CRNL1_HUMAN
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 03-AUG-2022, entry version 179.
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 AlphaFoldDB; Q9BZJ0; -.
DR SMR; Q9BZJ0; -.
DR BioGRID; 119487; 127.
DR CORUM; Q9BZJ0; -.
DR IntAct; Q9BZJ0; 50.
DR MINT; Q9BZJ0; -.
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 Antibodypedia; 9534; 65 antibodies from 13 providers.
DR DNASU; 51340; -.
DR Ensembl; ENST00000377340.6; ENSP00000366557.2; ENSG00000101343.15. [Q9BZJ0-1]
DR Ensembl; ENST00000496549.5; ENSP00000428436.1; ENSG00000101343.15. [Q9BZJ0-5]
DR Ensembl; ENST00000536226.2; ENSP00000440733.1; ENSG00000101343.15. [Q9BZJ0-2]
DR GeneID; 51340; -.
DR KEGG; hsa:51340; -.
DR MANE-Select; ENST00000536226.2; ENSP00000440733.1; NM_001278628.2; NP_001265557.1. [Q9BZJ0-2]
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; HIKVWIS; -.
DR PhylomeDB; Q9BZJ0; -.
DR TreeFam; TF300305; -.
DR PathwayCommons; Q9BZJ0; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9BZJ0; -.
DR BioGRID-ORCS; 51340; 763 hits in 1081 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 193 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; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11246; PTHR11246; 1.
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
