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Protein

Proliferation-associated protein 2G4

Gene

PA2G4

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

Functioni

May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity).By similarity5 Publications

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. poly(A) RNA binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: MGI
  4. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. cell proliferation Source: ProtInc
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: MGI
  5. positive regulation of cell differentiation Source: UniProtKB
  6. regulation of translation Source: UniProtKB-KW
  7. rRNA processing Source: UniProtKB-KW
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

RNA-binding

Protein family/group databases

MEROPSiM24.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferation-associated protein 2G4
Alternative name(s):
Cell cycle protein p38-2G4 homolog
Short name:
hG4-1
ErbB3-binding protein 1
Gene namesi
Name:PA2G4
Synonyms:EBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8550. PA2G4.

Subcellular locationi

Isoform 1 : Cytoplasm 2 Publications. Nucleusnucleolus 2 Publications
Note: Tranlocates to the nucleus upon treatment with HRG. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.1 Publication
Isoform 2 : Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: HPA
  6. nucleus Source: HPA
  7. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 223KYK → AYA: Loss of nucleolar localization. 1 Publication
Mutagenesisi361 – 3611S → A: Loss of phosphorylation and interaction with ERBB3 and HUWE1. 1 Publication
Mutagenesisi361 – 3611S → D: No effect on phosphorylation and loss of nucleolar localization. 1 Publication
Mutagenesisi363 – 3631S → A: No effect on in vitro phosphorylation by PKC. 1 Publication
Mutagenesisi364 – 3652RK → AA: Only partial nucleolar localization. 1 Publication
Mutagenesisi366 – 3661T → A: Decreases in vitro phosphorylation by PKC. 1 Publication

Organism-specific databases

PharmGKBiPA32877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 394393Proliferation-associated protein 2G4PRO_0000148989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine6 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei361 – 3611Phosphoserine; by PKC/PRKCD3 Publications
Modified residuei366 – 3661Phosphothreonine1 Publication
Modified residuei386 – 3861Phosphothreonine6 Publications

Post-translational modificationi

Phosphorylated on serine and threonine residues. Phosphorylation is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent and HRG-induced phosphorylation is predominantly PKC-independent. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.9 Publications
In cancer cells, isoform 2 is polyubiquitinated leading to its proteasomal degradation and phosphorylation by PKC/PRKCD enhances polyubiquitination.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UQ80.
PaxDbiQ9UQ80.
PRIDEiQ9UQ80.

2D gel databases

SWISS-2DPAGEQ9UQ80.

PTM databases

PhosphoSiteiQ9UQ80.

Expressioni

Tissue specificityi

Isoform 2 is undetectable whereas isoform 1 is strongly expressed in cancer cells (at protein level). Isoform 1 and isoform 2 are widely expressed, including heart, brain, lung, pancreas, skeletal muscle, kidney, placenta and liver.3 Publications

Gene expression databases

BgeeiQ9UQ80.
CleanExiHS_PA2G4.
ExpressionAtlasiQ9UQ80. baseline and differential.
GenevestigatoriQ9UQ80.

Organism-specific databases

HPAiCAB011711.
CAB012428.
HPA016484.

Interactioni

Subunit structurei

Isoform 2 interacts with the cytoplasmic domain of non-phosphorylated ERBB3; the interaction requires PKC activity. Interacts with AR. Treatment with HRG leads to dissociation from ERBB3 and increases association with AR. Interacts with NCL/nucleolin. Component of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the interaction is enhanced upon PA2G4 dephosphorylation. Interacts with AKT1 (By similarity). Isoform 1 and isoform 2 interact with RNF20. Isoform 2 interacts with HUWE1.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCLP193382EBI-924893,EBI-346967
RB1P064004EBI-924893,EBI-491274
SIN3AQ96ST34EBI-924893,EBI-347218

