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Q5H9R7

- PP6R3_HUMAN

UniProt

Q5H9R7 - PP6R3_HUMAN

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Protein
Serine/threonine-protein phosphatase 6 regulatory subunit 3
Gene
PPP6R3, C11orf23, KIAA1558, PP6R3, SAPL, SAPS3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein phosphatase binding Source: MGI

GO - Biological processi

  1. regulation of phosphoprotein phosphatase activity Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 6 regulatory subunit 3
Alternative name(s):
SAPS domain family member 3
Sporulation-induced transcript 4-associated protein SAPL
Gene namesi
Name:PPP6R3
Synonyms:C11orf23, KIAA1558, PP6R3, SAPL, SAPS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1173. PPP6R3.

Subcellular locationi

Cytoplasm. Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 873873Serine/threonine-protein phosphatase 6 regulatory subunit 3
PRO_0000046100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei579 – 5791Phosphoserine4 Publications
Modified residuei617 – 6171Phosphoserine6 Publications
Modified residuei722 – 7221Phosphoserine1 Publication
Modified residuei853 – 8531Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5H9R7.
PaxDbiQ5H9R7.
PRIDEiQ5H9R7.

PTM databases

PhosphoSiteiQ5H9R7.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, placenta, heart, pancreas, testis, brain, lung, liver, kidney, spleen, thymus, prostate, small intestine, colon and leukocytes.2 Publications

Gene expression databases

ArrayExpressiQ5H9R7.
BgeeiQ5H9R7.
GenevestigatoriQ5H9R7.

Organism-specific databases

HPAiCAB017183.
HPA038467.
HPA038468.

Interactioni

Subunit structurei

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 PPP6C and ANKRD28.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKRD28O150845EBI-355498,EBI-359567
PPP6CO007435EBI-355498,EBI-359751

Protein-protein interaction databases

BioGridi120579. 51 interactions.
IntActiQ5H9R7. 14 interactions.
MINTiMINT-5004961.

Structurei

3D structure databases

ProteinModelPortaliQ5H9R7.

Family & Domainsi

Sequence similaritiesi

Belongs to the SAPS family.

Phylogenomic databases

eggNOGiNOG303042.
HOVERGENiHBG069733.
KOiK15501.
OrthoDBiEOG7PGDQ3.
PhylomeDBiQ5H9R7.
TreeFamiTF313227.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR007587. SAPS.
[Graphical view]
PANTHERiPTHR12634. PTHR12634. 1 hit.
PfamiPF04499. SAPS. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5H9R7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK    50
AECLEDLVSF IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE 100
SLLMKLYSFL LNDSPLNPLL ASFFSKVLSI LISRKPEQIV DFLKKKHDFV 150
DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ DVLNWLNEEK IIQRLVEIVH 200
PSQEEDRHSN ASQSLCEIVR LSRDQMLQIQ NSTEPDPLLA TLEKQEIIEQ 250
LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS 300
VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGVLDPPV GNTRLNVIRL 350
ISSLLQTNTS SINGDLMELN SIGVILNMFF KYTWNNFLHT QVEICIALIL 400
ASPFENTENA TITDQDSTGD NLLLKHLFQK CQLIERILEA WEMNEKKQAE 450
GGRRHGYMGH LTRIANCIVH STDKGPNSAL VQQLIKDLPD EVRERWETFC 500
TSSLGETNKR NTVDLVTTCH IHSSSDDEID FKETGFSQDS SLQQAFSDYQ 550
MQQMTSNFID QFGFNDEKFA DQDDIGNVSF DRVSDINFTL NTNESGNIAL 600
FEACCKERIQ QFDDGGSDEE DIWEEKHIAF TPESQRRSSS GSTDSEESTD 650
SEEEDGAKQD LFEPSSANTE DKMEVDLSEP PNWSANFDVP METTHGAPLD 700
SVGSDVWSTE EPMPTKETGW ASFSEFTSSL STKDSLRSNS PVEMETSTEP 750
MDPLTPSAAA LAVQPEAAGS VAMEASSDGE EDAESTDKVT ETVMNGGMKE 800
TLSLTVDAKT ETAVFKSEEG KLSTSQDAAC KDAEECPETA EAKCAAPRPP 850
SSSPEQRTGQ PSAPGDTSVN GPV 873
Length:873
Mass (Da):97,669
Last modified:February 7, 2006 - v2
Checksum:i5B4C69991E7DE16F
GO
Isoform 2 (identifier: Q5H9R7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     544-549: Missing.

Show »
Length:867
Mass (Da):96,957
Checksum:i9E76BCA0E23EE3DE
GO
Isoform 3 (identifier: Q5H9R7-3) [UniParc]FASTAAdd to Basket

Also known as: B, C11orf23b, SAPLb

The sequence of this isoform differs from the canonical sequence as follows:
     326-376: Missing.
     516-544: Missing.
     857-873: RTGQPSAPGDTSVNGPV → SGVEIPALPGQWSQQ

Show »
Length:791
Mass (Da):88,909
Checksum:i1C936F03A484D53D
GO
Isoform 4 (identifier: Q5H9R7-4) [UniParc]FASTAAdd to Basket

Also known as: A, C11orf23a, SAPLa

The sequence of this isoform differs from the canonical sequence as follows:
     326-376: Missing.
     516-544: Missing.

