Full text data of ANKRD28
ANKRD28
(KIAA0379)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A; 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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A; 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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O15084
ID ANR28_HUMAN Reviewed; 1053 AA.
AC O15084; B4DES5; Q1WWL4; Q29RW6; Q3B857; Q6ULS0; Q6ZT57;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAY-2011, sequence version 5.
DT 22-JAN-2014, entry version 123.
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; Synonyms=KIAA0379;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning a new transcript of KIAA0379 protein in testis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-767 (ISOFORM 3).
RC TISSUE=Amygdala, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORMS 3 AND 4).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1C AND HNRPK,
RP PHOSPHORYLATION AT SER-1007 AND SER-1011, AND MUTAGENESIS OF
RP 1007-SER--SER-1011.
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
RT the transcriptional regulator hnRNP K.";
RL Cell. Signal. 18:1769-1778(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH PPP6C; PPP6R1 AND PPP6R3.
RX PubMed=18186651; DOI=10.1021/bi7022877;
RA Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
RT "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
RT domains.";
RL Biochemistry 47:1442-1451(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Putative regulatory subunit of protein phosphatase 6
CC (PP6) that may be involved in the recognition of phosphoprotein
CC substrates. Involved in the PP6-mediated dephosphorylation of
CC NFKBIE opposing its degradation in response to TNF-alpha.
CC Selectively inhibits the phosphatase activity of PPP1C. Targets
CC PPP1C to modulate HNRPK phosphorylation.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be
CC a heterotrimeric complex formed by the catalytic subunit, a SAPS
CC domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC containing regulatory subunit (ARS). Interacts with PPP1C and
CC HNRPK. Interacts with PPP6C, PPP6R1 and PPP6R3.
CC -!- INTERACTION:
CC Q14185:DOCK1; NbExp=4; IntAct=EBI-359567, EBI-446740;
CC O00743:PPP6C; NbExp=9; IntAct=EBI-359567, EBI-359751;
CC Q9UPN7:PPP6R1; NbExp=10; IntAct=EBI-359567, EBI-359745;
CC O75170:PPP6R2; NbExp=7; IntAct=EBI-359567, EBI-359739;
CC Q5H9R7:PPP6R3; NbExp=5; IntAct=EBI-359567, EBI-355498;
CC Q9H2K2:TNKS2; NbExp=3; IntAct=EBI-359567, EBI-4398527;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Seems to be
CC excluded from nucleoli.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O15084-3; Sequence=Displayed;
CC Name=2;
CC IsoId=O15084-2; Sequence=VSP_012433;
CC Note=Produced by alternative promoter usage;
CC Name=3;
CC IsoId=O15084-1; Sequence=VSP_041013;
CC Name=4;
CC IsoId=O15084-4; Sequence=VSP_041014;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 27 ANK repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ72374.1; Type=Frameshift; Positions=408;
CC Sequence=BAA20833.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC86737.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; AY367056; AAQ72374.1; ALT_FRAME; mRNA.
DR EMBL; AB002377; BAA20833.2; ALT_INIT; mRNA.
DR EMBL; AK126888; BAC86737.1; ALT_SEQ; mRNA.
DR EMBL; AK293770; BAG57186.1; -; mRNA.
DR EMBL; BC106948; AAI06949.2; -; mRNA.
DR EMBL; BC113868; AAI13869.1; -; mRNA.
DR EMBL; BC114476; AAI14477.1; -; mRNA.
DR RefSeq; NP_001182027.1; NM_001195098.1.
DR RefSeq; NP_001182028.1; NM_001195099.1.
DR RefSeq; NP_056014.2; NM_015199.3.
DR RefSeq; XP_005265052.1; XM_005264995.1.
DR RefSeq; XP_005265053.1; XM_005264996.1.
DR UniGene; Hs.335239; -.
DR ProteinModelPortal; O15084; -.
DR SMR; O15084; 8-999.
DR DIP; DIP-27583N; -.
