CSTF1_HUMAN
ID CSTF1_HUMAN Reviewed; 431 AA.
AC Q05048; Q5QPD8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Cleavage stimulation factor subunit 1;
DE AltName: Full=CF-1 50 kDa subunit;
DE AltName: Full=Cleavage stimulation factor 50 kDa subunit;
DE Short=CSTF 50 kDa subunit;
DE Short=CstF-50;
GN Name=CSTF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 101-119 AND 155-170.
RX PubMed=1358884; DOI=10.1016/s0021-9258(18)35861-7;
RA Takagaki Y., Manley J.L.;
RT "A human polyadenylation factor is a G protein beta-subunit homologue.";
RL J. Biol. Chem. 267:23471-23474(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP INTERACTION WITH BARD1, AND SUBCELLULAR LOCATION.
RX PubMed=10477523; DOI=10.1126/science.285.5433.1576;
RA Kleiman F.E., Manley J.L.;
RT "Functional interaction of BRCA1-associated BARD1 with polyadenylation
RT factor CstF-50.";
RL Science 285:1576-1579(1999).
RN [8]
RP SUBUNIT, INTERACTION WITH CSTF3, AND FUNCTION.
RX PubMed=10669729; DOI=10.1128/mcb.20.5.1515-1525.2000;
RA Takagaki Y., Manley J.L.;
RT "Complex protein interactions within the human polyadenylation machinery
RT identify a novel component.";
RL Mol. Cell. Biol. 20:1515-1525(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
CC -!- FUNCTION: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of mammalian pre-mRNAs (PubMed:10669729). May be
CC responsible for the interaction of CSTF with other factors to form a
CC stable complex on the pre-mRNA (PubMed:10669729).
CC {ECO:0000303|PubMed:10669729}.
CC -!- SUBUNIT: Homodimer (PubMed:10669729). The CSTF complex is composed of
CC CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa
CC subunit) (PubMed:10669729). Interacts (via repeats WD) directly with
CC CSTF3 (PubMed:10669729). Interacts (via repeat WD6) with BARD1
CC (PubMed:10477523). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:10477523, ECO:0000269|PubMed:10669729,
CC ECO:0000269|PubMed:26030138}.
CC -!- INTERACTION:
CC Q05048; Q99728: BARD1; NbExp=4; IntAct=EBI-1789619, EBI-473181;
CC Q05048; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-1789619, EBI-74615;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10477523}.
CC -!- DOMAIN: N-terminus mediates homodimerization.
CC {ECO:0000269|PubMed:10669729}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:1358884}.
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DR EMBL; L02547; AAA35691.1; -; mRNA.
DR EMBL; BT007138; AAP35802.1; -; mRNA.
DR EMBL; AK312774; BAG35638.1; -; mRNA.
DR EMBL; AL121914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75548.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75549.1; -; Genomic_DNA.
DR EMBL; BC001011; AAH01011.1; -; mRNA.
DR EMBL; BC007425; AAH07425.1; -; mRNA.
DR CCDS; CCDS13452.1; -.
DR PIR; A45142; A45142.
DR RefSeq; NP_001028693.1; NM_001033521.1.
DR RefSeq; NP_001028694.1; NM_001033522.1.
DR RefSeq; NP_001315.1; NM_001324.2.
DR RefSeq; XP_011526902.1; XM_011528600.1.
DR PDB; 6B3X; X-ray; 2.30 A; A=80-431.
DR PDBsum; 6B3X; -.
DR AlphaFoldDB; Q05048; -.
DR SMR; Q05048; -.
DR BioGRID; 107859; 85.
DR CORUM; Q05048; -.
DR IntAct; Q05048; 26.
DR MINT; Q05048; -.
DR STRING; 9606.ENSP00000217109; -.
DR GlyGen; Q05048; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q05048; -.
DR MetOSite; Q05048; -.
DR PhosphoSitePlus; Q05048; -.
DR SwissPalm; Q05048; -.
DR BioMuta; CSTF1; -.
DR REPRODUCTION-2DPAGE; IPI00011528; -.
DR EPD; Q05048; -.
DR jPOST; Q05048; -.
DR MassIVE; Q05048; -.
DR PaxDb; Q05048; -.
DR PeptideAtlas; Q05048; -.
DR PRIDE; Q05048; -.
DR ProteomicsDB; 58303; -.
DR Antibodypedia; 28869; 243 antibodies from 31 providers.
DR DNASU; 1477; -.
DR Ensembl; ENST00000217109.9; ENSP00000217109.4; ENSG00000101138.12.
DR GeneID; 1477; -.
DR KEGG; hsa:1477; -.
DR MANE-Select; ENST00000217109.9; ENSP00000217109.4; NM_001324.3; NP_001315.1.
DR UCSC; uc002xxm.2; human.
DR CTD; 1477; -.
DR DisGeNET; 1477; -.
DR GeneCards; CSTF1; -.
DR HGNC; HGNC:2483; CSTF1.
DR HPA; ENSG00000101138; Low tissue specificity.
DR MIM; 600369; gene.
DR neXtProt; NX_Q05048; -.
DR OpenTargets; ENSG00000101138; -.
DR PharmGKB; PA26985; -.
DR VEuPathDB; HostDB:ENSG00000101138; -.
DR eggNOG; KOG0640; Eukaryota.
DR GeneTree; ENSGT00910000144253; -.
DR HOGENOM; CLU_041619_0_0_1; -.
DR InParanoid; Q05048; -.
DR OMA; SNRCINT; -.
DR OrthoDB; 587820at2759; -.
DR PhylomeDB; Q05048; -.
DR TreeFam; TF314234; -.
DR PathwayCommons; Q05048; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q05048; -.
DR SIGNOR; Q05048; -.
DR BioGRID-ORCS; 1477; 579 hits in 1094 CRISPR screens.
DR ChiTaRS; CSTF1; human.
DR GeneWiki; CSTF1; -.
DR GenomeRNAi; 1477; -.
DR Pharos; Q05048; Tbio.
DR PRO; PR:Q05048; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q05048; protein.
DR Bgee; ENSG00000101138; Expressed in adrenal tissue and 160 other tissues.
DR ExpressionAtlas; Q05048; baseline and differential.
DR Genevisible; Q05048; HS.
DR GO; GO:0005848; C:mRNA cleavage stimulating factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR Gene3D; 1.20.960.50; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR044633; CstF1-like.
DR InterPro; IPR032028; CSTF1_dimer.
DR InterPro; IPR038184; CSTF1_dimer_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44133; PTHR44133; 1.
DR Pfam; PF16699; CSTF1_dimer; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..431
FT /note="Cleavage stimulation factor subunit 1"
FT /id="PRO_0000050944"
FT REPEAT 106..145
FT /note="WD 1"
FT REPEAT 171..210
FT /note="WD 2"
FT REPEAT 215..254
FT /note="WD 3"
FT REPEAT 260..301
FT /note="WD 4"
FT REPEAT 303..343
FT /note="WD 5"
FT REPEAT 395..430
FT /note="WD 6"
FT REGION 14..35
FT /note="Hydrophobic"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6B3X"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 229..240
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6B3X"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 301..306
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6B3X"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:6B3X"
SQ SEQUENCE 431 AA; 48358 MW; 88A5BE53022AD9E3 CRC64;
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN
DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG
QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA
FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT
LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF
EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV
FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR
ARFWYRRSTT D
