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Q9NP77

- SSU72_HUMAN

UniProt

Q9NP77 - SSU72_HUMAN

Protein

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Gene

SSU72

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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.3 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.2 Publications

    GO - Molecular functioni

    1. CTD phosphatase activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

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

    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
    ORF Names:HSPC182, PNAS-120
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25016. SSU72.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly in the cytosol.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121C → S: Abolishes phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670866.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194RNA polymerase II subunit A C-terminal domain phosphatase SSU72PRO_0000330012Add
    BLAST

    Proteomic databases

    MaxQBiQ9NP77.
    PaxDbiQ9NP77.
    PRIDEiQ9NP77.

    PTM databases

    PhosphoSiteiQ9NP77.

    Expressioni

    Gene expression databases

    BgeeiQ9NP77.
    CleanExiHS_SSU72.
    GenevestigatoriQ9NP77.

    Interactioni

    Subunit structurei

    Interacts with RB1. Interacts with GTF2B and CD226. Interacts with SYMPK.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD21O602169EBI-2515416,EBI-80739
    STAG2Q8N3U44EBI-2515416,EBI-1057252

    Protein-protein interaction databases

    BioGridi118869. 26 interactions.
    DIPiDIP-53666N.
    IntActiQ9NP77. 7 interactions.
    MINTiMINT-3071462.
    STRINGi9606.ENSP00000291386.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 1711
    Helixi18 – 2811
    Beta strandi32 – 376
    Beta strandi39 – 446
    Beta strandi53 – 553
    Helixi61 – 7818
    Helixi81 – 899
    Helixi98 – 1003
    Beta strandi106 – 1127
    Helixi113 – 12513
    Beta strandi133 – 1397
    Helixi145 – 16420
    Helixi168 – 18316
    Beta strandi187 – 1937

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O2QX-ray2.40B/E1-194[»]
    3O2SX-ray2.50B1-194[»]
    4H3HX-ray2.20B/E1-194[»]
    4H3KX-ray2.00B/E1-194[»]
    ProteinModelPortaliQ9NP77.
    SMRiQ9NP77. Positions 5-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NP77.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili160 – 18627Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SSU72 phosphatase family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5211.
    HOGENOMiHOG000183445.
    HOVERGENiHBG059831.
    InParanoidiQ9NP77.
    KOiK15544.
    OMAiNRPFLHT.
    OrthoDBiEOG7C2R2M.
    PhylomeDBiQ9NP77.
    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: Q9NP77-1) [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

    MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD    50
    KPNVYDFKTT YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN 100
    CKDLFDLILT CEERVYDQVV EDLNSREQET CQPVHVVNVD IQDNHEEATL 150
    GAFLICELCQ CIQHTEDMEN EIDELLQEFE EKSGRTFLHT VCFY 194
    Length:194
    Mass (Da):22,574
    Last modified:October 1, 2000 - v1
    Checksum:iCA3A3157A2388A77
    GO
    Isoform 2 (identifier: Q9NP77-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:153
    Mass (Da):16,931
    Checksum:i5451647A082E9559
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1832KS → RV in AAK07538. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei77 – 194118TQNGI…TVCFY → PSGLPFKNPPCGPPWKVLRV ARAQEACHPVQCTHWLLCLC ESLVSIPGARRIVHGLVPVP PMAVGVVRRTDTVWGSP in isoform 2. CuratedVSP_033005Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32.1. [Q9NP77-1]
    RefSeqiNP_054907.1. NM_014188.2. [Q9NP77-1]
    UniGeneiHs.30026.
    Hs.549751.
    Hs.732583.

    Genome annotation databases

    EnsembliENST00000291386; ENSP00000291386; ENSG00000160075. [Q9NP77-1]
    ENST00000359060; ENSP00000351955; ENSG00000160075. [Q9NP77-2]
    GeneIDi29101.
    KEGGihsa:29101.
    UCSCiuc001agd.3. human. [Q9NP77-1]
    uc001age.1. human. [Q9NP77-2]

    Polymorphism databases

    DMDMi74752877.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32.1. [Q9NP77-1 ]
    RefSeqi NP_054907.1. NM_014188.2. [Q9NP77-1 ]
    UniGenei Hs.30026.
    Hs.549751.
    Hs.732583.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O2Q X-ray 2.40 B/E 1-194 [» ]
    3O2S X-ray 2.50 B 1-194 [» ]
    4H3H X-ray 2.20 B/E 1-194 [» ]
    4H3K X-ray 2.00 B/E 1-194 [» ]
    ProteinModelPortali Q9NP77.
    SMRi Q9NP77. Positions 5-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118869. 26 interactions.
    DIPi DIP-53666N.
    IntActi Q9NP77. 7 interactions.
    MINTi MINT-3071462.
    STRINGi 9606.ENSP00000291386.

    PTM databases

    PhosphoSitei Q9NP77.

    Polymorphism databases

    DMDMi 74752877.

    Proteomic databases

    MaxQBi Q9NP77.
    PaxDbi Q9NP77.
    PRIDEi Q9NP77.

    Protocols and materials databases

    DNASUi 29101.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000291386 ; ENSP00000291386 ; ENSG00000160075 . [Q9NP77-1 ]
    ENST00000359060 ; ENSP00000351955 ; ENSG00000160075 . [Q9NP77-2 ]
    GeneIDi 29101.
    KEGGi hsa:29101.
    UCSCi uc001agd.3. human. [Q9NP77-1 ]
    uc001age.1. human. [Q9NP77-2 ]

    Organism-specific databases

    CTDi 29101.
    GeneCardsi GC01M001477.
    HGNCi HGNC:25016. SSU72.
    neXtProti NX_Q9NP77.
    PharmGKBi PA142670866.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5211.
    HOGENOMi HOG000183445.
    HOVERGENi HBG059831.
    InParanoidi Q9NP77.
    KOi K15544.
    OMAi NRPFLHT.
    OrthoDBi EOG7C2R2M.
    PhylomeDBi Q9NP77.
    TreeFami TF300194.

    Miscellaneous databases

    ChiTaRSi SSU72. human.
    EvolutionaryTracei Q9NP77.
    GenomeRNAii 29101.
    NextBioi 52137.
    PROi Q9NP77.

    Gene expression databases

    Bgeei Q9NP77.
    CleanExi HS_SSU72.
    Genevestigatori Q9NP77.

    Family and domain databases

    InterProi IPR006811. RNA_pol_II_suA.
    [Graphical view ]
    PANTHERi PTHR20383. PTHR20383. 1 hit.
    Pfami PF04722. Ssu72. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiSSU72_HUMAN
    AccessioniPrimary (citable) accession number: Q9NP77
    Secondary accession number(s): Q9BZS6, Q9H933
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3