RBL2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBL2A_HUMAN
• UniProt AC: Q9UBK7
• Protein Name: Rab-like protein 2A
• Gene Name: RABL2A
• Organism: Homo sapiens (Human).
• Sequence Length: 228
• Protein Description: Plays an essential role in male fertility, sperm intra-flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail..
• Protein Sequence: MAEDKTKPSELDQGKYDADDNVKIICLGDSAVGKSKLMERFLMDGFQPQQLSTYALTLYKHTATVDGKTILVDFWDTAGQERFQSMHASYYHKAHACIMVFDIQRKVTYRNLSTWYTELREFRPEIPCIVVANKIDDINVTQKSFNFAKKFSLPLYFVSAADGTNVVKLFNDAIRLAVSYKQNSQDFMDEIFQELENFSLEQEEEDVPDQEQSSSIETPSEEVASPHS

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
23	Acetylation	YDADDNVKIICLGDS CCCCCCEEEEEECCC	32.38	20167786
23	Ubiquitination	YDADDNVKIICLGDS CCCCCCEEEEEECCC	32.38	-
26	S-nitrosylation	DDNVKIICLGDSAVG CCCEEEEEECCCHHC	3.86	24105792
30	Phosphorylation	KIICLGDSAVGKSKL EEEEECCCHHCHHHH	24.05	30622161
34	Acetylation	LGDSAVGKSKLMERF ECCCHHCHHHHHHHH	37.51	20167786
34 (in isoform 3)	Ubiquitination	-	37.51	-
34	Ubiquitination	LGDSAVGKSKLMERF ECCCHHCHHHHHHHH	37.51	-
35	Acetylation	GDSAVGKSKLMERFL CCCHHCHHHHHHHHH	25.70	-
36 (in isoform 3)	Ubiquitination	-	56.17	-
52	Phosphorylation	GFQPQQLSTYALTLY CCCHHHHHHHHHEEE	18.29	-
57	Phosphorylation	QLSTYALTLYKHTAT HHHHHHHEEEEEEEE	21.62	-
59	Phosphorylation	STYALTLYKHTATVD HHHHHEEEEEEEEEC	8.76	-
85	Phosphorylation	AGQERFQSMHASYYH HCHHHHHHHHHHHHH	15.15	23663014
89	Phosphorylation	RFQSMHASYYHKAHA HHHHHHHHHHHHCCE	16.14	23663014
90	Phosphorylation	FQSMHASYYHKAHAC HHHHHHHHHHHCCEE	15.46	23663014
91	Phosphorylation	QSMHASYYHKAHACI HHHHHHHHHHCCEEE	8.37	23663014
141	Phosphorylation	KIDDINVTQKSFNFA CCCCCCCCHHHCCHH	26.28	20058876
143	Ubiquitination	DDINVTQKSFNFAKK CCCCCCHHHCCHHHH	47.88	-
144 (in isoform 2)	Ubiquitination	-	18.66	21890473
144	Phosphorylation	DINVTQKSFNFAKKF CCCCCHHHCCHHHHC	18.66	-
149	Ubiquitination	QKSFNFAKKFSLPLY HHHCCHHHHCCCCEE	50.65	-
149 (in isoform 3)	Ubiquitination	-	50.65	-
150	Ubiquitination	KSFNFAKKFSLPLYF HHCCHHHHCCCCEEE	36.43	-
150	Ubiquitination	KSFNFAKKFSLPLYF HHCCHHHHCCCCEEE	36.43	21890473
150 (in isoform 1)	Ubiquitination	-	36.43	21890473
150 (in isoform 3)	Ubiquitination	-	36.43	-
151 (in isoform 2)	Ubiquitination	-	10.00	21890473

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

Oops, there are no upstream regulatory protein records of RBL2A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RBL2A_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 RBL2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC5_HUMAN	SMC5	physical	22939629
SPTN1_HUMAN	SPTAN1	physical	22939629
SPTB2_HUMAN	SPTBN1	physical	22939629
SLK_HUMAN	SLK	physical	22939629
TBC9B_HUMAN	TBC1D9B	physical	22939629
CEP19_HUMAN	CEP19	physical	25416956
AKA11_HUMAN	AKAP11	physical	26186194
VP13A_HUMAN	VPS13A	physical	26186194
ALMS1_HUMAN	ALMS1	physical	26186194
MTO1_HUMAN	MTO1	physical	26186194
BRCA2_HUMAN	BRCA2	physical	26186194
DPOLA_HUMAN	POLA1	physical	26186194
P73_HUMAN	TP73	physical	26186194
TTF2_HUMAN	TTF2	physical	26186194
FIGL1_HUMAN	FIGNL1	physical	28514442
FHIT_HUMAN	FHIT	physical	28514442
ALMS1_HUMAN	ALMS1	physical	28514442
S23IP_HUMAN	SEC23IP	physical	28514442
MTO1_HUMAN	MTO1	physical	28514442
BRCA2_HUMAN	BRCA2	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.