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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

  • CTD phosphatase activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  • mRNA polyadenylation Source: UniProtKB
  • termination of RNA polymerase II transcription Source: GO_Central

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processmRNA processing

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.
SIGNORiQ9NP77.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000160075.11.
HGNCiHGNC:25016. SSU72.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12C → S: Abolishes phosphatase activity. 1 Publication1

Organism-specific databases

DisGeNETi29101.
OpenTargetsiENSG00000160075.
PharmGKBiPA142670866.

Chemistry databases

ChEMBLiCHEMBL3317331.

Polymorphism and mutation databases

BioMutaiSSU72.
DMDMi74752877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003300121 – 194RNA polymerase II subunit A C-terminal domain phosphatase SSU72Add BLAST194

Proteomic databases

EPDiQ9NP77.
MaxQBiQ9NP77.
PaxDbiQ9NP77.
PeptideAtlasiQ9NP77.
PRIDEiQ9NP77.

PTM databases

DEPODiQ9NP77.
iPTMnetiQ9NP77.
PhosphoSitePlusiQ9NP77.

Expressioni

Gene expression databases

BgeeiENSG00000160075.
CleanExiHS_SSU72.
GenevisibleiQ9NP77. HS.

Organism-specific databases

HPAiHPA069290.
HPA070604.

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi118869. 44 interactors.
CORUMiQ9NP77.
DIPiDIP-53666N.
IntActiQ9NP77. 10 interactors.
MINTiMINT-3071462.
STRINGi9606.ENSP00000291386.

Chemistry databases

BindingDBiQ9NP77.

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 17Combined sources11
Helixi18 – 28Combined sources11
Beta strandi32 – 37Combined sources6
Beta strandi39 – 44Combined sources6
Beta strandi53 – 55Combined sources3
Helixi61 – 78Combined sources18
Helixi81 – 89Combined sources9
Helixi98 – 100Combined sources3
Beta strandi106 – 112Combined sources7
Helixi113 – 125Combined sources13
Beta strandi133 – 139Combined sources7
Helixi145 – 164Combined sources20
Helixi168 – 183Combined sources16
Beta strandi187 – 193Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NP77.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili160 – 186Sequence analysisAdd BLAST27

Sequence similaritiesi

Belongs to the SSU72 phosphatase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2424. Eukaryota.
COG5211. LUCA.
GeneTreeiENSGT00390000010165.
HOGENOMiHOG000183445.
HOVERGENiHBG059831.
InParanoidiQ9NP77.
KOiK15544.
OMAiNRRIKKC.
OrthoDBiEOG091G0MLX.
PhylomeDBiQ9NP77.
TreeFamiTF300194.

Family and domain databases

InterProiView protein in InterPro
IPR006811. RNA_pol_II_suA.
PANTHERiPTHR20383. PTHR20383. 1 hit.
PfamiView protein in Pfam
PF04722. Ssu72. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti182 – 183KS → RV in AAK07538 (Ref. 3) Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03300577 – 194TQNGI…TVCFY → PSGLPFKNPPCGPPWKVLRV ARAQEACHPVQCTHWLLCLC ESLVSIPGARRIVHGLVPVP PMAVGVVRRTDTVWGSP in isoform 2. CuratedAdd BLAST118

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. No translation available.
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.4. human. [Q9NP77-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSSU72_HUMAN
AccessioniPrimary (citable) accession number: Q9NP77
Secondary accession number(s): Q9BZS6, Q9H933
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2000
Last modified: November 22, 2017
This is version 133 of the entry and version 1 of the sequence. See 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