ASHWN_HUMAN
ID ASHWN_HUMAN Reviewed; 232 AA.
AC Q9BVC5; B3KXN3; B4E2G9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ashwin;
GN Name=C2orf49;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASP-185.
RC TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, AND
RP IDENTIFICATION BY 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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-189; SER-193;
RP THR-197 AND THR-198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-193 AND THR-197, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
RX PubMed=21311021; DOI=10.1126/science.1197847;
RA Popow J., Englert M., Weitzer S., Schleiffer A., Mierzwa B., Mechtler K.,
RA Trowitzsch S., Will C.L., Luhrmann R., Soll D., Martinez J.;
RT "HSPC117 is the essential subunit of a human tRNA splicing ligase
RT complex.";
RL Science 331:760-764(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-143; SER-184;
RP SER-189; SER-193; THR-197 AND THR-198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP 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 [14]
RP IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
RX PubMed=24870230; DOI=10.1038/nature13284;
RA Popow J., Jurkin J., Schleiffer A., Martinez J.;
RT "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing
RT factors.";
RL Nature 511:104-107(2014).
CC -!- SUBUNIT: Component of the tRNA-splicing ligase complex.
CC {ECO:0000269|PubMed:21311021, ECO:0000269|PubMed:24870230}.
CC -!- INTERACTION:
CC Q9BVC5; P54253: ATXN1; NbExp=3; IntAct=EBI-5458641, EBI-930964;
CC Q9BVC5; O76024: WFS1; NbExp=3; IntAct=EBI-5458641, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVC5-2; Sequence=VSP_054353, VSP_054354;
CC -!- SIMILARITY: Belongs to the ashwin family. {ECO:0000305}.
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DR EMBL; AK127661; BAG54545.1; -; mRNA.
DR EMBL; AK304268; BAG65131.1; -; mRNA.
DR EMBL; AC012360; AAY15011.1; -; Genomic_DNA.
DR EMBL; BC001310; AAH01310.1; -; mRNA.
DR CCDS; CCDS2068.1; -. [Q9BVC5-1]
DR RefSeq; NP_001273466.1; NM_001286537.1.
DR RefSeq; NP_076998.1; NM_024093.2. [Q9BVC5-1]
DR RefSeq; XP_016860381.1; XM_017004892.1. [Q9BVC5-2]
DR AlphaFoldDB; Q9BVC5; -.
DR SMR; Q9BVC5; -.
DR BioGRID; 122525; 29.
DR ComplexPortal; CPX-6411; tRNA-splicing ligase complex.
DR CORUM; Q9BVC5; -.
DR IntAct; Q9BVC5; 12.
DR MINT; Q9BVC5; -.
DR STRING; 9606.ENSP00000258457; -.
DR GlyGen; Q9BVC5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVC5; -.
DR PhosphoSitePlus; Q9BVC5; -.
DR BioMuta; C2orf49; -.
DR DMDM; 74733311; -.
DR EPD; Q9BVC5; -.
DR jPOST; Q9BVC5; -.
DR MassIVE; Q9BVC5; -.
DR MaxQB; Q9BVC5; -.
DR PaxDb; Q9BVC5; -.
DR PeptideAtlas; Q9BVC5; -.
DR PRIDE; Q9BVC5; -.
DR ProteomicsDB; 5818; -.
DR ProteomicsDB; 79197; -. [Q9BVC5-1]
DR Antibodypedia; 47531; 155 antibodies from 21 providers.
DR DNASU; 79074; -.
DR Ensembl; ENST00000258457.7; ENSP00000258457.2; ENSG00000135974.10. [Q9BVC5-1]
DR GeneID; 79074; -.
DR KEGG; hsa:79074; -.
DR MANE-Select; ENST00000258457.7; ENSP00000258457.2; NM_024093.3; NP_076998.1.
DR UCSC; uc002tcs.3; human. [Q9BVC5-1]
DR CTD; 79074; -.
DR DisGeNET; 79074; -.
DR GeneCards; C2orf49; -.
DR HGNC; HGNC:28772; C2orf49.
DR HPA; ENSG00000135974; Low tissue specificity.
DR neXtProt; NX_Q9BVC5; -.
DR OpenTargets; ENSG00000135974; -.
DR PharmGKB; PA162379179; -.
DR VEuPathDB; HostDB:ENSG00000135974; -.
DR eggNOG; ENOG502S0PQ; Eukaryota.
DR GeneTree; ENSGT00390000007488; -.
DR InParanoid; Q9BVC5; -.
DR OMA; SRWGKRM; -.
DR OrthoDB; 1299864at2759; -.
DR PhylomeDB; Q9BVC5; -.
DR TreeFam; TF332084; -.
DR BioCyc; MetaCyc:ENSG00000135974-MON; -.
DR PathwayCommons; Q9BVC5; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q9BVC5; -.
DR BioGRID-ORCS; 79074; 47 hits in 1053 CRISPR screens.
DR ChiTaRS; C2orf49; human.
DR GenomeRNAi; 79074; -.
DR Pharos; Q9BVC5; Tbio.
DR PRO; PR:Q9BVC5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BVC5; protein.
DR Bgee; ENSG00000135974; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; Q9BVC5; baseline and differential.
DR Genevisible; Q9BVC5; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; IDA:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IEA:InterPro.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IC:ComplexPortal.
DR InterPro; IPR024887; Ashwin.
DR PANTHER; PTHR28359; PTHR28359; 1.
DR Pfam; PF15323; Ashwin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..232
FT /note="Ashwin"
FT /id="PRO_0000268859"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MRRLRVTTHASLRPSTSLPQRFLRGALWVADWGLLATTM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054353"
FT VAR_SEQ 131..172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054354"
FT VARIANT 185
FT /note="G -> D (in dbSNP:rs28930676)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_029759"
SQ SEQUENCE 232 AA; 25858 MW; 27A5611FA270FB3E CRC64;
MAGDVGGRSC TDSELLLHPE LLSQEFLLLT LEQKNIAVET DVRVNKDSLT DLYVQHAIPL
PQRDLPKNRW GKMMEKKREQ HEIKNETKRS STVDGLRKRP LIVFDGSSTS TSIKVKKTEN
GDNDRLKPPP QASFTSNAFR KLSNSSSSVS PLILSSNLPV NNKTEHNNND AKQNHDLTHR
KSPSGPVKSP PLSPVGTTPV KLKRAAPKEE AEAMNNLKPP QAKRKIQHVT WP
