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Protein

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Gene

SSU72

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.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

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

Organism-specific databases

HGNCiHGNC:25016. SSU72.

Subcellular locationi

  1. Nucleus
  2. Cytoplasm

  3. Note: Predominantly in the cytosol.

GO - Cellular componenti

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

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.

Polymorphism and mutation databases

BioMutaiSSU72.
DMDMi74752877.

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

DEPODiQ9NP77.
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 – 1711Combined sources
Helixi18 – 2811Combined sources
Beta strandi32 – 376Combined sources
Beta strandi39 – 446Combined sources
Beta strandi53 – 553Combined sources
Helixi61 – 7818Combined sources
Helixi81 – 899Combined sources
Helixi98 – 1003Combined sources
Beta strandi106 – 1127Combined sources
Helixi113 – 12513Combined sources
Beta strandi133 – 1397Combined sources
Helixi145 – 16420Combined sources
Helixi168 – 18316Combined sources
Beta strandi187 – 1937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010165.
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. AlignAdd to basket

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

        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
CKDLFDLILT CEERVYDQVV EDLNSREQET CQPVHVVNVD IQDNHEEATL
160 170 180 190
GAFLICELCQ CIQHTEDMEN EIDELLQEFE EKSGRTFLHT VCFY
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 (Ref. 3) Curated

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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiSSU72.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

PTM databases

DEPODiQ9NP77.
PhosphoSiteiQ9NP77.

Polymorphism and mutation databases

BioMutaiSSU72.
DMDMi74752877.

Proteomic databases

MaxQBiQ9NP77.
PaxDbiQ9NP77.
PRIDEiQ9NP77.

Protocols and materials databases

DNASUi29101.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi29101.
GeneCardsiGC01M001477.
HGNCiHGNC:25016. SSU72.
neXtProtiNX_Q9NP77.
PharmGKBiPA142670866.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5211.
GeneTreeiENSGT00390000010165.
HOGENOMiHOG000183445.
HOVERGENiHBG059831.
InParanoidiQ9NP77.
KOiK15544.
OMAiNRPFLHT.
OrthoDBiEOG7C2R2M.
PhylomeDBiQ9NP77.
TreeFamiTF300194.

Miscellaneous databases

ChiTaRSiSSU72. human.
EvolutionaryTraceiQ9NP77.
GenomeRNAii29101.
NextBioi52137.
PROiQ9NP77.

Gene expression databases

BgeeiQ9NP77.
CleanExiHS_SSU72.
GenevestigatoriQ9NP77.

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. 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: April 29, 2015
This is version 112 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

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.