ASCC2_DICDI
ID ASCC2_DICDI Reviewed; 941 AA.
AC Q54VC4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 2 homolog;
GN Name=ascc2; ORFNames=DDB_G0280455;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation (By
CC similarity). Involved in activation of the ribosome quality control
CC (RQC) pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1I8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H1I8}.
CC -!- SIMILARITY: Belongs to the ASCC2 family. {ECO:0000305}.
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DR EMBL; AAFI02000036; EAL67206.2; -; Genomic_DNA.
DR RefSeq; XP_641185.2; XM_636093.2.
DR AlphaFoldDB; Q54VC4; -.
DR SMR; Q54VC4; -.
DR STRING; 44689.DDB0304690; -.
DR PaxDb; Q54VC4; -.
DR EnsemblProtists; EAL67206; EAL67206; DDB_G0280455.
DR GeneID; 8622566; -.
DR KEGG; ddi:DDB_G0280455; -.
DR dictyBase; DDB_G0280455; ascc2.
DR eggNOG; KOG4501; Eukaryota.
DR HOGENOM; CLU_312031_0_0_1; -.
DR InParanoid; Q54VC4; -.
DR OMA; WRILDIC; -.
DR PhylomeDB; Q54VC4; -.
DR PRO; PR:Q54VC4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd14364; CUE_ASCC2; 1.
DR InterPro; IPR041800; ASCC2_CUE.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
PE 3: Inferred from homology;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..941
FT /note="Activating signal cointegrator 1 complex subunit 2
FT homolog"
FT /id="PRO_0000371329"
FT DOMAIN 563..606
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 531..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..64
FT /evidence="ECO:0000255"
FT COMPBIAS 706..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 109012 MW; 27C0FBD059F53DD8 CRC64;
MQQQQQPKVK LSKKDYIEKK EKEQQLLNNN NKVNREKDGK IMIEKNLQEK QDDILMNEKK
KQQSGLGIDK TFTLVINTLG HLEKKNDLDQ YWVLNNKEYH LSFITFLPAD NNEQGSSEES
ILFMNSDLSS LLKFQYNIFW SHCIFNKSLN EFIDSFLKFF KRDNQPIISL VNNNSVNNNN
NNNNSIIKKG SKDFNESKKL LFKRVFLVLV RMSLQQEKSG FITREFYSDL IYKNKLFTIP
KLFDIVSLYS SHARDAVTTM IQSIFDTQPN YYKDLLQHFQ LISKTLFELN QSLLNRNLLD
LLRLEDNYLM DIVYNLEQFI RIFPMGSHQL FDEYLMNLEK GGGDGNGGVL GWLTYFYEYI
IPIFNKENQK ASNKQVNLTP SIYVPLKQHI LSIFHTIFRH HFMIKLEQLQ LLIQDPCQLC
KKLPLDEISH RFFSLLGNIT SFSQQIIGST KSNRSKLFNE YFDNITSASI LYDYEQTYKL
SNFLDKLVTL DSSIDFTSYT YFMQLIGKPV SQDQKQIQKP KFKKSTTIID SNISSSSSSS
SSSSPSNATT TVKPILSNNP VIMNTVKIDQ VKSLFPDLGD WFVHCCLKYY NQDVEQVINA
LCDDSSLPPH LKSMDRSLSS DPSQPSKNIP TPTTTTTTTT TTDKPNNTTT ATTTTTTTTS
SSKSLEKSMN ELNISIGYEK IYDEKYDDSL EEFSGFSVQD GEKYNDEDED EKKDSENNTN
TEDQKHPTTS ASGRTPNESN NLGRPRQNNP NKGRKEDNRN NKQQTHSSHH SQPQQQQQQQ
PPQHQPQPHQ QPQQQPQPHQ HQQPQQQQPQ QPQHKQQPKP QQSKQHPQQQ PKQQPKQQPQ
QPKQQSQQQP KQHPQPQQPQ QPQPQPQPQP QQQQQQQQQQ QQQQQQRQPQ QPQQPQPQQQ
NQQQNQQQNQ QPKKSQNDDK PKPDKKPKGS YSKGGSVGGG R
