CTR9_XENLA
ID CTR9_XENLA Reviewed; 1157 AA.
AC Q4QR29; Q6DCM7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=RNA polymerase-associated protein CTR9 homolog;
DE AltName: Full=SH2 domain-binding protein 1;
GN Name=ctr9; Synonyms=sh2bp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II (By similarity).
CC PAF1C associates with RNA polymerase II, is involved in transcriptional
CC elongation and in histone modifications including methylation on
CC histone H3 'Lys-4' (H3K4me3) (By similarity).
CC {ECO:0000250|UniProtKB:Q6PD62}.
CC -!- SUBUNIT: Component of the PAF1 complex, which at least consists of
CC cdc73, paf1, leo1, ctr9 and rtf1 (By similarity). The PAF1 complex
CC interacts with PHF5A (By similarity). {ECO:0000250|UniProtKB:Q62018,
CC ECO:0000250|UniProtKB:Q6PD62}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62018}.
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DR EMBL; BC077978; AAH77978.1; -; mRNA.
DR EMBL; BC097638; AAH97638.1; -; mRNA.
DR RefSeq; NP_001086446.1; NM_001092977.1.
DR AlphaFoldDB; Q4QR29; -.
DR SMR; Q4QR29; -.
DR BioGRID; 103096; 1.
DR IntAct; Q4QR29; 1.
DR GeneID; 446236; -.
DR KEGG; xla:446236; -.
DR CTD; 446236; -.
DR Xenbase; XB-GENE-5946199; ctr9.S.
DR OMA; MSNCIEI; -.
DR OrthoDB; 396755at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 446236; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1157
FT /note="RNA polymerase-associated protein CTR9 homolog"
FT /id="PRO_0000231590"
FT REPEAT 41..75
FT /note="TPR 1"
FT REPEAT 129..162
FT /note="TPR 2"
FT REPEAT 163..196
FT /note="TPR 3"
FT REPEAT 198..231
FT /note="TPR 4"
FT REPEAT 235..268
FT /note="TPR 5"
FT REPEAT 306..339
FT /note="TPR 6"
FT REPEAT 341..374
FT /note="TPR 7"
FT REPEAT 412..444
FT /note="TPR 8"
FT REPEAT 451..484
FT /note="TPR 9"
FT REPEAT 497..530
FT /note="TPR 10"
FT REPEAT 531..564
FT /note="TPR 11"
FT REPEAT 566..598
FT /note="TPR 12"
FT REPEAT 613..646
FT /note="TPR 13"
FT REPEAT 648..680
FT /note="TPR 14"
FT REPEAT 681..714
FT /note="TPR 15"
FT REPEAT 717..750
FT /note="TPR 16"
FT REGION 889..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 936
FT /note="R -> K (in Ref. 1; AAH77978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1157 AA; 131613 MW; 6C23C99706311B19 CRC64;
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YFKQGKTEDF
VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKELI TQATLLYTMA
DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
GALAYYKKAL RTNPGCPAGV RLGMGHCFVK LNKLDKARLA FGRALDLNPT CVGALVGLAV
LELNNKEADS IKNGVQLLSK AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFAAASF VLPFFGLGQM YIYRGDKENA
SQCFEKVLKA YPNNYETMKI LGSLYAASDD QEKRDIAKSH LKKVTEQYPD DVEAWIELAQ
ILEQTDIQNA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
AKAEAEHDEH YYNSISVTTS YNLARLYEGL CEFHESEKLY KNILREHPNY VDCYLRLGAM
ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQND
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDSKNLFAA NGIGAVLAHK
GYVREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVL
LYLARALFKC GKLQECKQIL LKARHVAPND TVLMFNVALV LQRLATLVLK DEKSNLKAVL
NAVKELELAH RYFNYLSKVG DKMRFDLALA TSEARQCSDL LSQAQYHVAR ARKQDEEEKE
MRTKQEQEKE VLRQKLLKEQ EEKHLREIEE QKKLLEQRAQ YLEKTRNLLS FTGEMETPKE
KKQRGGGGRR SKKNGEFEEF VNDDSDEELA PRKKKRKKGG SSSGEQGEGG DEGEGGEKKK
KKRRKRPQKA AGSDDDEEQT PQSKKRQPKK KEKPAKLERT PPSMKGKIKS KAIISSSEDD
SDEDKLKIAD EGHARDSDSD DGPRKSQKRV ISDSDSDNGN KSGSDAGSPQ KSQRSDEDSD
NAFARKRRRQ ISGSDNDSAQ SRRSSGGSDN ESRAASNSAE SERGSDRGSD NEGSERASGN
QSEQEVEKSE RGSDESD
