ELP2_MOUSE
ID ELP2_MOUSE Reviewed; 831 AA.
AC Q91WG4; Q3TIH5; Q3TIT0; Q8CBW6; Q9ESY7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Elongator complex protein 2;
DE Short=ELP2;
DE AltName: Full=STAT3-interacting protein 1;
DE Short=StIP1;
GN Name=Elp2; Synonyms=Statip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH STAT3.
RX PubMed=10954736; DOI=10.1073/pnas.170192197;
RA Collum R.G., Brutsaert S., Lee G., Schindler C.;
RT "A Stat3-interacting protein (StIP1) regulates cytokine signal
RT transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10120-10125(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Diencephalon, Embryo, Kidney, Placenta, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine). The elongator comple catalyzes the
CC formation of carboxymethyluridine in the wobble base at position 34 in
CC tRNAs. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBUNIT: Component of the elongator complex which consists of ELP1,
CC ELP2, ELP3, ELP4, ELP5 and ELP6. Interacts with STAT3 and JAKs
CC (PubMed:10954736). {ECO:0000250|UniProtKB:Q6IA86,
CC ECO:0000269|PubMed:10954736}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WG4-2; Sequence=VSP_016534;
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly.
CC {ECO:0000250|UniProtKB:P42935}.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q6IA86}.
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DR EMBL; AF291064; AAG01032.1; -; mRNA.
DR EMBL; AK033246; BAC28210.1; -; mRNA.
DR EMBL; AK034457; BAC28716.1; -; mRNA.
DR EMBL; AK050960; BAC34477.1; -; mRNA.
DR EMBL; AK147826; BAE28163.1; -; mRNA.
DR EMBL; AK167725; BAE39766.1; -; mRNA.
DR EMBL; AK167853; BAE39871.1; -; mRNA.
DR EMBL; AK168370; BAE40302.1; -; mRNA.
DR EMBL; BC015284; AAH15284.1; -; mRNA.
DR EMBL; BC051943; AAH51943.1; -; mRNA.
DR CCDS; CCDS29103.1; -. [Q91WG4-1]
DR RefSeq; NP_067423.2; NM_021448.2. [Q91WG4-1]
DR AlphaFoldDB; Q91WG4; -.
DR SMR; Q91WG4; -.
DR BioGRID; 208427; 20.
DR STRING; 10090.ENSMUSP00000025120; -.
DR iPTMnet; Q91WG4; -.
DR PhosphoSitePlus; Q91WG4; -.
DR EPD; Q91WG4; -.
DR MaxQB; Q91WG4; -.
DR PaxDb; Q91WG4; -.
DR PeptideAtlas; Q91WG4; -.
DR PRIDE; Q91WG4; -.
DR ProteomicsDB; 277854; -. [Q91WG4-1]
DR ProteomicsDB; 277855; -. [Q91WG4-2]
DR Antibodypedia; 657; 129 antibodies from 24 providers.
DR DNASU; 58523; -.
DR Ensembl; ENSMUST00000025120; ENSMUSP00000025120; ENSMUSG00000024271. [Q91WG4-2]
DR Ensembl; ENSMUST00000234266; ENSMUSP00000157109; ENSMUSG00000024271. [Q91WG4-1]
DR GeneID; 58523; -.
DR KEGG; mmu:58523; -.
DR UCSC; uc008egx.1; mouse. [Q91WG4-1]
DR UCSC; uc012baj.1; mouse. [Q91WG4-2]
DR CTD; 55250; -.
DR MGI; MGI:1889642; Elp2.
DR VEuPathDB; HostDB:ENSMUSG00000024271; -.
DR eggNOG; KOG1063; Eukaryota.
DR GeneTree; ENSGT00390000000916; -.
DR HOGENOM; CLU_006430_1_0_1; -.
DR InParanoid; Q91WG4; -.
DR OMA; EHTKRVN; -.
DR OrthoDB; 461632at2759; -.
DR PhylomeDB; Q91WG4; -.
DR TreeFam; TF105985; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 58523; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Elp2; mouse.
DR PRO; PR:Q91WG4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91WG4; protein.
DR Bgee; ENSMUSG00000024271; Expressed in saccule of membranous labyrinth and 256 other tissues.
DR Genevisible; Q91WG4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; ISO:MGI.
DR GO; GO:0061133; F:endopeptidase activator activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 5.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW tRNA processing; WD repeat.
FT CHAIN 1..831
FT /note="Elongator complex protein 2"
FT /id="PRO_0000051242"
FT REPEAT 56..100
FT /note="WD 1"
FT REPEAT 105..152
FT /note="WD 2"
FT REPEAT 158..200
FT /note="WD 3"
FT REPEAT 205..246
FT /note="WD 4"
FT REPEAT 280..328
FT /note="WD 5"
FT REPEAT 338..377
FT /note="WD 6"
FT REPEAT 385..424
FT /note="WD 7"
FT REPEAT 438..476
FT /note="WD 8"
FT REPEAT 565..609
FT /note="WD 9"
FT REPEAT 612..651
FT /note="WD 10"
FT REPEAT 667..706
FT /note="WD 11"
FT REPEAT 718..762
FT /note="WD 12"
FT REPEAT 775..831
FT /note="WD 13"
FT VAR_SEQ 175..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016534"
FT CONFLICT 23
FT /note="S -> G (in Ref. 2; BAE39871)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="D -> E (in Ref. 1; AAG01032)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="A -> V (in Ref. 2; BAE39871)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="H -> N (in Ref. 2; BAE39871)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="G -> R (in Ref. 2; BAC28716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 93093 MW; 177290C8B633FDC4 CRC64;
MVSSVLEVSH VFCCPNRVRG ALSWNTGPGG LLAFGTSCSV VLYDPQKKVV ITNLNGHTAR
VNCLQWIRTE DGSPSNELVS GGSDNRVIHW ELENNQVLKS VRLQGHEGPV CAVHAIYQSG
PSEGEQHALI ASAASDSTVR IWSKKGSEVK YLQTLSFRDG FVLSVCLAIL PGTNVPVLAC
GDDDCRIHLY IQQDDQFQKA LSLCGHEDWI RGVEWATFGR DLFLASCSQD CLIRIWRLYM
KPASFETKDG SLRLKENTFT IKDGGVRTTV AVTLETVLAG HENWVNAVHW QPSFYKDGVL
QQPVRLLSAS MDKTMILWAP DEESGVWLEQ VRVGEVGGNT LGFYDCQFGE NGTMIIAHAF
HGALHLWKQS TVNPRQWAPE IVISGHFDGV QDLMWDPEGE FIITTSTDQT TRLFAPWKKK
DQKDRSQVTW HEIARPQIHG YNIKCLAMID RFQFVSGADE KVLRVFSAPR NFVENFSVIS
RQSLSHMLCD DQDLPEGATV PALGLSNKAL FQGDIASQPF EEDELISPAF GSPQVTFQPA
VLNEPPTEDH LLQNTLWPEI QKLYGHGYEI VCVACNNSKT LLASACKASQ KEHAAIILWS
TASWKQVQSL AFHTLTVTQM TFSPDDKFLL AVSRDRTWSL WKRQDATSSE FDPFFSLFAF
TNKITSVHSR IIWSCDWSPD NKYFFTGSRD KKVVVWGECK SSHNPMEHPI RPCSSILDVG
SSVTAVSVCP VLNPAQRYIV AIGLESGKIC IYSWNKTNQE INDWTSCVET NPSQSHSLGI
RRLCWKSCSD DDDDDDDDDT EQSEEGPEWL HFASCGEDHT VKIYRVNRRA L
