dbPTM

MELPH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MELPH_MOUSE
UniProt AC	Q91V27
Protein Name	Melanophilin
Gene Name	Mlph
Organism	Mus musculus (Mouse).
Sequence Length	590
Subcellular Localization	Melanosome.
Protein Description	Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A..
Protein Sequence	MGKRLDLSTLTDEEAEHVWAVVQRDFDLRRREEERLQGLKGKIQKESSKRELLSDTAHLNETHCARCLQPYRLLLNSRRQCLECSLFVCKSCSHAHPEEQGWLCDPCHLARVVKIGSLEWYYQHVRARFKRFGSAKVIRSLCGRLQGGGGSEPSLEEGNGDSEQTDEDGDLDTEARDQPLNSKKKKRLLSFRDVDFEEDSDHLVQPCSQTLGLSSVPESAHSLQSLSGEPYSEDTTSLEPEGLEETGARALGCRPSPEVQPCSPLPSGEDAHAELDSPAASCKSAFGTTAMPGTDDVRGKHLPSQYLADVDTSDEDSIQGPRAASQHSKRRARTVPETQILELNKRMSAVEHLLVHLENTVLPPSAQEPTVETHPSADTEEETLRRRLEELTSNISGSSTSSEDETKPDGTFLGGSPKVCTDTGHMETQERNPRSPGNPARPTKSTDEELSEMEDRVAMTASEVQQAESEISDIESRIAALRAAGLTVKPSGKPRRKSGIPIFLPRVTEKLDRIPKTPPADPDDQAKMPKATTAVPSLLRRKYSPSSQGVDSGSFDRKSVYRGSLTQRNPNGRRGTARHIFAKPVMAQQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
162	Phosphorylation	LEEGNGDSEQTDEDG CCCCCCCCCCCCCCC	32.76	22817900
165	Phosphorylation	GNGDSEQTDEDGDLD CCCCCCCCCCCCCCC	36.99	27087446
190	Phosphorylation	KKKKRLLSFRDVDFE HHHHHHHHHHCCCCC	23.87	24719451
256	Phosphorylation	RALGCRPSPEVQPCS CCCCCCCCCCCCCCC	17.84	19367708
263	Phosphorylation	SPEVQPCSPLPSGED CCCCCCCCCCCCCCC	35.83	22817900
267	Phosphorylation	QPCSPLPSGEDAHAE CCCCCCCCCCCCCHH	63.60	19367708
277	Phosphorylation	DAHAELDSPAASCKS CCCHHCCCCCHHCHH	29.12	22817900
284	Phosphorylation	SPAASCKSAFGTTAM CCCHHCHHHHCCCCC	32.91	19367708
312	Phosphorylation	QYLADVDTSDEDSIQ HHEECCCCCCHHHCC	37.62	27087446
313	Phosphorylation	YLADVDTSDEDSIQG HEECCCCCCHHHCCC	34.24	28978645
443	Phosphorylation	PGNPARPTKSTDEEL CCCCCCCCCCCHHHH	31.88	22817900
445	Phosphorylation	NPARPTKSTDEELSE CCCCCCCCCHHHHHH	43.50	22817900
446	Phosphorylation	PARPTKSTDEELSEM CCCCCCCCHHHHHHH	49.32	22817900
451	Phosphorylation	KSTDEELSEMEDRVA CCCHHHHHHHHHHHC	37.87	22817900
469	Phosphorylation	SEVQQAESEISDIES HHHHHHHHHHHHHHH	43.15	19367708
472	Phosphorylation	QQAESEISDIESRIA HHHHHHHHHHHHHHH	28.60	19367708
491	Phosphorylation	AGLTVKPSGKPRRKS CCCEECCCCCCCCCC	54.45	-
498	Phosphorylation	SGKPRRKSGIPIFLP CCCCCCCCCCCEECH	39.89	27180971
517	Phosphorylation	KLDRIPKTPPADPDD HHHCCCCCCCCCCCH	29.20	28978645
544	Phosphorylation	SLLRRKYSPSSQGVD HHHHHCCCCCCCCCC	22.72	28978645
546	Phosphorylation	LRRKYSPSSQGVDSG HHHCCCCCCCCCCCC	29.38	22817900
547	Phosphorylation	RRKYSPSSQGVDSGS HHCCCCCCCCCCCCC	34.05	22817900
554	Phosphorylation	SQGVDSGSFDRKSVY CCCCCCCCCCCCCEE	28.11	19367708
564	Phosphorylation	RKSVYRGSLTQRNPN CCCEECCCCCCCCCC	21.17	-
566	Phosphorylation	SVYRGSLTQRNPNGR CEECCCCCCCCCCCC	27.46	29109428

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
498	S	Phosphorylation	Kinase	PRKACA	P05132	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RB27A_MOUSE	Rab27a	physical	12578829

Drug and Disease Associations

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

Regulatory Network of MELPH_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; THR-165; SER-313;SER-445; THR-446 AND SER-544, AND MASS SPECTROMETRY.	19367708 [Abstract]