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Protein

Cleavage stimulation factor subunit 1

Gene

Cstf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-77595. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage stimulation factor subunit 1
Alternative name(s):
CF-1 50 kDa subunit
Cleavage stimulation factor 50 kDa subunit
Short name:
CSTF 50 kDa subunit
Short name:
CstF-50
Gene namesi
Name:Cstf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914587. Cstf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Cleavage stimulation factor subunit 1PRO_0000050945Add
BLAST

Proteomic databases

EPDiQ99LC2.
MaxQBiQ99LC2.
PaxDbiQ99LC2.
PeptideAtlasiQ99LC2.
PRIDEiQ99LC2.

PTM databases

iPTMnetiQ99LC2.
PhosphoSiteiQ99LC2.

Expressioni

Gene expression databases

BgeeiQ99LC2.
ExpressionAtlasiQ99LC2. baseline and differential.
GenevisibleiQ99LC2. MM.

Interactioni

Subunit structurei

Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). Interacts directly with CSTF3. Interacts with BARD1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212117. 1 interaction.
IntActiQ99LC2. 1 interaction.
MINTiMINT-4124130.
STRINGi10090.ENSMUSP00000112076.

Structurei

3D structure databases

ProteinModelPortaliQ99LC2.
SMRiQ99LC2. Positions 8-59, 104-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati106 – 14540WD 1Add
BLAST
Repeati171 – 21040WD 2Add
BLAST
Repeati215 – 25440WD 3Add
BLAST
Repeati260 – 30142WD 4Add
BLAST
Repeati303 – 34341WD 5Add
BLAST
Repeati395 – 43137WD 6Add
BLAST

Domaini

The WD6 domain is required for interaction with BARD1. WD domains are responsible for interaction with CSTF3 (By similarity).By similarity
N-terminus mediates homodimerization.By similarity

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0640. Eukaryota.
ENOG410XPWJ. LUCA.
GeneTreeiENSGT00840000129765.
HOGENOMiHOG000234077.
HOVERGENiHBG051144.
InParanoidiQ99LC2.
KOiK14406.
OMAiWELSTNR.
PhylomeDBiQ99LC2.
TreeFamiTF314234.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032028. CSTF1_dimer.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16699. CSTF1_dimer. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL
60 70 80 90 100
LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE
110 120 130 140 150
TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV
160 170 180 190 200
MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF
210 220 230 240 250
DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ
260 270 280 290 300
CFVSCNPQDQ HTDAICSVNY NPSANMYVTG SKDGCIKLWD GVSNRCITTF
310 320 330 340 350
EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS
360 370 380 390 400
GRQVHRTQAV FNHTEDYILL PDERTISLCC WDSRTAERRN LLSLGHNNIV
410 420 430
RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT D
Length:431
Mass (Da):48,382
Last modified:June 1, 2001 - v1
Checksum:i8BD7BEFE422824D2
GO

Sequence cautioni

The sequence BAB27929.1 differs from that shown. Reason: Frameshift at position 314. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011943 mRNA. Translation: BAB27929.1. Frameshift.
AK050686 mRNA. Translation: BAC34379.1.
AK078667 mRNA. Translation: BAC37353.1.
AK145001 mRNA. Translation: BAE26180.1.
BC003440 mRNA. Translation: AAH03440.1.
CCDSiCCDS17130.1.
RefSeqiNP_077161.1. NM_024199.2.
XP_006500135.2. XM_006500072.2.
UniGeneiMm.26944.

Genome annotation databases

EnsembliENSMUST00000116375; ENSMUSP00000112076; ENSMUSG00000027498.
GeneIDi67337.
KEGGimmu:67337.
UCSCiuc008ocp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011943 mRNA. Translation: BAB27929.1. Frameshift.
AK050686 mRNA. Translation: BAC34379.1.
AK078667 mRNA. Translation: BAC37353.1.
AK145001 mRNA. Translation: BAE26180.1.
BC003440 mRNA. Translation: AAH03440.1.
CCDSiCCDS17130.1.
RefSeqiNP_077161.1. NM_024199.2.
XP_006500135.2. XM_006500072.2.
UniGeneiMm.26944.

3D structure databases

ProteinModelPortaliQ99LC2.
SMRiQ99LC2. Positions 8-59, 104-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212117. 1 interaction.
IntActiQ99LC2. 1 interaction.
MINTiMINT-4124130.
STRINGi10090.ENSMUSP00000112076.

PTM databases

iPTMnetiQ99LC2.
PhosphoSiteiQ99LC2.

Proteomic databases

EPDiQ99LC2.
MaxQBiQ99LC2.
PaxDbiQ99LC2.
PeptideAtlasiQ99LC2.
PRIDEiQ99LC2.

Protocols and materials databases

DNASUi67337.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000116375; ENSMUSP00000112076; ENSMUSG00000027498.
GeneIDi67337.
KEGGimmu:67337.
UCSCiuc008ocp.1. mouse.

Organism-specific databases

CTDi1477.
MGIiMGI:1914587. Cstf1.

Phylogenomic databases

eggNOGiKOG0640. Eukaryota.
ENOG410XPWJ. LUCA.
GeneTreeiENSGT00840000129765.
HOGENOMiHOG000234077.
HOVERGENiHBG051144.
InParanoidiQ99LC2.
KOiK14406.
OMAiWELSTNR.
PhylomeDBiQ99LC2.
TreeFamiTF314234.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-77595. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

PROiQ99LC2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LC2.
ExpressionAtlasiQ99LC2. baseline and differential.
GenevisibleiQ99LC2. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032028. CSTF1_dimer.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16699. CSTF1_dimer. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Egg, Embryo and Mammary gland.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiCSTF1_MOUSE
AccessioniPrimary (citable) accession number: Q99LC2
Secondary accession number(s): Q3UMB8, Q8BJW1, Q9CSU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.