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Protein

Serine/threonine-protein phosphatase 6 catalytic subunit

Gene

PPP6C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7.4 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Manganese 1By similarity
Metal bindingi55 – 551Manganese 1By similarity
Metal bindingi81 – 811Manganese 1By similarity
Metal bindingi81 – 811Manganese 2By similarity
Metal bindingi113 – 1131Manganese 2By similarity
Active sitei114 – 1141Proton donorBy similarity
Metal bindingi163 – 1631Manganese 2By similarity
Metal bindingi237 – 2371Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: MGI

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: ProtInc
  2. protein dephosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 6 catalytic subunit (EC:3.1.3.16)
Short name:
PP6C
Cleaved into the following chain:
Gene namesi
Name:PPP6C
Synonyms:PPP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9323. PPP6C.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Serine/threonine-protein phosphatase 6 catalytic subunitPRO_0000424504Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 305304Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processedPRO_0000058877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00743.
PaxDbiO00743.
PeptideAtlasiO00743.
PRIDEiO00743.

2D gel databases

OGPiO00743.

PTM databases

DEPODiO00743.
PhosphoSiteiO00743.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissues tested with highest expression levels in testis, heart, kidney, brain, stomach, liver and skeletal muscle and lowest in placenta, lung colon and spleen.2 Publications

Inductioni

Regulated by IL2/interleukin-2 in peripheral blood T cells.1 Publication

Gene expression databases

BgeeiO00743.
CleanExiHS_PPP6C.
ExpressionAtlasiO00743. baseline and differential.
GenevestigatoriO00743.

Organism-specific databases

HPAiHPA050940.

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 IGBP1, MAP3K7, NFKBIE, PPP6R1, PPP6R2 and PPP6R3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKRD28O150849EBI-359751,EBI-359567
IGBP1P7831810EBI-359751,EBI-1055954
MAP3K7O433184EBI-359751,EBI-358684
PPP6R1Q9UPN711EBI-359751,EBI-359745
PPP6R2O751708EBI-359751,EBI-359739
PPP6R3Q5H9R75EBI-359751,EBI-355498
TIPRLO756634EBI-359751,EBI-1054735

Protein-protein interaction databases

BioGridi111529. 33 interactions.
DIPiDIP-27581N.
IntActiO00743. 20 interactions.
MINTiMINT-1139697.
STRINGi9606.ENSP00000392147.

Structurei

3D structure databases

ProteinModelPortaliO00743.
SMRiO00743. Positions 5-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074961.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiO00743.
KOiK15498.
OMAiENWAVSP.
OrthoDBiEOG74N5H2.
PhylomeDBiO00743.
TreeFamiTF105563.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00743-1) [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

        10         20         30         40         50
MAPLDLDKYV EIARLCKYLP ENDLKRLCDY VCDLLLEESN VQPVSTPVTV
60 70 80 90 100
CGDIHGQFYD LCELFRTGGQ VPDTNYIFMG DFVDRGYYSL ETFTYLLALK
110 120 130 140 150
AKWPDRITLL RGNHESRQIT QVYGFYDECQ TKYGNANAWR YCTKVFDMLT
160 170 180 190 200
VAALIDEQIL CVHGGLSPDI KTLDQIRTIE RNQEIPHKGA FCDLVWSDPE
210 220 230 240 250
DVDTWAISPR GAGWLFGAKV TNEFVHINNL KLICRAHQLV HEGYKFMFDE
260 270 280 290 300
KLVTVWSAPN YCYRCGNIAS IMVFKDVNTR EPKLFRAVPD SERVIPPRTT

TPYFL
Length:305
Mass (Da):35,144
Last modified:July 1, 1997 - v1
Checksum:i55E95DB6CEA7CFF4
GO
Isoform 2 (identifier: O00743-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-79: Missing.

Show »
Length:283
Mass (Da):32,532
Checksum:iC2334512732059DC
GO
Isoform 3 (identifier: O00743-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-25: K → KVSPICGLAPSGCGAPAGRPFLSPGPPPVFHFLRFLKE

Show »
Length:342
Mass (Da):38,947
Checksum:iC26CAD5C8016F112
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 644LCEL → AG in AAD45400 (PubMed:10227379).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 251K → KVSPICGLAPSGCGAPAGRP FLSPGPPPVFHFLRFLKE in isoform 3. 1 PublicationVSP_041158
Alternative sequencei58 – 7922Missing in isoform 2. 1 PublicationVSP_038376Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92972 mRNA. Translation: CAA63549.1.
AF035158 mRNA. Translation: AAD45400.2.
AK295190 mRNA. Translation: BAH12005.1.
AK299087 mRNA. Translation: BAH12945.1.
AK312332 mRNA. Translation: BAG35253.1.
BT019708 mRNA. Translation: AAV38514.1.
AL445930 Genomic DNA. Translation: CAI13677.1.
CH471090 Genomic DNA. Translation: EAW87611.1.
BC006990 mRNA. Translation: AAH06990.1.
CCDSiCCDS48018.1. [O00743-3]
CCDS48019.1. [O00743-2]
CCDS6861.1. [O00743-1]
RefSeqiNP_001116827.1. NM_001123355.1. [O00743-3]
NP_001116841.1. NM_001123369.1. [O00743-2]
NP_002712.1. NM_002721.4. [O00743-1]
UniGeneiHs.744091.

