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Q8IZL8

- PELP1_HUMAN

UniProt

Q8IZL8 - PELP1_HUMAN

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Protein

Proline-, glutamic acid- and leucine-rich protein 1

Gene
PELP1, HMX3, MNAR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.12 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-, glutamic acid- and leucine-rich protein 1
Alternative name(s):
Modulator of non-genomic activity of estrogen receptor
Transcription factor HMX3
Gene namesi
Name:PELP1
Synonyms:HMX3, MNAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30134. PELP1.

Subcellular locationi

Nucleusnucleoplasm By similarity. Nucleus. Cytoplasm
Note: Mainly found in the nucleoplasm, with low levels detected in the cytoplasm By similarity. Also found associated with the plasma membrane. Mainly in cytoplasm in a subset of breast tumors. Localization is widely deregulated in endometrial cancers with predominantly cytoplasm localization in high-grade endometrial tumors.4 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. MLL1 complex Source: UniProtKB
  3. nucleolus Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11301129Proline-, glutamic acid- and leucine-rich protein 1PRO_0000252135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei13 – 131Phosphoserine By similarity
Modified residuei477 – 4771Phosphoserine3 Publications
Modified residuei481 – 4811Phosphoserine4 Publications
Modified residuei488 – 4881Phosphothreonine1 Publication
Modified residuei745 – 7451Phosphothreonine2 Publications
Modified residuei1033 – 10331Phosphoserine3 Publications
Modified residuei1043 – 10431Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8IZL8.
PaxDbiQ8IZL8.
PRIDEiQ8IZL8.

PTM databases

PhosphoSiteiQ8IZL8.

Expressioni

Tissue specificityi

Isoform 2 is expressed in breast cancer cell lines. Isoform 1 is widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ8IZL8.
BgeeiQ8IZL8.
CleanExiHS_HMX3.
HS_PELP1.
GenevestigatoriQ8IZL8.

Organism-specific databases

HPAiHPA053966.
HPA060760.

Interactioni

Subunit structurei

Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3. Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with ESR1 and ESR2 and this interaction is enhanced by 17-beta-estradiol. Interacts with CREBBP, EP300, AR and NR3C1 in a ligand-dependent manner. Forms two complexes in the presence of 17-beta-estradiol; one with SRC and ESR1 and another with LCK and ESR1. Interacts with histone H1 and H3 with a greater affinity for H1. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Core component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
H3F3BP8424311EBI-716449,EBI-120658
KDM1AO603416EBI-716449,EBI-710124
MDN1Q9NU223EBI-716449,EBI-1050480
NFKB1P198382EBI-716449,EBI-300010
NPM1P067483EBI-716449,EBI-78579
SENP3Q9H4L45EBI-716449,EBI-2880236
SUMO2P619564EBI-716449,EBI-473220
WDR18Q9BV383EBI-716449,EBI-727429

Protein-protein interaction databases

BioGridi117973. 48 interactions.
IntActiQ8IZL8. 22 interactions.
MINTiMINT-1185355.
STRINGi9606.ENSP00000301396.

Structurei

3D structure databases

ProteinModelPortaliQ8IZL8.
SMRiQ8IZL8. Positions 370-407.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi33 – 375LXXLL motif 1
Motifi69 – 735LXXLL motif 2
Motifi111 – 1155LXXLL motif 3
Motifi155 – 1595LXXLL motif 4
Motifi177 – 1815LXXLL motif 5
Motifi264 – 2685LXXLL motif 6
Motifi271 – 2755LXXLL motif 7
Motifi364 – 3685LXXLL motif 8
Motifi459 – 4635LXXLL motif 9
Motifi579 – 5835LXXLL motif 10
Motifi584 – 5885LXXLL motif 11

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi633 – 872240Pro-richAdd
BLAST
Compositional biasi888 – 1101214Glu-richAdd
BLAST
Compositional biasi977 – 1083107Pro-richAdd
BLAST

Domaini

The Glu-rich region mediates histones interaction.2 Publications
The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1.2 Publications

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG42117.
HOVERGENiHBG080634.
KOiK16913.
OrthoDBiEOG7NW68H.
PhylomeDBiQ8IZL8.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012980. Uncharacterised_NUC202.
[Graphical view]
PfamiPF08166. NUC202. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

