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Database: UniProt
Entry: Q9BZJ0
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Original site: Q9BZJ0 
ID   CRNL1_HUMAN             Reviewed;         848 AA.
AC   Q9BZJ0; A8K9T4; Q5JY64; Q8WYI5; Q9BZI9; Q9BZJ1; Q9BZJ2; Q9GZW7; Q9H8F8;
AC   Q9NQH5; Q9NYD8;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 4.
DT   29-SEP-2021, entry version 176.
DE   RecName: Full=Crooked neck-like protein 1;
DE   AltName: Full=Crooked neck homolog;
DE            Short=hCrn;
GN   Name=CRNKL1; Synonyms=CRN; ORFNames=CGI-201, MSTP021;
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; 3; 4 AND 5), TISSUE SPECIFICITY,
RP   AND VARIANT ARG-35.
RX   PubMed=11342225; DOI=10.1016/s0167-4781(00)00295-5;
RA   Lai C.-H., Chiu J.-Y., Lin W.-C.;
RT   "Identification of the human crooked neck gene by comparative gene
RT   identification.";
RL   Biochim. Biophys. Acta 1517:449-454(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND IDENTIFICATION IN SPLICEOSOMAL COMPLEX WITH HPRP8BP
RP   AND SNRPB2.
RC   TISSUE=T lymphoblast;
RX   PubMed=12084575; DOI=10.1016/s0167-4781(02)00368-8;
RA   Chung S., Zhou Z., Huddleston K.A., Harrison D.A., Reed R., Coleman T.A.,
RA   Rymond B.C.;
RT   "Crooked neck is a component of the human spliceosome and implicated in the
RT   splicing process.";
RL   Biochim. Biophys. Acta 1576:287-297(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   TISSUE=Heart;
RA   Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L.,
RA   Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H.,
RA   Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q.,
RA   Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP   COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12801913; DOI=10.1093/jb/mvg079;
RA   Amada N., Tezuka T., Mayeda A., Araki K., Takei N., Todokoro K., Nawa H.;
RT   "A novel rat orthologue and homologue for the Drosophila crooked neck gene
RT   in neural stem cells and their immediate descendants.";
RL   J. Biochem. 133:615-623(2003).
RN   [8]
RP   INTERACTION WITH PPIL2 AND HSP90.
RX   PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
RA   Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
RT   "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular
RT   chaperones.";
RL   Genes Cells 9:533-548(2004).
RN   [9]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [10]
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [14] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
CC   -!- FUNCTION: Involved in pre-mRNA splicing process.
CC       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12084575,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC       PubMed:28502770, PubMed:28076346). Present in a spliceosome complex
CC       assembled in vitro containing CRNKL1, HPRP8BP and SNRPB2
CC       (PubMed:12084575). Isoform 2 seems to be predominant in the spliceosome
CC       complex (PubMed:12084575). Interacts with PPIL2 (via the PPIase
CC       cyclophilin-type domain); they may form a trimeric complex with HSP90
CC       (PubMed:15189447). {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:12084575, ECO:0000269|PubMed:15189447}.
CC   -!- INTERACTION:
CC       Q9BZJ0; Q8WUD4: CCDC12; NbExp=2; IntAct=EBI-1049701, EBI-2557572;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:12801913, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770}. Nucleus speckle
CC       {ECO:0000269|PubMed:12084575}. Note=Colocalizes with core spliceosomal
CC       snRNP proteins (PubMed:12084575). {ECO:0000269|PubMed:12084575}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Type-II;
CC         IsoId=Q9BZJ0-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q9BZJ0-2; Sequence=VSP_002058;
CC       Name=3;
CC         IsoId=Q9BZJ0-3; Sequence=VSP_002059;
CC       Name=4; Synonyms=Type-III;
CC         IsoId=Q9BZJ0-4; Sequence=VSP_002059, VSP_002062;
CC       Name=5; Synonyms=type-IV;
CC         IsoId=Q9BZJ0-5; Sequence=VSP_002060, VSP_002061;
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11342225). Highly
CC       expressed in testis (PubMed:12084575). Not detected in brain and lung
CC       (PubMed:12084575). {ECO:0000269|PubMed:11342225,
CC       ECO:0000269|PubMed:12084575}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14303.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB14485.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF255443; AAF65571.2; -; mRNA.
