HTSF1_PONAB
ID HTSF1_PONAB Reviewed; 754 AA.
AC Q5RB63;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=HIV Tat-specific factor 1 homolog;
GN Name=HTATSF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a general transcription factor playing a role in
CC the process of transcriptional elongation. May mediate the reciprocal
CC stimulatory effect of splicing on transcriptional elongation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin. Interacts with GTF2F2/RAP30
CC and POLR2A. Interacts with TCERG1/CA150. Interacts with SF3A2/SAP62 and
CC the spliceosomal U small nuclear ribonucleoproteins (snRNPs) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The RRM domains mediate interaction with U snRNPs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HTATSF1 family. {ECO:0000305}.
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DR EMBL; CR858792; CAH90997.1; -; mRNA.
DR RefSeq; NP_001125576.1; NM_001132104.1.
DR AlphaFoldDB; Q5RB63; -.
DR STRING; 9601.ENSPPYP00000023249; -.
DR Ensembl; ENSPPYT00000024220; ENSPPYP00000023249; ENSPPYG00000020765.
DR GeneID; 100172491; -.
DR KEGG; pon:100172491; -.
DR CTD; 27336; -.
DR eggNOG; KOG1548; Eukaryota.
DR GeneTree; ENSGT00390000009902; -.
DR InParanoid; Q5RB63; -.
DR OrthoDB; 1542889at2759; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd12281; RRM1_TatSF1_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034393; TatSF1-like.
DR InterPro; IPR034392; TatSF1-like_RRM1.
DR PANTHER; PTHR15608; PTHR15608; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT CHAIN 2..754
FT /note="HIV Tat-specific factor 1 homolog"
FT /id="PRO_0000248606"
FT DOMAIN 133..218
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 264..349
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..754
FT /note="Mediates interaction with the P-TEFb complex"
FT /evidence="ECO:0000250"
FT REGION 433..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..651
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..717
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 297
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGC0"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGC0"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 633
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43719"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43719"
SQ SEQUENCE 754 AA; 85778 MW; A655A4F1839E5D43 CRC64;
MSGTNLDGND EFDEQLRMQE LYGDGKDGDT QTDAGGEPDS LGQQPTDTPY EWDLDKKAWF
PKITEDFIAT YQANYGFSND GASSSTANVE DVHARTAEEP PQEKAPEPTD PRKKGEKRKA
ESGWFHVEED RNTNVYVSGL PPDITVDEFI QLMSKFGIIM RDPQTEEFKV KLYKDNQGNL
KGDGLCCYLK RESVELALKL LDEDEIRGYK LHVEVAKFQL KGEYDASKKK KKCKDYKKKL
SMQQKQLDWR PERRAGPSRM RHERVVIIKN MFHPMDFEDD PLVLNEIRED LRVECSKFGQ
IRKLLLFDRH PDGVASVSFR DPEEADYCIQ TLDGRWFGGR QITAQAWDGT TDYQVEETSR
EREERLRGWE AFLNAPEANR GLRRSDSVSA SERAGPSRAR HFSEHPSTSK MNAQETATGM
AFEEPIDEKK FEKTEDGGEF EEGASENNAK ESSPEKEAEE GCPGKESEEG CPKRGFEGSC
SQKESEEGNP LRGSEEGSPK KESKKKTLRN DCEENGFAKE SEDDPNKESE EEVGPTKESE
EDDSEKESDE DCSEKQSEDG SEREFEENGL EKDLDEEGSE KELHENVLDK ELEENDSENS
EFEDDGSEKV LDEEGSEREF DEDSDEKEEE EDTYEKVFDD ESNEKEDEEY ADEKGLEAAD
KKEEEGDADE KLFEESDDKE DEDADGKEVE DADEKLFEDD DSNEKLFDEE EDSNEKLFDD
SDERGTLGGF GSVEEGPLST GSSFILSSDD DDDI