DR IntAct; O15084; 72.
DR MINT; MINT-1150737; -.
DR STRING; 9606.ENSP00000382379; -.
DR PhosphoSite; O15084; -.
DR PaxDb; O15084; -.
DR PRIDE; O15084; -.
DR DNASU; 23243; -.
DR Ensembl; ENST00000383777; ENSP00000373287; ENSG00000206560.
DR Ensembl; ENST00000399451; ENSP00000382379; ENSG00000206560.
DR Ensembl; ENST00000412318; ENSP00000397341; ENSG00000206560.
DR GeneID; 23243; -.
DR KEGG; hsa:23243; -.
DR UCSC; uc003cai.1; human.
DR CTD; 23243; -.
DR GeneCards; GC03M015708; -.
DR H-InvDB; HIX0003106; -.
DR HGNC; HGNC:29024; ANKRD28.
DR MIM; 611122; gene.
DR neXtProt; NX_O15084; -.
DR PharmGKB; PA134880251; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000033959; -.
DR HOVERGEN; HBG067697; -.
DR InParanoid; O15084; -.
DR KO; K15502; -.
DR OMA; DMLNDSD; -.
DR OrthoDB; EOG7QG436; -.
DR GenomeRNAi; 23243; -.
DR NextBio; 44912; -.
DR PRO; PR:O15084; -.
DR ArrayExpress; O15084; -.
DR Bgee; O15084; -.
DR CleanEx; HS_ANKRD28; -.
DR Genevestigator; O15084; -.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR Pfam; PF00023; Ank; 22.
DR Pfam; PF12796; Ank_2; 1.
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 Alternative promoter usage; Alternative splicing; ANK repeat;
KW Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1 1053 Serine/threonine-protein phosphatase 6
FT regulatory ankyrin repeat subunit A.
FT /FTId=PRO_0000066919.
FT REPEAT 40 69 ANK 1.
FT REPEAT 73 102 ANK 2.
FT REPEAT 106 135 ANK 3.
FT REPEAT 139 168 ANK 4.
FT REPEAT 172 201 ANK 5.
FT REPEAT 205 234 ANK 6.
FT REPEAT 238 267 ANK 7.
FT REPEAT 271 301 ANK 8.
FT REPEAT 305 334 ANK 9.
FT REPEAT 338 367 ANK 10.
FT REPEAT 371 400 ANK 11.
FT REPEAT 404 433 ANK 12.
FT REPEAT 437 466 ANK 13.
FT REPEAT 470 500 ANK 14.
FT REPEAT 504 534 ANK 15.
FT REPEAT 549 578 ANK 16.
FT REPEAT 582 611 ANK 17.
FT REPEAT 616 645 ANK 18.
FT REPEAT 652 681 ANK 19.
FT REPEAT 685 714 ANK 20.
FT REPEAT 718 747 ANK 21.
FT REPEAT 755 784 ANK 22.
FT REPEAT 787 817 ANK 23.
FT REPEAT 822 851 ANK 24.
FT REPEAT 855 885 ANK 25.
FT REPEAT 889 918 ANK 26.
FT REPEAT 925 954 ANK 27.
FT MOD_RES 1007 1007 Phosphoserine.
FT MOD_RES 1011 1011 Phosphoserine.
FT VAR_SEQ 1 154 Missing (in isoform 2).
FT /FTId=VSP_012433.
FT VAR_SEQ 1 9 MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENK
FT SLHSPPSGNVLVRY (in isoform 3).
FT /FTId=VSP_041013.
FT VAR_SEQ 1 9 MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENK
FT SLHSPPSGNVL (in isoform 4).
FT /FTId=VSP_041014.
FT MUTAGEN 1007 1011 SKTVS->AKTVA: Marked decrease in
FT phosphorylation. Increased PPP1C-binding.
FT No effect on HNRPK-binding.
FT CONFLICT 293 293 V -> A (in Ref. 1; AAQ72374).
