dbPTM

RAB32_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB32_HUMAN
UniProt AC	Q13637
Protein Name	Ras-related protein Rab-32
Gene Name	RAB32
Organism	Homo sapiens (Human).
Sequence Length	225
Subcellular Localization	Mitochondrion . Mitochondrion outer membrane Lipid-anchor . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane Lipid-anchor Cytoplasmic side . Melanosome . Melanosome membrane . Recruited to phagosomes containing S.aureus
Protein Description	Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. [PubMed: 12186851 Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis]
Protein Sequence	MAGGGAGDPGLGAAAAPAPETREHLFKVLVIGELGVGKTSIIKRYVHQLFSQHYRATIGVDFALKVLNWDSRTLVRLQLWDIAGQERFGNMTRVYYKEAVGAFVVFDISRSSTFEAVLKWKSDLDSKVHLPNGSPIPAVLLANKCDQNKDSSQSPSQVDQFCKEHGFAGWFETSAKDNINIEEAARFLVEKILVNHQSFPNEENDVDKIKLDQETLRAENKSQCC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGGGAGDP ------CCCCCCCCC	25.90	22223895
21	Phosphorylation	AAAPAPETREHLFKV CCCCCHHHHHHHHHH	40.05	20068231
40	Phosphorylation	ELGVGKTSIIKRYVH CCCCCHHHHHHHHHH	26.29	24719451
51	Phosphorylation	RYVHQLFSQHYRATI HHHHHHHHHHHHHHC	25.33	29457462
54	Phosphorylation	HQLFSQHYRATIGVD HHHHHHHHHHHCCCC	8.36	-
71	Phosphorylation	LKVLNWDSRTLVRLQ EEECCCCCCCEEEEE	20.84	11784320
73	Phosphorylation	VLNWDSRTLVRLQLW ECCCCCCCEEEEEEE	33.29	28450419
112	Phosphorylation	VFDISRSSTFEAVLK EEECCCCCCHHHHHH	35.69	22985185
134	Phosphorylation	KVHLPNGSPIPAVLL CEECCCCCCCCHHHC	26.71	25159151
149	Ubiquitination	ANKCDQNKDSSQSPS CCCCCCCCCCCCCHH	54.04	29967540
151	Phosphorylation	KCDQNKDSSQSPSQV CCCCCCCCCCCHHHH	31.70	23663014
152	Phosphorylation	CDQNKDSSQSPSQVD CCCCCCCCCCHHHHH	44.82	25159151
154	Phosphorylation	QNKDSSQSPSQVDQF CCCCCCCCHHHHHHH	28.59	21815630
156	Phosphorylation	KDSSQSPSQVDQFCK CCCCCCHHHHHHHHH	48.35	21712546
163	Ubiquitination	SQVDQFCKEHGFAGW HHHHHHHHHHCCCEE	54.77	29967540
191	Ubiquitination	AARFLVEKILVNHQS HHHHHHHHHHHCCCC	33.58	29967540
208	Ubiquitination	NEENDVDKIKLDQET CCCCCCHHHCCCHHH	41.40	29967540
210	Ubiquitination	ENDVDKIKLDQETLR CCCCHHHCCCHHHHH	52.32	33845483
224	Geranylgeranylation	RAENKSQCC------ HHHHHHHCC------	3.72	-
225	Geranylgeranylation	AENKSQCC------- HHHHHHCC-------	4.91	-

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 RAB32_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAB32_HUMAN !!

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 RAB32_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAP2_HUMAN	PRKAR2A	physical	12186851
CLH2_HUMAN	CLTCL1	physical	26186194
RAE2_HUMAN	CHML	physical	26186194
RAE1_HUMAN	CHM	physical	26186194
RAB38_HUMAN	RAB38	physical	26186194
PGTA_HUMAN	RABGGTA	physical	26186194
ABCA2_HUMAN	ABCA2	physical	26496610
MRE11_HUMAN	MRE11A	physical	26496610
FUBP1_HUMAN	FUBP1	physical	26496610
INADL_HUMAN	INADL	physical	26496610
TRI29_HUMAN	TRIM29	physical	26496610
P20L1_HUMAN	PHF20L1	physical	26496610
RUFY2_HUMAN	RUFY2	physical	26496610
DOCK6_HUMAN	DOCK6	physical	26496610
SHRM3_HUMAN	SHROOM3	physical	26496610
K2013_HUMAN	KIAA2013	physical	26496610
SPICE_HUMAN	SPICE1	physical	26496610
RAB38_HUMAN	RAB38	physical	28514442
GDIA_HUMAN	GDI1	physical	28514442
RAE2_HUMAN	CHML	physical	28514442
RAE1_HUMAN	CHM	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
PGTA_HUMAN	RABGGTA	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 RAB32_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY.	18691976 [Abstract]