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

Q8IZL8-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAVLSGPS AGSAAGVPGG TGGLSAVSSG PRLRLLLLES VSGLLQPRTG     50
SAVAPVHPPN RSAPHLPGLM CLLRLHGSVG GAQNLSALGA LVSLSNARLS 100
SIKTRFEGLC LLSLLVGESP TELFQQHCVS WLRSIQQVLQ TQDPPATMEL 150
AVAVLRDLLR YAAQLPALFR DISMNHLPGL LTSLLGLRPE CEQSALEGMK 200
ACMTYFPRAC GSLKGKLASF FLSRVDALSP QLQQLACECY SRLPSLGAGF 250
SQGLKHTESW EQELHSLLAS LHTLLGALYE GAETAPVQNE GPGVEMLLSS 300
EDGDAHVLLQ LRQRFSGLAR CLGLMLSSEF GAPVSVPVQE ILDFICRTLS 350
VSSKNISLHG DGPLRLLLLP SIHLEALDLL SALILACGSR LLRFGILIGR 400
LLPQVLNSWS IGRDSLSPGQ ERPYSTVRTK VYAILELWVQ VCGASAGMLQ 450
GGASGEALLT HLLSDISPPA DALKLRSPRG SPDGSLQTGK PSAPKKLKLD 500
VGEAMAPPSH RKGDSNANSD VCAAALRGLS RTILMCGPLI KEETHRRLHD 550
LVLPLVMGVQ QGEVLGSSPY TSSRCRRELY CLLLALLLAP SPRCPPPLAC 600
ALQAFSLGQR EDSLEVSSFC SEALVTCAAL THPRVPPLQP MGPTCPTPAP 650
VPPPEAPSPF RAPPFHPPGP MPSVGSMPSA GPMPSAGPMP SAGPVPSARP 700
GPPTTANHLG LSVPGLVSVP PRLLPGPENH RAGSNEDPIL APSGTPPPTI 750
PPDETFGGRV PRPAFVHYDK EEASDVEISL ESDSDDSVVI VPEGLPPLPP 800
PPPSGATPPP IAPTGPPTAS PPVPAKEEPE ELPAAPGPLP PPPPPPPPVP 850
GPVTLPPPQL VPEGTPGGGG PPALEEDLTV ININSSDEEE EEEEEEEEEE 900
EEEEEEEEDF EEEEEDEEEY FEEEEEEEEE FEEEFEEEEG ELEEEEEEED 950
EEEEEELEEV EDLEFGTAGG EVEEGAPPPP TLPPALPPPE SPPKVQPEPE 1000
PEPGLLLEVE EPGTEEERGA DTAPTLAPEA LPSQGEVERE GESPAAGPPP 1050
QELVEEEPSA PPTLLEEETE DGSDKVQPPP ETPAEEEMET ETEAEALQEK 1100
EQDDTAAMLA DFIDCPPDDE KPPPPTEPDS 1130
Length:1,130
Mass (Da):119,700
Last modified:October 3, 2006 - v2
Checksum:i7B0DEE7A198DA9A6
GO

Sequence cautioni

The sequence AAC17708.2 differs from that shown. Reason: Intron retention.
The sequence AAC17708.2 differs from that shown. Reason: Frameshift at positions 656 and 672.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1126 – 11261T → S.
Corresponds to variant rs9436 [ dbSNP | Ensembl ].
VAR_027766

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in AAC17708. 1 Publication
Sequence conflicti896 – 8961E → G in AAN41255. 1 Publication
Sequence conflicti1069 – 10691T → P in AAN41255. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF547989 mRNA. Translation: AAN41255.1.
BC002875 mRNA. Translation: AAH02875.2.
BC010457 mRNA. Translation: AAH10457.2.
BC069058 mRNA. Translation: AAH69058.1.
U88153 mRNA. Translation: AAC17708.2. Sequence problems.
AY882602 mRNA. Translation: AAW80659.1.
RefSeqiNP_001265170.1. NM_001278241.1.
NP_055204.3. NM_014389.2.
UniGeneiHs.744899.

Genome annotation databases

GeneIDi27043.
KEGGihsa:27043.
UCSCiuc002fyi.4. human.

Polymorphism databases

DMDMi115502553.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF547989 mRNA. Translation: AAN41255.1 .
BC002875 mRNA. Translation: AAH02875.2 .
BC010457 mRNA. Translation: AAH10457.2 .
BC069058 mRNA. Translation: AAH69058.1 .
U88153 mRNA. Translation: AAC17708.2 . Sequence problems.
AY882602 mRNA. Translation: AAW80659.1 .
RefSeqi NP_001265170.1. NM_001278241.1.
NP_055204.3. NM_014389.2.
UniGenei Hs.744899.