FT CONFLICT 500 500 I -> V (in Ref. 1; AAQ72374 and 4;
FT BAC86737).
SQ SEQUENCE 1053 AA; 112966 MW; BDB4855193364585 CRC64;
MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL
ILSGARVNAK DSKWLTPLHR AVASCSEEAV QVLLKHSADV NARDKNWQTP LHIAAANKAV
KCAEALVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA
AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN
TPLHVACYNG QDVVVNELID CGAIVNQKNE 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 VKDYILKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS
VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR
TPIHLSAACG HIGVLGALLQ SAASMDANPA TADNHGYTAL HWACYNGHET CVELLLEQEV
FQKTEGNAFS PLHCAVINDN EGAAEMLIDT LGASIVNATD SKGRTPLHAA AFTDHVECLQ
LLLSHNAQVN SVDSTGKTPL MMAAENGQTN TVEMLVSSAS AELTLQDNSK NTALHLACSK
GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY
TPALACAPNK DVADCLALIL ATMMPVSSSS PLSSLTFNAI NRYTNTSKTV SFEALPIMRN
EPSSYCSFNN IGGEQEYLYT DVDELNDSDS ETY
//
ID ANR28_HUMAN Reviewed; 1053 AA.
AC O15084; B4DES5; Q1WWL4; Q29RW6; Q3B857; Q6ULS0; Q6ZT57;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAY-2011, sequence version 5.
DT 22-JAN-2014, entry version 123.
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; Synonyms=KIAA0379;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning a new transcript of KIAA0379 protein in testis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-767 (ISOFORM 3).
RC TISSUE=Amygdala, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORMS 3 AND 4).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1C AND HNRPK,
RP PHOSPHORYLATION AT SER-1007 AND SER-1011, AND MUTAGENESIS OF
RP 1007-SER--SER-1011.
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
RT the transcriptional regulator hnRNP K.";
RL Cell. Signal. 18:1769-1778(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH PPP6C; PPP6R1 AND PPP6R3.
RX PubMed=18186651; DOI=10.1021/bi7022877;
RA Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
RT "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
RT domains.";
RL Biochemistry 47:1442-1451(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Putative regulatory subunit of protein phosphatase 6
CC (PP6) that may be involved in the recognition of phosphoprotein
CC substrates. Involved in the PP6-mediated dephosphorylation of
CC NFKBIE opposing its degradation in response to TNF-alpha.
CC Selectively inhibits the phosphatase activity of PPP1C. Targets
CC PPP1C to modulate HNRPK phosphorylation.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be
CC a heterotrimeric complex formed by the catalytic subunit, a SAPS
CC domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC containing regulatory subunit (ARS). Interacts with PPP1C and
CC HNRPK. Interacts with PPP6C, PPP6R1 and PPP6R3.
CC -!- INTERACTION:
CC Q14185:DOCK1; NbExp=4; IntAct=EBI-359567, EBI-446740;
CC O00743:PPP6C; NbExp=9; IntAct=EBI-359567, EBI-359751;
CC Q9UPN7:PPP6R1; NbExp=10; IntAct=EBI-359567, EBI-359745;
CC O75170:PPP6R2; NbExp=7; IntAct=EBI-359567, EBI-359739;
CC Q5H9R7:PPP6R3; NbExp=5; IntAct=EBI-359567, EBI-355498;
CC Q9H2K2:TNKS2; NbExp=3; IntAct=EBI-359567, EBI-4398527;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Seems to be
CC excluded from nucleoli.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O15084-3; Sequence=Displayed;
CC Name=2;
CC IsoId=O15084-2; Sequence=VSP_012433;
CC Note=Produced by alternative promoter usage;
CC Name=3;
CC IsoId=O15084-1; Sequence=VSP_041013;
CC Name=4;
CC IsoId=O15084-4; Sequence=VSP_041014;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 27 ANK repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ72374.1; Type=Frameshift; Positions=408;
CC Sequence=BAA20833.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC86737.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; AY367056; AAQ72374.1; ALT_FRAME; mRNA.
