dbPTM

PARL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PARL_HUMAN
UniProt AC	Q9H300
Protein Name	Presenilins-associated rhomboid-like protein, mitochondrial
Gene Name	PARL
Organism	Homo sapiens (Human).
Sequence Length	379
Subcellular Localization	Mitochondrion inner membrane Multi-pass membrane protein . P-beta: Nucleus . Translocated into the nucleus by an unknown mechanism (PubMed:17116872).
Protein Description	Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals (By similarity). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain..
Protein Sequence	MAWRGWAQRGWGCGQAWGASVGGRSCEELTAVLTPPQLLGRRFNFFIQQKCGFRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	RKVEPRRSDPGTSGE CCCCCCCCCCCCCCC	49.81	22817900
69	Phosphorylation	PRRSDPGTSGEAYKR CCCCCCCCCCCHHHH	38.66	22817900
70	Phosphorylation	RRSDPGTSGEAYKRS CCCCCCCCCCHHHHC	40.32	22817900
75	Ubiquitination	GTSGEAYKRSALIPP CCCCCHHHHCCCCCC	47.10	21890473
75 (in isoform 2)	Ubiquitination	-	47.10	21890473
75 (in isoform 1)	Ubiquitination	-	47.10	21890473
97	Phosphorylation	PSPYPIRSLIKPLFF CCCCCHHHHHHHHEE	34.86	24719451
131	Phosphorylation	LKSRVQSYFDGIKAD HHHHHHHHHCCCCCH	6.65	22817900
136	Ubiquitination	QSYFDGIKADWLDSI HHHHCCCCCHHHHHC	45.91	21890473
136 (in isoform 2)	Ubiquitination	-	45.91	21890473
136 (in isoform 1)	Ubiquitination	-	45.91	21890473
147	Ubiquitination	LDSIRPQKEGDFRKE HHHCCCCCCCCHHHH	67.36	-
187	Phosphorylation	FCLWRVPSLQRTMIR HHHHCCHHHHHHHHH	33.99	26091039
191 (in isoform 2)	Phosphorylation	-	12.18	23090842
195 (in isoform 2)	Phosphorylation	-	10.57	23090842
197 (in isoform 2)	Phosphorylation	-	20.75	23090842
198 (in isoform 2)	Phosphorylation	-	30.80	23090842
202 (in isoform 2)	Phosphorylation	-	25.26	23090842
203 (in isoform 2)	Phosphorylation	-	41.13	23090842
206 (in isoform 2)	Phosphorylation	-	4.86	23090842
210 (in isoform 2)	Phosphorylation	-	3.77	23090842
211 (in isoform 2)	Phosphorylation	-	3.54	23090842
282	Phosphorylation	GASGAIMTVLAAVCT CHHHHHHHHHHHHHH	13.27	-
312 (in isoform 2)	Ubiquitination	-	4.46	21890473
362 (in isoform 1)	Ubiquitination	-	48.00	21890473
362	Ubiquitination	KNREPLVKIWHEIRT CCCHHHHHHHHHHHH	48.00	21890473

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
65	S	Phosphorylation	17116872
The cleavage is inhibited when residues Ser-65, Thr-69 and Ser-70 are all phosphorylated.
69	T	Phosphorylation	17116872
The cleavage is inhibited when residues Ser-65, Thr-69 and Ser-70 are all phosphorylated.
70	S	Phosphorylation	17116872
The cleavage is inhibited when residues Ser-65, Thr-69 and Ser-70 are all phosphorylated.

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 PARL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ENAH_HUMAN	ENAH	physical	26186194
EF2KT_HUMAN	EEF2KMT	physical	26186194
CAH10_HUMAN	CA10	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
EF2KT_HUMAN	EEF2KMT	physical	28514442
CAH10_HUMAN	CA10	physical	28514442
ENAH_HUMAN	ENAH	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442

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.

Regulatory Network of PARL_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation and cleavage of presenilin-associated rhomboid-likeprotein (PARL) promotes changes in mitochondrial morphology."; Jeyaraju D.V., Xu L., Letellier M.-C., Bandaru S., Zunino R.,Berg E.A., McBride H.M., Pellegrini L.; Proc. Natl. Acad. Sci. U.S.A. 103:18562-18567(2006). Cited for: FUNCTION, PHOSPHORYLATION AT SER-65; THR-69 AND SER-70 OF P-BETA,MUTAGENESIS OF SER-65; THR-69 AND SER-70, SUBCELLULAR LOCATION,TOPOLOGY, AND BETA-CLEAVAGE.	17116872 [Abstract]