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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform

Gene

PPP2R5D

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

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

GO - Molecular functioni

  1. protein phosphatase type 2A regulator activity Source: ProtInc
  2. protein serine/threonine phosphatase activity Source: Reactome

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. dephosphorylation Source: GOC
  3. energy reserve metabolic process Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. glycolytic process Source: Reactome
  6. innate immune response Source: Reactome
  7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  9. nervous system development Source: ProtInc
  10. neurotrophin TRK receptor signaling pathway Source: Reactome
  11. pathogenesis Source: Reactome
  12. regulation of catalytic activity Source: GOC
  13. small molecule metabolic process Source: Reactome
  14. stress-activated MAPK cascade Source: Reactome
  15. toll-like receptor 10 signaling pathway Source: Reactome
  16. toll-like receptor 2 signaling pathway Source: Reactome
  17. toll-like receptor 3 signaling pathway Source: Reactome
  18. toll-like receptor 4 signaling pathway Source: Reactome
  19. toll-like receptor 5 signaling pathway Source: Reactome
  20. toll-like receptor 9 signaling pathway Source: Reactome
  21. toll-like receptor signaling pathway Source: Reactome
  22. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  23. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  24. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_228060. truncations of AMER1 destabilize the destruction complex.
REACT_228137. S45 mutants of beta-catenin aren't phosphorylated.
REACT_228159. S33 mutants of beta-catenin aren't phosphorylated.
REACT_228196. APC truncation mutants have impaired AXIN binding.
REACT_228251. S37 mutants of beta-catenin aren't phosphorylated.
REACT_228261. T41 mutants of beta-catenin aren't phosphorylated.
REACT_228285. AXIN missense mutants destabilize the destruction complex.
REACT_228314. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_23879. Platelet sensitization by LDL.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
SignaLinkiQ14738.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
Alternative name(s):
PP2A B subunit isoform B'-delta
PP2A B subunit isoform B56-delta
PP2A B subunit isoform PR61-delta
PP2A B subunit isoform R5-delta
Gene namesi
Name:PPP2R5D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9312. PPP2R5D.

Subcellular locationi

Cytoplasm. Nucleus
Note: Nuclear in interphase, nuclear during mitosis.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
  3. nucleus Source: ProtInc
  4. protein phosphatase type 2A complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33676.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 602602Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoformPRO_0000071452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei573 – 5731Phosphoserine2 Publications
Modified residuei598 – 5981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14738.
PaxDbiQ14738.
PRIDEiQ14738.

PTM databases

PhosphoSiteiQ14738.

Expressioni

Tissue specificityi

Isoform Delta-2 is widely expressed. Isoform Delta-1 is highly expressed in brain.

Inductioni

By retinoic acid; in neuroblastoma cell lines.

Gene expression databases

BgeeiQ14738.
CleanExiHS_PPP2R5D.
ExpressionAtlasiQ14738. baseline and differential.
GenevestigatoriQ14738.

Organism-specific databases

HPAiHPA029045.
HPA029046.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGOL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ClockO087852EBI-396563,EBI-79859From a different organism.
PPFIA1Q131362EBI-396563,EBI-745426
PPP2R1AP301534EBI-396563,EBI-302388
PPP2R1BP301542EBI-396563,EBI-357094

Protein-protein interaction databases

BioGridi111520. 41 interactions.
DIPiDIP-29961N.
IntActiQ14738. 26 interactions.
MINTiMINT-5006095.
STRINGi9606.ENSP00000417963.

Structurei

3D structure databases

ProteinModelPortaliQ14738.
SMRiQ14738. Positions 110-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 3821
Repeati39 – 4022
Repeati41 – 4223
Repeati43 – 4424
Repeati45 – 4625
Repeati47 – 4826; approximate
Repeati49 – 5027; approximate
Repeati51 – 5228

