dbPTM

SHLB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHLB1_HUMAN
UniProt AC	Q9Y371
Protein Name	Endophilin-B1
Gene Name	SH3GLB1
Organism	Homo sapiens (Human).
Sequence Length	365
Subcellular Localization	Cytoplasm . Golgi apparatus membrane Peripheral membrane protein. Mitochondrion outer membrane Peripheral membrane protein . Cytoplasmic vesicle, autophagosome membrane . Midbody . Association with the Golgi apparatus depends on the cell type (By
Protein Description	May be required for normal outer mitochondrial membrane dynamics. [PubMed: 15452144 Required for coatomer-mediated retrograde transport in certain cells (By similarity May recruit other proteins to membranes with high curvature. May promote membrane fusion]
Protein Sequence	MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETRNSSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYLSNNNQTSVTPVPSVLPNAIGSSAMASTSGLVITSPSNLSDLKECSGSRKARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGKVPITYLELLN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNIMDFNV -------CCCCCCCH	7.47	22814378
9 (in isoform 2)	Ubiquitination	-	43.08	-
9	Ubiquitination	NIMDFNVKKLAADAG CCCCCCHHHHHHHHH	43.08	-
10	Ubiquitination	IMDFNVKKLAADAGT CCCCCHHHHHHHHHH	38.79	-
10 (in isoform 2)	Ubiquitination	-	38.79	-
17	Phosphorylation	KLAADAGTFLSRAVQ HHHHHHHHHHHHHHH	24.11	28555341
20	Phosphorylation	ADAGTFLSRAVQFTE HHHHHHHHHHHHHHH	17.63	28555341
26	Phosphorylation	LSRAVQFTEEKLGQA HHHHHHHHHHHHCHH	26.58	22210691
29 (in isoform 2)	Ubiquitination	-	52.24	-
29	Ubiquitination	AVQFTEEKLGQAEKT HHHHHHHHHCHHHHH	52.24	-
35 (in isoform 2)	Ubiquitination	-	50.76	-
35	Ubiquitination	EKLGQAEKTELDAHL HHHCHHHHHHHHHHH	50.76	-
48 (in isoform 2)	Ubiquitination	-	48.45	-
48	Acetylation	HLENLLSKAECTKIW HHHHHHHHHHHHHHH	48.45	26051181
48	Ubiquitination	HLENLLSKAECTKIW HHHHHHHHHHHHHHH	48.45	-
53	Ubiquitination	LSKAECTKIWTEKIM HHHHHHHHHHHHHHH	48.15	-
53 (in isoform 2)	Ubiquitination	-	48.15	-
58 (in isoform 2)	Ubiquitination	-	40.50	-
58	Ubiquitination	CTKIWTEKIMKQTEV HHHHHHHHHHHHHCH	40.50	-
61	Ubiquitination	IWTEKIMKQTEVLLQ HHHHHHHHHHCHHCC	58.50	-
61 (in isoform 2)	Ubiquitination	-	58.50	-
80	Phosphorylation	ARIEEFVYEKLDRKA CCHHHHHHHHCCCCC	16.80	25159151
80 (in isoform 2)	Phosphorylation	-	16.80	25147952
82 (in isoform 2)	Ubiquitination	-	37.69	21906983
82 (in isoform 1)	Ubiquitination	-	37.69	21906983
82	Ubiquitination	IEEFVYEKLDRKAPS HHHHHHHHCCCCCCC	37.69	2190698
89	Phosphorylation	KLDRKAPSRINNPEL HCCCCCCCCCCCHHH	51.13	26552605
100	Phosphorylation	NPELLGQYMIDAGTE CHHHHHHHEECCCCC	8.34	26552605
106	Phosphorylation	QYMIDAGTEFGPGTA HHEECCCCCCCCCCH	29.84	26552605
112	Phosphorylation	GTEFGPGTAYGNALI CCCCCCCCHHHCEEE	21.60	26552605
114	Phosphorylation	EFGPGTAYGNALIKC CCCCCCHHHCEEEEC	15.68	26552605
124	Phosphorylation	ALIKCGETQKRIGTA EEEECCCHHHCCCCC	25.36	26552605
138	Phosphorylation	ADRELIQTSALNFLT CCHHHHHHHHHHHHH	14.69	20068231
139	Phosphorylation	DRELIQTSALNFLTP CHHHHHHHHHHHHHH	17.87	20068231
