RAE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAE1_HUMAN
• UniProt AC: P24386
• Protein Name: Rab proteins geranylgeranyltransferase component A 1
• Gene Name: CHM
• Organism: Homo sapiens (Human).
• Sequence Length: 653
• Subcellular Localization: Cytoplasm, cytosol .
• Protein Description: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation..
• Protein Sequence: MADTLPSEFDVIVIGTGLPESIIAAACSRSGRRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDIVSDSPVWQDQILENEEAIALSRKDKTIQHVEVFCYASQDLHEDVEEAGALQKNHALVTSANSTEAADSAFLPTEDESLSTMSCEMLTEQTPSSDPENALEVNGAEVTGEKENHCDDKTCVPSTSAEDMSENVPIAEDTTEQPKKNRITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGRVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCMEYEKYPDEYKGYEEITFYEYLKTQKLTPNLQYIVMHSIAMTSETASSTIDGLKATKNFLHCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIIDQFGQRIISEHFLVEDSYFPENMCSRVQYRQISRAVLITDRSVLKTDSDQQISILTVPAEEPGTFAVRVIELCSSTMTCMKGTYLVHLTCTSSKTAREDLESVVQKLFVPYTEMEIENEQVEKPRILWALYFNMRDSSDISRSCYNDLPSNVYVCSGPDCGLGNDNAVKQAETLFQEICPNEDFCPPPPNPEDIILDGDSLQPEASESSAIPEANSETFKESTNLGNLEESSE

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
4	Phosphorylation	----MADTLPSEFDV ----CCCCCCCCCCE	30.91	23663014
7	Phosphorylation	-MADTLPSEFDVIVI -CCCCCCCCCCEEEE	54.75	23663014
16	Phosphorylation	FDVIVIGTGLPESII CCEEEECCCCCHHHH	25.15	23663014
21	Phosphorylation	IGTGLPESIIAAACS ECCCCCHHHHHHHHC	19.84	23663014
28	Phosphorylation	SIIAAACSRSGRRVL HHHHHHHCCCCCEEE	25.42	23663014
30	Phosphorylation	IAAACSRSGRRVLHV HHHHHCCCCCEEEEE	21.98	27762562
39	Phosphorylation	RRVLHVDSRSYYGGN CEEEEEECCCCCCCC	23.26	-
70	Phosphorylation	QENSDIVSDSPVWQD HHCCCCCCCCCHHHH	32.48	28348404
72	Phosphorylation	NSDIVSDSPVWQDQI CCCCCCCCCHHHHHH	17.53	28348404
89	Phosphorylation	NEEAIALSRKDKTIQ CHHHHHHHCCCCCCC	28.41	24719451
131	Phosphorylation	LVTSANSTEAADSAF EEECCCCCHHHHCCC	29.47	24275569
145	Phosphorylation	FLPTEDESLSTMSCE CCCCCCCCCCCCCHH	39.68	29759185
190	Phosphorylation	DDKTCVPSTSAEDMS CCCCCCCCCCHHHHH	18.01	28555341
191	Phosphorylation	DKTCVPSTSAEDMSE CCCCCCCCCHHHHHC	26.36	28985074
222	Ubiquitination	ITYSQIIKEGRRFNI CCHHHHHHCCCCCCH	56.60	-
233	Phosphorylation	RFNIDLVSKLLYSRG CCCHHHHHHHHHHCC	25.53	24043423
237	Phosphorylation	DLVSKLLYSRGLLID HHHHHHHHHCCHHHH	13.52	19835603
238	Phosphorylation	LVSKLLYSRGLLIDL HHHHHHHHCCHHHHH	21.60	19835603
249	Phosphorylation	LIDLLIKSNVSRYAE HHHHHHHCCHHHHHH	35.16	30622161
252	Phosphorylation	LLIKSNVSRYAEFKN HHHHCCHHHHHHHCC	24.67	30622161
254	Phosphorylation	IKSNVSRYAEFKNIT HHCCHHHHHHHCCHH	11.72	22817900
305	Phosphorylation	FLTFCMEYEKYPDEY HHHHHHHHHHCCCCC	7.28	22817900
323	Phosphorylation	EEITFYEYLKTQKLT EEEEHHHHHHHCCCC	11.34	22468782
330	Phosphorylation	YLKTQKLTPNLQYIV HHHHCCCCCCHHHEE	19.71	22468782
403	O-linked_Glycosylation	GIYCLRHSVQCLVVD HHHHHHHCEEEEEEE	13.88	30620550
466	Phosphorylation	TDRSVLKTDSDQQIS ECCCEECCCCCCCEE	36.25	24719451
468	Phosphorylation	RSVLKTDSDQQISIL CCEECCCCCCCEEEE	42.42	24719451
484	Phosphorylation	VPAEEPGTFAVRVIE EECCCCCCEEHHHHH	21.09	24719451
494	Phosphorylation	VRVIELCSSTMTCMK HHHHHHHHCCCEECC	41.28	-
495	Phosphorylation	RVIELCSSTMTCMKG HHHHHHHCCCEECCC	22.62	-
503	Phosphorylation	TMTCMKGTYLVHLTC CCEECCCEEEEEEEE	14.25	24043423
504	Phosphorylation	MTCMKGTYLVHLTCT CEECCCEEEEEEEEC	18.52	24043423
509	Phosphorylation	GTYLVHLTCTSSKTA CEEEEEEEECCCCHH	10.00	24043423
511	Phosphorylation	YLVHLTCTSSKTARE EEEEEEECCCCHHHH	30.69	24043423
512	Phosphorylation	LVHLTCTSSKTARED EEEEEECCCCHHHHH	31.80	24043423
513	Phosphorylation	VHLTCTSSKTAREDL EEEEECCCCHHHHHH	18.84	24043423
651	Phosphorylation	NLGNLEESSE----- CCCCCCCCCC-----	30.32	25159151
652	Phosphorylation	LGNLEESSE------ CCCCCCCCC------	51.08	25159151

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

Oops, there are no upstream regulatory protein records of RAE1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAE1_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 RAE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB1A_HUMAN	RAB1A	physical	8294464
RAB3A_HUMAN	RAB3A	physical	8294464
RAB5A_HUMAN	RAB5A	physical	8294464
RAB6A_HUMAN	RAB6A	physical	8294464

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 303100: Choroideremia (CHM)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-652, ANDMASS SPECTROMETRY.
PubMed: 19413330

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-305, AND MASSSPECTROMETRY.
PubMed: 17287340