DR EMBL; AB002377; BAA20833.2; ALT_INIT; mRNA.
DR EMBL; AK126888; BAC86737.1; ALT_SEQ; mRNA.
DR EMBL; AK293770; BAG57186.1; -; mRNA.
DR EMBL; BC106948; AAI06949.2; -; mRNA.
DR EMBL; BC113868; AAI13869.1; -; mRNA.
DR EMBL; BC114476; AAI14477.1; -; mRNA.
DR RefSeq; NP_001182027.1; NM_001195098.1.
DR RefSeq; NP_001182028.1; NM_001195099.1.
DR RefSeq; NP_056014.2; NM_015199.3.
DR RefSeq; XP_005265052.1; XM_005264995.1.
DR RefSeq; XP_005265053.1; XM_005264996.1.
DR UniGene; Hs.335239; -.
DR ProteinModelPortal; O15084; -.
DR SMR; O15084; 8-999.
DR DIP; DIP-27583N; -.
DR IntAct; O15084; 72.
DR MINT; MINT-1150737; -.
DR STRING; 9606.ENSP00000382379; -.
DR PhosphoSite; O15084; -.
DR PaxDb; O15084; -.
DR PRIDE; O15084; -.
DR DNASU; 23243; -.
DR Ensembl; ENST00000383777; ENSP00000373287; ENSG00000206560.
DR Ensembl; ENST00000399451; ENSP00000382379; ENSG00000206560.
DR Ensembl; ENST00000412318; ENSP00000397341; ENSG00000206560.
DR GeneID; 23243; -.
DR KEGG; hsa:23243; -.
DR UCSC; uc003cai.1; human.
DR CTD; 23243; -.
DR GeneCards; GC03M015708; -.
DR H-InvDB; HIX0003106; -.
DR HGNC; HGNC:29024; ANKRD28.
DR MIM; 611122; gene.
DR neXtProt; NX_O15084; -.
DR PharmGKB; PA134880251; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000033959; -.
DR HOVERGEN; HBG067697; -.
DR InParanoid; O15084; -.
DR KO; K15502; -.
DR OMA; DMLNDSD; -.
DR OrthoDB; EOG7QG436; -.
DR GenomeRNAi; 23243; -.
DR NextBio; 44912; -.
DR PRO; PR:O15084; -.
DR ArrayExpress; O15084; -.
DR Bgee; O15084; -.
DR CleanEx; HS_ANKRD28; -.
DR Genevestigator; O15084; -.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR Pfam; PF00023; Ank; 22.
DR Pfam; PF12796; Ank_2; 1.
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 Alternative promoter usage; Alternative splicing; ANK repeat;
KW Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1 1053 Serine/threonine-protein phosphatase 6
FT regulatory ankyrin repeat subunit A.
FT /FTId=PRO_0000066919.
FT REPEAT 40 69 ANK 1.
FT REPEAT 73 102 ANK 2.
FT REPEAT 106 135 ANK 3.
FT REPEAT 139 168 ANK 4.
FT REPEAT 172 201 ANK 5.
FT REPEAT 205 234 ANK 6.
FT REPEAT 238 267 ANK 7.
FT REPEAT 271 301 ANK 8.
FT REPEAT 305 334 ANK 9.
FT REPEAT 338 367 ANK 10.
FT REPEAT 371 400 ANK 11.
FT REPEAT 404 433 ANK 12.
FT REPEAT 437 466 ANK 13.
FT REPEAT 470 500 ANK 14.
FT REPEAT 504 534 ANK 15.
FT REPEAT 549 578 ANK 16.
FT REPEAT 582 611 ANK 17.
FT REPEAT 616 645 ANK 18.
FT REPEAT 652 681 ANK 19.
FT REPEAT 685 714 ANK 20.
FT REPEAT 718 747 ANK 21.
FT REPEAT 755 784 ANK 22.
FT REPEAT 787 817 ANK 23.
