dbPTM

GFAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GFAP_HUMAN
UniProt AC	P14136
Protein Name	Glial fibrillary acidic protein
Gene Name	GFAP
Organism	Homo sapiens (Human).
Sequence Length	432
Subcellular Localization	Cytoplasm . Associated with intermediate filaments.
Protein Description	GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells..
Protein Sequence	MERRRITSAARRSYVSSGEMMVGGLAPGRRLGPGTRLSLARMPPPLPTRVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MERRRITSAARRSY -CCHHHHCHHHHHHH	15.53	12686604
8	Phosphorylation	MERRRITSAARRSYV CCHHHHCHHHHHHHH	19.98	11918673
11	Methylation	RRITSAARRSYVSSG HHHCHHHHHHHHCCC	28.00	-
11	Dimethylation	RRITSAARRSYVSSG HHHCHHHHHHHHCCC	28.00	-
12	Methylation	RITSAARRSYVSSGE HHCHHHHHHHHCCCC	27.84	-
13	Phosphorylation	ITSAARRSYVSSGEM HCHHHHHHHHCCCCC	25.08	12177195
14	Phosphorylation	TSAARRSYVSSGEMM CHHHHHHHHCCCCCE	11.53	20886841
16	Phosphorylation	AARRSYVSSGEMMVG HHHHHHHCCCCCEEC	25.13	22210691
17	Phosphorylation	ARRSYVSSGEMMVGG HHHHHHCCCCCEECC	28.82	20886841
30	Citrullination	GGLAPGRRLGPGTRL CCCCCCCCCCCCCCC	50.33	-
30	Citrullination	GGLAPGRRLGPGTRL CCCCCCCCCCCCCCC	50.33	23828821
36	Citrullination	RRLGPGTRLSLARMP CCCCCCCCCHHCCCC	28.35	-
36	Citrullination	RRLGPGTRLSLARMP CCCCCCCCCHHCCCC	28.35	23828821
38	Phosphorylation	LGPGTRLSLARMPPP CCCCCCCHHCCCCCC	19.38	12177195
53	Phosphorylation	LPTRVDFSLAGALNA CCCCCCHHHHHHHHH	16.91	24076635
82	Phosphorylation	ELNDRFASYIEKVRF HHHHHHHHHHHHHHH	24.75	24076635
95	Acetylation	RFLEQQNKALAAELN HHHHHHHHHHHHHHH	40.20	62025399
110	Phosphorylation	QLRAKEPTKLADVYQ HHHCCCCCCHHHHHH	39.52	22210691
116	Phosphorylation	PTKLADVYQAELREL CCCHHHHHHHHHHHH	11.53	22210691
131	Phosphorylation	RLRLDQLTANSARLE HHHHHHHHHCHHHHH	20.40	24076635
134	Phosphorylation	LDQLTANSARLEVER HHHHHHCHHHHHHHH	16.58	24076635
150	Phosphorylation	NLAQDLATVRQKLQD CHHHHHHHHHHHHHH	24.42	20886841
154	Acetylation	DLATVRQKLQDETNL HHHHHHHHHHHHHHH	37.24	62025401
172	Phosphorylation	AENNLAAYRQEADEA HHHCHHHHHHHHHHH	13.76	24927040
180	Phosphorylation	RQEADEATLARLDLE HHHHHHHHHHHHHHH	20.92	30377224
189	Acetylation	ARLDLERKIESLEEE HHHHHHHHHHHHHHH	41.26	62025403
192	Phosphorylation	DLERKIESLEEEIRF HHHHHHHHHHHHHHH	44.55	24076635
228	Acetylation	HVELDVAKPDLTAAL CCEECCCCCCHHHHH	38.62	62025405
240	Phosphorylation	AALKEIRTQYEAMAS HHHHHHHHHHHHHHH	40.96	-
242	Phosphorylation	LKEIRTQYEAMASSN HHHHHHHHHHHHHCC	12.68	22817900
247	Phosphorylation	TQYEAMASSNMHEAE HHHHHHHHCCHHHHH	14.79	24076635
248	Phosphorylation	QYEAMASSNMHEAEE HHHHHHHCCHHHHHH	28.74	24076635
260	Acetylation	AEEWYRSKFADLTDA HHHHHHHHHHHHHHH	35.26	8394869
265	Phosphorylation	RSKFADLTDAAARNA HHHHHHHHHHHHHHH	24.92	24076635
270	Citrullination	DLTDAAARNAELLRQ HHHHHHHHHHHHHHH	37.86	23828821
270	Citrullination	DLTDAAARNAELLRQ HHHHHHHHHHHHHHH	37.86	-
291	Phosphorylation	DYRRQLQSLTCDLES HHHHHHHHHHCCHHH	33.95	24076635
293	Phosphorylation	RRQLQSLTCDLESLR HHHHHHHHCCHHHHC	14.82	24076635
298	Phosphorylation	SLTCDLESLRGTNES HHHCCHHHHCCCCHH	30.57	24076635
302	Phosphorylation	DLESLRGTNESLERQ CHHHHCCCCHHHHHH	29.40	24076635
305	Phosphorylation	SLRGTNESLERQMRE HHCCCCHHHHHHHHH	37.29	20886841
323	Phosphorylation	RHVREAASYQEALAR HHHHHHHHHHHHHHH	34.10	24076635
324	Phosphorylation	HVREAASYQEALARL HHHHHHHHHHHHHHH	12.97	24927040
337	Phosphorylation	RLEEEGQSLKDEMAR HHHHHHHCHHHHHHH	48.52	24076635
339	Acetylation	EEEGQSLKDEMARHL HHHHHCHHHHHHHHH	57.81	62025407
349	Phosphorylation	MARHLQEYQDLLNVK HHHHHHHHHHHHHHH	8.38	-
366	Phosphorylation	LDIEIATYRKLLEGE HHHHHHHHHHHHCCC	9.20	18083107
383	Phosphorylation	RITIPVQTFSNLQIR CEEEEEEEECCCEEE	29.30	24076635
383	O-linked_Glycosylation	RITIPVQTFSNLQIR CEEEEEEEECCCEEE	29.30	30379171
385	Phosphorylation	TIPVQTFSNLQIRET EEEEEEECCCEEEEC	39.76	24076635
393	Phosphorylation	NLQIRETSLDTKSVS CCEEEECCCCCCCCC	21.35	7822264
397 (in isoform 2)	Phosphorylation	-	48.83	-
398	Phosphorylation	ETSLDTKSVSEGHLK ECCCCCCCCCCCCCC	32.73	25332170
406	Citrullination	VSEGHLKRNIVVKTV CCCCCCCCCEEEEEE	44.46	-
406	Citrullination	VSEGHLKRNIVVKTV CCCCCCCCCEEEEEE	44.46	23828821
416 (in isoform 2)	Phosphorylation	-	34.96	22210691
416	Citrullination	VVKTVEMRDGEVIKE EEEEEECCCCCCHHH	34.96	-
416	Citrullination	VVKTVEMRDGEVIKE EEEEEECCCCCCHHH	34.96	23828821
424	Phosphorylation	DGEVIKESKQEHKDV CCCCHHHHHHHHCCC	34.34	29396893

