SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UQ80

- PA2G4_HUMAN

UniProt

Q9UQ80 - PA2G4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Proliferation-associated protein 2G4
Gene
PA2G4, EBP1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.4 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. cell proliferation Source: ProtInc
  3. negative regulation of transcription, DNA-templated Source: MGI
  4. rRNA processing Source: UniProtKB-KW
  5. regulation of translation Source: UniProtKB-KW
  6. 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

Cytoplasm. Nucleusnucleolus
Note: Tranlocates to the nucleus upon treatment with HRG.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. nucleolus Source: UniProtKB
  4. nucleus Source: MGI
  5. 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
Mutagenesisi363 – 3631S → A: No effect on in vitro phosphorylation by PKC. 1 Publication
Mutagenesisi364 – 3652RK → AA: Only partial nucleolar localization.
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 – 11Removed1 Publication
Chaini2 – 394393Proliferation-associated protein 2G4
PRO_0000148989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine6 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei361 – 3611Phosphoserine2 Publications
Modified residuei366 – 3661Phosphothreonine Inferred
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UQ80.
PaxDbiQ9UQ80.
PRIDEiQ9UQ80.

2D gel databases

SWISS-2DPAGEQ9UQ80.

PTM databases

PhosphoSiteiQ9UQ80.

Expressioni

Tissue specificityi

Expressed in several cell lines tested, including primary and transformed cell lines.1 Publication

Gene expression databases

ArrayExpressiQ9UQ80.
BgeeiQ9UQ80.
CleanExiHS_PA2G4.
GenevestigatoriQ9UQ80.

Organism-specific databases

HPAiCAB011711.
CAB012428.
HPA016484.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111075. 77 interactions.
IntActiQ9UQ80. 43 interactions.
MINTiMINT-5000754.
STRINGi9606.ENSP00000302886.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UQ80.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4847Necessary for nucleolar localization
Add
BLAST
Regioni46 – 549RNA-binding
Regioni301 – 39494Necessary for nucleolar localization
Add
BLAST
Regioni361 – 37515Interaction with RNA By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M24 family.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000168207.
HOVERGENiHBG053117.
InParanoidiQ9UQ80.
OMAiICHFSPI.
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]

Sequencei

Sequence statusi: Complete.

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

Q9UQ80-1 [UniParc]FASTAAdd to Basket

« Hide

MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE    50
KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL 100
KEGDLVKIDL GVHVDGFIAN VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA 150
EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT 200
IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD 250
PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE 300
LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ 350
DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGD 394
Length:394
Mass (Da):43,787
Last modified:January 23, 2007 - v3
Checksum:iCD45466507AD6047
GO

Sequence cautioni

The sequence AAD00646.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811A → P in AAB91536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59435 mRNA. Translation: AAB91536.1.
U87954 mRNA. Translation: AAD00646.1. Different initiation.
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.
GeneIDi5036.
KEGGihsa:5036.
UCSCiuc001sjm.3. human.

Polymorphism databases

DMDMi13632817.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59435 mRNA. Translation: AAB91536.1 .
U87954 mRNA. Translation: AAD00646.1 . Different initiation.
AF104670 , AF104668 , AF104669 Genomic DNA. Translation: AAD05561.1 .
BC001951 mRNA. Translation: AAH01951.1 .
BC007561 mRNA. Translation: AAH07561.1 .
BC069786 mRNA. Translation: AAH69786.1 .
CCDSi CCDS8902.1.
RefSeqi NP_006182.2. NM_006191.2.
UniGenei Hs.524498.
Hs.745109.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q8K X-ray 1.60 A 2-394 [» ]
3J2I electron microscopy 11.90 A 1-394 [» ]
ProteinModelPortali Q9UQ80.
SMRi Q9UQ80. Positions 7-362.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111075. 77 interactions.
IntActi Q9UQ80. 43 interactions.
MINTi MINT-5000754.
STRINGi 9606.ENSP00000302886.

Protein family/group databases

MEROPSi M24.973.

PTM databases

PhosphoSitei Q9UQ80.

Polymorphism databases

DMDMi 13632817.

2D gel databases

SWISS-2DPAGE Q9UQ80.

Proteomic databases

MaxQBi Q9UQ80.
PaxDbi Q9UQ80.
PRIDEi Q9UQ80.

Protocols and materials databases

DNASUi 5036.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303305 ; ENSP00000302886 ; ENSG00000170515 .
GeneIDi 5036.
KEGGi hsa:5036.
UCSCi uc001sjm.3. human.

Organism-specific databases

CTDi 5036.
GeneCardsi GC12P056498.
HGNCi HGNC:8550. PA2G4.
HPAi CAB011711.
CAB012428.
HPA016484.
MIMi 602145. gene.
neXtProti NX_Q9UQ80.
PharmGKBi PA32877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000168207.
HOVERGENi HBG053117.
InParanoidi Q9UQ80.
OMAi ICHFSPI.
OrthoDBi EOG7SFHXD.
PhylomeDBi Q9UQ80.
TreeFami TF300010.

Miscellaneous databases

EvolutionaryTracei Q9UQ80.
GeneWikii PA2G4.
GenomeRNAii 5036.
NextBioi 19404.
PROi Q9UQ80.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UQ80.
Bgeei Q9UQ80.
CleanExi HS_PA2G4.
Genevestigatori Q9UQ80.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProi IPR004545. Pap_1.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00495. crvDNA_42K. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  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], INTERACTION WITH ERBB3, SUBCELLULAR LOCATION.
    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].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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].
  17. "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.
  18. "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.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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].
  21. "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].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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 METAL COFACTOR, 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: July 9, 2014
This is version 145 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.

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