Show »
Length:793
Mass (Da):88,952
Checksum:iAC5BEE22285932F4
GO
Isoform 5 (identifier: Q5H9R7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     817-817: S → RVLKSYR

Show »
Length:879
Mass (Da):98,485
Checksum:iE0AE6571756853C1
GO
Isoform 6 (identifier: Q5H9R7-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     516-544: Missing.

Show »
Length:844
Mass (Da):94,445
Checksum:iADB89AA9C567C580
GO

Sequence cautioni

The sequence AAZ99639.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA91978.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB13384.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAB71396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti842 – 8421A → V.
Corresponds to variant rs34009811 [ dbSNP | Ensembl ].
VAR_057720

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 37651Missing in isoform 3 and isoform 4.
VSP_017140Add
BLAST
Alternative sequencei516 – 54429Missing in isoform 3, isoform 4 and isoform 6.
VSP_017141Add
BLAST
Alternative sequencei544 – 5496Missing in isoform 2.
VSP_017142
Alternative sequencei817 – 8171S → RVLKSYR in isoform 5.
VSP_017143
Alternative sequencei857 – 87317RTGQP…VNGPV → SGVEIPALPGQWSQQ in isoform 3.
VSP_017144Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921P → S in CAH18675. 1 Publication
Sequence conflicti443 – 4431M → V in BAB71396. 1 Publication
Sequence conflicti477 – 4771N → S in CAI45957. 1 Publication
Sequence conflicti677 – 6771L → P in CAI45957. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF264779 mRNA. Translation: AAG36934.1.
AF264780 mRNA. Translation: AAG36935.1.
DQ111954 mRNA. Translation: AAZ99639.2. Different initiation.
AB046778 mRNA. Translation: BAB13384.2. Different initiation.
AL834471 mRNA. Translation: CAD39130.1.
CR749815 mRNA. Translation: CAH18675.1.
CR933658 mRNA. Translation: CAI45957.1.
BC007738 mRNA. Translation: AAH07738.2.
BC105933 mRNA. Translation: AAI05934.1.
BC105934 mRNA. Translation: AAI05935.1.
BC107599 mRNA. Translation: AAI07600.1.
AK001920 mRNA. Translation: BAA91978.1. Different initiation.
AK057250 mRNA. Translation: BAB71396.1. Different initiation.
CCDSiCCDS53671.1. [Q5H9R7-5]
CCDS53672.1. [Q5H9R7-1]
CCDS53673.1. [Q5H9R7-2]
CCDS53674.1. [Q5H9R7-6]
CCDS53675.1. [Q5H9R7-3]
CCDS8182.1. [Q5H9R7-4]
RefSeqiNP_001157632.1. NM_001164160.1. [Q5H9R7-5]
NP_001157633.1. NM_001164161.1. [Q5H9R7-1]
NP_001157634.1. NM_001164162.1. [Q5H9R7-2]
NP_001157635.1. NM_001164163.1. [Q5H9R7-6]
NP_001157636.1. NM_001164164.1. [Q5H9R7-3]
NP_060782.2. NM_018312.4. [Q5H9R7-4]
XP_006718676.1. XM_006718613.1. [Q5H9R7-1]
XP_006718677.1. XM_006718614.1. [Q5H9R7-2]
XP_006718681.1. XM_006718618.1. [Q5H9R7-6]
XP_006718687.1. XM_006718624.1. [Q5H9R7-4]
UniGeneiHs.503022.

Genome annotation databases

EnsembliENST00000265636; ENSP00000265636; ENSG00000110075. [Q5H9R7-4]
ENST00000393800; ENSP00000377389; ENSG00000110075. [Q5H9R7-1]
ENST00000393801; ENSP00000377390; ENSG00000110075. [Q5H9R7-5]
ENST00000524845; ENSP00000431415; ENSG00000110075. [Q5H9R7-6]
ENST00000524904; ENSP00000433058; ENSG00000110075. [Q5H9R7-2]
ENST00000529710; ENSP00000437329; ENSG00000110075. [Q5H9R7-3]
GeneIDi55291.
KEGGihsa:55291.
UCSCiuc001onu.3. human. [Q5H9R7-4]
uc001onv.3. human. [Q5H9R7-5]
uc001onw.3. human. [Q5H9R7-1]
uc001onx.3. human. [Q5H9R7-2]
uc001ony.4. human. [Q5H9R7-6]
uc009ysh.3. human. [Q5H9R7-3]

