Hypothalamus;
RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION (ISOFORM 6), AND DNA-BINDING (ISOFORM 6).
RX PubMed=15963946; DOI=10.1016/j.bbrc.2005.05.172;
RA Zhao Y., Zheng J., Ling Y., Hou L., Zhang B.;
RT "Transcriptional upregulation of DNA polymerase beta by TEIF.";
RL Biochem. Biophys. Res. Commun. 333:908-916(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18556652; DOI=10.1074/jbc.M801869200;
RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
RA Presley J.F., McPherson P.S.;
RT "Scyl1, mutated in a recessive form of spinocerebellar
RT neurodegeneration, regulates COPI-mediated retrograde traffic.";
RL J. Biol. Chem. 283:22774-22786(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-479; TYR-495; HIS-663 AND SER-755.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Regulates COPI-mediated retrograde traffic. Has no
CC detectable kinase activity in vitro.
CC -!- FUNCTION: Isoform 6 acts as transcriptional activator. It binds to
CC three different types of GC-rich DNA binding sites (box-A, -B and
CC -C) in the beta-polymerase promoter region. It also binds to the
CC TERT promoter region.
CC -!- SUBUNIT: Interacts with GORAB. Interacts with COPA, COPB1 and
CC COPB2 (By similarity). Homooligomer. Interacts with AP2B1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Endoplasmic reticulum-Golgi
CC intermediate compartment. Golgi apparatus, cis-Golgi network.
CC Note=Localized to the Endoplasmic reticulum-Golgi intermediate and
CC cis-Golgi in an ARF1-independent manner.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Cytoplasmic
CC throughout the cell cycle.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Cytoplasmic
CC throughout the cell cycle.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC Note=Cytoplasmic during interphase and centrosomal during mitosis,
CC it localizes to the centrosomes in a microtubule-independent
CC manner.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96KG9-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 1;
CC IsoId=Q96KG9-2; Sequence=VSP_020504;
CC Name=3; Synonyms=Variant 2;
CC IsoId=Q96KG9-3; Sequence=VSP_020504, VSP_020506;
CC Note=Non-canonical splice junctions;
CC Name=4;
CC IsoId=Q96KG9-4; Sequence=VSP_020508;
CC Name=5;
CC IsoId=Q96KG9-5; Sequence=VSP_020503, VSP_020505;
CC Name=6;
CC IsoId=Q96KG9-6; Sequence=VSP_020507;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC -!- SIMILARITY: Contains 3 HEAT repeats.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09726.1; Type=Frameshift; Positions=289, 307;
CC Sequence=AAG17902.1; Type=Frameshift; Positions=Several;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB047077; BAB55454.1; -; mRNA.
DR EMBL; AB051427; BAB55458.1; -; mRNA.
DR EMBL; AB051428; BAB55459.1; -; mRNA.
DR EMBL; AF297709; AAG17902.1; ALT_FRAME; mRNA.
DR EMBL; AP000769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74399.1; -; Genomic_DNA.
DR EMBL; BC009967; AAH09967.2; -; mRNA.
DR EMBL; BC069233; AAH69233.1; -; mRNA.
DR EMBL; AF255613; AAF81422.1; -; Genomic_DNA.
DR EMBL; AF225424; AAG09726.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001041683.1; NM_001048218.1.
DR RefSeq; NP_065731.3; NM_020680.3.
DR RefSeq; XP_005274176.1; XM_005274119.1.
DR RefSeq; XP_005274177.1; XM_005274120.1.
DR UniGene; Hs.238839; -.
DR ProteinModelPortal; Q96KG9; -.
DR SMR; Q96KG9; 29-526.
DR IntAct; Q96KG9; 9.
DR MINT; MINT-3055065; -.
DR STRING; 9606.ENSP00000270176; -.
DR PhosphoSite; Q96KG9; -.
DR DMDM; 74762671; -.
DR PaxDb; Q96KG9; -.
DR PRIDE; Q96KG9; -.
DR DNASU; 57410; -.
DR Ensembl; ENST00000270176; ENSP00000270176; ENSG00000142186.
DR Ensembl; ENST00000279270; ENSP00000279270; ENSG00000142186.
DR Ensembl; ENST00000420247; ENSP00000408192; ENSG00000142186.
DR Ensembl; ENST00000527630; ENSP00000433450; ENSG00000142186.
DR Ensembl; ENST00000533862; ENSP00000437254; ENSG00000142186.
DR GeneID; 57410; -.
DR KEGG; hsa:57410; -.
DR UCSC; uc001oea.1; human.
DR CTD; 57410; -.
DR GeneCards; GC11P065292; -.
