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CTR9_XENTR
ID   CTR9_XENTR              Reviewed;        1172 AA.
AC   Q6DEU9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=RNA polymerase-associated protein CTR9 homolog;
DE   AltName: Full=SH2 domain-binding protein 1;
GN   Name=ctr9; Synonyms=sh2bp1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC076995; AAH76995.1; -; mRNA.
DR   RefSeq; NP_001005076.1; NM_001005076.1.
DR   AlphaFoldDB; Q6DEU9; -.
DR   SMR; Q6DEU9; -.
DR   STRING; 8364.ENSXETP00000029922; -.
DR   PRIDE; Q6DEU9; -.
DR   DNASU; 448648; -.
DR   GeneID; 448648; -.
DR   KEGG; xtr:448648; -.
DR   CTD; 9646; -.
DR   Xenbase; XB-GENE-5946075; ctr9.
DR   eggNOG; KOG2002; Eukaryota.
DR   InParanoid; Q6DEU9; -.
DR   OrthoDB; 396755at2759; -.
DR   Reactome; R-XTR-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-XTR-75955; RNA Polymerase II Transcription Elongation.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
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:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR   GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR   GO; GO:0045638; P:negative regulation of myeloid cell differentiation; 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:2001162; P:positive regulation of histone H3-K79 methylation; ISS:UniProtKB.
DR   GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0019827; P:stem cell population maintenance; 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..1172
FT                   /note="RNA polymerase-associated protein CTR9 homolog"
FT                   /id="PRO_0000231591"
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..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..993
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1172 AA;  132661 MW;  D06657138B0E22E9 CRC64;
     MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALGLE YYKQVKTEDF
     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 YYNAISVTTT YNLARLYEGL CEFHESEKLY KNILREHPNY VDCYLRLGAM
     ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQND
     TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDSKNLYAA NGIGAVLAHK
     GYVREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVL
     LYLARALFKC GKLQECKQIL LKARHVAPND TVLMFNVALV LQRLATLVLK DEKSNLKAVL
     NAVKELELAH RYFNYLSKVG DKMRFDLALA ASEARQCSDL LSQAQYHVAR ARKQDEEEKE
     LRAKQEQEKE ILRQKLIKEQ EEKRLKEIEE QKKLLEQRAQ YVEKTRNLLN FTGEMETPKE
     KKQRGGGGGG GGRRSKKNGE FDEFVNDDSD EDLAPRKKKR KKGGGSSGSG GEQGEGGEEG
     EGGEKKKKKR RKRPQKGGDG SDDDEDQAPQ PKKRQPKKRE KPAKFERTPP SMKGKIKSKA
     IISSSEDDSD EDKLKIADEG HGRGSNSDSD EGPRTQAKKR IMSDSDSDNA NKSGSGAGSP
     QKSPQSDGDS DNNAWARKRR RQDSGSDNDS AQSRRSSGGS DNESRAASRS PESQRGSDRG
     SDNEGSARAS PNESEQEASN NEKSDRGSDD SD
 
 
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