Q9NP77 (SSU72_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation 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_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	CTD phosphatase activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 194

194

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

PRO_0000330012

Regions

Coiled coil

160 – 186

27

Potential

Natural variations

Alternative sequence

77 – 194

118

TQNGI…TVCFY → PSGLPFKNPPCGPPWKVLRV ARAQEACHPVQCTHWLLCLC ESLVSIPGARRIVHGLVPVP PMAVGVVRRTDTVWGSP in isoform 2.

VSP_033005

Experimental info

Mutagenesis

12

1

C → S: Abolishes phosphatase activity. Ref.1

Sequence conflict

182 – 183

2

KS → RV in AAK07538. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

194

Helix Strand Turn

Details...

Beta strand

7 – 17

11

Helix

18 – 28

11

Beta strand

32 – 37

6

Beta strand

39 – 44

6

Beta strand

53 – 55

3

Helix

61 – 78

18

Helix

81 – 89

9

Helix

98 – 100

3

Beta strand

106 – 112

7

Helix

113 – 125

13

Beta strand

133 – 139

7

Helix

145 – 164

20

Helix

168 – 183

16

Beta strand

187 – 193

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CA3A3157A2388A77	FASTA	194	22,574
	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
	Isoform 2 [UniParc]. Checksum: 5451647A082E9559	FASTA	153	16,931
	10 20 30 40 50 60 MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT 70 80 90 100 110 120 YDQMYNDLLR KDKELYPSGL PFKNPPCGPP WKVLRVARAQ EACHPVQCTH WLLCLCESLV 130 140 150 SIPGARRIVH GLVPVPPMAV GVVRRTDTVW GSP

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.

IPI

IPI00023556.
IPI00073512.

RefSeq

NP_054907.1. NM_014188.2.

UniGene

Hs.30026.
Hs.549751.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9NP77.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-53666N.

IntAct

Q9NP77. 3 interactions.

STRING

9606.ENSP00000291386.

PTM databases

PhosphoSite

Q9NP77.

Polymorphism databases

DMDM

74752877.

Proteomic databases

PaxDb

Q9NP77.

PRIDE

Q9NP77.

Protocols and materials databases

DNASU

29101.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000291386; ENSP00000291386; ENSG00000160075.
ENST00000359060; ENSP00000351955; ENSG00000160075.

GeneID

29101.

KEGG

hsa:29101.

UCSC

uc001agd.3. human.
uc001age.1. human.

Organism-specific databases

CTD

29101.

GeneCards

GC01M001477.

HGNC

HGNC:25016. SSU72.

neXtProt

NX_Q9NP77.

PharmGKB

PA142670866.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5211.

HOGENOM

HOG000183445.

HOVERGEN

HBG059831.

InParanoid

Q9NP77.

KO

K15544.

OMA

SMEAHNF.

OrthoDB

EOG49PB0D.

PhylomeDB

Q9NP77.

Gene expression databases

ArrayExpress

Q9NP77.

Bgee

Q9NP77.

CleanEx

HS_SSU72.

Genevestigator

Q9NP77.

Family and domain databases

InterPro

IPR006811. RNA_pol_II_suA.
[Graphical view]

PANTHER

PTHR20383. PTHR20383. 1 hit.

Pfam

PF04722. Ssu72. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SSU72. human.

EvolutionaryTrace

Q9NP77.

GenomeRNAi

29101.

NextBio

52137.

Entry information

Entry name

SSU72_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.