DR HGNC; HGNC:14372; SCYL1.
DR HPA; HPA015015; -.
DR MIM; 607982; gene.
DR neXtProt; NX_Q96KG9; -.
DR PharmGKB; PA31812; -.
DR eggNOG; NOG293900; -.
DR HOVERGEN; HBG082065; -.
DR InParanoid; Q96KG9; -.
DR KO; K08876; -.
DR OMA; GANPRVR; -.
DR OrthoDB; EOG7RJPQX; -.
DR PhylomeDB; Q96KG9; -.
DR SignaLink; Q96KG9; -.
DR ChiTaRS; SCYL1; human.
DR GeneWiki; SCYL1; -.
DR GenomeRNAi; 57410; -.
DR NextBio; 63536; -.
DR PRO; PR:Q96KG9; -.
DR ArrayExpress; Q96KG9; -.
DR Bgee; Q96KG9; -.
DR CleanEx; HS_SCYL1; -.
DR Genevestigator; Q96KG9; -.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; DNA-binding; ER-Golgi transport;
KW Golgi apparatus; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1 808 N-terminal kinase-like protein.
FT /FTId=PRO_0000249541.
FT DOMAIN 14 314 Protein kinase.
FT REPEAT 350 388 HEAT 1.
FT REPEAT 389 427 HEAT 2.
FT REPEAT 507 545 HEAT 3.
FT REGION 793 808 Interaction with COPB1 (By similarity).
FT COILED 761 797 Potential.
FT COMPBIAS 589 619 Pro-rich.
FT MOD_RES 754 754 Phosphoserine.
FT VAR_SEQ 603 626 TPEGVPAPAPTPVPATPTTSGHWE -> SRPARRPLGDAGG
FT GQGHSRGQQHC (in isoform 5).
FT /FTId=VSP_020503.
FT VAR_SEQ 606 622 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_020504.
FT VAR_SEQ 627 808 Missing (in isoform 5).
FT /FTId=VSP_020505.
FT VAR_SEQ 628 711 Missing (in isoform 3).
FT /FTId=VSP_020506.
FT VAR_SEQ 678 808 VSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDG
FT TRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDN
FT WEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPM
FT KLGARKLD -> SPTGAAGKLRAPGNRAGRSQAPRSHLLTV
FT HGWPASITGVAQSPATRATPSLPCLHVPAPSRGQTLGVRTT
FT GRASRLTVDRSRLSWPGRSARSGGGRWRPNAPRGRWPRAP
FT (in isoform 6).
FT /FTId=VSP_020507.
FT VAR_SEQ 750 808 PRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKR
FT AERKVAKGPMKLGARKLD -> DRSRLSWPGRSARSGGGRW
FT RPNAPRGRWPRAP (in isoform 4).
FT /FTId=VSP_020508.
FT VARIANT 479 479 P -> L (in dbSNP:rs55977709).
FT /FTId=VAR_041364.
FT VARIANT 495 495 H -> Y (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041365.
FT VARIANT 663 663 Q -> H (in dbSNP:rs56076708).
FT /FTId=VAR_041366.
FT VARIANT 755 755 W -> S (in dbSNP:rs56077405).
FT /FTId=VAR_041367.
FT CONFLICT 168 169 GN -> AT (in Ref. 2; AAG17902).
FT CONFLICT 530 530 I -> F (in Ref. 7; AAG09726).
FT CONFLICT 574 574 V -> W (in Ref. 7; AAG09726).