FT REPEAT 822 851 ANK 24.
FT REPEAT 855 885 ANK 25.
FT REPEAT 889 918 ANK 26.
FT REPEAT 925 954 ANK 27.
FT MOD_RES 1007 1007 Phosphoserine.
FT MOD_RES 1011 1011 Phosphoserine.
FT VAR_SEQ 1 154 Missing (in isoform 2).
FT /FTId=VSP_012433.
FT VAR_SEQ 1 9 MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENK
FT SLHSPPSGNVLVRY (in isoform 3).
FT /FTId=VSP_041013.
FT VAR_SEQ 1 9 MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENK
FT SLHSPPSGNVL (in isoform 4).
FT /FTId=VSP_041014.
FT MUTAGEN 1007 1011 SKTVS->AKTVA: Marked decrease in
FT phosphorylation. Increased PPP1C-binding.
FT No effect on HNRPK-binding.
FT CONFLICT 293 293 V -> A (in Ref. 1; AAQ72374).
FT CONFLICT 500 500 I -> V (in Ref. 1; AAQ72374 and 4;
FT BAC86737).
SQ SEQUENCE 1053 AA; 112966 MW; BDB4855193364585 CRC64;
MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL
ILSGARVNAK DSKWLTPLHR AVASCSEEAV QVLLKHSADV NARDKNWQTP LHIAAANKAV
KCAEALVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA
AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN
TPLHVACYNG QDVVVNELID CGAIVNQKNE 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 VKDYILKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS
VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR
TPIHLSAACG HIGVLGALLQ SAASMDANPA TADNHGYTAL HWACYNGHET CVELLLEQEV
FQKTEGNAFS PLHCAVINDN EGAAEMLIDT LGASIVNATD SKGRTPLHAA AFTDHVECLQ
LLLSHNAQVN SVDSTGKTPL MMAAENGQTN TVEMLVSSAS AELTLQDNSK NTALHLACSK
GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY
TPALACAPNK DVADCLALIL ATMMPVSSSS PLSSLTFNAI NRYTNTSKTV SFEALPIMRN
EPSSYCSFNN IGGEQEYLYT DVDELNDSDS ETY
//
MIM
611122
*RECORD*
*FIELD* NO
611122
*FIELD* TI
*611122 ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 28; ANKRD28
;;PHOSPHATASE INTERACTOR TARGETING K PROTEIN; PITK;;
read moreKIAA0379
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1997) cloned ANKRD28, which they designated
KIAA0379. The deduced 882-amino acid protein shares 30.8% identity with
ANKRD3 (605706). RT-PCR analysis detected ubiquitous expression in all
human tissues tested.
By searching for PP1 (see 176875)-binding proteins in rabbit skeletal
muscle, followed by database analysis, Kwiek et al. (2006) identified
ANKRD28, which they called PITK. ANKRD28 contains putative PP1-binding
motifs at either terminus and 28 successive ankyrin repeats. Western
blot analysis of multiple mouse tissues revealed expression of ANKRD28
at similar levels in all tissues tested. In COS-7 cells,
immunofluorescence microscopy localized ANKRD28 to subnuclear bodies
with exclusion from nucleoli.
GENE FUNCTION
By in vitro studies, Kwiek et al. (2006) showed that recombinant ANKRD28
selectively inhibited the phosphorylase activity of PP1C in a
dose-dependent manner. Phosphorylation of ser1013 and ser1017, which lie
within the putative PP1-binding motif, negatively regulated ANKRD28
binding to PP1C. Immunoprecipitation studies showed that ANKRD28 bound
to hnRNP-K (600712). ANKRD28 selectively regulated phosphorylation of
hnRNP-K at ser284, an effect that was enhanced in vivo by an
S1013A/S1017A double mutant, suggesting that ANKRD28 targets PP1 in a
regulated manner to dephosphorylate hnRNP-K selectively at ser284.
