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Q9NP77 (SSU72_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Short name=CTD phosphatase SSU72
EC=3.1.3.16
Gene names
Name:SSU72
ORF Names:HSPC182, PNAS-120
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.11

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.10 Ref.11

Subunit structure

Interacts with RB1. Interacts with GTF2B and CD226. Interacts with SYMPK. Ref.1 Ref.10 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly in the cytosol.

Sequence similarities

Belongs to the SSU72 phosphatase family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay Ref.10. Source: UniProtKB

mRNA polyadenylation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionCTD phosphatase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NP77-1)

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.
Isoform 2 (identifier: Q9NP77-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-194: TQNGILHMLD...RTFLHTVCFY → PSGLPFKNPP...RRTDTVWGSP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194RNA polymerase II subunit A C-terminal domain phosphatase SSU72
PRO_0000330012

Regions

Coiled coil160 – 18627 Potential

Natural variations

Alternative sequence77 – 194118TQNGI…TVCFY → PSGLPFKNPPCGPPWKVLRV ARAQEACHPVQCTHWLLCLC ESLVSIPGARRIVHGLVPVP PMAVGVVRRTDTVWGSP in isoform 2.
VSP_033005

Experimental info

Mutagenesis121C → S: Abolishes phosphatase activity. Ref.1
Sequence conflict182 – 1832KS → RV in AAK07538. Ref.3

Secondary structure

........................... 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: CA3A3157A2388A77

FASTA19422,574
        10         20         30         40         50         60 
MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT 

        70         80         90        100        110        120 
YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN CKDLFDLILT CEERVYDQVV 

       130        140        150        160        170        180 
EDLNSREQET CQPVHVVNVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE 

       190 
EKSGRTFLHT VCFY 

« Hide

Isoform 2 [UniParc].

Checksum: 5451647A082E9559
Show »

FASTA15316,931

References

« Hide 'large scale' references
[1]"Conserved and specific functions of mammalian ssu72."
St Pierre B., Liu X., Kha L.C., Zhu X., Ryan O., Jiang Z., Zacksenhaus E.
Nucleic Acids Res. 33:464-477(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1; GTF2B AND CD226, MUTAGENESIS OF CYS-12.
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[3]"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Promyelocytic leukemia.
[4]"Full-length sequencing of 100 cDNA clones from human adult skeletal muscle."
Stanchi F., Lanfranchi G.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta, Teratocarcinoma and Tongue.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Muscle.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex."
Xiang K., Nagaike T., Xiang S., Kilic T., Beh M.M., Manley J.L., Tong L.
Nature 467:729-733(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SYMPK, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SYMPK.
[11]"An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72."
Xiang K., Manley J.L., Tong L.
Genes Dev. 26:2265-2270(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYMPK, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SYMPK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF161530 mRNA. Translation: AAF29145.1.
AF277178 mRNA. Translation: AAK07538.1.
AJ276409 mRNA. Translation: CAC81713.1.
AK001809 mRNA. Translation: BAA91921.1.
AK023110 mRNA. Translation: BAB14410.1.
AK291324 mRNA. Translation: BAF84013.1.
AL645728 Genomic DNA. Translation: CAI22945.1.
AL645728 Genomic DNA. Translation: CAI22947.1.
CH471183 Genomic DNA. Translation: EAW56182.1.
CH471183 Genomic DNA. Translation: EAW56183.1.
BC008070 mRNA. Translation: AAH08070.1.
RefSeqNP_054907.1. NM_014188.2.
UniGeneHs.30026.
Hs.549751.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O2QX-ray2.40B/E1-194[»]
3O2SX-ray2.50B1-194[»]
4H3HX-ray2.20B/E1-194[»]
4H3KX-ray2.00B/E1-194[»]
ProteinModelPortalQ9NP77.
SMRQ9NP77. Positions 5-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118869. 24 interactions.
DIPDIP-53666N.
IntActQ9NP77. 7 interactions.
MINTMINT-3071462.
STRING9606.ENSP00000291386.

PTM databases

PhosphoSiteQ9NP77.

Polymorphism databases

DMDM74752877.

Proteomic databases

PaxDbQ9NP77.
PRIDEQ9NP77.

Protocols and materials databases

DNASU29101.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291386; ENSP00000291386; ENSG00000160075. [Q9NP77-1]
ENST00000359060; ENSP00000351955; ENSG00000160075. [Q9NP77-2]
GeneID29101.
KEGGhsa:29101.
UCSCuc001agd.3. human. [Q9NP77-1]
uc001age.1. human. [Q9NP77-2]

Organism-specific databases

CTD29101.
GeneCardsGC01M001477.
HGNCHGNC:25016. SSU72.
neXtProtNX_Q9NP77.
PharmGKBPA142670866.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5211.
HOGENOMHOG000183445.
HOVERGENHBG059831.
InParanoidQ9NP77.
KOK15544.
OMANRPFLHT.
OrthoDBEOG7C2R2M.
PhylomeDBQ9NP77.
TreeFamTF300194.

Gene expression databases

BgeeQ9NP77.
CleanExHS_SSU72.
GenevestigatorQ9NP77.

Family and domain databases

InterProIPR006811. RNA_pol_II_suA.
[Graphical view]
PANTHERPTHR20383. PTHR20383. 1 hit.
PfamPF04722. Ssu72. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSSU72. human.
EvolutionaryTraceQ9NP77.
GenomeRNAi29101.
NextBio52137.
PROQ9NP77.

Entry information

Entry nameSSU72_HUMAN
AccessionPrimary (citable) accession number: Q9NP77
Secondary accession number(s): Q9BZS6, Q9H933
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM