RNPL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNPL1_HUMAN
• UniProt AC: Q9HAU8
• Protein Name: Aminopeptidase RNPEPL1 {ECO:0000305|PubMed:19508204}
• Gene Name: RNPEPL1 {ECO:0000303|PubMed:11017071, ECO:0000312|HGNC:HGNC:10079}
• Organism: Homo sapiens (Human).
• Sequence Length: 725
• Protein Description: Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine..
• Protein Sequence: MAAQCCCRQAPGAEAAPVRPPPEPPPALDVASASSAQLFRLRHLQLGLELRPEARELAGCLVLELCALRPAPRALVLDAHPALRLHSAAFRRAPAAAAETPCAFAFSAPGPGPAPPPPLPAFPEAPGSEPACCPLAFRVDPFTDYGSSLTVTLPPELQAHQPFQVILRYTSTDAPAIWWLDPELTYGCAKPFVFTQGHSVCNRSFFPCFDTPAVKCTYSAVVKAPSGVQVLMSATRSAYMEEEGVFHFHMEHPVPAYLVALVAGDLKPADIGPRSRVWAEPCLLPTATSKLSGAVEQWLSAAERLYGPYMWGRYDIVFLPPSFPIVAMENPCLTFIISSILESDEFLVIDVIHEVAHSWFGNAVTNATWEEMWLSEGLATYAQRRITTETYGAAFTCLETAFRLDALHRQMKLLGEDSPVSKLQVKLEPGVNPSHLMNLFTYEKGYCFVYYLSQLCGDPQRFDDFLRAYVEKYKFTSVVAQDLLDSFLSFFPELKEQSVDCRAGLEFERWLNATGPPLAEPDLSQGSSLTRPVEALFQLWTAEPLDQAAASASAIDISKWRTFQTALFLDRLLDGSPLPQEVVMSLSKCYSSLLDSMNAEIRIRWLQIVVRNDYYPDLHRVRRFLESQMSRMYTIPLYEDLCTGALKSFALEVFYQTQGRLHPNLRRAIQQILSQGLGSSTEPASEPSTELGKAEADTDSDAQALLLGDEAPSSAISLRDVNVSA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
69	Phosphorylation	VLELCALRPAPRALV HHHHHHCCCCCEEEE	23.60	26074081
75	Phosphorylation	LRPAPRALVLDAHPA CCCCCEEEEECCCHH	23.44	26074081
78	Phosphorylation	APRALVLDAHPALRL CCEEEEECCCHHHHH	10.92	26074081
83	Phosphorylation	VLDAHPALRLHSAAF EECCCHHHHHHHHHH	13.19	26074081
191	Ubiquitination	LTYGCAKPFVFTQGH HCCCCCCCEEEECCC	43.08	21906983
300	Phosphorylation	GAVEQWLSAAERLYG HHHHHHHHHHHHHHC	38.26	26074081
306	Phosphorylation	LSAAERLYGPYMWGR HHHHHHHHCCCCCCC	7.85	26074081
309	Phosphorylation	AERLYGPYMWGRYDI HHHHHCCCCCCCEEE	5.25	26074081
314	Phosphorylation	GPYMWGRYDIVFLPP CCCCCCCEEEEEECC	6.00	26074081
331	Phosphorylation	PIVAMENPCLTFIIS CEEECCCHHHHHHHH	20.98	-
334	Phosphorylation	AMENPCLTFIISSIL ECCCHHHHHHHHHHH	22.57	-
418	Phosphorylation	MKLLGEDSPVSKLQV HHHHCCCCCCCEEEE	9.58	30619164
422	Ubiquitination	GEDSPVSKLQVKLEP CCCCCCCEEEEEECC	5.87	22817900
426	Ubiquitination	PVSKLQVKLEPGVNP CCCEEEEEECCCCCH	22.93	22817900
562	Phosphorylation	IDISKWRTFQTALFL CCHHHHCHHHHHHHH		-
565	Phosphorylation	SKWRTFQTALFLDRL HHHCHHHHHHHHHHH		-
627	Phosphorylation	RVRRFLESQMSRMYT HHHHHHHHHHHHHCC		29759185

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

Oops, there are no upstream regulatory protein records of RNPL1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNPL1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RNPL1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RNPL1_HUMAN !!

Drug and Disease Associations

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