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Protein

Astrocytic phosphoprotein PEA-15

Gene

PEA15

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

Functioni

Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface.By similarity2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Sugar transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5673001. RAF/MAP kinase cascade.
SignaLinkiQ15121.
SIGNORiQ15121.

Names & Taxonomyi

Protein namesi
Recommended name:
Astrocytic phosphoprotein PEA-15
Alternative name(s):
15 kDa phosphoprotein enriched in astrocytes
Phosphoprotein enriched in diabetes
Short name:
PED
Gene namesi
Name:PEA15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8822. PEA15.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • microtubule associated complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33166.

Polymorphism and mutation databases

BioMutaiPEA15.
DMDMi32470612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Astrocytic phosphoprotein PEA-15PRO_0000191282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei104 – 1041PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15121.
MaxQBiQ15121.
PaxDbiQ15121.
PRIDEiQ15121.
TopDownProteomicsiQ15121-1. [Q15121-1]

PTM databases

iPTMnetiQ15121.
PhosphoSiteiQ15121.

Miscellaneous databases

PMAP-CutDBQ15121.

Expressioni

Tissue specificityi

Ubiquitously expressed. Most abundant in tissues such as heart, brain, muscle and adipose tissue which utilize glucose as an energy source. Lower expression in glucose-producing tissues. Higher levels of expression are found in tissues from individuals with type 2 diabetes than in controls.1 Publication

Gene expression databases

BgeeiQ15121.
CleanExiHS_PEA15.
ExpressionAtlasiQ15121. baseline and differential.
GenevisibleiQ15121. HS.

Organism-specific databases

HPAiHPA028356.

Interactioni

Subunit structurei

Binds RPS6KA3, MAPK3 and MAPK1. Transient interaction with PLD1 and PLD2 (By similarity). Interacts with CASP8 and FADD.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2IPQ9NYB02EBI-714410,EBI-750109

Protein-protein interaction databases

BioGridi114230. 17 interactions.
IntActiQ15121. 13 interactions.
MINTiMINT-141556.
STRINGi9606.ENSP00000353660.

Structurei

Secondary structure

130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1313Combined sources
Helixi17 – 2711Combined sources
Turni28 – 303Combined sources
Helixi32 – 343Combined sources
Helixi42 – 5110Combined sources
Helixi61 – 699Combined sources
Helixi73 – 9018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IZ5X-ray3.19E/F/G/H1-130[»]
4IZAX-ray1.93B1-96[»]
ProteinModelPortaliQ15121.
SMRiQ15121. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8179DEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 10710Microtubule-bindingSequence analysis
Regioni122 – 1298Microtubule-bindingSequence analysis

Sequence similaritiesi

Contains 1 DED (death effector) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00390000000230.
HOGENOMiHOG000049048.
HOVERGENiHBG053557.
InParanoidiQ15121.
OMAiSPVMAEY.
OrthoDBiEOG7D2FGM.
PhylomeDBiQ15121.
TreeFamiTF332405.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED_dom.
IPR029546. PEA15.
[Graphical view]
PANTHERiPTHR15094:SF0. PTHR15094:SF0. 1 hit.
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15121-1) [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
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE
60 70 80 90 100
SHNKLDKDNL SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT
110 120 130
RIPSAKKYKD IIRQPSEEEI IKLAPPPKKA
Length:130
Mass (Da):15,040
Last modified:July 3, 2003 - v2
Checksum:i8D0F93A40B299FB2
GO
Isoform 2 (identifier: Q15121-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEDEGNKLCQAPPWPGQTSPVM

Note: No experimental confirmation available.
Show »
Length:151
Mass (Da):17,307
Checksum:i4BA064CDB2A9AA53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in CAA60499 (PubMed:8662970).Curated
Sequence conflicti8 – 81L → F in CAA60499 (PubMed:8662970).Curated
Sequence conflicti62 – 621Y → I in CAA60499 (PubMed:8662970).Curated
Sequence conflicti124 – 1241A → G in CAA60499 (PubMed:8662970).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEDEGNKLCQAPPWPGQTSP VM in isoform 2. 1 PublicationVSP_056174

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86809 mRNA. Translation: CAA60499.1.
Y13736 mRNA. Translation: CAA74076.1.
AF153274, AF153273 Genomic DNA. Translation: AAD56775.1.
AK095879 mRNA. Translation: BAG53155.1.
AL121987 Genomic DNA. No translation available.
AL139011 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW52735.1.
BC002426 mRNA. Translation: AAH02426.1.
BC022554 mRNA. Translation: AAH22554.1.
BT007252 mRNA. Translation: AAP35916.1.
CCDSiCCDS1199.1. [Q15121-1]
CCDS72954.1. [Q15121-2]
PIRiS55384.
RefSeqiNP_001284505.1. NM_001297576.1. [Q15121-2]
NP_001284506.1. NM_001297577.1. [Q15121-1]
NP_001284507.1. NM_001297578.1.
NP_003759.1. NM_003768.4. [Q15121-1]
XP_006711662.1. XM_006711599.2. [Q15121-1]
UniGeneiHs.517216.

