SCYL1_HUMAN
ID SCYL1_HUMAN Reviewed; 808 AA.
AC Q96KG9; A6NJF1; Q96G50; Q96KG8; Q96KH1; Q9HAW5; Q9HBL3; Q9NR53;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
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; ORFNames=HT019;
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;
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 gene
RT NTKL: mitosis-specific centrosomal localization of an alternatively spliced
RT 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., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 SEQUENCE
RP [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 project:
RT 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 encompassing
RT the markers D11S4933 and D11S546: mapping of 11 genes and 3 tumor-
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 clathrin-
RT 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 neurodegeneration,
RT regulates COPI-mediated retrograde traffic.";
RL J. Biol. Chem. 283:22774-22786(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INVOLVEMENT IN SCAR21, AND FUNCTION.
RX PubMed=26581903; DOI=10.1016/j.ajhg.2015.10.011;
RA Schmidt W.M., Rutledge S.L., Schuele R., Mayerhofer B., Zuechner S.,
RA Boltshauser E., Bittner R.E.;
RT "Disruptive SCYL1 mutations underlie a syndrome characterized by recurrent
RT episodes of liver failure, peripheral neuropathy, cerebellar atrophy, and
RT ataxia.";
RL Am. J. Hum. Genet. 97:855-861(2015).
RN [16]
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., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA 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 protein traffic at the
CC interface between the Golgi apparatus and the endoplasmic reticulum
CC (PubMed:18556652). Involved in the maintenance of the Golgi apparatus
CC morphology (PubMed:26581903). Has no detectable kinase activity in
CC vitro (PubMed:18556652). {ECO:0000269|PubMed:18556652,
CC ECO:0000269|PubMed:26581903}.
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 -C)
CC in the beta-polymerase promoter region. It also binds to the TERT
CC promoter region. {ECO:0000269|PubMed:18556652}.
CC -!- SUBUNIT: Interacts with GORAB. Interacts with COPA, COPB1 and COPB2 (By
CC similarity). Homooligomer. Interacts with AP2B1. {ECO:0000250,
CC ECO:0000269|PubMed:12036289, ECO:0000269|PubMed:16903783}.
CC -!- INTERACTION:
CC Q96KG9; P63010: AP2B1; NbExp=2; IntAct=EBI-949287, EBI-432924;
CC Q96KG9-4; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-12023020, EBI-16429430;
CC Q96KG9-4; O15169: AXIN1; NbExp=3; IntAct=EBI-12023020, EBI-710484;
CC Q96KG9-4; P26196: DDX6; NbExp=5; IntAct=EBI-12023020, EBI-351257;
CC Q96KG9-4; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-12023020, EBI-726510;
CC Q96KG9-4; Q13526: PIN1; NbExp=3; IntAct=EBI-12023020, EBI-714158;
CC Q96KG9-4; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12023020, EBI-742388;
CC Q96KG9-4; Q15560: TCEA2; NbExp=3; IntAct=EBI-12023020, EBI-710310;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:18556652}. Endoplasmic
CC reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:18556652}.
CC Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18556652}.
CC Note=Localized to the Endoplasmic reticulum-Golgi intermediate and cis-
CC 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, cytoskeleton,
CC microtubule organizing center, centrosome. Note=Cytoplasmic during
CC interphase and centrosomal during mitosis, it localizes to the
CC centrosomes in a microtubule-independent manner.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus
CC {ECO:0000269|PubMed:15504359}.
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 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. {ECO:0000269|PubMed:12036289}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 21 (SCAR21)
CC [MIM:616719]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAR21 is characterized by cerebellar
CC atrophy and ataxia with onset in early childhood. Patients also
CC manifest recurrent episodes of liver failure, hepatic fibrosis and a
CC peripheral neuropathy. {ECO:0000269|PubMed:26581903}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Non-canonical splice junctions.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09726.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG17902.1; Type=Frameshift; Evidence={ECO:0000305};
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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 CCDS; CCDS41672.1; -. [Q96KG9-1]
DR CCDS; CCDS44646.1; -. [Q96KG9-2]
DR RefSeq; NP_001041683.1; NM_001048218.1. [Q96KG9-2]
DR RefSeq; NP_065731.3; NM_020680.3. [Q96KG9-1]
DR RefSeq; XP_005274177.1; XM_005274120.3. [Q96KG9-4]
DR AlphaFoldDB; Q96KG9; -.
DR SMR; Q96KG9; -.
DR BioGRID; 121512; 113.
DR CORUM; Q96KG9; -.
DR IntAct; Q96KG9; 75.
DR MINT; Q96KG9; -.
DR STRING; 9606.ENSP00000270176; -.
DR DrugBank; DB05036; Grn163l.
DR GlyGen; Q96KG9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96KG9; -.
DR PhosphoSitePlus; Q96KG9; -.
DR BioMuta; SCYL1; -.
DR DMDM; 74762671; -.
DR EPD; Q96KG9; -.
DR jPOST; Q96KG9; -.
DR MassIVE; Q96KG9; -.
DR MaxQB; Q96KG9; -.
DR PaxDb; Q96KG9; -.
DR PeptideAtlas; Q96KG9; -.
DR PRIDE; Q96KG9; -.