145	Phosphorylation	TSALNFLTPLRNFIE HHHHHHHHHHHHHHH	19.01	20068231
155	Phosphorylation	RNFIEGDYKTIAKER HHHHHCCHHHHHHHH	22.38	28060719
156	Sumoylation	NFIEGDYKTIAKERK HHHHCCHHHHHHHHH	37.89	-
156	Sumoylation	NFIEGDYKTIAKERK HHHHCCHHHHHHHHH	37.89	-
156	Ubiquitination	NFIEGDYKTIAKERK HHHHCCHHHHHHHHH	37.89	-
156 (in isoform 2)	Ubiquitination	-	37.89	-
157	Phosphorylation	FIEGDYKTIAKERKL HHHCCHHHHHHHHHH	21.67	28060719
176 (in isoform 2)	Ubiquitination	-	35.58	-
176	Ubiquitination	RLDLDAAKTRLKKAK CCCHHHHHHHHHHHH	35.58	-
187	Phosphorylation	KKAKAAETRNSSEQE HHHHHHHHCCCHHHH	30.35	28102081
190	Phosphorylation	KAAETRNSSEQELRI HHHHHCCCHHHHHHH	31.77	26462736
191	Phosphorylation	AAETRNSSEQELRIT HHHHCCCHHHHHHHH	47.01	30622161
236	Phosphorylation	DFVEAQMTYYAQCYQ HHHHHHHHHHHHHHH	10.99	24043423
237	Phosphorylation	FVEAQMTYYAQCYQY HHHHHHHHHHHHHHH	7.46	24043423
238	Phosphorylation	VEAQMTYYAQCYQYM HHHHHHHHHHHHHHH	4.88	24043423
242	Phosphorylation	MTYYAQCYQYMLDLQ HHHHHHHHHHHHHHH	7.21	24043423
244	Phosphorylation	YYAQCYQYMLDLQKQ HHHHHHHHHHHHHHH	3.52	24043423
254	Phosphorylation	DLQKQLGSFPSNYLS HHHHHHCCCCHHHHC	42.44	20068231
257	Phosphorylation	KQLGSFPSNYLSNNN HHHCCCCHHHHCCCC	35.78	20068231
259	Phosphorylation	LGSFPSNYLSNNNQT HCCCCHHHHCCCCCC	18.82	20068231
261	Phosphorylation	SFPSNYLSNNNQTSV CCCHHHHCCCCCCCC	27.44	20068231
266	Phosphorylation	YLSNNNQTSVTPVPS HHCCCCCCCCCCCCC	27.56	20068231
267	Phosphorylation	LSNNNQTSVTPVPSV HCCCCCCCCCCCCCC	17.77	20068231
269	Phosphorylation	NNNQTSVTPVPSVLP CCCCCCCCCCCCCCC	20.52	20068231
273	Phosphorylation	TSVTPVPSVLPNAIG CCCCCCCCCCCCCCC	36.20	20068231
281	Phosphorylation	VLPNAIGSSAMASTS CCCCCCCCCCCCCCC	14.60	20068231
282	Phosphorylation	LPNAIGSSAMASTSG CCCCCCCCCCCCCCC	19.49	20068231
286	Phosphorylation	IGSSAMASTSGLVIT CCCCCCCCCCCEEEE	15.26	20068231
287	Phosphorylation	GSSAMASTSGLVITS CCCCCCCCCCEEEEC	19.78	20068231
288	Phosphorylation	SSAMASTSGLVITSP CCCCCCCCCEEEECC	27.86	20068231
293	Phosphorylation	STSGLVITSPSNLSD CCCCEEEECCCCHHH	27.40	20068231
294	Phosphorylation	TSGLVITSPSNLSDL CCCEEEECCCCHHHH	18.40	20068231
296	Phosphorylation	GLVITSPSNLSDLKE CEEEECCCCHHHHHH	50.61	20068231
299	Phosphorylation	ITSPSNLSDLKECSG EECCCCHHHHHHCCC	45.18	20068231
307	Phosphorylation	DLKECSGSRKARVLY HHHHCCCCCCEEEEE	17.83	28258704
314	Phosphorylation	SRKARVLYDYDAANS CCCEEEEECCCCCCC	15.03	20068231
316	Phosphorylation	KARVLYDYDAANSTE CEEEEECCCCCCCHH	8.23	20068231
321	Phosphorylation	YDYDAANSTELSLLA ECCCCCCCHHHHHHH	20.66	20068231
322	Phosphorylation	DYDAANSTELSLLAD CCCCCCCHHHHHHHC	40.53	20068231
325	Phosphorylation	AANSTELSLLADEVI CCCCHHHHHHHCCEE	18.33	20068231
333	Phosphorylation	LLADEVITVFSVVGM HHHCCEEEHEEEECC	22.22	20068231
336	Phosphorylation	DEVITVFSVVGMDSD CCEEEHEEEECCCCH	16.14	20068231
342	Phosphorylation	FSVVGMDSDWLMGER EEEECCCCHHHCCCC	23.07	20068231
355	Sumoylation	ERGNQKGKVPITYLE CCCCCCCCCEEEEEE	52.45	-
355	Ubiquitination	ERGNQKGKVPITYLE CCCCCCCCCEEEEEE	52.45	-
376 (in isoform 2)	Ubiquitination	-		-

