ANR28_MOUSE
ID ANR28_MOUSE Reviewed; 1053 AA.
AC Q505D1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A;
DE Short=PP6-ARS-A;
DE Short=Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A;
DE AltName: Full=Ankyrin repeat domain-containing protein 28;
DE AltName: Full=Phosphatase interactor targeting protein hnRNP K;
DE Short=PITK;
GN Name=Ankrd28;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16564677; DOI=10.1016/j.cellsig.2006.01.019;
RA Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
RT "PITK, a PP1 targeting subunit that modulates the phosphorylation of the
RT transcriptional regulator hnRNP K.";
RL Cell. Signal. 18:1769-1778(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6)
CC that may be involved in the recognition of phosphoprotein substrates.
CC Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its
CC degradation in response to TNF-alpha. Selectively inhibits the
CC phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK
CC phosphorylation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
CC containing subunit (PP6R) and an ankyrin repeat-domain containing
CC regulatory subunit (ARS). Interacts with PPP1C and HNRPK. Interacts
CC with PPP6C, PPP6R1 and PPP6R3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Seems to be excluded
CC from nucleoli. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:16564677}.
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DR EMBL; BC094609; AAH94609.1; -; mRNA.
DR EMBL; BC051456; AAH51456.1; -; mRNA.
DR CCDS; CCDS36858.1; -.
DR RefSeq; NP_001019775.1; NM_001024604.2.
DR AlphaFoldDB; Q505D1; -.
DR SMR; Q505D1; -.
DR BioGRID; 222872; 11.
DR IntAct; Q505D1; 12.
DR STRING; 10090.ENSMUSP00000014640; -.
DR iPTMnet; Q505D1; -.
DR PhosphoSitePlus; Q505D1; -.
DR EPD; Q505D1; -.
DR jPOST; Q505D1; -.
DR MaxQB; Q505D1; -.
DR PaxDb; Q505D1; -.
DR PeptideAtlas; Q505D1; -.
DR PRIDE; Q505D1; -.
DR ProteomicsDB; 296256; -.
DR Antibodypedia; 26857; 113 antibodies from 22 providers.
DR DNASU; 105522; -.
DR Ensembl; ENSMUST00000014640; ENSMUSP00000014640; ENSMUSG00000014496.
DR GeneID; 105522; -.
DR KEGG; mmu:105522; -.
DR UCSC; uc007sxz.1; mouse.
DR CTD; 23243; -.
DR MGI; MGI:2145661; Ankrd28.
DR VEuPathDB; HostDB:ENSMUSG00000014496; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00950000182908; -.
DR HOGENOM; CLU_000134_58_0_1; -.
DR InParanoid; Q505D1; -.
DR OMA; YNGHLEM; -.
DR PhylomeDB; Q505D1; -.
DR TreeFam; TF312824; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR BioGRID-ORCS; 105522; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ankrd28; mouse.
DR PRO; PR:Q505D1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q505D1; protein.
DR Bgee; ENSMUSG00000014496; Expressed in plantaris and 255 other tissues.
DR ExpressionAtlas; Q505D1; baseline and differential.
DR Genevisible; Q505D1; MM.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 11.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 8.
DR Pfam; PF13637; Ank_4; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 28.
DR SUPFAM; SSF48403; SSF48403; 4.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 24.
PE 1: Evidence at protein level;
KW ANK repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1053
FT /note="Serine/threonine-protein phosphatase 6 regulatory
FT ankyrin repeat subunit A"
FT /id="PRO_0000244571"
FT REPEAT 40..69
FT /note="ANK 1"
FT REPEAT 73..102
FT /note="ANK 2"
FT REPEAT 106..135
FT /note="ANK 3"
FT REPEAT 139..168
FT /note="ANK 4"
FT REPEAT 172..201
FT /note="ANK 5"
FT REPEAT 205..234
FT /note="ANK 6"
FT REPEAT 238..267
FT /note="ANK 7"
FT REPEAT 271..301
FT /note="ANK 8"
FT REPEAT 305..334
FT /note="ANK 9"
FT REPEAT 338..367
FT /note="ANK 10"
FT REPEAT 371..400
FT /note="ANK 11"
FT REPEAT 404..433
FT /note="ANK 12"
FT REPEAT 437..466
FT /note="ANK 13"
FT REPEAT 470..500
FT /note="ANK 14"
FT REPEAT 504..534
FT /note="ANK 15"
FT REPEAT 549..578
FT /note="ANK 16"
FT REPEAT 582..611
FT /note="ANK 17"
FT REPEAT 616..645
FT /note="ANK 18"
FT REPEAT 652..681
FT /note="ANK 19"
FT REPEAT 685..714
FT /note="ANK 20"
FT REPEAT 718..747
FT /note="ANK 21"
FT REPEAT 755..786
FT /note="ANK 22"
FT REPEAT 788..817
FT /note="ANK 23"
FT REPEAT 822..851
FT /note="ANK 24"
FT REPEAT 855..885
FT /note="ANK 25"
FT REPEAT 889..918
FT /note="ANK 26"
FT REPEAT 925..954
FT /note="ANK 27"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15084"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1053 AA; 112898 MW; D7649AF1D1F22F62 CRC64;
MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL
ILSGARVNAK DSKWLTPLHR AVASCSEEAV QILLKHSADV NARDKNWQTP LHIAAANKAV
KCAESLVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA
AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN
TPLHVACYNG QDVVVNELID CGANVNQKNE KGFTPLHFAA ASTHGALCLE LLVGNGADVN
MKSKDGKTPL HMTALHGRFS RSQTIIQSGA VIDCEDKNGN TPLHIAARYG HELLINTLIT
SGADTAKRGI HGMFPLHLAA LSGFSDCCRK LLSSGFDIDT PDDFGRTCLH AAAAGGNLEC
LNLLLNTGAD FNKKDKFGRS PLHYAAANCN YQCLFALVGS GASVNDLDER GCTPLHYAAT
SDTDGKCLEY LLRNDANPGI RDKQGYNAVH YSAAYGHRLC LQLIASETPL DVLMETSGTD
MLSDSDNRAT ISPLHLAAYH GHHQALEVLV QSLLDLDVRN SSGRTPLDLA AFKGHVECVD
VLINQGASIL VKDYVLKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS
VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR
TPIHLSAACG HIGVLGALLQ SATSVDANPA VVDNHGYTAL HWACYNGHET CVELLLEQDV
FQKIDGNAFS PLHCAVINDN EGAAEMLIDS LGASIVNATD SKGRTPLHAA AFTDHVECLQ
LLLSQNAQVN SADSTGKTPL MMAAENGQTN TVEMLVSSAS ADLTLQDKSK NTALHLACGK
GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY
TPALACAPNK DVADCLALIL ATMMPVSSSS PLTSLTFNAI NRYTNTSKTV SFEALPIMRN
EASSYCSFNN IGGEQEYLYT DVDELNDSDS ETY