DR   EMBL; AF318302; AAK01924.1; -; mRNA.
DR   EMBL; AF318303; AAK01925.1; -; mRNA.
DR   EMBL; AF318304; AAK01926.1; -; mRNA.
DR   EMBL; AF318305; AAK01927.1; -; mRNA.
DR   EMBL; AF111802; AAL39004.1; -; mRNA.
DR   EMBL; AK023246; BAB14485.1; ALT_INIT; mRNA.
DR   EMBL; AK023728; BAB14659.1; -; mRNA.
DR   EMBL; AK292799; BAF85488.1; -; mRNA.
DR   EMBL; AL035454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK022908; BAB14303.1; ALT_INIT; mRNA.
DR   CCDS; CCDS33446.1; -. [Q9BZJ0-1]
DR   CCDS; CCDS63238.1; -. [Q9BZJ0-2]
DR   CCDS; CCDS63239.1; -. [Q9BZJ0-3]
DR   RefSeq; NP_001265554.1; NM_001278625.1.
DR   RefSeq; NP_001265555.1; NM_001278626.1.
DR   RefSeq; NP_001265556.1; NM_001278627.1.
DR   RefSeq; NP_001265557.1; NM_001278628.1. [Q9BZJ0-2]
DR   RefSeq; NP_057736.4; NM_016652.5. [Q9BZJ0-1]
DR   PDB; 5MQF; EM; 5.90 A; O=1-848.
DR   PDB; 5XJC; EM; 3.60 A; J=1-848.
DR   PDB; 5YZG; EM; 4.10 A; J=1-848.
DR   PDB; 5Z56; EM; 5.10 A; J=1-848.
DR   PDB; 5Z57; EM; 6.50 A; J=1-848.
DR   PDB; 5Z58; EM; 4.90 A; J=1-848.
DR   PDB; 6FF4; EM; 16.00 A; O=1-848.
DR   PDB; 6FF7; EM; 4.50 A; O=1-848.
DR   PDB; 6ICZ; EM; 3.00 A; J=1-848.
DR   PDB; 6ID0; EM; 2.90 A; J=1-848.
DR   PDB; 6ID1; EM; 2.86 A; J=1-848.
DR   PDB; 6QDV; EM; 3.30 A; S=1-848.
DR   PDB; 6ZYM; EM; 3.40 A; O=1-848.
DR   PDB; 7A5P; EM; 5.00 A; O=1-848.
DR   PDB; 7ABI; EM; 8.00 A; O=1-848.
DR   PDB; 7DVQ; EM; 2.89 A; J=1-848.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 5Z58; -.
DR   PDBsum; 6FF4; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6ZYM; -.
DR   PDBsum; 7A5P; -.
DR   PDBsum; 7ABI; -.
DR   PDBsum; 7DVQ; -.
DR   SMR; Q9BZJ0; -.
DR   BioGRID; 119487; 93.
DR   CORUM; Q9BZJ0; -.
DR   IntAct; Q9BZJ0; 49.
DR   STRING; 9606.ENSP00000366557; -.
DR   GlyGen; Q9BZJ0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BZJ0; -.
DR   PhosphoSitePlus; Q9BZJ0; -.
DR   BioMuta; CRNKL1; -.
DR   DMDM; 147744555; -.
DR   EPD; Q9BZJ0; -.
DR   jPOST; Q9BZJ0; -.
DR   MassIVE; Q9BZJ0; -.
DR   MaxQB; Q9BZJ0; -.
DR   PaxDb; Q9BZJ0; -.
DR   PeptideAtlas; Q9BZJ0; -.
DR   PRIDE; Q9BZJ0; -.
DR   ProteomicsDB; 79851; -. [Q9BZJ0-1]
DR   ProteomicsDB; 79852; -. [Q9BZJ0-2]
DR   ProteomicsDB; 79853; -. [Q9BZJ0-3]
DR   ProteomicsDB; 79854; -. [Q9BZJ0-4]
DR   ProteomicsDB; 79855; -. [Q9BZJ0-5]
DR   Antibodypedia; 9534; 64 antibodies.
