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Q8IZL8

- PELP1_HUMAN

UniProt

Q8IZL8 - PELP1_HUMAN

Protein

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

Gene

PELP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (03 Oct 2006)
      Previous versions | rss
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    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

    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. MLL1 complex Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671186.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    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 – 131PhosphoserineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1.

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → V in AAC17708. (PubMed:11481323)Curated
    Sequence conflicti896 – 8961E → G in AAN41255. (PubMed:12415108)Curated
    Sequence conflicti1069 – 10691T → P in AAN41255. (PubMed:12415108)Curated

    Natural variant

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

    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

    EnsembliENST00000574876; ENSP00000461625; ENSG00000141456.
    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

    Ensembli ENST00000574876 ; ENSP00000461625 ; ENSG00000141456 .
    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

    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: October 1, 2014
    This is version 106 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