Microarray analysis found that expression of ANKRD28 resulted in altered
expression of 47 genes, including marked induction of MEK5 (MAP2K5;
602520). Expression of only 2 of these genes was altered by the
S1013A/S1017A double mutant, indicating the importance of
phosphorylation in ANKRD28 function. In addition, the effects of ANKRD28
and S1013A/S1017A double-mutant ANKRD28 could be modulated by
coexpression of hnRNP-K.
MAPPING
By radiation hybrid analysis, Nagase et al. (1997) mapped the ANKRD28
gene to chromosome 3. Kwiek et al. (2006) noted that the ANKRD28 gene
maps to chromosome 3p25.1.
*FIELD* RF
1. Kwiek, N. C.; Thacker, D. F.; Datto, M. B.; Megosh, H. B.; Haystead,
T. A. J.: PITK, a PP1 targeting subunit that modulates the phosphorylation
of the transcriptional regulator hnRNP K. Cell. Signal. 18: 1769-1778,
2006.
2. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
*FIELD* CD
Jennifer L. Goldstein: 6/19/2007
*FIELD* ED
carol: 01/02/2008
wwang: 6/20/2007
*RECORD*
*FIELD* NO
611122
*FIELD* TI
*611122 ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 28; ANKRD28
;;PHOSPHATASE INTERACTOR TARGETING K PROTEIN; PITK;;
read moreKIAA0379
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1997) cloned ANKRD28, which they designated
KIAA0379. The deduced 882-amino acid protein shares 30.8% identity with
ANKRD3 (605706). RT-PCR analysis detected ubiquitous expression in all
human tissues tested.
By searching for PP1 (see 176875)-binding proteins in rabbit skeletal
muscle, followed by database analysis, Kwiek et al. (2006) identified
ANKRD28, which they called PITK. ANKRD28 contains putative PP1-binding
motifs at either terminus and 28 successive ankyrin repeats. Western
blot analysis of multiple mouse tissues revealed expression of ANKRD28
at similar levels in all tissues tested. In COS-7 cells,
immunofluorescence microscopy localized ANKRD28 to subnuclear bodies
with exclusion from nucleoli.
GENE FUNCTION
By in vitro studies, Kwiek et al. (2006) showed that recombinant ANKRD28
selectively inhibited the phosphorylase activity of PP1C in a
dose-dependent manner. Phosphorylation of ser1013 and ser1017, which lie
within the putative PP1-binding motif, negatively regulated ANKRD28
binding to PP1C. Immunoprecipitation studies showed that ANKRD28 bound
to hnRNP-K (600712). ANKRD28 selectively regulated phosphorylation of
hnRNP-K at ser284, an effect that was enhanced in vivo by an
S1013A/S1017A double mutant, suggesting that ANKRD28 targets PP1 in a
regulated manner to dephosphorylate hnRNP-K selectively at ser284.
Microarray analysis found that expression of ANKRD28 resulted in altered
expression of 47 genes, including marked induction of MEK5 (MAP2K5;
602520). Expression of only 2 of these genes was altered by the
S1013A/S1017A double mutant, indicating the importance of
phosphorylation in ANKRD28 function. In addition, the effects of ANKRD28
and S1013A/S1017A double-mutant ANKRD28 could be modulated by
coexpression of hnRNP-K.
MAPPING
By radiation hybrid analysis, Nagase et al. (1997) mapped the ANKRD28
gene to chromosome 3. Kwiek et al. (2006) noted that the ANKRD28 gene
maps to chromosome 3p25.1.
*FIELD* RF
1. Kwiek, N. C.; Thacker, D. F.; Datto, M. B.; Megosh, H. B.; Haystead,
T. A. J.: PITK, a PP1 targeting subunit that modulates the phosphorylation
of the transcriptional regulator hnRNP K. Cell. Signal. 18: 1769-1778,
2006.
2. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
*FIELD* CD
Jennifer L. Goldstein: 6/19/2007
*FIELD* ED
carol: 01/02/2008
wwang: 6/20/2007