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 52168 X 2 AA approximate tandem repeats of Q-PAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi523 – 5308SH3-binding; class ISequence Analysis
Motifi548 – 56518Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOVERGENiHBG000009.
InParanoidiQ14738.
KOiK11584.
OMAiGSGRAEM.
OrthoDBiEOG7C2R2S.
PhylomeDBiQ14738.
TreeFamiTF105556.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform Delta-1 (identifier: Q14738-1) [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
MPYKLKKEKE PPKVAKCTAK PSSSGKDGGG ENTEEAQPQP QPQPQPQAQS
60 70 80 90 100
QPPSSNKRPS NSTPPPTQLS KIKYSGGPQI VKKERRQSSS RFNLSKNREL
110 120 130 140 150
QKLPALKDSP TQEREELFIQ KLRQCCVLFD FVSDPLSDLK FKEVKRAGLN
160 170 180 190 200
EMVEYITHSR DVVTEAIYPE AVTMFSVNLF RTLPPSSNPT GAEFDPEEDE
210 220 230 240 250
PTLEAAWPHL QLVYEFFLRF LESPDFQPNI AKKYIDQKFV LALLDLFDSE
260 270 280 290 300
DPRERDFLKT ILHRIYGKFL GLRAYIRRQI NHIFYRFIYE TEHHNGIAEL
310 320 330 340 350
LEILGSIING FALPLKEEHK MFLIRVLLPL HKVKSLSVYH PQLAYCVVQF
360 370 380 390 400
LEKESSLTEP VIVGLLKFWP KTHSPKEVMF LNELEEILDV IEPSEFSKVM
410 420 430 440 450
EPLFRQLAKC VSSPHFQVAE RALYYWNNEY IMSLISDNAA RVLPIMFPAL
460 470 480 490 500
YRNSKSHWNK TIHGLIYNAL KLFMEMNQKL FDDCTQQYKA EKQKGRFRMK
510 520 530 540 550
EREEMWQKIE ELARLNPQYP MFRAPPPLPP VYSMETETPT AEDIQLLKRT
560 570 580 590 600
VETEAVQMLK DIKKEKVLLR RKSELPQDVY TIKALEAHKR AEEFLTASQE

AL
Length:602
Mass (Da):69,992
Last modified:November 1, 1996 - v1
Checksum:iF15F71AF4E565387
GO
Isoform Delta-2 (identifier: Q14738-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-116: Missing.

Show »
Length:570
Mass (Da):66,181
Checksum:i978213A7CD1B21A5
GO
Isoform Delta-3 (identifier: Q14738-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-116: Missing.

Show »
Length:496
Mass (Da):58,453
Checksum:iA57661F8B20731CB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531P → S Found in a patient with delayed psychomotor development, no speech and cataracts. 1 Publication
VAR_069414

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei11 – 116106Missing in isoform Delta-3. 1 PublicationVSP_005110Add
BLAST
Alternative sequencei85 – 11632Missing in isoform Delta-2. 3 PublicationsVSP_005111Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76702 mRNA. Translation: AAB69751.1.
AB000634 mRNA. Translation: BAA20381.1.
AB000635 mRNA. Translation: BAA20382.1.
D78360 mRNA. Translation: BAA11372.1.
AK290604 mRNA. Translation: BAF83293.1.
AB451342 mRNA. Translation: BAG70156.1.
AB451357 mRNA. Translation: BAG70171.1.
AL136304 Genomic DNA. Translation: CAI19791.1.
CH471081 Genomic DNA. Translation: EAX04133.1.
BC010692 mRNA. Translation: AAH10692.1.
BC001095 mRNA. Translation: AAH01095.1.
BC001175 mRNA. Translation: AAH01175.1.
CCDSiCCDS43464.1. [Q14738-3]
CCDS4878.1. [Q14738-1]
CCDS55002.1. [Q14738-2]
PIRiS68686.
RefSeqiNP_001257405.1. NM_001270476.1.
NP_006236.1. NM_006245.3. [Q14738-1]
NP_851307.1. NM_180976.2. [Q14738-2]
NP_851308.1. NM_180977.2. [Q14738-3]
UniGeneiHs.533308.

Genome annotation databases

EnsembliENST00000394110; ENSP00000377669; ENSG00000112640. [Q14738-2]
ENST00000461010; ENSP00000420674; ENSG00000112640. [Q14738-3]
ENST00000485511; ENSP00000417963; ENSG00000112640. [Q14738-1]
GeneIDi5528.
KEGGihsa:5528.
UCSCiuc003oth.4. human. [Q14738-1]
uc010jyd.4. human. [Q14738-3]
uc021yzq.2. human. [Q14738-2]

