dbPTM

RAE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAE2_HUMAN
UniProt AC	P26374
Protein Name	Rab proteins geranylgeranyltransferase component A 2
Gene Name	CHML
Organism	Homo sapiens (Human).
Sequence Length	656
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family..
Protein Sequence	MADNLPTEFDVVIIGTGLPESILAAACSRSGQRVLHIDSRSYYGGNWASFSFSGLLSWLKEYQQNNDIGEESTVVWQDLIHETEEAITLRKKDETIQHTEAFCYASQDMEDNVEEIGALQKNPSLGVSNTFTEVLDSALPEESQLSYFNSDEMPAKHTQKSDTEISLEVTDVEESVEKEKYCGDKTCMHTVSDKDGDKDESKSTVEDKADEPIRNRITYSQIVKEGRRFNIDLVSKLLYSQGLLIDLLIKSDVSRYVEFKNVTRILAFREGKVEQVPCSRADVFNSKELTMVEKRMLMKFLTFCLEYEQHPDEYQAFRQCSFSEYLKTKKLTPNLQHFVLHSIAMTSESSCTTIDGLNATKNFLQCLGRFGNTPFLFPLYGQGEIPQGFCRMCAVFGGIYCLRHKVQCFVVDKESGRCKAIIDHFGQRINAKYFIVEDSYLSEETCSNVQYKQISRAVLITDQSILKTDLDQQTSILIVPPAEPGACAVRVTELCSSTMTCMKDTYLVHLTCSSSKTAREDLESVVKKLFTPYTETEINEEELTKPRLLWALYFNMRDSSGISRSSYNGLPSNVYVCSGPDCGLGNEHAVKQAETLFQEIFPTEEFCPPPPNPEDIIFDGDDKQPEAPGTNNVVMAKLESSEESKNLESPEKHLQN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
158	Phosphorylation	DEMPAKHTQKSDTEI CCCCCCCCCCCCCEE	36.66	26471730
161	Phosphorylation	PAKHTQKSDTEISLE CCCCCCCCCCEEEEE	39.69	21712546
163	Phosphorylation	KHTQKSDTEISLEVT CCCCCCCCEEEEEEE	42.16	24245541
166	Phosphorylation	QKSDTEISLEVTDVE CCCCCEEEEEEECHH	16.55	21712546
170	Phosphorylation	TEISLEVTDVEESVE CEEEEEEECHHHHHH	25.59	27251275
175	Phosphorylation	EVTDVEESVEKEKYC EEECHHHHHHHHCCC	23.28	30266825
181	Phosphorylation	ESVEKEKYCGDKTCM HHHHHHCCCCCCCCE	11.62	24719451
190	Phosphorylation	GDKTCMHTVSDKDGD CCCCCEEEEECCCCC	8.53	24719451
192	O-linked_Glycosylation	KTCMHTVSDKDGDKD CCCEEEEECCCCCCC	39.85	30379171
235	Phosphorylation	RFNIDLVSKLLYSQG CCCHHHHHHHHHCCC	25.53	-
260	Ubiquitination	VSRYVEFKNVTRILA HHHHHHCCCCCEEEE	36.68	24816145
287	Ubiquitination	RADVFNSKELTMVEK HHHCCCCHHCCHHHH	58.82	23000965
290	Phosphorylation	VFNSKELTMVEKRML CCCCHHCCHHHHHHH	21.91	29396449
302	Phosphorylation	RMLMKFLTFCLEYEQ HHHHHHHHHHHHHHH	18.55	-
314	Phosphorylation	YEQHPDEYQAFRQCS HHHCHHHHHHHHHCC	16.72	-
419	Ubiquitination	DKESGRCKAIIDHFG ECCCCCEEEHHHHHH	41.06	29967540
464	Phosphorylation	AVLITDQSILKTDLD EEEECCCCHHCCCCC	32.47	24719451
528	Ubiquitination	DLESVVKKLFTPYTE HHHHHHHHHCCCCCC	36.90	29967540
567	Phosphorylation	SGISRSSYNGLPSNV CCCCCCCCCCCCCCE	17.94	28961369
578	Phosphorylation	PSNVYVCSGPDCGLG CCCEEEECCCCCCCC	43.23	28961369
640	Phosphorylation	VVMAKLESSEESKNL EEEEECCCCHHHHCC	54.19	26270265
641	Phosphorylation	VMAKLESSEESKNLE EEEECCCCHHHHCCC	35.69	21712546
644	Phosphorylation	KLESSEESKNLESPE ECCCCHHHHCCCCHH	23.85	29214152
649	Phosphorylation	EESKNLESPEKHLQN HHHHCCCCHHHHHCC	41.34	29255136

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 RAE2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAE2_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 RAE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB1A_HUMAN	RAB1A	physical	9730828
RAB5A_HUMAN	RAB5A	physical	9730828
RAB1A_HUMAN	RAB1A	physical	8294464
RAB3A_HUMAN	RAB3A	physical	8294464
RAB5A_HUMAN	RAB5A	physical	8294464
RAB6A_HUMAN	RAB6A	physical	8294464
PSA1_HUMAN	PSMA1	physical	26344197

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 RAE2_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-649, AND MASSSPECTROMETRY.	18669648 [Abstract]