Protein-protein interaction databases

BioGridi111075. 87 interactions.
IntActiQ9UQ80. 44 interactions.
MINTiMINT-5000754.
STRINGi9606.ENSP00000302886.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 3824Combined sources
Helixi45 – 6117Combined sources
Beta strandi72 – 8211Combined sources
Beta strandi85 – 873Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi117 – 12610Combined sources
Helixi137 – 15620Combined sources
Helixi163 – 17513Combined sources
Turni176 – 1783Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 2045Combined sources
Helixi207 – 2126Combined sources
Beta strandi223 – 23311Combined sources
Beta strandi246 – 2494Combined sources
Helixi260 – 27314Combined sources
Helixi280 – 2823Combined sources
Helixi287 – 29812Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi316 – 32611Combined sources
Beta strandi329 – 3324Combined sources
Helixi340 – 3423Combined sources
Helixi352 – 3598Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8KX-ray1.60A2-394[»]
3J2Ielectron microscopy11.90A1-394[»]
ProteinModelPortaliQ9UQ80.
SMRiQ9UQ80. Positions 7-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UQ80.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4847Necessary for nucleolar localization1 PublicationAdd
BLAST
Regioni46 – 549RNA-binding1 Publication
Regioni301 – 39494Necessary for nucleolar localization1 PublicationAdd
BLAST
Regioni361 – 37515Interaction with RNABy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24 family.Curated

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00530000063220.
HOGENOMiHOG000168207.
HOVERGENiHBG053117.
InParanoidiQ9UQ80.
OMAiKNWAVTE.
OrthoDBiEOG7SFHXD.
PhylomeDBiQ9UQ80.
TreeFamiTF300010.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProiIPR004545. Pap_1.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00495. crvDNA_42K. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1Curated (identifier: Q9UQ80-1) [UniParc]FASTAAdd to Basket

Also known as: p481 Publication

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
MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE
60 70 80 90 100
KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL
110 120 130 140 150
KEGDLVKIDL GVHVDGFIAN VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA
160 170 180 190 200
EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT
210 220 230 240 250
IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD
260 270 280 290 300
PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE
310 320 330 340 350
LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ
360 370 380 390
DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGD
Length:394
Mass (Da):43,787
Last modified:January 23, 2007 - v3
Checksum:iCD45466507AD6047
GO
Isoform 2Curated (identifier: Q9UQ80-2) [UniParc]FASTAAdd to Basket

Also known as: p421 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.

Show »
Length:340
Mass (Da):38,059
Checksum:i639A83ADD56290A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811A → P in AAB91536. (PubMed:9345902)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454Missing in isoform 2. 1 PublicationVSP_057325Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59435 mRNA. Translation: AAB91536.1.
U87954 mRNA. Translation: AAD00646.1.
AF104670, AF104668, AF104669 Genomic DNA. Translation: AAD05561.1.
BC001951 mRNA. Translation: AAH01951.1.
BC007561 mRNA. Translation: AAH07561.1.
BC069786 mRNA. Translation: AAH69786.1.
CCDSiCCDS8902.1.
RefSeqiNP_006182.2. NM_006191.2.
UniGeneiHs.524498.
Hs.745109.

Genome annotation databases

EnsembliENST00000303305; ENSP00000302886; ENSG00000170515. [Q9UQ80-1]
GeneIDi5036.
KEGGihsa:5036.
UCSCiuc001sjm.3. human.

Polymorphism databases

DMDMi13632817.

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
U59435 mRNA. Translation: AAB91536.1.
U87954 mRNA. Translation: AAD00646.1.
AF104670, AF104668, AF104669 Genomic DNA. Translation: AAD05561.1.
BC001951 mRNA. Translation: AAH01951.1.
BC007561 mRNA. Translation: AAH07561.1.
BC069786 mRNA. Translation: AAH69786.1.
CCDSiCCDS8902.1.
RefSeqiNP_006182.2. NM_006191.2.
UniGeneiHs.524498.
Hs.745109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8KX-ray1.60A2-394[»]
3J2Ielectron microscopy11.90A1-394[»]
ProteinModelPortaliQ9UQ80.
SMRiQ9UQ80. Positions 7-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111075. 87 interactions.
IntActiQ9UQ80. 44 interactions.
MINTiMINT-5000754.
STRINGi9606.ENSP00000302886.

Protein family/group databases

MEROPSiM24.973.

PTM databases

PhosphoSiteiQ9UQ80.

Polymorphism databases

DMDMi13632817.

2D gel databases

SWISS-2DPAGEQ9UQ80.

Proteomic databases

MaxQBiQ9UQ80.
PaxDbiQ9UQ80.
PRIDEiQ9UQ80.

Protocols and materials databases

DNASUi5036.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303305; ENSP00000302886; ENSG00000170515. [Q9UQ80-1]
GeneIDi5036.
KEGGihsa:5036.
UCSCiuc001sjm.3. human.

