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O15084 (ANR28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A

Short name=PP6-ARS-A
Short name=Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A
Alternative name(s):
Ankyrin repeat domain-containing protein 28
Phosphatase interactor targeting protein hnRNP K
Short name=PITK
Gene names
Name:ANKRD28
Synonyms:KIAA0379
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1053 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Subunit structure

Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP1C and HNRPK. Interacts with PPP6C, PPP6R1 and PPP6R3. Ref.6 Ref.7

Subcellular location

Nucleusnucleoplasm. Note: Seems to be excluded from nucleoli. Ref.6

Sequence similarities

Contains 27 ANK repeats.

Sequence caution

The sequence AAQ72374.1 differs from that shown. Reason: Frameshift at position 408.

The sequence BAA20833.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC86737.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7PubMed 19118547PubMed 21187329PubMed 23414517PubMed 24255178. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15084-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O15084-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-154: Missing.
Note: Produced by alternative promoter usage.
Isoform 3 (identifier: O15084-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAFLKLRDQ → MSRVCIVVLEEVEDESPAFISKLPQENKSLHSPPSGNVLVRY
Isoform 4 (identifier: O15084-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAFLKLRDQ → MSRVCIVVLEEVEDESPAFISKLPQENKSLHSPPSGNVL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10531053Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
PRO_0000066919

Regions

Repeat40 – 6930ANK 1
Repeat73 – 10230ANK 2
Repeat106 – 13530ANK 3
Repeat139 – 16830ANK 4
Repeat172 – 20130ANK 5
Repeat205 – 23430ANK 6
Repeat238 – 26730ANK 7
Repeat271 – 30131ANK 8
Repeat305 – 33430ANK 9
Repeat338 – 36730ANK 10
Repeat371 – 40030ANK 11
Repeat404 – 43330ANK 12
Repeat437 – 46630ANK 13
Repeat470 – 50031ANK 14
Repeat504 – 53431ANK 15
Repeat549 – 57830ANK 16
Repeat582 – 61130ANK 17
Repeat616 – 64530ANK 18
Repeat652 – 68130ANK 19
Repeat685 – 71430ANK 20
Repeat718 – 74730ANK 21
Repeat755 – 78430ANK 22
Repeat787 – 81731ANK 23
Repeat822 – 85130ANK 24
Repeat855 – 88531ANK 25
Repeat889 – 91830ANK 26
Repeat925 – 95430ANK 27

Amino acid modifications

Modified residue10071Phosphoserine Ref.6
Modified residue10111Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 154154Missing in isoform 2.
VSP_012433
Alternative sequence1 – 99MAFLKLRDQ → MSRVCIVVLEEVEDESPAFI SKLPQENKSLHSPPSGNVLV RY in isoform 3.
VSP_041013
Alternative sequence1 – 99MAFLKLRDQ → MSRVCIVVLEEVEDESPAFI SKLPQENKSLHSPPSGNVL in isoform 4.
VSP_041014

Experimental info

Mutagenesis1007 – 10115SKTVS → AKTVA: Marked decrease in phosphorylation. Increased PPP1C-binding. No effect on HNRPK-binding. Ref.6
Sequence conflict2931V → A in AAQ72374. Ref.1
Sequence conflict5001I → V in AAQ72374. Ref.1
Sequence conflict5001I → V in BAC86737. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 3, 2011. Version 5.
Checksum: BDB4855193364585

FASTA1,053112,966
        10         20         30         40         50         60 
MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL 

        70         80         90        100        110        120 
ILSGARVNAK DSKWLTPLHR AVASCSEEAV QVLLKHSADV NARDKNWQTP LHIAAANKAV 

       130        140        150        160        170        180 
KCAEALVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA 

       190        200        210        220        230        240 
AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN 

       250        260        270        280        290        300 
TPLHVACYNG QDVVVNELID CGAIVNQKNE KGFTPLHFAA ASTHGALCLE LLVGNGADVN 

       310        320        330        340        350        360 
MKSKDGKTPL HMTALHGRFS RSQTIIQSGA VIDCEDKNGN TPLHIAARYG HELLINTLIT 

       370        380        390        400        410        420 
SGADTAKRGI HGMFPLHLAA LSGFSDCCRK LLSSGFDIDT PDDFGRTCLH AAAAGGNLEC 

       430        440        450        460        470        480 
LNLLLNTGAD FNKKDKFGRS PLHYAAANCN YQCLFALVGS GASVNDLDER GCTPLHYAAT 

       490        500        510        520        530        540 
SDTDGKCLEY LLRNDANPGI RDKQGYNAVH YSAAYGHRLC LQLIASETPL DVLMETSGTD 

       550        560        570        580        590        600 
MLSDSDNRAT ISPLHLAAYH GHHQALEVLV QSLLDLDVRN SSGRTPLDLA AFKGHVECVD 

