Q8IZL8 (PELP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PELP1
Synonyms:	HMX3, MNAR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1130 AA.
Sequence status	Complete.
Protein existence	Evidence 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.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.22
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 MLL, 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.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.22
Subcellular location	Nucleus › nucleoplasm 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.1 Ref.9 Ref.10 Ref.22
Tissue specificity	Isoform 2 is expressed in breast cancer cell lines. Isoform 1 is widely expressed. Ref.1
Domain	The Glu-rich region mediates histones interaction. Ref.1 Ref.8 The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1. Ref.1 Ref.8
Sequence caution	The sequence AAC17708.2 differs from that shown. Reason: Frameshift at positions 656 and 672.

Ontologies

Keywords
Biological process	Transcription
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NFKB1	P19838	2	EBI-716449,EBI-300010

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IZL8-1)

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.

Isoform 2 (identifier: Q8IZL8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-356: I → IVSGICHLFR...TLYLCPFFLQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1130	1130	Proline-, glutamic acid- and leucine-rich protein 1		PRO_0000252135
Regions
	Motif	33 – 37	5	LXXLL motif 1
	Motif	69 – 73	5	LXXLL motif 2
	Motif	111 – 115	5	LXXLL motif 3
	Motif	155 – 159	5	LXXLL motif 4
	Motif	177 – 181	5	LXXLL motif 5
	Motif	264 – 268	5	LXXLL motif 6
	Motif	271 – 275	5	LXXLL motif 7
	Motif	364 – 368	5	LXXLL motif 8
	Motif	459 – 463	5	LXXLL motif 9
	Motif	579 – 583	5	LXXLL motif 10
	Motif	584 – 588	5	LXXLL motif 11
	Compositional bias	633 – 872	240	Pro-rich
	Compositional bias	888 – 1101	214	Glu-rich
	Compositional bias	977 – 1083	107	Pro-rich
Amino acid modifications
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	477	1	Phosphoserine Ref.18 Ref.19 Ref.21
	Modified residue	481	1	Phosphoserine Ref.13 Ref.18 Ref.19 Ref.21
	Modified residue	488	1	Phosphothreonine Ref.21
	Modified residue	745	1	Phosphothreonine Ref.18 Ref.21
	Modified residue	1033	1	Phosphoserine Ref.17 Ref.19 Ref.21
	Modified residue	1043	1	Phosphoserine Ref.18 Ref.21
Natural variations
	Alternative sequence	356	1	I → IVSGICHLFRALAQDTRQPG KYWGPESPQTVSSWSPSQRA STFVQITSLPMCRDTGAQCQ SVANASLGEGEFGDSAESLL RGPAILLTFHPGSILEDRGL ILLGEMRSGVGFLTYVYICK WSFPVSVSLWLSLSSSTLYL CPFFLQ in isoform 2.		VSP_020880
	Natural variant	1126	1	T → S. Corresponds to variant rs9436 [ dbSNP | Ensembl ].		VAR_027766
Experimental info
	Sequence conflict	2	1	A → V in AAC17708. Ref.1
	Sequence conflict	698 – 699	2	AR → DS in AAC17708. Ref.1
	Sequence conflict	708	1	H → L in AAC17708. Ref.1
	Sequence conflict	889	1	E → EEEEEGEEEE in AAC17708. Ref.1
	Sequence conflict	896	1	E → G in AAN41255. Ref.2
	Sequence conflict	1069	1	T → P in AAN41255. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2006. Version 2. Checksum: 7B0DEE7A198DA9A6	FASTA	1,130	119,700
	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
	Isoform 2 [UniParc]. Checksum: 6A6F25E149C58C6C	FASTA	1,275	135,495
