UniProt Accession

 SSU72_HUMAN; Q9NP77; Q9BZS6; Q9H933 

Genbank Protein ID

 AF161530; AF277178; AJ276409; AK001809; AK023110; AK291324; AL645728; AL645728; CH471183; CH471183; BC008070 

Genbank Nucleotide ID

 AAF29145.1; AAK07538.1; CAC81713.1; BAA91921.1; BAB14410.1; BAF84013.1; CAI22945.1; CAI22947.1; EAW56182.1; EAW56183.1; AAH08070.1 

Protein Name

 RNA polymerase II subunit A C-terminal domain phosphatase SSU72 

Protein Synonyms/Alias

 CTD phosphatase SSU72 

Gene Name

 SSU72 

Gene Synonyms/Alias

 HSPC182; PNAS-120 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
28	EAHNILSKRGFSVRS	ubiquitination	[1, 2, 3, 4]
43	FGTGTHVKLPGPAPD	ubiquitination	[1, 3, 4]
51	LPGPAPDKPNVYDFK	ubiquitination	[2, 3]
58	KPNVYDFKTTYDQMY	ubiquitination	[2]
71	MYNDLLRKDKELYTQ	ubiquitination	[3]
73	NDLLRKDKELYTQNG	ubiquitination	[1, 3, 4, 5, 6]
102	PERFQNCKDLFDLIL	ubiquitination	[3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 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. 

Sequence Annotation

  

Keyword

 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Hydrolase; mRNA processing; Nucleus; Protein phosphatase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 194 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008420; F:CTD phosphatase activity; IDA:UniProtKB.
 GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
 GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB. 

Interpro

 IPR006811; RNA_pol_II_suA. 

Pfam

 PF04722; Ssu72 

SMART

  

PROSITE

  

PRINTS