DR   DNASU; 51340; -.
DR   Ensembl; ENST00000377340; ENSP00000366557; ENSG00000101343. [Q9BZJ0-1]
DR   Ensembl; ENST00000496549; ENSP00000428436; ENSG00000101343. [Q9BZJ0-5]
DR   Ensembl; ENST00000536226; ENSP00000440733; ENSG00000101343. [Q9BZJ0-2]
DR   GeneID; 51340; -.
DR   KEGG; hsa:51340; -.
DR   UCSC; uc002wrs.5; human. [Q9BZJ0-1]
DR   CTD; 51340; -.
DR   DisGeNET; 51340; -.
DR   GeneCards; CRNKL1; -.
DR   HGNC; HGNC:15762; CRNKL1.
DR   HPA; ENSG00000101343; Low tissue specificity.
DR   MIM; 610952; gene.
DR   neXtProt; NX_Q9BZJ0; -.
DR   OpenTargets; ENSG00000101343; -.
DR   PharmGKB; PA26886; -.
DR   VEuPathDB; HostDB:ENSG00000101343; -.
DR   eggNOG; KOG1915; Eukaryota.
DR   GeneTree; ENSGT00550000074931; -.
DR   HOGENOM; CLU_2687132_0_0_1; -.
DR   InParanoid; Q9BZJ0; -.
DR   OMA; FTFSKIW; -.
DR   PhylomeDB; Q9BZJ0; -.
DR   TreeFam; TF300305; -.
DR   PathwayCommons; Q9BZJ0; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 51340; 759 hits in 1023 CRISPR screens.
DR   ChiTaRS; CRNKL1; human.
DR   GenomeRNAi; 51340; -.
DR   Pharos; Q9BZJ0; Tbio.
DR   PRO; PR:Q9BZJ0; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9BZJ0; protein.
DR   Bgee; ENSG00000101343; Expressed in calcaneal tendon and 228 other tissues.
DR   ExpressionAtlas; Q9BZJ0; baseline and differential.
DR   Genevisible; Q9BZJ0; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF02184; HAT; 2.
DR   SMART; SM00386; HAT; 13.
DR   SUPFAM; SSF48452; SSF48452; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Spliceosome.
FT   CHAIN           1..848
FT                   /note="Crooked neck-like protein 1"
FT                   /id="PRO_0000205719"
FT   REPEAT          222..254
FT                   /note="HAT 1"
FT   REPEAT          256..288
FT                   /note="HAT 2"
FT   REPEAT          290..322
FT                   /note="HAT 3"
FT   REPEAT          324..355
FT                   /note="HAT 4"
FT   REPEAT          357..388
FT                   /note="HAT 5"
FT   REPEAT          390..425
FT                   /note="HAT 6"
FT   REPEAT          427..461
FT                   /note="HAT 7"
FT   REPEAT          471..503
FT                   /note="HAT 8"
FT   REPEAT          505..539
FT                   /note="HAT 9"
FT   REPEAT          549..585
FT                   /note="HAT 10"
FT   REPEAT          587..618
FT                   /note="HAT 11"
FT   REPEAT          620..652
FT                   /note="HAT 12"
FT   REPEAT          654..688
FT                   /note="HAT 13"
FT   REPEAT          690..721
FT                   /note="HAT 14"
FT   REPEAT          726..767
FT                   /note="HAT 15"
FT   REPEAT          769..807
FT                   /note="HAT 16"
FT   REPEAT          809..834
FT                   /note="HAT 17"
FT   REGION          81..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..628
FT                   /note="Mediates interaction with HSP90"
FT                   /evidence="ECO:0000250|UniProtKB:P63154"
FT   REGION          827..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..161
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11342225,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_002058"
FT   VAR_SEQ         23..74
FT                   /note="TSRLELRSYSLAGRHGSTEPLVLAWSSQFRRLTWGCALDALHRSPCVAASQH
FT                   -> ILASLLVSTALPTSSAAPGRRTPRAAARRTRSLVTMETVPPPSRLKREVKGQ (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11342225"
FT                   /id="VSP_002060"
FT   VAR_SEQ         23..34
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11342225"
FT                   /id="VSP_002059"
FT   VAR_SEQ         75..848
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11342225"
FT                   /id="VSP_002061"
FT   VAR_SEQ         117..848
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11342225"
FT                   /id="VSP_002062"
FT   VARIANT         35
FT                   /note="G -> R (in dbSNP:rs7508949)"
FT                   /evidence="ECO:0000269|PubMed:11342225"
FT                   /id="VAR_024995"
FT   VARIANT         51
FT                   /note="F -> L (in dbSNP:rs2273058)"
FT                   /id="VAR_049318"
FT   VARIANT         111
FT                   /note="Q -> H (in dbSNP:rs2255258)"
FT                   /id="VAR_049319"
FT   VARIANT         158
FT                   /note="T -> A (in dbSNP:rs2255255)"
FT                   /id="VAR_049320"
FT   VARIANT         843
FT                   /note="V -> I (in dbSNP:rs35201190)"
