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Q8IZL8 (PELP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline-, glutamic acid- and leucine-rich protein 1
Alternative name(s):
Modulator of non-genomic activity of estrogen receptor
Transcription factor HMX3
Gene names
Name:PELP1
Synonyms:HMX3, MNAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.24

Subunit structure

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. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.24

Subcellular location

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. Ref.3 Ref.9 Ref.10 Ref.24

Tissue specificity

Isoform 2is expressed in breast cancer cell lines. Isoform 1is widely expressed. Ref.3

Domain

The Glu-rich region mediates histones interaction. Ref.3 Ref.8

The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1. Ref.3 Ref.8

Sequence caution

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

The sequence AAC17708.2 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionActivator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16169070PubMed 20195357PubMed 20448663PubMed 21326211. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 11301129Proline-, glutamic acid- and leucine-rich protein 1
PRO_0000252135

Regions

Motif33 – 375LXXLL motif 1
Motif69 – 735LXXLL motif 2
Motif111 – 1155LXXLL motif 3
Motif155 – 1595LXXLL motif 4
Motif177 – 1815LXXLL motif 5
Motif264 – 2685LXXLL motif 6
Motif271 – 2755LXXLL motif 7
Motif364 – 3685LXXLL motif 8
Motif459 – 4635LXXLL motif 9
Motif579 – 5835LXXLL motif 10
Motif584 – 5885LXXLL motif 11
Compositional bias633 – 872240Pro-rich
Compositional bias888 – 1101214Glu-rich
Compositional bias977 – 1083107Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.23 Ref.25
Modified residue131Phosphoserine By similarity
Modified residue4771Phosphoserine Ref.18 Ref.20 Ref.22
Modified residue4811Phosphoserine Ref.13 Ref.18 Ref.20 Ref.22
Modified residue4881Phosphothreonine Ref.22
Modified residue7451Phosphothreonine Ref.18 Ref.22
Modified residue10331Phosphoserine Ref.17 Ref.20 Ref.22
Modified residue10431Phosphoserine Ref.18 Ref.22

Natural variations

Natural variant11261T → S.
Corresponds to variant rs9436 [ dbSNP | Ensembl ].
VAR_027766

Experimental info

Sequence conflict21A → V in AAC17708. Ref.3
Sequence conflict8961E → G in AAN41255. Ref.1
Sequence conflict10691T → P in AAN41255. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8IZL8 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 7B0DEE7A198DA9A6

FASTA1,130119,700
        10         20         30         40         50         60 
MAAAVLSGPS AGSAAGVPGG TGGLSAVSSG PRLRLLLLES VSGLLQPRTG SAVAPVHPPN 

        70         80         90        100        110        120 
RSAPHLPGLM CLLRLHGSVG GAQNLSALGA LVSLSNARLS SIKTRFEGLC LLSLLVGESP 

       130        140        150        160        170        180 
TELFQQHCVS WLRSIQQVLQ TQDPPATMEL AVAVLRDLLR YAAQLPALFR DISMNHLPGL 

       190        200        210        220        230        240 
LTSLLGLRPE CEQSALEGMK ACMTYFPRAC GSLKGKLASF FLSRVDALSP QLQQLACECY 

       250        260        270        280        290        300 
SRLPSLGAGF SQGLKHTESW EQELHSLLAS LHTLLGALYE GAETAPVQNE GPGVEMLLSS 

       310        320        330        340        350        360 
EDGDAHVLLQ LRQRFSGLAR CLGLMLSSEF GAPVSVPVQE ILDFICRTLS VSSKNISLHG 

       370        380        390        400        410        420 
DGPLRLLLLP SIHLEALDLL SALILACGSR LLRFGILIGR LLPQVLNSWS IGRDSLSPGQ 

       430        440        450        460        470        480 
ERPYSTVRTK VYAILELWVQ VCGASAGMLQ GGASGEALLT HLLSDISPPA DALKLRSPRG 