SQ SEQUENCE 808 AA; 89631 MW; E87A2957DDCCE937 CRC64;
MWFFARDPVR DFPFELIPEP PEGGLPGPWA LHRGRKKATG SPVSIFVYDV KPGAEEQTQV
AKAAFKRFKT LRHPNILAYI DGLETEKCLH VVTEAVTPLG IYLKARVEAG GLKELEISWG
LHQIVKALSF LVNDCSLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPRKGIPE
LEQYDPPELA DSSGRVVREK WSADMWRLGC LIWEVFNGPL PRAAALRNPG KIPKTLVPHY
CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
LDAFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKF LSAEEYQQKI IPVVVKMFSS
TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVVHGFLDT NPAIREQTVK SMLLLAPKLN
EANLNVELMK HFARLQAKDE QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATRDPF
APSRVAGVLG FAATHNLYSM NDCAQKILPV LCGLTVDPEK SVRDQAFKAI RSFLSKLESV
SEDPTQLEEV EKDVHAASSP GMGGAAASWA GWAVTGVSSL TSKLIRSHPT TAPTETNIPQ
RPTPEGVPAP APTPVPATPT TSGHWETQEE DKDTAEDSST ADRWDDEDWG SLEQEAESVL
AQQDDWSTGG QVSRASQVSN SDHKSSKSPE SDWSSWEAEG SWEQGWQEPS SQEPPPDGTR
LASEYNWGGP ESSDKGDPFA TLSARPSTQP RPDSWGEDNW EGLETDSRQV KAELARKKRE
ERRREMEAKR AERKVAKGPM KLGARKLD
//
MIM
607982
*RECORD*
*FIELD* NO
607982
*FIELD* TI
*607982 SCY1-LIKE 1; SCYL1
;;N-TERMINAL KINASE-LIKE; NTKL
*FIELD* TX
CLONING
Liu et al. (2000) cloned mouse Scyl1, which they called p105, from an
read moreadipocyte cell line cDNA library. The deduced 806-amino acid protein has
a calculated molecular mass of about 89 kD. Scyl1 shares significant
sequence similarity with kinases, but its putative kinase domain lacks
subdomain 1 of the 12 characteristic subdomains, and it is missing
highly conserved residues in other subdomains, suggesting that Scyl1 is
not a functional kinase. Western blot analysis of mouse tissues found
that Scyl1 has an apparent molecular mass of about 105 kD and is present
in all tissues examined. Western blot analysis of subcellular fractions
indicated that mouse Scyl1 is primarily cytosolic and that it is present
in low density microsomes.
By large-scale sequencing of a mammary gland cDNA library, followed by
nested PCR and 5-prime RACE, Kato et al. (2002) cloned SCYL1, which they
called NTKL. The deduced 808-amino acid protein has a calculated
molecular mass of 89.6 kD. Kato et al. (2002) also cloned 2 splice
variants that harbor internal deletions and encode proteins of 791 and
707 amino acids, which they termed variant 1 and variant 2,
respectively. NTKL has an N-terminal kinase-like domain and a C-terminal
cluster of basic amino acids. NTKL shares 90% amino acid identity with
mouse Ntkl, and like mouse Ntkl, it does not contain kinase subdomain 1.
NTKL also shares sequence similarity with the S. cerevisiae Scy1
protein. Northern blot analysis detected a 2.8-kb transcript in all
tissues tested.
GENE FUNCTION
Using NTKL carrying 2 different epitope tags, Kato et al. (2002) found
that NTKL forms multimers following transfection into COS-7 cells. They
determined that NTKL forms a 300-kD trimer using crosslinking reagents.
Biochemical analysis revealed no phosphorylation or autophosphorylation
activity. Kato et al. (2002) found that the 707-amino acid NTKL variant,
variant 2, localized to centrosomes during mitosis. During interphase,
fluorescence-tagged variant 2 localized in the cytoplasm as well as
centrosomes. However, at the beginning of mitosis, the fluorescence
appeared as a pair of bright nuclear foci that followed centrosome
localization throughout mitosis, while maintaining diffuse cytoplasmic
labeling. Endogenous variant 2 in HeLa cells showed a similar staining
pattern. Centrosomal localization was independent of microtubules.
Di et al. (2003) identified an Ntkl-binding protein (GORAB; 607983) in
mouse that colocalized with Ntkl in cytoplasm and showed ubiquitous
expression.
GENE STRUCTURE
Kato et al. (2002) determined that the SCYL1 gene contains 18 exons and
spans about 15 kb. Alternative splicing produces variant 1, which lacks
half of exon 14, and variant 2, which lacks most of exon 14, all of exon
15, and half of exon 16.
MAPPING
By genomic sequence analysis, Liu et al. (2000) and Kato et al. (2002)
mapped the SCYL1 gene to chromosome 11q13.
*FIELD* RF
1. Di, Y.; Li, J.; Fang, J.; Xu, Z.; He, X.; Zhang, F.; Ling, J.;
Li, X.; Xu, D.; Li, L.; Li, Y.-Y.; Huo, K.: Cloning and characterization
of a novel gene which encodes a protein interacting with the mitosis-associated
kinase-like protein NTKL. J. Hum. Genet. 48: 315-321, 2003.
2. Kato, M.; Yano, K.; Morotomi-Yano, K.; Saito, H.; Miki, Y.: Identification
and characterization of the human protein kinase-like gene NTKL: mitosis-specific
centrosomal localization of an alternatively spliced isoform. Genomics 79:
760-767, 2002.
3. Liu, S. C. H.; Lane, W. S.; Lienhard, G. E.: Cloning and preliminary
characterization of a 105 kDa protein with an N-terminal kinase-like
domain. Biochim. Biophys. Acta 1517: 148-152, 2000.