FT                   /id="VAR_049321"
FT   CONFLICT        213
FT                   /note="K -> R (in Ref. 1; AAF65571/AAK01924/AAK01925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="V -> A (in Ref. 4; BAB14659)"
FT                   /evidence="ECO:0000305"
FT   HELIX           191..199
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           217..238
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           243..253
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           258..271
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           276..288
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           292..305
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           310..322
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           326..337
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           343..356
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           359..372
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           376..388
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           392..405
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          408..410
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           411..413
FT                   /evidence="ECO:0007829|PDB:6FF4"
FT   HELIX           414..425
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           430..439
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            440..444
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           452..466
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           478..490
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           497..512
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           521..533
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            538..540
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   HELIX           541..554
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           560..568
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           574..580
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            585..587
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            590..593
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           594..596
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           599..602
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           610..623
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            632..634
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           635..642
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           650..659
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           668..678
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           684..695
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           700..707
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           719..730
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           742..754
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           765..774
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           782..799
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   INIT_MET        Q9BZJ0-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         Q9BZJ0-2:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   848 AA;  100452 MW;  E30A39E981BC50AC CRC64;
     MTATVENLTF QKDTLGNAVD KNTSRLELRS YSLAGRHGST EPLVLAWSSQ FRRLTWGCAL
     DALHRSPCVA ASQHGVTHLI RSSRTPHSTR CRKEDAQPGH HGNGAASVTA QARGQRSVLQ
     VPLPVPRSCL FSESFVVSVS SQSRFLASVP GTGVQRSTAA DMAASTAAGK QRIPKVAKVK
     NKAPAEVQIT AEQLLREAKE RELELLPPPP QQKITDEEEL NDYKLRKRKT FEDNIRKNRT
     VISNWIKYAQ WEESLKEIQR ARSIYERALD VDYRNITLWL KYAEMEMKNR QVNHARNIWD
     RAITTLPRVN QFWYKYTYME EMLGNVAGAR QVFERWMEWQ PEEQAWHSYI NFELRYKEVD
     RARTIYERFV LVHPDVKNWI KYARFEEKHA YFAHARKVYE RAVEFFGDEH MDEHLYVAFA
     KFEENQKEFE RVRVIYKYAL DRISKQDAQE LFKNYTIFEK KFGDRRGIED IIVSKRRFQY
     EEEVKANPHN YDAWFDYLRL VESDAEAEAV REVYERAIAN VPPIQEKRHW KRYIYLWINY
     ALYEELEAKD PERTRQVYQA SLELIPHKKF TFAKMWILYA QFEIRQKNLS LARRALGTSI
     GKCPKNKLFK VYIELELQLR EFDRCRKLYE KFLEFGPENC TSWIKFAELE TILGDIDRAR
     AIYELAISQP RLDMPEVLWK SYIDFEIEQE ETERTRNLYR RLLQRTQHVK VWISFAQFEL
     SSGKEGSLTK CRQIYEEANK TMRNCEEKEE RLMLLESWRS FEEEFGTASD KERVDKLMPE
     KVKKRRKVQT DDGSDAGWEE YFDYIFPEDA ANQPNLKLLA MAKLWKKQQQ EKEDAEHHPD
     EDVDESES
//
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