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Protein

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Gene

Ssu72

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

GO - Molecular functioni

  1. CTD phosphatase activity Source: UniProtKB

GO - Biological processi

  1. dephosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  2. mRNA polyadenylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

mRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (EC:3.1.3.16)
Short name:
CTD phosphatase SSU72
Gene namesi
Name:Ssu72
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1916241. Ssu72.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: Predominantly in the cytosol.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194RNA polymerase II subunit A C-terminal domain phosphatase SSU72PRO_0000330013Add
BLAST

Proteomic databases

MaxQBiQ9CY97.
PaxDbiQ9CY97.
PRIDEiQ9CY97.

PTM databases

PhosphoSiteiQ9CY97.

Expressioni

Tissue specificityi

Highly expressed in the brain. Expressed at low level in most tissues.1 Publication

Developmental stagei

At E10.5, low level expression detected throughout the embryo with relative accumulation in spinal cord and brain folds. At E13.5, highly expressed in the CNS both in the ventricular (mitotic) and marginal (post mitotic) zones, in the PNS in dorsal root and trigeminal ganglia, and the developing gut. During development, expression in the central nervous system and peripheral nervous system persists, and expression in the intestine is further induced. Expression in the intestine is observed throughout the mucosal villi, which contains epithelial cells and other cell types. High expression is also detected in the lens. No expression is seen in other tissues such as liver, lung, bone, cardiac and skeletal muscles.1 Publication

Gene expression databases

BgeeiQ9CY97.
GenevestigatoriQ9CY97.

Interactioni

Subunit structurei

Interacts with RB1. Interacts with GTF2B and CD226. Interacts with SYMPK (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9CY97. 1 interaction.
MINTiMINT-4125924.
STRINGi10090.ENSMUSP00000030905.

Structurei

3D structure databases

ProteinModelPortaliQ9CY97.
SMRiQ9CY97. Positions 5-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili160 – 18728Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SSU72 phosphatase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5211.
GeneTreeiENSGT00390000010165.
HOGENOMiHOG000183445.
HOVERGENiHBG059831.
InParanoidiQ9CY97.
KOiK15544.
OMAiMESHAML.
OrthoDBiEOG7C2R2M.
PhylomeDBiQ9CY97.
TreeFamiTF300194.

Family and domain databases

InterProiIPR006811. RNA_pol_II_suA.
[Graphical view]
PANTHERiPTHR20383. PTHR20383. 1 hit.
PfamiPF04722. Ssu72. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CY97-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD
60 70 80 90 100
KPNVYDFKTT YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN
110 120 130 140 150
CTDLFDLILT CEERVYDQVV EDLNSREQET CQPVHVVNVD IQDNHEEATL
160 170 180 190
GAFLICELCQ CIQHTEDMEN EIDELLQEFE EKSGRAFLHT VCFY
Length:194
Mass (Da):22,517
Last modified:June 1, 2001 - v1
Checksum:i51B89AC7BCD79486
GO
Isoform 2 (identifier: Q9CY97-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: IQHTEDMENEIDELLQEFEEKSGRAFLHTVCFY → VSLSSWVLLGLLIATYKNKIK

Note: No experimental confirmation available.

Show »
Length:182
Mass (Da):20,862
Checksum:i5F3F793A72405661
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591T → P in BAB23890. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei162 – 19433IQHTE…TVCFY → VSLSSWVLLGLLIATYKNKI K in isoform 2. 1 PublicationVSP_033006Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005220 mRNA. Translation: BAB23890.1.
AK019168 mRNA. Translation: BAB31582.1.
AK148783 mRNA. Translation: BAE28662.1.
AL670236 Genomic DNA. Translation: CAM18380.1.
AL670236 Genomic DNA. Translation: CAM18381.1.
BC016544 mRNA. Translation: AAH16544.1.
CCDSiCCDS19036.1. [Q9CY97-1]
RefSeqiNP_081175.2. NM_026899.3. [Q9CY97-1]
UniGeneiMm.294770.
Mm.483261.

Genome annotation databases

EnsembliENSMUST00000030905; ENSMUSP00000030905; ENSMUSG00000029038. [Q9CY97-1]
ENSMUST00000105595; ENSMUSP00000101220; ENSMUSG00000029038. [Q9CY97-2]
GeneIDi68991.
KEGGimmu:68991.
UCSCiuc008wek.2. mouse. [Q9CY97-2]
uc008wel.2. mouse. [Q9CY97-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005220 mRNA. Translation: BAB23890.1.
AK019168 mRNA. Translation: BAB31582.1.
AK148783 mRNA. Translation: BAE28662.1.
AL670236 Genomic DNA. Translation: CAM18380.1.
AL670236 Genomic DNA. Translation: CAM18381.1.
BC016544 mRNA. Translation: AAH16544.1.
CCDSiCCDS19036.1. [Q9CY97-1]
RefSeqiNP_081175.2. NM_026899.3. [Q9CY97-1]
UniGeneiMm.294770.
Mm.483261.

3D structure databases

ProteinModelPortaliQ9CY97.
SMRiQ9CY97. Positions 5-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CY97. 1 interaction.
MINTiMINT-4125924.
STRINGi10090.ENSMUSP00000030905.

PTM databases

PhosphoSiteiQ9CY97.

Proteomic databases

MaxQBiQ9CY97.
PaxDbiQ9CY97.
PRIDEiQ9CY97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030905; ENSMUSP00000030905; ENSMUSG00000029038. [Q9CY97-1]
ENSMUST00000105595; ENSMUSP00000101220; ENSMUSG00000029038. [Q9CY97-2]
GeneIDi68991.
KEGGimmu:68991.
UCSCiuc008wek.2. mouse. [Q9CY97-2]
uc008wel.2. mouse. [Q9CY97-1]

Organism-specific databases

CTDi29101.
MGIiMGI:1916241. Ssu72.

Phylogenomic databases

eggNOGiCOG5211.
GeneTreeiENSGT00390000010165.
HOGENOMiHOG000183445.
HOVERGENiHBG059831.
InParanoidiQ9CY97.
KOiK15544.
OMAiMESHAML.
OrthoDBiEOG7C2R2M.
PhylomeDBiQ9CY97.
TreeFamiTF300194.

Miscellaneous databases

NextBioi328359.
PROiQ9CY97.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CY97.
GenevestigatoriQ9CY97.

Family and domain databases

InterProiIPR006811. RNA_pol_II_suA.
[Graphical view]
PANTHERiPTHR20383. PTHR20383. 1 hit.
PfamiPF04722. Ssu72. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo and Sympathetic ganglion.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSSU72_MOUSE
AccessioniPrimary (citable) accession number: Q9CY97
Secondary accession number(s): Q3UF99, Q91YL1, Q9DB51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 87 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

External Data

Dasty 3

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 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.