Genome annotation databases

EnsembliENST00000360472; ENSP00000353660; ENSG00000162734. [Q15121-1]
ENST00000368076; ENSP00000357055; ENSG00000162734. [Q15121-2]
GeneIDi8682.
KEGGihsa:8682.
UCSCiuc001fvk.4. human. [Q15121-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86809 mRNA. Translation: CAA60499.1.
Y13736 mRNA. Translation: CAA74076.1.
AF153274, AF153273 Genomic DNA. Translation: AAD56775.1.
AK095879 mRNA. Translation: BAG53155.1.
AL121987 Genomic DNA. No translation available.
AL139011 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW52735.1.
BC002426 mRNA. Translation: AAH02426.1.
BC022554 mRNA. Translation: AAH22554.1.
BT007252 mRNA. Translation: AAP35916.1.
CCDSiCCDS1199.1. [Q15121-1]
CCDS72954.1. [Q15121-2]
PIRiS55384.
RefSeqiNP_001284505.1. NM_001297576.1. [Q15121-2]
NP_001284506.1. NM_001297577.1. [Q15121-1]
NP_001284507.1. NM_001297578.1.
NP_003759.1. NM_003768.4. [Q15121-1]
XP_006711662.1. XM_006711599.2. [Q15121-1]
UniGeneiHs.517216.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IZ5X-ray3.19E/F/G/H1-130[»]
4IZAX-ray1.93B1-96[»]
ProteinModelPortaliQ15121.
SMRiQ15121. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114230. 17 interactions.
IntActiQ15121. 13 interactions.
MINTiMINT-141556.
STRINGi9606.ENSP00000353660.

PTM databases

iPTMnetiQ15121.
PhosphoSiteiQ15121.

Polymorphism and mutation databases

BioMutaiPEA15.
DMDMi32470612.

Proteomic databases

EPDiQ15121.
MaxQBiQ15121.
PaxDbiQ15121.
PRIDEiQ15121.
TopDownProteomicsiQ15121-1. [Q15121-1]

Protocols and materials databases

DNASUi8682.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360472; ENSP00000353660; ENSG00000162734. [Q15121-1]
ENST00000368076; ENSP00000357055; ENSG00000162734. [Q15121-2]
GeneIDi8682.
KEGGihsa:8682.
UCSCiuc001fvk.4. human. [Q15121-1]

Organism-specific databases

CTDi8682.
GeneCardsiPEA15.
HGNCiHGNC:8822. PEA15.
HPAiHPA028356.
MIMi603434. gene.
neXtProtiNX_Q15121.
PharmGKBiPA33166.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00390000000230.
HOGENOMiHOG000049048.
HOVERGENiHBG053557.
InParanoidiQ15121.
OMAiSPVMAEY.
OrthoDBiEOG7D2FGM.
PhylomeDBiQ15121.
TreeFamiTF332405.

Enzyme and pathway databases

ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5673001. RAF/MAP kinase cascade.
SignaLinkiQ15121.
SIGNORiQ15121.

Miscellaneous databases

ChiTaRSiPEA15. human.
GeneWikiiPEA15.
GenomeRNAii8682.
NextBioi32565.
PMAP-CutDBQ15121.
PROiQ15121.
SOURCEiSearch...

Gene expression databases

BgeeiQ15121.
CleanExiHS_PEA15.
ExpressionAtlasiQ15121. baseline and differential.
GenevisibleiQ15121. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED_dom.
IPR029546. PEA15.
[Graphical view]
PANTHERiPTHR15094:SF0. PTHR15094:SF0. 1 hit.
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs conserved on their full length in mouse and human."
    Estelles A., Yokoyama M., Nothias F., Vincent J.-D., Glowinski J., Vernier P., Chneiweiss H.
    J. Biol. Chem. 271:14800-14806(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus."
    Condorelli G., Vigliotta G., Iavarone C., Caruso M., Tocchetti C.G., Andreozzi F., Cafieri A., Tecce M.F., Formisano P., Beguinot L., Beguinot F.
    EMBO J. 17:3858-3866(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Heart.
  3. "Molecular characterization of the human PEA15 gene on 1q21-q22 and association with type 2 diabetes mellitus in Pima Indians."
    Wolford J.K., Bogardus C., Ossowski V., Prochazka M.
    Gene 241:143-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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 2).
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Brain and Skin.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 55-83 AND 89-98, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis."
    Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.
    Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CASP8 AND FADD.
  11. "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-104 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: 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. "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-61 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-104 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPEA15_HUMAN
AccessioniPrimary (citable) accession number: Q15121
Secondary accession number(s): B1AKZ3, O00511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 3, 2003
Last modified: May 11, 2016
This is version 141 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.