	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 VSSKNIVSGI 370 380 390 400 410 420 CHLFRALAQD TRQPGKYWGP ESPQTVSSWS PSQRASTFVQ ITSLPMCRDT GAQCQSVANA 430 440 450 460 470 480 SLGEGEFGDS AESLLRGPAI LLTFHPGSIL EDRGLILLGE MRSGVGFLTY VYICKWSFPV 490 500 510 520 530 540 SVSLWLSLSS STLYLCPFFL QSLHGDGPLR LLLLPSIHLE ALDLLSALIL ACGSRLLRFG 550 560 570 580 590 600 ILIGRLLPQV LNSWSIGRDS LSPGQERPYS TVRTKVYAIL ELWVQVCGAS AGMLQGGASG 610 620 630 640 650 660 EALLTHLLSD ISPPADALKL RSPRGSPDGS LQTGKPSAPK KLKLDVGEAM APPSHRKGDS 670 680 690 700 710 720 NANSDVCAAA LRGLSRTILM CGPLIKEETH RRLHDLVLPL VMGVQQGEVL GSSPYTSSRC 730 740 750 760 770 780 RRELYCLLLA LLLAPSPRCP PPLACALQAF SLGQREDSLE VSSFCSEALV TCAALTHPRV 790 800 810 820 830 840 PPLQPMGPTC PTPAPVPPPE APSPFRAPPF HPPGPMPSVG SMPSAGPMPS AGPMPSAGPV 850 860 870 880 890 900 PSARPGPPTT ANHLGLSVPG LVSVPPRLLP GPENHRAGSN EDPILAPSGT PPPTIPPDET 910 920 930 940 950 960 FGGRVPRPAF VHYDKEEASD VEISLESDSD DSVVIVPEGL PPLPPPPPSG ATPPPIAPTG 970 980 990 1000 1010 1020 PPTASPPVPA KEEPEELPAA PGPLPPPPPP PPPVPGPVTL PPPQLVPEGT PGGGGPPALE 1030 1040 1050 1060 1070 1080 EDLTVININS SDEEEEEEEE EEEEEEEEEE EEEDFEEEEE DEEEYFEEEE EEEEEFEEEF 1090 1100 1110 1120 1130 1140 EEEEGELEEE EEEEDEEEEE ELEEVEDLEF GTAGGEVEEG APPPPTLPPA LPPPESPPKV 1150 1160 1170 1180 1190 1200 QPEPEPEPGL LLEVEEPGTE EERGADTAPT LAPEALPSQG EVEREGESPA AGPPPQELVE 1210 1220 1230 1240 1250 1260 EEPSAPPTLL EEETEDGSDK VQPPPETPAE EEMETETEAE ALQEKEQDDT AAMLADFIDC 1270 PPDDEKPPPP TEPDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 2), FUNCTION, INTERACTION WITH ESR1; CREBBP AND EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
[2]	"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] (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1; ESR2; AR; NR3C1 AND SRC.
[3]	"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: Brain, Lung and Testis.
[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 (ISOFORM 1).
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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, MASS SPECTROMETRY.
[22]	"Five Friends of Methylated 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U88153 mRNA. Translation: AAC17708.2. Frameshift. AF547989 mRNA. Translation: AAN41255.1. BC002875 mRNA. Translation: AAH02875.2. BC010457 mRNA. Translation: AAH10457.2. BC069058 mRNA. Translation: AAH69058.1. AY882602 mRNA. Translation: AAW80659.1.
IPI	IPI00006702. IPI00787089.
RefSeq	NP_055204.2. NM_014389.2.
UniGene	Hs.741234.
3D structure databases
ProteinModelPortal	Q8IZL8.
SMR	Q8IZL8. Positions 374-443, 571-633.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IZL8. 9 interactions.
MINT	MINT-1185355.
STRING	9606.ENSP00000301396.
PTM databases
PhosphoSite	Q8IZL8.
Polymorphism databases
DMDM	115502553.
Proteomic databases
PaxDb	Q8IZL8.
PRIDE	Q8IZL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000574876; ENSP00000461625; ENSG00000141456.
GeneID	27043.
KEGG	hsa:27043.
UCSC	uc002fyi.4. human.
Organism-specific databases
CTD	27043.
GeneCards	GC17M004574.
HGNC	HGNC:30134. PELP1.
MIM	609455. gene.
neXtProt	NX_Q8IZL8.
PharmGKB	PA142671186.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42117.
HOVERGEN	HBG080634.
OrthoDB	EOG4FJ889.
Gene expression databases
ArrayExpress	Q8IZL8.
Bgee	Q8IZL8.
CleanEx	HS_HMX3. HS_PELP1.
Genevestigator	Q8IZL8.
Family and domain databases
InterPro	IPR012980. Uncharacterised_NUC202. [Graphical view]
Pfam	PF08166. NUC202. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PELP1. human.
GenomeRNAi	27043.
NextBio	49622.
SOURCE	Search...

Entry information

Entry name

PELP1_HUMAN

Accession

Primary (citable) accession number: Q8IZL8
Secondary accession number(s): O15450 , Q5EGN3, Q6NTE6, Q96FT1, Q9BU60

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.