ID   SSU72_MOUSE             Reviewed;         194 AA.
AC   Q9CY97; Q3UF99; Q91YL1; Q9DB51;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE            Short=CTD phosphatase SSU72;
DE            EC=3.1.3.16;
GN   Name=Ssu72;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15659578; DOI=10.1093/nar/gki171;
RA   St Pierre B., Liu X., Kha L.C., Zhu X., Ryan O., Jiang Z., Zacksenhaus E.;
RT   "Conserved and specific functions of mammalian ssu72.";
RL   Nucleic Acids Res. 33:464-477(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of
CC       the C-terminal domain of RNA polymerase II. Plays a role in RNA
CC       processing and termination. Plays a role in pre-mRNA polyadenylation
CC       via its interaction with SYMPK. {ECO:0000269|PubMed:15659578}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SUBUNIT: Interacts with GTF2B (via C-terminus); this interaction is
CC       inhibited by SYMPK. Interacts with RB1. Interacts with CD226. Interacts
CC       with SYMPK. {ECO:0000250|UniProtKB:Q9NP77}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly in the cytosol. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CY97-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CY97-2; Sequence=VSP_033006;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain. Expressed at low
CC       level in most tissues. {ECO:0000269|PubMed:15659578}.
CC   -!- DEVELOPMENTAL STAGE: At 10.5 dpc, low level expression detected
CC       throughout the embryo with relative accumulation in spinal cord and
CC       brain folds. At 13.5 dpc, highly expressed in the CNS both in the
CC       ventricular (mitotic) and marginal (post mitotic) zones, in the PNS in
CC       dorsal root and trigeminal ganglia, and the developing gut. During
CC       development, expression in the central nervous system and peripheral
CC       nervous system persists, and expression in the intestine is further
CC       induced. Expression in the intestine is observed throughout the mucosal
CC       villi, which contains epithelial cells and other cell types. High
CC       expression is also detected in the lens. No expression is seen in other
CC       tissues such as liver, lung, bone, cardiac and skeletal muscles.
CC       {ECO:0000269|PubMed:15659578}.
CC   -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR   EMBL; AK005220; BAB23890.1; -; mRNA.
DR   EMBL; AK019168; BAB31582.1; -; mRNA.
DR   EMBL; AK148783; BAE28662.1; -; mRNA.
DR   EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016544; AAH16544.1; -; mRNA.
DR   CCDS; CCDS19036.1; -. [Q9CY97-1]
DR   RefSeq; NP_081175.2; NM_026899.3. [Q9CY97-1]
DR   AlphaFoldDB; Q9CY97; -.
DR   SMR; Q9CY97; -.
DR   STRING; 10090.ENSMUSP00000030905; -.
DR   iPTMnet; Q9CY97; -.
DR   PhosphoSitePlus; Q9CY97; -.
DR   SwissPalm; Q9CY97; -.
DR   EPD; Q9CY97; -.
DR   MaxQB; Q9CY97; -.
DR   PaxDb; 10090-ENSMUSP00000030905; -.
DR   PeptideAtlas; Q9CY97; -.
DR   ProteomicsDB; 254566; -. [Q9CY97-1]
DR   ProteomicsDB; 254567; -. [Q9CY97-2]
DR   Pumba; Q9CY97; -.
DR   Antibodypedia; 26440; 148 antibodies from 21 providers.
DR   DNASU; 68991; -.
DR   Ensembl; ENSMUST00000030905.9; ENSMUSP00000030905.3; ENSMUSG00000029038.10. [Q9CY97-1]
DR   Ensembl; ENSMUST00000105595.2; ENSMUSP00000101220.2; ENSMUSG00000029038.10. [Q9CY97-2]
DR   GeneID; 68991; -.
DR   KEGG; mmu:68991; -.
DR   UCSC; uc008wek.2; mouse. [Q9CY97-2]
DR   UCSC; uc008wel.2; mouse. [Q9CY97-1]
DR   AGR; MGI:1916241; -.
DR   CTD; 29101; -.
DR   MGI; MGI:1916241; Ssu72.
DR   VEuPathDB; HostDB:ENSMUSG00000029038; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   GeneTree; ENSGT00390000010165; -.
DR   HOGENOM; CLU_062463_2_1_1; -.
DR   InParanoid; Q9CY97; -.
DR   OMA; PNCYEFG; -.
DR   OrthoDB; 63608at2759; -.
DR   PhylomeDB; Q9CY97; -.
DR   TreeFam; TF300194; -.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   BioGRID-ORCS; 68991; 31 hits in 78 CRISPR screens.
DR   ChiTaRS; Ssu72; mouse.
DR   PRO; PR:Q9CY97; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9CY97; Protein.
DR   Bgee; ENSMUSG00000029038; Expressed in granulocyte and 269 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; ISS:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISO:MGI.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR006811; RNA_pol_II_suA.
DR   PANTHER; PTHR20383; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR   PANTHER; PTHR20383:SF11; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE SSU72; 1.
DR   Pfam; PF04722; Ssu72; 1.
DR   Genevisible; Q9CY97; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Hydrolase; mRNA processing;
KW   Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..194
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000330013"
FT   COILED          160..187
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         162..194
FT                   /note="IQHTEDMENEIDELLQEFEEKSGRAFLHTVCFY -> VSLSSWVLLGLLIAT
FT                   YKNKIK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033006"
FT   CONFLICT        59
FT                   /note="T -> P (in Ref. 1; BAB23890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22517 MW;  51B89AC7BCD79486 CRC64;
     MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT
     YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN CTDLFDLILT CEERVYDQVV
     EDLNSREQET CQPVHVVNVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE
     EKSGRAFLHT VCFY
//