*FIELD* CD
Patricia A. Hartz: 7/25/2003
*FIELD* ED
wwang: 04/04/2011
wwang: 4/17/2009
terry: 7/20/2004
mgross: 7/25/2003
*RECORD*
*FIELD* NO
607982
*FIELD* TI
*607982 SCY1-LIKE 1; SCYL1
;;N-TERMINAL KINASE-LIKE; NTKL
*FIELD* TX
CLONING
Liu et al. (2000) cloned mouse Scyl1, which they called p105, from an
read moreadipocyte cell line cDNA library. The deduced 806-amino acid protein has
a calculated molecular mass of about 89 kD. Scyl1 shares significant
sequence similarity with kinases, but its putative kinase domain lacks
subdomain 1 of the 12 characteristic subdomains, and it is missing
highly conserved residues in other subdomains, suggesting that Scyl1 is
not a functional kinase. Western blot analysis of mouse tissues found
that Scyl1 has an apparent molecular mass of about 105 kD and is present
in all tissues examined. Western blot analysis of subcellular fractions
indicated that mouse Scyl1 is primarily cytosolic and that it is present
in low density microsomes.
By large-scale sequencing of a mammary gland cDNA library, followed by
nested PCR and 5-prime RACE, Kato et al. (2002) cloned SCYL1, which they
called NTKL. The deduced 808-amino acid protein has a calculated
molecular mass of 89.6 kD. Kato et al. (2002) also cloned 2 splice
variants that harbor internal deletions and encode proteins of 791 and
707 amino acids, which they termed variant 1 and variant 2,
respectively. NTKL has an N-terminal kinase-like domain and a C-terminal
cluster of basic amino acids. NTKL shares 90% amino acid identity with
mouse Ntkl, and like mouse Ntkl, it does not contain kinase subdomain 1.
NTKL also shares sequence similarity with the S. cerevisiae Scy1
protein. Northern blot analysis detected a 2.8-kb transcript in all
tissues tested.
GENE FUNCTION
Using NTKL carrying 2 different epitope tags, Kato et al. (2002) found
that NTKL forms multimers following transfection into COS-7 cells. They
determined that NTKL forms a 300-kD trimer using crosslinking reagents.
Biochemical analysis revealed no phosphorylation or autophosphorylation
activity. Kato et al. (2002) found that the 707-amino acid NTKL variant,
variant 2, localized to centrosomes during mitosis. During interphase,
fluorescence-tagged variant 2 localized in the cytoplasm as well as
centrosomes. However, at the beginning of mitosis, the fluorescence
appeared as a pair of bright nuclear foci that followed centrosome
localization throughout mitosis, while maintaining diffuse cytoplasmic
labeling. Endogenous variant 2 in HeLa cells showed a similar staining
pattern. Centrosomal localization was independent of microtubules.
Di et al. (2003) identified an Ntkl-binding protein (GORAB; 607983) in
mouse that colocalized with Ntkl in cytoplasm and showed ubiquitous
expression.
GENE STRUCTURE
Kato et al. (2002) determined that the SCYL1 gene contains 18 exons and
spans about 15 kb. Alternative splicing produces variant 1, which lacks
half of exon 14, and variant 2, which lacks most of exon 14, all of exon
15, and half of exon 16.
MAPPING
By genomic sequence analysis, Liu et al. (2000) and Kato et al. (2002)
mapped the SCYL1 gene to chromosome 11q13.
*FIELD* RF
1. Di, Y.; Li, J.; Fang, J.; Xu, Z.; He, X.; Zhang, F.; Ling, J.;
Li, X.; Xu, D.; Li, L.; Li, Y.-Y.; Huo, K.: Cloning and characterization
of a novel gene which encodes a protein interacting with the mitosis-associated
kinase-like protein NTKL. J. Hum. Genet. 48: 315-321, 2003.
2. Kato, M.; Yano, K.; Morotomi-Yano, K.; Saito, H.; Miki, Y.: Identification
and characterization of the human protein kinase-like gene NTKL: mitosis-specific
centrosomal localization of an alternatively spliced isoform. Genomics 79:
760-767, 2002.
3. Liu, S. C. H.; Lane, W. S.; Lienhard, G. E.: Cloning and preliminary
characterization of a 105 kDa protein with an N-terminal kinase-like
domain. Biochim. Biophys. Acta 1517: 148-152, 2000.
*FIELD* CD
Patricia A. Hartz: 7/25/2003
*FIELD* ED
wwang: 04/04/2011
wwang: 4/17/2009
terry: 7/20/2004
mgross: 7/25/2003