ID   CSTFT_HUMAN             Reviewed;         616 AA.
AC   Q9H0L4; B2RAR9; O75174; Q53HK6; Q7LGE8; Q8N6T1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Cleavage stimulation factor subunit 2 tau variant;
DE   AltName: Full=CF-1 64 kDa subunit tau variant;
DE   AltName: Full=Cleavage stimulation factor 64 kDa subunit tau variant;
DE            Short=CSTF 64 kDa subunit tau variant;
DE   AltName: Full=TauCstF-64;
GN   Name=CSTF2T; Synonyms=KIAA0689;
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].
RC   TISSUE=Testis;
RX   PubMed=12408968; DOI=10.1016/s0888-7543(02)96862-x;
RA   Dass B., McDaniel L., Schultz R.A., Attaya E., MacDonald C.C.;
RT   "The gene CSTF2T, encoding the human variant CstF-64 polyadenylation
RT   protein CstF-64, lacks introns and may be associated with male sterility.";
RL   Genomics 80:509-514(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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 MRNA].
RC   TISSUE=Coronary artery;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-616.
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND SER-563, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: May play a significant role in AAUAAA-independent mRNA
CC       polyadenylation in germ cells. Directly involved in the binding to pre-
CC       mRNAs (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9H0L4; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-747012, EBI-357530;
CC       Q9H0L4; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-747012, EBI-12811889;
CC       Q9H0L4; Q9UMD9: COL17A1; NbExp=3; IntAct=EBI-747012, EBI-2528742;
CC       Q9H0L4; P78358: CTAG1B; NbExp=3; IntAct=EBI-747012, EBI-1188472;
CC       Q9H0L4; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-747012, EBI-751587;
CC       Q9H0L4; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-747012, EBI-12193763;
CC       Q9H0L4; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-747012, EBI-12018822;
CC       Q9H0L4; Q9P0K8: FOXJ2; NbExp=3; IntAct=EBI-747012, EBI-2869608;
CC       Q9H0L4; O14964: HGS; NbExp=3; IntAct=EBI-747012, EBI-740220;
CC       Q9H0L4; Q14847-2: LASP1; NbExp=3; IntAct=EBI-747012, EBI-9088686;
CC       Q9H0L4; Q96KN3: PKNOX2; NbExp=5; IntAct=EBI-747012, EBI-2692890;
CC       Q9H0L4; Q9H7B4: SMYD3; NbExp=3; IntAct=EBI-747012, EBI-347919;
CC       Q9H0L4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-747012, EBI-11959123;
CC       Q9H0L4; Q8IWL8: STH; NbExp=5; IntAct=EBI-747012, EBI-12843506;
CC       Q9H0L4; Q08117-2: TLE5; NbExp=6; IntAct=EBI-747012, EBI-11741437;
CC       Q9H0L4; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-747012, EBI-12815137;
CC       Q9H0L4; Q9UMX0: UBQLN1; NbExp=7; IntAct=EBI-747012, EBI-741480;
CC       Q9H0L4; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-747012, EBI-10173939;
CC       Q9H0L4; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-747012, EBI-947187;
CC       Q9H0L4; A0A1U9X8X8; NbExp=3; IntAct=EBI-747012, EBI-17234977;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; AY130299; AAN05429.1; -; mRNA.
DR   EMBL; AL136747; CAB66681.1; -; mRNA.
DR   EMBL; AK222574; BAD96294.1; -; mRNA.
DR   EMBL; AK314318; BAG36966.1; -; mRNA.
DR   EMBL; CH471083; EAW54142.1; -; Genomic_DNA.
DR   EMBL; BC028239; AAH28239.1; -; mRNA.
DR   EMBL; AB014589; BAA31664.1; -; mRNA.
DR   CCDS; CCDS7245.1; -.
DR   RefSeq; NP_056050.1; NM_015235.2.
DR   AlphaFoldDB; Q9H0L4; -.
DR   SMR; Q9H0L4; -.
DR   BioGRID; 116881; 168.
DR   ComplexPortal; CPX-2703; Cleavage stimulation factor complex, CSTF2T variant.
DR   IntAct; Q9H0L4; 43.
DR   MINT; Q9H0L4; -.
DR   STRING; 9606.ENSP00000332444; -.
DR   GlyCosmos; Q9H0L4; 2 sites, 1 glycan.
DR   GlyGen; Q9H0L4; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H0L4; -.
DR   MetOSite; Q9H0L4; -.
DR   PhosphoSitePlus; Q9H0L4; -.
DR   BioMuta; CSTF2T; -.
DR   DMDM; 71153234; -.
DR   REPRODUCTION-2DPAGE; IPI00550906; -.
DR   EPD; Q9H0L4; -.
DR   jPOST; Q9H0L4; -.
DR   MassIVE; Q9H0L4; -.
DR   MaxQB; Q9H0L4; -.
DR   PaxDb; 9606-ENSP00000332444; -.
DR   PeptideAtlas; Q9H0L4; -.
DR   ProteomicsDB; 80293; -.
DR   Pumba; Q9H0L4; -.
DR   Antibodypedia; 27941; 234 antibodies from 28 providers.
DR   DNASU; 23283; -.
DR   Ensembl; ENST00000331173.6; ENSP00000332444.4; ENSG00000177613.9.
DR   GeneID; 23283; -.
DR   KEGG; hsa:23283; -.
DR   MANE-Select; ENST00000331173.6; ENSP00000332444.4; NM_015235.3; NP_056050.1.
DR   UCSC; uc001jjp.4; human.
DR   AGR; HGNC:17086; -.
DR   CTD; 23283; -.
DR   DisGeNET; 23283; -.