Genome annotation databases

EnsembliENST00000373547; ENSP00000362648; ENSG00000119414. [O00743-1]
ENST00000415905; ENSP00000411744; ENSG00000119414. [O00743-2]
ENST00000451402; ENSP00000392147; ENSG00000119414. [O00743-3]
GeneIDi5537.
KEGGihsa:5537.
UCSCiuc004bpg.4. human. [O00743-1]
uc010mwv.3. human. [O00743-3]
uc010mww.3. human. [O00743-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92972 mRNA. Translation: CAA63549.1.
AF035158 mRNA. Translation: AAD45400.2.
AK295190 mRNA. Translation: BAH12005.1.
AK299087 mRNA. Translation: BAH12945.1.
AK312332 mRNA. Translation: BAG35253.1.
BT019708 mRNA. Translation: AAV38514.1.
AL445930 Genomic DNA. Translation: CAI13677.1.
CH471090 Genomic DNA. Translation: EAW87611.1.
BC006990 mRNA. Translation: AAH06990.1.
CCDSiCCDS48018.1. [O00743-3]
CCDS48019.1. [O00743-2]
CCDS6861.1. [O00743-1]
RefSeqiNP_001116827.1. NM_001123355.1. [O00743-3]
NP_001116841.1. NM_001123369.1. [O00743-2]
NP_002712.1. NM_002721.4. [O00743-1]
UniGeneiHs.744091.

3D structure databases

ProteinModelPortaliO00743.
SMRiO00743. Positions 5-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111529. 33 interactions.
DIPiDIP-27581N.
IntActiO00743. 20 interactions.
MINTiMINT-1139697.
STRINGi9606.ENSP00000392147.

PTM databases

DEPODiO00743.
PhosphoSiteiO00743.

2D gel databases

OGPiO00743.

Proteomic databases

MaxQBiO00743.
PaxDbiO00743.
PeptideAtlasiO00743.
PRIDEiO00743.

Protocols and materials databases

DNASUi5537.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373547; ENSP00000362648; ENSG00000119414. [O00743-1]
ENST00000415905; ENSP00000411744; ENSG00000119414. [O00743-2]
ENST00000451402; ENSP00000392147; ENSG00000119414. [O00743-3]
GeneIDi5537.
KEGGihsa:5537.
UCSCiuc004bpg.4. human. [O00743-1]
uc010mwv.3. human. [O00743-3]
uc010mww.3. human. [O00743-2]

Organism-specific databases

CTDi5537.
GeneCardsiGC09M127908.
HGNCiHGNC:9323. PPP6C.
HPAiHPA050940.
MIMi612725. gene.
neXtProtiNX_O00743.
PharmGKBiPA33687.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074961.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiO00743.
KOiK15498.
OMAiENWAVSP.
OrthoDBiEOG74N5H2.
PhylomeDBiO00743.
TreeFamiTF105563.

Miscellaneous databases

ChiTaRSiPPP6C. human.
GeneWikiiPPP6C.
GenomeRNAii5537.
NextBioi21450.
PROiO00743.
SOURCEiSearch...

Gene expression databases

BgeeiO00743.
CleanExiHS_PPP6C.
ExpressionAtlasiO00743. baseline and differential.
GenevestigatoriO00743.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation."
    Bastians H., Ponstingl H.
    J. Cell Sci. 109:2865-2874(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "Identification of a type 6 protein Ser/Thr phosphatase regulated by interleukin-2 stimulation."
    Filali M., Li S., Kim H.W., Wadzinski B., Kamoun M.
    J. Cell. Biochem. 73:153-163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION.
    Tissue: Brain.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Cerebellum.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Urinary bladder.
  8. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (FEB-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 67-100; 118-140; 145-171; 211-231 AND 252-275, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  9. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
    Chen J., Peterson R.T., Schreiber S.L.
    Biochem. Biophys. Res. Commun. 247:827-832(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGBP1.
  10. "Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon."
    Stefansson B., Brautigan D.L.
    J. Biol. Chem. 281:22624-22634(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIE; PPP6R1 AND PPP6R2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway."
    Kajino T., Ren H., Iemura S., Natsume T., Stefansson B., Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J.
    J. Biol. Chem. 281:39891-39896(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K7.
  12. "Protein phosphatase PP6 N terminal domain restricts G1 to S phase progression in human cancer cells."
    Stefansson B., Brautigan D.L.
    Cell Cycle 6:1386-1392(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains."
    Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.
    Biochemistry 47:1442-1451(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD28; PPP6R1; PPP6R2 AND PPP6R3.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPPP6_HUMAN
AccessioniPrimary (citable) accession number: O00743
Secondary accession number(s): B2R5V6
, B7Z2W9, B7Z5K9, Q5U0A2, Q9UIC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 146 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.