dbPTM

PELP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PELP1_MOUSE
UniProt AC	Q9DBD5
Protein Name	Proline-, glutamic acid- and leucine-rich protein 1
Gene Name	Pelp1
Organism	Mus musculus (Mouse).
Sequence Length	1123
Subcellular Localization	Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus . Cytoplasm . Mainly found in the nucleoplasm, with low levels detected in the cytoplasm. Also found associated with the plasma membrane.
Protein Description	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 (By similarity). 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. [PubMed: 22872859 Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates pre-60S association of the critical remodeling factor MDN1 (By similarity]
Protein Sequence	MAAAVLSGASAGSPAGAPGGPGGLSAVGSGPRLRLLLLESISGLLQPRTASPVAPVHPPIQWAPHLPGLMCLLRLHGTAGGAQNLSALGALVNLSNAHLGSIKTRFEGLCLLSLLIGESPTELFQQHCVSWLRSIQQVLQSQDSPSTMELAVAVLRDLLRHASQLPTLFRDISTNHLPGLLTSLLGLRPECEQSALEGMKACVTYFPRACGSLKGKLASFFLSRLDSLNPQLQQLACECYSRLPSLGAGFSQGLKHTENWEQELHSLLTSLHSLLGSLFEETEPAPVQSEGPGIEMLLSHSEDGNTHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQEILDLICRILGISSKNINLLGDGPLRLLLLPSLHLEALDLLSALILACGSRLLRFGALISRLLPQVLNAWSTGRDTLAPGQERPYSTIRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPADALKLCSTRGSSDGGLQSGKPSAPKKLKLDMGEALAPPSQRKGDRNANSDVCAAALRGLSRTILMCGPLIKEETHRRLHDLVLPLVMSVQQGEVLGSSPYNSSCCRLGLYRLLLALLLAPSPRCPPPLACALKAFSLGQWEDSLEVSSFCSEALVTCAALTHPRVPPLQSSGPACPTPAPVPPPEAPSSFRAPAFHPPGPMPSIGAVPSTGPLPSAGPIPTVGSMASTGQVPSRPGPPATANHLGLSVPGLVSVPPRLLPGPENHRAGSGEDPVLAPSGTPPPSIPPDETFGGRVPRPAFVHYDKEEASDVEISLESDSDDSVVIVPEGLPSLPPAPPSGTPPPAAPAGPPTASPPVPAKEDSEELPATPGPPPPPPPPPPPASGPVTLPPPQLVPEGTPGGGGPTAMEEDLTVININSSDEEEEEEEEEEEEDEDEEEEDFEEEEEDEEEYFEEEEEEEEFEEEFEEEEGELEEEEEEEEEELDEVEDVEFGSAGEVEEGGPPPPTLPPALPPSDSPKVQPEAEPEPGLLLEVEEPGPEEVPGPETAPTLAPEVLPSQEEGEQEVGSPAAGPPQELVEESSAPPALLEEGTEGGGDKVPPPPETPAEEMETEAEVPAPQEKEQDDTAAMLADFIDCPPDDEKPPPATEPDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAVLSGA ------CCCHHHCCC	18.55	19131326
7	Phosphorylation	-MAAAVLSGASAGSP -CCCHHHCCCCCCCC	26.22	26824392
10	Phosphorylation	AAVLSGASAGSPAGA CHHHCCCCCCCCCCC	36.37	27566939
13	Phosphorylation	LSGASAGSPAGAPGG HCCCCCCCCCCCCCC	15.99	26824392
25	Phosphorylation	PGGPGGLSAVGSGPR CCCCCCHHCCCCCHH	24.96	25619855
29	Phosphorylation	GGLSAVGSGPRLRLL CCHHCCCCCHHHHHH	38.74	25619855
49	Phosphorylation	SGLLQPRTASPVAPV HHCCCCCCCCCCCCC	37.86	26745281
51	Phosphorylation	LLQPRTASPVAPVHP CCCCCCCCCCCCCCC	21.21	26745281
478	Phosphorylation	ADALKLCSTRGSSDG HHHHHHHCCCCCCCC	31.41	26643407
479	Phosphorylation	DALKLCSTRGSSDGG HHHHHHCCCCCCCCC	37.74	26643407
482	Phosphorylation	KLCSTRGSSDGGLQS HHHCCCCCCCCCCCC	23.20	28833060
483	Phosphorylation	LCSTRGSSDGGLQSG HHCCCCCCCCCCCCC	43.00	28833060
489	Phosphorylation	SSDGGLQSGKPSAPK CCCCCCCCCCCCCCC	54.55	28833060
510	Phosphorylation	GEALAPPSQRKGDRN CHHCCCHHHCCCCCC	41.37	29895711
648	Phosphorylation	SSGPACPTPAPVPPP CCCCCCCCCCCCCCC	31.78	22006019
740	Phosphorylation	PENHRAGSGEDPVLA CCCCCCCCCCCCCCC	37.72	22942356
749	Phosphorylation	EDPVLAPSGTPPPSI CCCCCCCCCCCCCCC	50.09	26824392
751	Phosphorylation	PVLAPSGTPPPSIPP CCCCCCCCCCCCCCC	36.64	27087446
755	Phosphorylation	PSGTPPPSIPPDETF CCCCCCCCCCCCCCC	54.20	25521595
761	Phosphorylation	PSIPPDETFGGRVPR CCCCCCCCCCCCCCC	34.65	25619855
1029	Phosphorylation	LAPEVLPSQEEGEQE CCCCCCCCCCCCCCC	46.17	-
1039	Phosphorylation	EGEQEVGSPAAGPPQ CCCCCCCCCCCCCCH	19.28	-
1053	Phosphorylation	QELVEESSAPPALLE HHHHHHCCCCCHHHC	48.34	-
1076	Phosphorylation	KVPPPPETPAEEMET CCCCCCCCCHHHHCC	33.31	25338131

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
751	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PELP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PELP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PELP1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PELP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND MASSSPECTROMETRY.	15345747 [Abstract]