IWS1_RAT
ID IWS1_RAT Reviewed; 764 AA.
AC Q3SWT4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein IWS1 homolog;
DE AltName: Full=IWS1-like protein;
GN Name=Iws1; Synonyms=Iws1l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-183; SER-261;
RP SER-263; SER-295; SER-307; SER-309; SER-321; SER-342; SER-344; SER-360;
RP SER-365; SER-367; SER-371; SER-383; SER-385; SER-457 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription factor which plays a key role in defining the
CC composition of the RNA polymerase II (RNAPII) elongation complex and in
CC modulating the production of mature mRNA transcripts. Acts as an
CC assembly factor to recruit various factors to the RNAPII elongation
CC complex and is recruited to the complex via binding to the
CC transcription elongation factor SUPT6H bound to the C-terminal domain
CC (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex
CC recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone
CC modifying enzymes (such as SETD2) to ensure proper mRNA splicing,
CC efficient mRNA export and elongation-coupled H3K36 methylation, a
CC signature chromatin mark of active transcription (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SUPT6H; binds preferentially to the POLR2A-
CC bound SUPT6H. Interacts with ALYREF/THOC4, SETD2 and PRMT5 (By
CC similarity). Interacts with HDGFRP2 (By similarity). Interacts (via IBM
CC motif) with PSIP1 (via IBD domain); phosphorylation increases its
CC affinity for PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q96ST2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q96ST2}.
CC -!- SIMILARITY: Belongs to the IWS1 family. {ECO:0000305}.
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DR EMBL; BC104700; AAI04701.1; -; mRNA.
DR RefSeq; NP_001030090.1; NM_001034918.1.
DR RefSeq; XP_006254634.1; XM_006254572.3.
DR AlphaFoldDB; Q3SWT4; -.
DR SMR; Q3SWT4; -.
DR STRING; 10116.ENSRNOP00000057730; -.
DR iPTMnet; Q3SWT4; -.
DR PhosphoSitePlus; Q3SWT4; -.
DR PaxDb; Q3SWT4; -.
DR PRIDE; Q3SWT4; -.
DR Ensembl; ENSRNOT00000061011; ENSRNOP00000057730; ENSRNOG00000014630.
DR GeneID; 291705; -.
DR KEGG; rno:291705; -.
DR UCSC; RGD:1304762; rat.
DR CTD; 55677; -.
DR RGD; 1304762; Iws1.
DR eggNOG; KOG1793; Eukaryota.
DR GeneTree; ENSGT00720000108834; -.
DR InParanoid; Q3SWT4; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q3SWT4; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000014630; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q3SWT4; baseline and differential.
DR Genevisible; Q3SWT4; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:2001253; P:regulation of histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:0090239; P:regulation of histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR Pfam; PF08711; Med26; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..764
FT /note="Protein IWS1 homolog"
FT /id="PRO_0000083348"
FT DOMAIN 560..638
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 1..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..764
FT /note="Interaction with SUPT6H and ALYREF"
FT /evidence="ECO:0000250"
FT REGION 642..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 415..441
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT COMPBIAS 30..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1D8"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
SQ SEQUENCE 764 AA; 85448 MW; A2327EF16763D095 CRC64;
MDSEYYSGDQ SDDGGATPVQ DERDSGSDGE DDVNEQHSGS DTGSVDRHSE NETSDREDGL
TKIHNGTDSE NDEPSNVHAS DSESEELHRP KDSDSESEEH AESPASDSEN EAVHQQGSDS
EKEELLNGHA SDSEKEEGRK HAASDSETED TLQPQGSESD SEDPPRPQAS DSESEEPPKP
RISDSESEEL PKPRISDSES EDPPRPQVSD SESEELPKPR VSDSESEDPP RPQASDSESE
ELPKPRVSDS ESEDPQKGPA SDSEAEDASR HKEKPESEDS DGENKREDSE VQNESDGHAD
RKGLHSSDSE EEEPKRQKID SDDDGEKEGD EKVAKRKAAV LSDSEDEDKA SAAKKSRVIS
DADDSDSDVV SDKSGKREKT VASDSEEEVG KEESSVKKSE EKDLFGSDSE SGNEEENLIA
DIFGESGDEE EEEFTGFNQE DLEEEKNETQ LKEAEDSDSD DNIKRGKHMD FLSDFEMMLQ
RKKSMCGKRR RNRDGGTFIS DADDVVSAMI VKMNEAAEED RQLNNQKKPA LKKLTLLPTV
VMHLKKQDLK ETFIDSGVMS AIKEWLSPLP DRSLPALKIR EELLKILQEL PSVSQETLKH
SGIGRAVMYL YKHPKESRSN KDMAGKLINE WSRPIFGLTS NYKGMTREER EQRDLEQMPQ
RRRMSSTGGQ TPRRDLEKVL TGEEKALRPG DPGFCARARV PMPSNKDYVV RPKWNVEMES
SRPGILKKGL SRLEKHKRRF AEQKRLSQMH RAVKFSIEGN RMPL