Polymorphism databases

DMDMi7387495.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76702 mRNA. Translation: AAB69751.1.
AB000634 mRNA. Translation: BAA20381.1.
AB000635 mRNA. Translation: BAA20382.1.
D78360 mRNA. Translation: BAA11372.1.
AK290604 mRNA. Translation: BAF83293.1.
AB451342 mRNA. Translation: BAG70156.1.
AB451357 mRNA. Translation: BAG70171.1.
AL136304 Genomic DNA. Translation: CAI19791.1.
CH471081 Genomic DNA. Translation: EAX04133.1.
BC010692 mRNA. Translation: AAH10692.1.
BC001095 mRNA. Translation: AAH01095.1.
BC001175 mRNA. Translation: AAH01175.1.
CCDSiCCDS43464.1. [Q14738-3]
CCDS4878.1. [Q14738-1]
CCDS55002.1. [Q14738-2]
PIRiS68686.
RefSeqiNP_001257405.1. NM_001270476.1.
NP_006236.1. NM_006245.3. [Q14738-1]
NP_851307.1. NM_180976.2. [Q14738-2]
NP_851308.1. NM_180977.2. [Q14738-3]
UniGeneiHs.533308.

3D structure databases

ProteinModelPortaliQ14738.
SMRiQ14738. Positions 110-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111520. 41 interactions.
DIPiDIP-29961N.
IntActiQ14738. 26 interactions.
MINTiMINT-5006095.
STRINGi9606.ENSP00000417963.

PTM databases

PhosphoSiteiQ14738.

Polymorphism databases

DMDMi7387495.

Proteomic databases

MaxQBiQ14738.
PaxDbiQ14738.
PRIDEiQ14738.

Protocols and materials databases

DNASUi5528.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394110; ENSP00000377669; ENSG00000112640. [Q14738-2]
ENST00000461010; ENSP00000420674; ENSG00000112640. [Q14738-3]
ENST00000485511; ENSP00000417963; ENSG00000112640. [Q14738-1]
GeneIDi5528.
KEGGihsa:5528.
UCSCiuc003oth.4. human. [Q14738-1]
uc010jyd.4. human. [Q14738-3]
uc021yzq.2. human. [Q14738-2]

Organism-specific databases

CTDi5528.
GeneCardsiGC06P042952.
HGNCiHGNC:9312. PPP2R5D.
HPAiHPA029045.
HPA029046.
MIMi601646. gene.
neXtProtiNX_Q14738.
PharmGKBiPA33676.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOVERGENiHBG000009.
InParanoidiQ14738.
KOiK11584.
OMAiGSGRAEM.
OrthoDBiEOG7C2R2S.
PhylomeDBiQ14738.
TreeFamiTF105556.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_228060. truncations of AMER1 destabilize the destruction complex.
REACT_228137. S45 mutants of beta-catenin aren't phosphorylated.
REACT_228159. S33 mutants of beta-catenin aren't phosphorylated.
REACT_228196. APC truncation mutants have impaired AXIN binding.
REACT_228251. S37 mutants of beta-catenin aren't phosphorylated.
REACT_228261. T41 mutants of beta-catenin aren't phosphorylated.
REACT_228285. AXIN missense mutants destabilize the destruction complex.
REACT_228314. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_23879. Platelet sensitization by LDL.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
SignaLinkiQ14738.

Miscellaneous databases

GeneWikiiPPP2R5D.
GenomeRNAii5528.
NextBioi21410.
PROiQ14738.
SOURCEiSearch...

Gene expression databases

BgeeiQ14738.
CleanExiHS_PPP2R5D.
ExpressionAtlasiQ14738. baseline and differential.
GenevestigatoriQ14738.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
    McCright B., Rivers A.M., Audlin S., Virshup D.M.
    J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-1).
    Tissue: Fetal brain.
  2. "Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory subunit (B'' or delta) of human protein phosphatase 2A."
    Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.
    FEBS Lett. 408:52-56(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1 AND DELTA-3).
    Tissue: Brain cortex.
  3. "Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of human protein phosphatase 2A."
    Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y., Hayashi H., Kagamiyama H., Takeda M.
    FEBS Lett. 379:107-111(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-2), PROTEIN SEQUENCE OF 501-508; 550-559; 573-580 AND 584-601 (DELTA-1).
    Tissue: Bone marrow and Brain cortex.
  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.
    , 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 DELTA-2).
    Tissue: Heart.
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-1).
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 DELTA-1 AND DELTA-2).
    Tissue: Colon, Eye and Kidney.
  9. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL1.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT SER-53.

Entry informationi

Entry namei2A5D_HUMAN
AccessioniPrimary (citable) accession number: Q14738
Secondary accession number(s): A8K3I9
, B5BUA6, O00494, O00696, Q15171, Q5TC39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 161 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 6
    Human chromosome 6: 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

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.