Organism-specific databases

CTDi5036.
GeneCardsiGC12P056498.
HGNCiHGNC:8550. PA2G4.
HPAiCAB011711.
CAB012428.
HPA016484.
MIMi602145. gene.
neXtProtiNX_Q9UQ80.
PharmGKBiPA32877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00530000063220.
HOGENOMiHOG000168207.
HOVERGENiHBG053117.
InParanoidiQ9UQ80.
OMAiKNWAVTE.
OrthoDBiEOG7SFHXD.
PhylomeDBiQ9UQ80.
TreeFamiTF300010.

Miscellaneous databases

ChiTaRSiPA2G4. human.
EvolutionaryTraceiQ9UQ80.
GeneWikiiPA2G4.
GenomeRNAii5036.
NextBioi19404.
PROiQ9UQ80.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UQ80.
CleanExiHS_PA2G4.
ExpressionAtlasiQ9UQ80. baseline and differential.
GenevestigatoriQ9UQ80.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProiIPR004545. Pap_1.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00495. crvDNA_42K. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a protein highly homologous to the mouse cell cycle protein p38-2G4."
    Lamartine J., Seri M., Cinti R., Heitzmann F., Creaven M., Radomski N., Jost E., Lenoir G.M., Romeo G., Sylla B.S.
    Cytogenet. Cell Genet. 78:31-35(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin."
    Yoo J.Y., Wang X.W., Rishi A.K., Lessor T., Xia X.M., Gustafson T.A., Hamburger A.W.
    Br. J. Cancer 82:683-690(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Genomic structure of the human PA2G4 gene."
    Caroli F., Lamartine J., Sylla B.S., Romeo G., Seri M.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Skin.
  5. Cited for: PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211; 216-236; 264-281 AND 299-364, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma, Mammary carcinoma and Ovarian carcinoma.
  6. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND 377-394, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "Regulation of the ErbB3 binding protein Ebp1 by protein kinase C."
    Lessor T.J., Hamburger A.W.
    Mol. Cell. Endocrinol. 175:185-191(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB3, PHOSPHORYLATION, PHOSPHORYLATION BY PKC, PHOSPHORYLATION AT THR-366, MUTAGENESIS OF SER-363 AND THR-366.
  8. "Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation."
    Xia X., Cheng A., Lessor T., Zhang Y., Hamburger A.W.
    J. Cell. Physiol. 187:209-217(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH RB1.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases."
    Zhang Y., Woodford N., Xia X., Hamburger A.W.
    Nucleic Acids Res. 31:2168-2177(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION, INTERACTION WITH HDAC2.
  11. "EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes."
    Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.
    Oncogene 23:4454-4465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RRNA PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX, ASSOCIATION WITH RRNA, ASSOCIATION WITH U3 SNORNA, MUTAGENESIS OF 20-LYS--LYS-22 AND 364-ARG-LYS-365.
  12. "Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling."
    Zhang Y., Hamburger A.W.
    Br. J. Cancer 92:140-146(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH ERBB3 AND AR.
  13. "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-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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 THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Ebp1 isoforms distinctively regulate cell survival and differentiation."
    Liu Z., Ahn J.Y., Liu X., Ye K.
    Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH ERBB3, PHOSPHORYLATION AT SER-361, MUTAGENESIS OF SER-361.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor."
    Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J., Sun S.Y., Zhou W., Gu W., Ye K.
    Mol. Biol. Cell 20:757-768(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYUBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH RNF20 AND HUWE1, TISSUE SPECIFICITY, MUTAGENESIS OF SER-361.
  19. "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 THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions."
    Kowalinski E., Bange G., Bradatsch B., Hurt E., Wild K., Sinning I.
    FEBS Lett. 581:4450-4454(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH 5S RIBOSOMAL RNA, LACK OF AMINOPEPTIDASE ACTIVITY.

Entry informationi

Entry nameiPA2G4_HUMAN
AccessioniPrimary (citable) accession number: Q9UQ80
Secondary accession number(s): O43846, Q9UM59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 150 of the entry and version 3 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

Caution

Although it belongs to the peptidase M24 family, it does not contain metal cofactors and lacks aminopeptidase activity.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. Peptidase families
    Classification of peptidase families and list of entries
  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.