       610        620        630        640        650        660 
VLINQGASIL VKDYILKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS 

       670        680        690        700        710        720 
VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR 

       730        740        750        760        770        780 
TPIHLSAACG HIGVLGALLQ SAASMDANPA TADNHGYTAL HWACYNGHET CVELLLEQEV 

       790        800        810        820        830        840 
FQKTEGNAFS PLHCAVINDN EGAAEMLIDT LGASIVNATD SKGRTPLHAA AFTDHVECLQ 

       850        860        870        880        890        900 
LLLSHNAQVN SVDSTGKTPL MMAAENGQTN TVEMLVSSAS AELTLQDNSK NTALHLACSK 

       910        920        930        940        950        960 
GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY 

       970        980        990       1000       1010       1020 
TPALACAPNK DVADCLALIL ATMMPVSSSS PLSSLTFNAI NRYTNTSKTV SFEALPIMRN 

      1030       1040       1050 
EPSSYCSFNN IGGEQEYLYT DVDELNDSDS ETY 

« Hide

Isoform 2 [UniParc].

Checksum: E06723898ABF4B08
Show »

FASTA89996,161
Isoform 3 [UniParc].

Checksum: 47A3F97E5C72F0E8
Show »

FASTA1,086116,543
Isoform 4 [UniParc].

Checksum: 349BC9338F251E08
Show »

FASTA1,083116,124

References

« Hide 'large scale' references
[1]"Cloning a new transcript of KIAA0379 protein in testis."
Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Testis.
[2]"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."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-767 (ISOFORM 3).
Tissue: Amygdala and Cerebellum.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORMS 3 AND 4).
[6]"PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K."
Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.
Cell. Signal. 18:1769-1778(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1C AND HNRPK, PHOSPHORYLATION AT SER-1007 AND SER-1011, MUTAGENESIS OF 1007-SER--SER-1011.
[7]"Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains."
Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.
Biochemistry 47:1442-1451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP6C; PPP6R1 AND PPP6R3.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY367056 mRNA. Translation: AAQ72374.1. Frameshift.
AB002377 mRNA. Translation: BAA20833.2. Different initiation.
AK126888 mRNA. Translation: BAC86737.1. Sequence problems.
AK293770 mRNA. Translation: BAG57186.1.
BC106948 mRNA. Translation: AAI06949.2.
BC113868 mRNA. Translation: AAI13869.1.
BC114476 mRNA. Translation: AAI14477.1.
CCDSCCDS46769.1. [O15084-3]
RefSeqNP_001182027.1. NM_001195098.1. [O15084-2]
NP_001182028.1. NM_001195099.1. [O15084-2]
NP_056014.2. NM_015199.3. [O15084-3]
XP_005265053.1. XM_005264996.2. [O15084-4]
UniGeneHs.335239.

3D structure databases

ProteinModelPortalO15084.
SMRO15084. Positions 8-1022.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116847. 57 interactions.
DIPDIP-27583N.
IntActO15084. 74 interactions.
MINTMINT-1150737.
STRING9606.ENSP00000382379.

PTM databases

PhosphoSiteO15084.

Proteomic databases

MaxQBO15084.
PaxDbO15084.
PRIDEO15084.

Protocols and materials databases

DNASU23243.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383777; ENSP00000373287; ENSG00000206560. [O15084-1]
ENST00000399451; ENSP00000382379; ENSG00000206560. [O15084-3]
ENST00000412318; ENSP00000397341; ENSG00000206560. [O15084-3]
GeneID23243.
KEGGhsa:23243.
UCSCuc003cai.1. human. [O15084-3]
uc003cal.1. human. [O15084-4]
uc003cam.2. human. [O15084-1]

Organism-specific databases

CTD23243.
GeneCardsGC03M015708.
H-InvDBHIX0003106.
HGNCHGNC:29024. ANKRD28.
HPAHPA052925.
MIM611122. gene.
neXtProtNX_O15084.
PharmGKBPA134880251.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000033959.
HOVERGENHBG067697.
InParanoidO15084.
KOK15502.
OMADMLNDSD.
OrthoDBEOG7QG436.
TreeFamTF312824.

Gene expression databases

ArrayExpressO15084.
BgeeO15084.
CleanExHS_ANKRD28.
GenevestigatorO15084.

Family and domain databases

Gene3D1.25.40.20. 4 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 22 hits.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 28 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 4 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 24 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23243.
NextBio44912.
PROO15084.
SOURCESearch...

Entry information

Entry nameANR28_HUMAN
AccessionPrimary (citable) accession number: O15084
Secondary accession number(s): B4DES5 expand/collapse secondary AC list , Q1WWL4, Q29RW6, Q3B857, Q6ULS0, Q6ZT57
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM