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O75170 (PP6R2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 subunit 2
Alternative name(s):
SAPS domain family member 2
Gene names
Name:PPP6R2
Synonyms:KIAA0685, PP6R2, SAPS2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of protein phospatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Ref.5

Subunit structure

Protein phospatase 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 PPP6C and NFKBIE. Interacts with ANKRD28. Ref.5 Ref.6

Subcellular location

Cytoplasm Ref.5.

Tissue specificity

Ubiquitously expressed with strongest expression in the testis followed by liver, heart, kidney, brain and placenta. Ref.5

Sequence similarities

Belongs to the SAPS family.

Sequence caution

The sequence BAA31660.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

   Molecular functionprotein binding

Inferred from physical interaction Ref.6. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP6CO007432EBI-359739,EBI-359751

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75170-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: O75170-2)

The sequence of this isoform differs from the canonical sequence as follows:
     535-561: Missing.
     709-709: E → EA
     792-799: SQASYFAV → F
     952-966: KTDAPPEGAALNGPV → QMPRQKELP
Note: No experimental confirmation available.
Isoform 3 (identifier: O75170-3)

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: S → SR
     535-561: Missing.
     792-799: SQASYFAV → F
Isoform 4 (identifier: O75170-4)

The sequence of this isoform differs from the canonical sequence as follows:
     535-561: Missing.
     792-799: SQASYFAV → F
Isoform 5 (identifier: O75170-5)

The sequence of this isoform differs from the canonical sequence as follows:
     792-799: SQASYFAV → F
Isoform 6 (identifier: O75170-6)

The sequence of this isoform differs from the canonical sequence as follows:
     58-84: Missing.
     535-561: Missing.
     792-799: SQASYFAV → F

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 966966Serine/threonine-protein phosphatase 6 regulatory subunit 2
PRO_0000046098

Regions

Compositional bias820 – 8256Poly-Ser

Amino acid modifications

Modified residue2891Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10
Modified residue7701Phosphoserine Ref.9

Natural variations

Alternative sequence58 – 8427Missing in isoform 6.
VSP_037767
Alternative sequence2441S → SR in isoform 3.
VSP_037768
Alternative sequence535 – 56127Missing in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_030758
Alternative sequence7091E → EA in isoform 2.
VSP_030759
Alternative sequence792 – 7998SQASYFAV → F in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_030760
Alternative sequence952 – 96615KTDAP…LNGPV → QMPRQKELP in isoform 2.
VSP_030761
Natural variant6331D → E.
Corresponds to variant rs11555194 [ dbSNP | Ensembl ].
VAR_058402
Natural variant7321R → K.
Corresponds to variant rs13057311 [ dbSNP | Ensembl ].
VAR_058403

Experimental info

Sequence conflict2241D → G in BAH13719. Ref.2
Sequence conflict8061A → T in BAH13719. Ref.2
Sequence conflict8351Q → H in AAH52995. Ref.4

Sequences

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

Last modified January 15, 2008. Version 2.
Checksum: D3BC10EADB98FB62

FASTA966104,942
        10         20         30         40         50         60 
MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVSL 

        70         80         90        100        110        120 
ITQDPPLDME EKVRFKYPNT ACELLTCDVP QISDRLGGDE SLLSLLYDFL DHEPPLNPLL 

       130        140        150        160        170        180 
ASFFSKTIGN LIARKTEQVI TFLKKKDKFI SLVLKHIGTS ALMDLLLRLV SCVEPAGLRQ 

       190        200        210        220        230        240 
DVLHWLNEEK VIQRLVELIH PSQDEDRQSN ASQTLCDIVR LGRDQGSQLQ EALEPDPLLT 

       250        260        270        280        290        300 
ALESQDCVEQ LLKNMFDGDR TESCLVSGTQ VLLTLLETRR VGTEGLVDSF SQGLERSYAV 

       310        320        330        340        350        360 
SSSVLHGIEP RLKDFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPS 

       370        380        390        400        410        420 
INQELCRLNT MDLLLDLFFK YTWNNFLHFQ VELCIAAILS HAAREERTEA SGSESRVEPP 

       430        440        450        460        470        480 
HENGNRSLET PQPAASLPDN TMVTHLFQKC CLVQRILEAW EANDHTQAAG GMRRGNMGHL 

       490        500        510        520        530        540 
TRIANAVVQN LERGPVQTHI SEVIRGLPAD CRGRWESFVE ETLTETNRRN TVDLVSTHHL 

       550        560        570        580        590        600 
HSSSEDEDIE GAFPNELSLQ QAFSDYQIQQ MTANFVDQFG FNDEEFADQD DNINAPFDRI 

       610        620        630        640        650        660 
AEINFNIDAD EDSPSAALFE ACCSDRIQPF DDDEDEDIWE DSDTRCAARV MARPRFGAPH 

       670        680        690        700        710        720 
ASESCSKNGP ERGGQDGKAS LEAHRDAPGA GAPPAPGKKE APPVEGDSEG AMWTAVFDEP 

       730        740        750        760        770        780 
ANSTPTAPGV VRDVGSSVWA AGTSAPEEKG WAKFTDFQPF CCSESGPRCS SPVDTECSHA 

       790        800        810        820        830        840 
EGSRSQGPEK ASQASYFAVS PASPCAWNVC VTRKAPLLAS DSSSSGGSHS EDGDQKAASA 

       850        860        870        880        890        900 
MDAVSRGPGR EAPPLPTVAR TEEAVGRVGC ADSRLLSPAC PAPKEVTAAP AVAVPPEATV 

       910        920        930        940        950        960 
AITTALSKAG PAIPTPAVSS ALAVAVPLGP IMAVTAAPAM VATLGTVTKD GKTDAPPEGA 


ALNGPV 

« Hide

Isoform 2 [UniParc].

Checksum: DE1A1A4F2F66A0F9
Show »

FASTA927101,007
Isoform 3 [UniParc].

Checksum: D74E382158135767
Show »

FASTA933101,402
Isoform 4 [UniParc].

Checksum: 0E22A2912F2A1F2A
Show »

FASTA932101,246
Isoform 5 [UniParc].

Checksum: 6C9F6F32B2768517
Show »

FASTA959104,235
Isoform 6 [UniParc].

Checksum: 2B49E60FADD6D84D
Show »

FASTA90598,126

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Testis.
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 6).
Tissue: Brain, Lymph, Muscle, Placenta and Skin.
[5]"Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon."
Stefansson B., Brautigan D.L.
J. Biol. Chem. 281:22624-22634(2006) [PubMed: 16769727] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"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: 18186651] [Abstract]
Cited for: INTERACTION WITH PPP6C AND ANKRD28.
[7]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-770, MASS SPECTROMETRY.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014585 mRNA. Translation: BAA31660.2. Different initiation.
AK302472 mRNA. Translation: BAH13719.1.
AL096767, AL671545, AL954743 Genomic DNA. Translation: CAO03456.1.
AL096767, AL671545, AL954743 Genomic DNA. Translation: CAO03457.1.
AL096767, AL671545, AL954743 Genomic DNA. Translation: CAO03458.1.
AL096767, AL671545, AL954743 Genomic DNA. Translation: CAO03459.1.
AL954743, AL096767, AL671545 Genomic DNA. Translation: CAO03561.1.
AL954743, AL096767, AL671545 Genomic DNA. Translation: CAO03562.1.
AL954743, AL096767, AL671545 Genomic DNA. Translation: CAO03563.1.
AL954743, AL096767, AL671545 Genomic DNA. Translation: CAO03564.1.
AL671545, AL096767, AL954743 Genomic DNA. Translation: CAO03642.1.
AL671545, AL096767, AL954743 Genomic DNA. Translation: CAO03643.1.
AL671545, AL096767, AL954743 Genomic DNA. Translation: CAO03644.1.
AL671545, AL096767, AL954743 Genomic DNA. Translation: CAO03645.1.
BC000976 mRNA. Translation: AAH00976.2.
BC006568 mRNA. Translation: AAH06568.1.
BC032664 mRNA. Translation: AAH32664.1.
BC041698 mRNA. Translation: AAH41698.1.
BC052995 mRNA. Translation: AAH52995.1.
IPIIPI00375638.
IPI00414872.
IPI00853540.
IPI00853587.
IPI00939295.
IPI00942736.
PIRT00357.
RefSeqNP_001229827.1. NM_001242898.1.
NP_001229828.1. NM_001242899.1.
NP_001229829.1. NM_001242900.1.
NP_055493.2. NM_014678.4.
UniGeneHs.449098.
Hs.729287.

3D structure databases

ProteinModelPortalO75170.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27539N.
IntActO75170. 6 interactions.
MINTMINT-2867235.
STRINGO75170.

PTM databases

PhosphoSiteO75170.

Proteomic databases

PRIDEO75170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216061; ENSP00000216061; ENSG00000100239.
ENST00000395746; ENSP00000379095; ENSG00000100239.
GeneID9701.
KEGGhsa:9701.
UCSCuc003bky.1. human.
uc003blb.1. human.

Organism-specific databases

CTD9701.
GeneCardsGC22P050782.
HGNCHGNC:19253. PPP6R2.
HPAHPA030656.
MIM610877. gene.
neXtProtNX_O75170.
PharmGKBPA165378360.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13592.
GeneTreeENSGT00390000009899.
HOVERGENHBG069733.
InParanoidO75170.
OMAPPKKKAI.
PhylomeDBO75170.

Gene expression databases

ArrayExpressO75170.
BgeeO75170.
CleanExHS_SAPS2.
GenevestigatorO75170.
GermOnlineENSG00000100239. Homo sapiens.

Family and domain databases

InterProIPR007587. SAPS.
[Graphical view]
KOK15500.
PANTHERPTHR12634. SAPS. 1 hit.
PfamPF04499. SAPS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry namePP6R2_HUMAN
AccessionPrimary (citable) accession number: O75170
Secondary accession number(s): A6PVG3 expand/collapse secondary AC list , B7Z7T3, Q5U5P3, Q7Z2L2, Q7Z5G5, Q7Z731, Q9UGB9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 90 of the entry and version 2 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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families