DR ProteomicsDB; 77069; -. [Q96KG9-1]
DR ProteomicsDB; 77070; -. [Q96KG9-2]
DR ProteomicsDB; 77071; -. [Q96KG9-3]
DR ProteomicsDB; 77072; -. [Q96KG9-4]
DR ProteomicsDB; 77073; -. [Q96KG9-5]
DR ProteomicsDB; 77074; -. [Q96KG9-6]
DR Antibodypedia; 7388; 166 antibodies from 25 providers.
DR DNASU; 57410; -.
DR Ensembl; ENST00000270176.10; ENSP00000270176.5; ENSG00000142186.18. [Q96KG9-1]
DR Ensembl; ENST00000420247.6; ENSP00000408192.2; ENSG00000142186.18. [Q96KG9-2]
DR Ensembl; ENST00000533862.5; ENSP00000437254.1; ENSG00000142186.18. [Q96KG9-6]
DR GeneID; 57410; -.
DR KEGG; hsa:57410; -.
DR MANE-Select; ENST00000270176.10; ENSP00000270176.5; NM_020680.4; NP_065731.3.
DR UCSC; uc001oea.2; human. [Q96KG9-1]
DR CTD; 57410; -.
DR DisGeNET; 57410; -.
DR GeneCards; SCYL1; -.
DR HGNC; HGNC:14372; SCYL1.
DR HPA; ENSG00000142186; Low tissue specificity.
DR MalaCards; SCYL1; -.
DR MIM; 607982; gene.
DR MIM; 616719; phenotype.
DR neXtProt; NX_Q96KG9; -.
DR OpenTargets; ENSG00000142186; -.
DR Orphanet; 466794; Acute infantile liver failure-cerebellar ataxia-peripheral sensory motor neuropathy syndrome.
DR PharmGKB; PA31812; -.
DR VEuPathDB; HostDB:ENSG00000142186; -.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151054; -.
DR HOGENOM; CLU_010392_0_1_1; -.
DR InParanoid; Q96KG9; -.
DR OMA; LIRDQAN; -.
DR OrthoDB; 1074965at2759; -.
DR PhylomeDB; Q96KG9; -.
DR TreeFam; TF313435; -.
DR PathwayCommons; Q96KG9; -.
DR SignaLink; Q96KG9; -.
DR SIGNOR; Q96KG9; -.
DR BioGRID-ORCS; 57410; 165 hits in 1121 CRISPR screens.
DR ChiTaRS; SCYL1; human.
DR GeneWiki; SCYL1; -.
DR GenomeRNAi; 57410; -.
DR Pharos; Q96KG9; Tbio.
DR PRO; PR:Q96KG9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96KG9; protein.
DR Bgee; ENSG00000142186; Expressed in apex of heart and 173 other tissues.
DR ExpressionAtlas; Q96KG9; baseline and differential.
DR Genevisible; Q96KG9; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA: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:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW DNA-binding; ER-Golgi transport; Golgi apparatus; Intellectual disability;
KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Spinocerebellar ataxia; Transcription; Transcription regulation; Transport.
FT CHAIN 1..808
FT /note="N-terminal kinase-like protein"
FT /id="PRO_0000249541"
FT DOMAIN 14..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 350..388
FT /note="HEAT 1"
FT REPEAT 389..427
FT /note="HEAT 2"
FT REPEAT 507..545
FT /note="HEAT 3"
FT REGION 540..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..808
FT /note="Interaction with COPB1"
FT /evidence="ECO:0000250"
FT COILED 761..797
FT /evidence="ECO:0000255"
FT COMPBIAS 587..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 603..626
FT /note="TPEGVPAPAPTPVPATPTTSGHWE -> SRPARRPLGDAGGGQGHSRGQQHC
FT (in isoform 5)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020503"
FT VAR_SEQ 606..622
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12036289"
FT /id="VSP_020504"
FT VAR_SEQ 627..808
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020505"
FT VAR_SEQ 628..711
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12036289"
FT /id="VSP_020506"
FT VAR_SEQ 678..808
FT /note="VSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDGTRLASEYNWGG
FT PESSDKGDPFATLSARPSTQPRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEA
FT KRAERKVAKGPMKLGARKLD -> SPTGAAGKLRAPGNRAGRSQAPRSHLLTVHGWPAS
FT ITGVAQSPATRATPSLPCLHVPAPSRGQTLGVRTTGRASRLTVDRSRLSWPGRSARSGG
FT GRWRPNAPRGRWPRAP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15504359"
FT /id="VSP_020507"
FT VAR_SEQ 750..808
FT /note="PRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPMK
FT LGARKLD -> DRSRLSWPGRSARSGGGRWRPNAPRGRWPRAP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020508"
FT VARIANT 479
FT /note="P -> L (in dbSNP:rs55977709)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041364"
FT VARIANT 495
FT /note="H -> Y (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041365"
FT VARIANT 663
FT /note="Q -> H (in dbSNP:rs56076708)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041366"
FT VARIANT 755
FT /note="W -> S (in dbSNP:rs56077405)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041367"
FT CONFLICT 168..169
FT /note="GN -> AT (in Ref. 2; AAG17902)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="I -> F (in Ref. 7; AAG09726)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="V -> W (in Ref. 7; AAG09726)"
FT /evidence="ECO:0000305"
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