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
7	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
7	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
7	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
7	T	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
7	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
8	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
13	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
13	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
13	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
13	S	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
13	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
13	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
13	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
17	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
17	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
17	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
17	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
38	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
38	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
38	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	GAN	Q9H2C0	PMID:27798231

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDLI1_HUMAN	PDLIM1	physical	16189514
K0408_HUMAN	KIAA0408	physical	16189514
PDLI7_HUMAN	PDLIM7	physical	16189514
VIME_HUMAN	VIM	physical	16189514
SH3Y1_HUMAN	SH3YL1	physical	16189514
P121A_HUMAN	POM121	physical	16189514
GRAP2_HUMAN	GRAP2	physical	16189514
RIBC2_HUMAN	RIBC2	physical	16189514
NHRF3_HUMAN	PDZK1	physical	16189514
GCP4_HUMAN	TUBGCP4	physical	16189514
CEP76_HUMAN	CEP76	physical	16189514
PDC6I_HUMAN	PDCD6IP	physical	12771190
A4_HUMAN	APP	physical	21832049
NEMO_HUMAN	IKBKG	physical	21988832
GFAP_HUMAN	GFAP	physical	25416956
GOGA2_HUMAN	GOLGA2	physical	25416956
K1C13_HUMAN	KRT13	physical	25416956
K1C15_HUMAN	KRT15	physical	25416956
RBTN2_HUMAN	LMO2	physical	25416956
MOS_HUMAN	MOS	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
RORA_HUMAN	RORA	physical	25416956
PIAS2_HUMAN	PIAS2	physical	25416956
NXF1_HUMAN	NXF1	physical	25416956
FA50B_HUMAN	FAM50B	physical	25416956
SH3Y1_HUMAN	SH3YL1	physical	25416956
PPL13_HUMAN	LGALS14	physical	25416956
ZC21C_HUMAN	ZC2HC1C	physical	25416956
PIHD2_HUMAN	PIH1D2	physical	25416956
CF206_HUMAN	C6orf165	physical	25416956
DESM_HUMAN	DES	physical	28514442
AINX_HUMAN	INA	physical	28514442
NEST_HUMAN	NES	physical	28514442
UBR1_HUMAN	UBR1	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
203450	Alexander disease (ALXDRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GFAP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Functional significance of the specific sites phosphorylated indesmin at cleavage furrow: Aurora-B may phosphorylate and regulatetype III intermediate filaments during cytokinesis coordinatedly withRho-kinase."; Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K.,Inagaki M.; Mol. Biol. Cell 14:1489-1500(2003). Cited for: PHOSPHORYLATION AT THR-7; SER-13 AND SER-38.	12686604 [Abstract]
"Phosphorylation of glial fibrillary acidic protein at the same sitesby cleavage furrow kinase and Rho-associated kinase."; Kosako H., Amano M., Yanagida M., Tanabe K., Nishi Y., Kaibuchi K.,Inagaki M.; J. Biol. Chem. 272:10333-10336(1997). Cited for: PHOSPHORYLATION AT THR-7; SER-13 AND SER-38.	9099667 [Abstract]