DR   GeneCards; CSTF2T; -.
DR   HGNC; HGNC:17086; CSTF2T.
DR   HPA; ENSG00000177613; Low tissue specificity.
DR   MIM; 611968; gene.
DR   neXtProt; NX_Q9H0L4; -.
DR   OpenTargets; ENSG00000177613; -.
DR   PharmGKB; PA134933809; -.
DR   VEuPathDB; HostDB:ENSG00000177613; -.
DR   eggNOG; KOG0108; Eukaryota.
DR   GeneTree; ENSGT00940000161661; -.
DR   HOGENOM; CLU_028601_3_1_1; -.
DR   InParanoid; Q9H0L4; -.
DR   OMA; GMQGASK; -.
DR   OrthoDB; 179465at2759; -.
DR   PhylomeDB; Q9H0L4; -.
DR   TreeFam; TF314948; -.
DR   PathwayCommons; Q9H0L4; -.
DR   Reactome; R-HSA-72187; mRNA 3'-end processing.
DR   Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR   SignaLink; Q9H0L4; -.
DR   BioGRID-ORCS; 23283; 11 hits in 1161 CRISPR screens.
DR   GeneWiki; CSTF2T; -.
DR   GenomeRNAi; 23283; -.
DR   Pharos; Q9H0L4; Tbio.
DR   PRO; PR:Q9H0L4; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9H0L4; Protein.
DR   Bgee; ENSG00000177613; Expressed in endothelial cell and 211 other cell types or tissues.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR   CDD; cd12671; RRM_CSTF2_CSTF2T; 1.
DR   Gene3D; 1.25.40.630; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.20.70; Transcription termination and cleavage factor, C-terminal domain; 1.
DR   InterPro; IPR025742; CSTF2_hinge.
DR   InterPro; IPR026896; CSTF_C.
DR   InterPro; IPR038192; CSTF_C_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR45735; CLEAVAGE STIMULATION FACTOR SUBUNIT 2; 1.
DR   PANTHER; PTHR45735:SF3; CLEAVAGE STIMULATION FACTOR SUBUNIT 2 TAU VARIANT; 1.
DR   Pfam; PF14327; CSTF2_hinge; 1.
DR   Pfam; PF14304; CSTF_C; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q9H0L4; HS.
PE   1: Evidence at protein level;
KW   mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..616
FT                   /note="Cleavage stimulation factor subunit 2 tau variant"
FT                   /id="PRO_0000081534"
FT   DOMAIN          16..94
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REPEAT          418..422
FT                   /note="1-1"
FT   REPEAT          423..427
FT                   /note="1-2; approximate"
FT   REPEAT          428..432
FT                   /note="1-3; approximate"
FT   REPEAT          433..437
FT                   /note="1-4; approximate"
FT   REPEAT          438..442
FT                   /note="1-5; approximate"
FT   REPEAT          443..447
FT                   /note="1-6"
FT   REPEAT          448..452
FT                   /note="1-7; approximate"
FT   REPEAT          453..457
FT                   /note="1-8; approximate"
FT   REPEAT          458..462
FT                   /note="1-9; approximate"
FT   REPEAT          505..509
FT                   /note="2-1"
FT   REPEAT          510..514
FT                   /note="2-2"
FT   REPEAT          515..519
FT                   /note="2-3"
FT   REPEAT          520..524
FT                   /note="2-4"
FT   REPEAT          525..529
FT                   /note="2-5; approximate"
FT   REPEAT          530..534
FT                   /note="2-6"
FT   REPEAT          535..539
FT                   /note="2-7; approximate"
FT   REPEAT          540..544
FT                   /note="2-8; approximate"
FT   REPEAT          545..549
FT                   /note="2-9; approximate"
FT   REGION          203..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..462
FT                   /note="9 X 5 AA tandem repeats of M-E-T-R-[AG]"
FT   REGION          505..549
FT                   /note="9 X 5 AA tandem repeats of G-[AT]-G-[MI]-Q"
FT   REGION          542..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         320
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CONFLICT        22
FT                   /note="N -> S (in Ref. 4; BAD96294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="K -> R (in Ref. 6; AAH28239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   616 AA;  64437 MW;  916BB9B0802AC847 CRC64;
     MSSLAVRDPA MDRSLRSVFV GNIPYEATEE QLKDIFSEVG SVVSFRLVYD RETGKPKGYG
     FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGPAAPI IDSPYGDPID
     PEDAPESITR AVASLPPEQM FELMKQMKLC VQNSHQEARN MLLQNPQLAY ALLQAQVVMR
     IMDPEIALKI LHRKIHVTPL IPGKSQSVSV SGPGPGPGPG LCPGPNVLLN QQNPPAPQPQ
     HLARRPVKDI PPLMQTPIQG GIPAPGPIPA AVPGAGPGSL TPGGAMQPQL GMPGVGPVPL
     ERGQVQMSDP RAPIPRGPVT PGGLPPRGLL GDAPNDPRGG TLLSVTGEVE PRGYLGPPHQ
     GPPMHHASGH DTRGPSSHEM RGGPLGDPRL LIGEPRGPMI DQRGLPMDGR GGRDSRAMET
     RAMETEVLET RVMERRGMET CAMETRGMEA RGMDARGLEM RGPVPSSRGP MTGGIQGPGP
     INIGAGGPPQ GPRQVPGISG VGNPGAGMQG TGIQGTGMQG AGIQGGGMQG AGIQGVSIQG
     GGIQGGGIQG ASKQGGSQPS SFSPGQSQVT PQDQEKAALI MQVLQLTADQ IAMLPPEQRQ
     SILILKEQIQ KSTGAS
//