UniProt Accession

 PDS5A_HUMAN; Q29RF7; Q2TTR5; Q68DF7; Q8N7J4; Q8NG14; Q9Y4D4 

Genbank Protein ID

 AY550968; AK098331; BC041361; BC114218; BC126225; AF294791; CR749425; AB014548 

Genbank Nucleotide ID

 AAT52214.1; BAC05286.1; AAH41361.1; AAI14219.1; AAI26226.1; AAM82347.1; CAH18263.1; BAA31623.1 

Protein Name

 Sister chromatid cohesion protein PDS5 homolog A 

Protein Synonyms/Alias

 Cell proliferation-inducing gene 54 protein; Sister chromatid cohesion protein 112; SCC-112 

Gene Name

 PDS5A 

Gene Synonyms/Alias

 KIAA0648; PDS5; PIG54 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
35	GVKEITDKITTDEMI	ubiquitination	[1]
43	ITTDEMIKRLKMVVK	ubiquitination	[2]
50	KRLKMVVKTFMDMDQ	ubiquitination	[2]
131	LKGLEDTKSPQFNRY	ubiquitination	[2]
222	PAHKNLNKQSFDLAK	ubiquitination	[1]
292	PQLEFKLKSNDGEER	ubiquitination	[2, 3]
308	AVVRLLAKLFGSKDS	ubiquitination	[4]
366	KDLTEYLKVRSHDPE	acetylation	[5]
366	KDLTEYLKVRSHDPE	ubiquitination	[1, 2, 3, 4, 5]
507	KALNEMWKCQNMLRS	ubiquitination	[1]
557	GKAQDFVKKFNQVLG	acetylation	[5]
568	QVLGDDEKLRSQLEL	ubiquitination	[1, 2, 3, 5]
633	EAISALVKLMNKSIE	ubiquitination	[1]
637	ALVKLMNKSIEGTAD	ubiquitination	[2]
708	IFRNTGHKIETDLPQ	ubiquitination	[1, 6]
729	PILHQKAKRGTPHQA	ubiquitination	[1]
805	VVANFIVKDLLMNDR	ubiquitination	[1]
882	TEQKRISKSDMSRLR	ubiquitination	[1, 5]
974	HARQCLLKNISIRRE	acetylation	[7]
974	HARQCLLKNISIRRE	ubiquitination	[1, 4]
984	SIRREYIKQNPMATE	ubiquitination	[1]
1058	KKMAENIKLTRDAQS	ubiquitination	[1]
1113	KFFTQPEKDFCNDKS	acetylation	[5]
1113	KFFTQPEKDFCNDKS	ubiquitination	[1]
1146	GVLGAVNKPLSATGR	acetylation	[5, 7, 8, 9]
1211	IISVTPVKNIDPVKN	acetylation	[5, 7, 8, 9]
1211	IISVTPVKNIDPVKN	ubiquitination	[4, 5]
1219	NIDPVKNKEINSDQA	acetylation	[5]
1219	NIDPVKNKEINSDQA	ubiquitination	[2]
1267	SGPPAPSKPRRGRRP	acetylation	[5]
1290	TKNDDLNKPINKGRK	acetylation	[5, 7, 8, 9]

Reference

 [1] 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]
 [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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. 

Sequence Annotation

 REPEAT 393 429 HEAT.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 1146 1146 N6-acetyllysine.
 MOD_RES 1195 1195 Phosphoserine.
 MOD_RES 1208 1208 Phosphothreonine.
 MOD_RES 1211 1211 N6-acetyllysine.
 MOD_RES 1290 1290 N6-acetyllysine.
 MOD_RES 1305 1305 Phosphoserine.  

Keyword

 Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1337 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB. 

Interpro

 IPR011989; ARM-like.
 IPR016024; ARM-type_fold. 

Pfam

  

SMART

  

PROSITE

 PS50077; HEAT_REPEAT 

PRINTS