3D structure databases

ProteinModelPortali Q8IZL8.
SMRi Q8IZL8. Positions 370-407.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117973. 48 interactions.
IntActi Q8IZL8. 22 interactions.
MINTi MINT-1185355.
STRINGi 9606.ENSP00000301396.

PTM databases

PhosphoSitei Q8IZL8.

Polymorphism databases

DMDMi 115502553.

Proteomic databases

MaxQBi Q8IZL8.
PaxDbi Q8IZL8.
PRIDEi Q8IZL8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 27043.
KEGGi hsa:27043.
UCSCi uc002fyi.4. human.

Organism-specific databases

CTDi 27043.
GeneCardsi GC17M004574.
HGNCi HGNC:30134. PELP1.
HPAi HPA053966.
HPA060760.
MIMi 609455. gene.
neXtProti NX_Q8IZL8.
PharmGKBi PA142671186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42117.
HOVERGENi HBG080634.
KOi K16913.
OrthoDBi EOG7NW68H.
PhylomeDBi Q8IZL8.

Miscellaneous databases

ChiTaRSi PELP1. human.
GenomeRNAii 27043.
NextBioi 49622.
PROi Q8IZL8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IZL8.
Bgeei Q8IZL8.
CleanExi HS_HMX3.
HS_PELP1.
Genevestigatori Q8IZL8.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR012980. Uncharacterised_NUC202.
[Graphical view ]
Pfami PF08166. NUC202. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
    Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; AR; NR3C1 AND SRC.
  2. "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: Brain, Lung and Testis.
  3. "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha."
    Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R.
    J. Biol. Chem. 276:38272-38279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-356, FUNCTION, INTERACTION WITH ESR1; CREBBP AND EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
  4. "Human transcription factor HMX3."
    Lei W., Harrod K.S.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-1130.
  5. "Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein."
    Balasenthil S., Vadlamudi R.K.
    J. Biol. Chem. 278:22119-22127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RB1.
  6. "Characterization of the interactions of estrogen receptor and MNAR in the activation of cSrc."
    Barletta F., Wong C.-W., McNally C., Komm B.S., Katzenellenbogen B., Cheskis B.J.
    Mol. Endocrinol. 18:1096-1108(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1 AND SRC.
  7. "Potential role of a novel transcriptional coactivator PELP1 in histone H1 displacement in cancer cells."
    Nair S.S., Mishra S.K., Yang Z., Balasenthil S., Kumar R., Vadlamudi R.K.
    Cancer Res. 64:6416-6423(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H1 AND H3.
  8. "The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains."
    Choi Y.B., Ko J.K., Shin J.
    J. Biol. Chem. 279:50930-50941(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH HDAC2.
  9. "Deregulation of estrogen receptor coactivator proline-, glutamic acid-, and leucine-rich protein-1/modulator of nongenomic activity of estrogen receptor in human endometrial tumors."
    Vadlamudi R.K., Balasenthil S., Broaddus R.R., Gustafsson J.-A., Kumar R.
    J. Clin. Endocrinol. Metab. 89:6130-6138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Functional implications of altered subcellular localization of PELP1 in breast cancer cells."
    Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z., Sahin A.A., Kumar R.
    Cancer Res. 65:7724-7732(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PI3K AND EGFR, SUBCELLULAR LOCATION.
  11. "Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation."
    Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.
    Cancer Res. 65:5571-5577(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STAT3.
  12. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway."
    Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.
    J. Biol. Chem. 281:15394-15404(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RXRA.
  15. "Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) interacts with PELP1 and activates MAPK."
    Rayala S.K., den Hollander P., Balasenthil S., Molli P.R., Bean A.J., Vadlamudi R.K., Wang R.-A., Kumar R.
    J. Biol. Chem. 281:4395-4403(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HRS.
  16. "NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression."
    Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G.
    Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUMO2.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-745 AND SER-1043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND SER-1033, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-488; THR-745; SER-1033 AND SER-1043, 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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, SUBCELLULAR LOCATION.
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPELP1_HUMAN
AccessioniPrimary (citable) accession number: Q8IZL8
Secondary accession number(s): O15450
, Q5EGN3, Q6NTE6, Q96FT1, Q9BU60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

External Data

Dasty 3

Similar proteinsi