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
80	Y	Phosphorylation	Kinase	SRC	P12931	PSP
145	T	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
145	T	Phosphorylation		21499257
Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization.

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 SHLB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3K1_HUMAN	SH3KBP1	physical	11894096
M4K3_RAT	Map4k3	physical	11384986
SHLB2_HUMAN	SH3GLB2	physical	11161816
BAX_HUMAN	BAX	physical	11259440
SHLB2_HUMAN	SH3GLB2	physical	20562859
UBP7_HUMAN	USP7	physical	20562859
CUL2_HUMAN	CUL2	physical	20562859
KLD10_HUMAN	KLHDC10	physical	20562859
ITCH_HUMAN	ITCH	physical	19341794
A4_HUMAN	APP	physical	21832049
AASD1_HUMAN	AARSD1	physical	22863883
ARC1A_HUMAN	ARPC1A	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
CALR_HUMAN	CALR	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
KAPCA_HUMAN	PRKACA	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	25416956
SHLB2_HUMAN	SH3GLB2	physical	25416956
ZN576_HUMAN	ZNF576	physical	25416956
CKLF5_HUMAN	CMTM5	physical	25416956
FUND1_HUMAN	FUNDC1	physical	25416956
CCD22_HUMAN	CCDC22	physical	26344197
COMD3_HUMAN	COMMD3	physical	26344197
DSCR3_HUMAN	DSCR3	physical	26344197
FAD1_HUMAN	FLAD1	physical	26344197
RPR1A_HUMAN	RPRD1A	physical	26344197
UBC9_HUMAN	UBE2I	physical	26344197
UBP14_HUMAN	USP14	physical	26344197
SYWC_HUMAN	WARS	physical	26344197
XPO7_HUMAN	XPO7	physical	26344197
HTAI2_HUMAN	HTATIP2	physical	21252234
ACSL4_HUMAN	ACSL4	physical	21252234
RAB5A_HUMAN	RAB5A	physical	21252234
PRCC_HUMAN	PRCC	physical	27173435
SEPT7_HUMAN	SEPT7	physical	27173435
CHRD1_HUMAN	CHORDC1	physical	27173435
SARNP_HUMAN	SARNP	physical	27173435
COPZ1_HUMAN	COPZ1	physical	27173435
GORS2_HUMAN	GORASP2	physical	27173435
SEP11_HUMAN	SEPT11	physical	27173435
DRG1_HUMAN	DRG1	physical	27173435

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 SHLB1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Cdk5-mediated phosphorylation of endophilin B1 is required forinduced autophagy in models of Parkinson's disease."; Wong A.S., Lee R.H., Cheung A.Y., Yeung P.K., Chung S.K., Cheung Z.H.,Ip N.Y.; Nat. Cell Biol. 13:568-579(2011). Cited for: PHOSPHORYLATION AT THR-145, AND MUTAGENESIS OF THR-145.	21499257 [Abstract]

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