       490        500        510        520        530        540 
SPDGSLQTGK PSAPKKLKLD VGEAMAPPSH RKGDSNANSD VCAAALRGLS RTILMCGPLI 

       550        560        570        580        590        600 
KEETHRRLHD LVLPLVMGVQ QGEVLGSSPY TSSRCRRELY CLLLALLLAP SPRCPPPLAC 

       610        620        630        640        650        660 
ALQAFSLGQR EDSLEVSSFC SEALVTCAAL THPRVPPLQP MGPTCPTPAP VPPPEAPSPF 

       670        680        690        700        710        720 
RAPPFHPPGP MPSVGSMPSA GPMPSAGPMP SAGPVPSARP GPPTTANHLG LSVPGLVSVP 

       730        740        750        760        770        780 
PRLLPGPENH RAGSNEDPIL APSGTPPPTI PPDETFGGRV PRPAFVHYDK EEASDVEISL 

       790        800        810        820        830        840 
ESDSDDSVVI VPEGLPPLPP PPPSGATPPP IAPTGPPTAS PPVPAKEEPE ELPAAPGPLP 

       850        860        870        880        890        900 
PPPPPPPPVP GPVTLPPPQL VPEGTPGGGG PPALEEDLTV ININSSDEEE EEEEEEEEEE 

       910        920        930        940        950        960 
EEEEEEEEDF EEEEEDEEEY FEEEEEEEEE FEEEFEEEEG ELEEEEEEED EEEEEELEEV 

       970        980        990       1000       1010       1020 
EDLEFGTAGG EVEEGAPPPP TLPPALPPPE SPPKVQPEPE PEPGLLLEVE EPGTEEERGA 

      1030       1040       1050       1060       1070       1080 
DTAPTLAPEA LPSQGEVERE GESPAAGPPP QELVEEEPSA PPTLLEEETE DGSDKVQPPP 

      1090       1100       1110       1120       1130 
ETPAEEEMET ETEAEALQEK EQDDTAAMLA DFIDCPPDDE KPPPPTEPDS 

« Hide

References

« Hide 'large scale' references
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001265170.1. NM_001278241.1.
NP_055204.3. NM_014389.2.
UniGeneHs.744899.

3D structure databases

ProteinModelPortalQ8IZL8.
SMRQ8IZL8. Positions 370-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117973. 47 interactions.
IntActQ8IZL8. 22 interactions.
MINTMINT-1185355.
STRING9606.ENSP00000301396.

PTM databases

PhosphoSiteQ8IZL8.

Polymorphism databases

DMDM115502553.

Proteomic databases

MaxQBQ8IZL8.
PaxDbQ8IZL8.
PRIDEQ8IZL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID27043.
KEGGhsa:27043.

Organism-specific databases

CTD27043.
GeneCardsGC17M004574.
HGNCHGNC:30134. PELP1.
HPAHPA053966.
HPA060760.
MIM609455. gene.
neXtProtNX_Q8IZL8.
PharmGKBPA142671186.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42117.
HOVERGENHBG080634.
KOK16913.
OrthoDBEOG7NW68H.
PhylomeDBQ8IZL8.

Gene expression databases

ArrayExpressQ8IZL8.
BgeeQ8IZL8.
CleanExHS_HMX3.
HS_PELP1.
GenevestigatorQ8IZL8.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR012980. Uncharacterised_NUC202.
[Graphical view]
PfamPF08166. NUC202. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

ChiTaRSPELP1. human.
GenomeRNAi27043.
NextBio49622.
PROQ8IZL8.
SOURCESearch...

Entry information

Entry namePELP1_HUMAN
AccessionPrimary (citable) accession number: Q8IZL8
Secondary accession number(s): O15450 expand/collapse secondary AC list , Q5EGN3, Q6NTE6, Q96FT1, Q9BU60
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM