CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000373
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A 
Protein Synonyms/Alias
 PP6-ARS-A; Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A; Ankyrin repeat domain-containing protein 28; Phosphatase interactor targeting protein hnRNP K; PITK 
Gene Name
 ANKRD28 
Gene Synonyms/Alias
 KIAA0379 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAFLKLRDQPSLubiquitination[1]
73RVNAKDSKWLTPLHRacetylation[2]
73RVNAKDSKWLTPLHRubiquitination[3]
171ANINAFDKKDRRAIHacetylation[2]
390GFSDCCRKLLSSGFDubiquitination[1]
711ALLQHGAKCLLRDSRubiquitination[1]
1008NRYTNTSKTVSFEALubiquitination[1, 4, 5, 6]
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] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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
 Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation. 
Sequence Annotation
 REPEAT 40 69 ANK 1.
 REPEAT 73 102 ANK 2.
 REPEAT 106 135 ANK 3.
 REPEAT 139 168 ANK 4.
 REPEAT 172 201 ANK 5.
 REPEAT 205 234 ANK 6.
 REPEAT 238 267 ANK 7.
 REPEAT 271 301 ANK 8.
 REPEAT 305 334 ANK 9.
 REPEAT 338 367 ANK 10.
 REPEAT 371 400 ANK 11.
 REPEAT 404 433 ANK 12.
 REPEAT 437 466 ANK 13.
 REPEAT 470 500 ANK 14.
 REPEAT 504 534 ANK 15.
 REPEAT 549 578 ANK 16.
 REPEAT 582 611 ANK 17.
 REPEAT 616 645 ANK 18.
 REPEAT 652 681 ANK 19.
 REPEAT 685 714 ANK 20.
 REPEAT 718 747 ANK 21.
 REPEAT 755 784 ANK 22.
 REPEAT 787 817 ANK 23.
 REPEAT 822 851 ANK 24.
 REPEAT 855 885 ANK 25.
 REPEAT 889 918 ANK 26.
 REPEAT 925 954 ANK 27.
 MOD_RES 84 84 Phosphoserine (By similarity).
 MOD_RES 1007 1007 Phosphoserine.
 MOD_RES 1011 1011 Phosphoserine.  
Keyword
 Alternative promoter usage; Alternative splicing; ANK repeat; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1053 AA 
Protein Sequence
MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL 60
ILSGARVNAK DSKWLTPLHR AVASCSEEAV QVLLKHSADV NARDKNWQTP LHIAAANKAV 120
KCAEALVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA 180
AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN 240
TPLHVACYNG QDVVVNELID CGAIVNQKNE KGFTPLHFAA ASTHGALCLE LLVGNGADVN 300
MKSKDGKTPL HMTALHGRFS RSQTIIQSGA VIDCEDKNGN TPLHIAARYG HELLINTLIT 360
SGADTAKRGI HGMFPLHLAA LSGFSDCCRK LLSSGFDIDT PDDFGRTCLH AAAAGGNLEC 420
LNLLLNTGAD FNKKDKFGRS PLHYAAANCN YQCLFALVGS GASVNDLDER GCTPLHYAAT 480
SDTDGKCLEY LLRNDANPGI RDKQGYNAVH YSAAYGHRLC LQLIASETPL DVLMETSGTD 540
MLSDSDNRAT ISPLHLAAYH GHHQALEVLV QSLLDLDVRN SSGRTPLDLA AFKGHVECVD 600
VLINQGASIL VKDYILKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS 660
VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR 720
TPIHLSAACG HIGVLGALLQ SAASMDANPA TADNHGYTAL HWACYNGHET CVELLLEQEV 780
FQKTEGNAFS PLHCAVINDN EGAAEMLIDT LGASIVNATD SKGRTPLHAA AFTDHVECLQ 840
LLLSHNAQVN SVDSTGKTPL MMAAENGQTN TVEMLVSSAS AELTLQDNSK NTALHLACSK 900
GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY 960
TPALACAPNK DVADCLALIL ATMMPVSSSS PLSSLTFNAI NRYTNTSKTV SFEALPIMRN 1020
EPSSYCSFNN IGGEQEYLYT DVDELNDSDS ETY 1053 
Gene Ontology
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom. 
Pfam
 PF00023; Ank
 PF12796; Ank_2 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS
 PR01415; ANKYRIN.