Polymorphism databases

DMDMi88941982.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF264779 mRNA. Translation: AAG36934.1 .
AF264780 mRNA. Translation: AAG36935.1 .
DQ111954 mRNA. Translation: AAZ99639.2 . Different initiation.
AB046778 mRNA. Translation: BAB13384.2 . Different initiation.
AL834471 mRNA. Translation: CAD39130.1 .
CR749815 mRNA. Translation: CAH18675.1 .
CR933658 mRNA. Translation: CAI45957.1 .
BC007738 mRNA. Translation: AAH07738.2 .
BC105933 mRNA. Translation: AAI05934.1 .
BC105934 mRNA. Translation: AAI05935.1 .
BC107599 mRNA. Translation: AAI07600.1 .
AK001920 mRNA. Translation: BAA91978.1 . Different initiation.
AK057250 mRNA. Translation: BAB71396.1 . Different initiation.
CCDSi CCDS53671.1. [Q5H9R7-5 ]
CCDS53672.1. [Q5H9R7-1 ]
CCDS53673.1. [Q5H9R7-2 ]
CCDS53674.1. [Q5H9R7-6 ]
CCDS53675.1. [Q5H9R7-3 ]
CCDS8182.1. [Q5H9R7-4 ]
RefSeqi NP_001157632.1. NM_001164160.1. [Q5H9R7-5 ]
NP_001157633.1. NM_001164161.1. [Q5H9R7-1 ]
NP_001157634.1. NM_001164162.1. [Q5H9R7-2 ]
NP_001157635.1. NM_001164163.1. [Q5H9R7-6 ]
NP_001157636.1. NM_001164164.1. [Q5H9R7-3 ]
NP_060782.2. NM_018312.4. [Q5H9R7-4 ]
XP_006718676.1. XM_006718613.1. [Q5H9R7-1 ]
XP_006718677.1. XM_006718614.1. [Q5H9R7-2 ]
XP_006718681.1. XM_006718618.1. [Q5H9R7-6 ]
XP_006718687.1. XM_006718624.1. [Q5H9R7-4 ]
UniGenei Hs.503022.

3D structure databases

ProteinModelPortali Q5H9R7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120579. 51 interactions.
IntActi Q5H9R7. 14 interactions.
MINTi MINT-5004961.

PTM databases

PhosphoSitei Q5H9R7.

Polymorphism databases

DMDMi 88941982.

Proteomic databases

MaxQBi Q5H9R7.
PaxDbi Q5H9R7.
PRIDEi Q5H9R7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265636 ; ENSP00000265636 ; ENSG00000110075 . [Q5H9R7-4 ]
ENST00000393800 ; ENSP00000377389 ; ENSG00000110075 . [Q5H9R7-1 ]
ENST00000393801 ; ENSP00000377390 ; ENSG00000110075 . [Q5H9R7-5 ]
ENST00000524845 ; ENSP00000431415 ; ENSG00000110075 . [Q5H9R7-6 ]
ENST00000524904 ; ENSP00000433058 ; ENSG00000110075 . [Q5H9R7-2 ]
ENST00000529710 ; ENSP00000437329 ; ENSG00000110075 . [Q5H9R7-3 ]
GeneIDi 55291.
KEGGi hsa:55291.
UCSCi uc001onu.3. human. [Q5H9R7-4 ]
uc001onv.3. human. [Q5H9R7-5 ]
uc001onw.3. human. [Q5H9R7-1 ]
uc001onx.3. human. [Q5H9R7-2 ]
uc001ony.4. human. [Q5H9R7-6 ]
uc009ysh.3. human. [Q5H9R7-3 ]

Organism-specific databases

CTDi 55291.
GeneCardsi GC11P068229.
HGNCi HGNC:1173. PPP6R3.
HPAi CAB017183.
HPA038467.
HPA038468.
MIMi 610879. gene.
neXtProti NX_Q5H9R7.
PharmGKBi PA25487.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303042.
HOVERGENi HBG069733.
KOi K15501.
OrthoDBi EOG7PGDQ3.
PhylomeDBi Q5H9R7.
TreeFami TF313227.

Miscellaneous databases

ChiTaRSi PPP6R3. human.
GenomeRNAii 55291.
NextBioi 59478.
PROi Q5H9R7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5H9R7.
Bgeei Q5H9R7.
Genevestigatori Q5H9R7.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR007587. SAPS.
[Graphical view ]
PANTHERi PTHR12634. PTHR12634. 1 hit.
Pfami PF04499. SAPS. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13."
    Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.
    Genomics 72:231-242(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, TISSUE SPECIFICITY.
  2. Guergnon J., Stefansson B., Brautigan D.L.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-873 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-873 (ISOFORMS 1/2/4/6).
    Tissue: Colon carcinoma, Melanoma and Seminal plasma.
  6. "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] (ISOFORMS 1 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 650-873 (ISOFORMS 1/2/4/6).
    Tissue: Muscle.
  7. "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.
    , 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] OF 221-873 (ISOFORM 1).
    Tissue: Placenta and Testis.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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: SUBCELLULAR LOCATION, INTERACTION WITH PPP6C AND ANKRD28.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP6R3_HUMAN
AccessioniPrimary (citable) accession number: Q5H9R7
Secondary accession number(s): Q3B7I1
, Q3I4Y0, Q3KR35, Q68CR3, Q7L4R8, Q8N3B2, Q96MB2, Q9H2K5, Q9H2K6, Q9HCL4, Q9NUY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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