G45IP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: G45IP_HUMAN
• UniProt AC: Q8TAE8
• Protein Name: Growth arrest and DNA damage-inducible proteins-interacting protein 1
• Gene Name: GADD45GIP1
• Organism: Homo sapiens (Human).
• Sequence Length: 222
• Subcellular Localization: Mitochondrion . Nucleus . Using N-terminally tagged constructs, has been found in the nucleus (PubMed:12482659). C-terminally tagged constructs are targeted exclusively to mitochondria (PubMed:22453275). This discrepancy may be explained by masking o
• Protein Description: Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occurs also in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis..
• Protein Sequence: MAASVRQARSLLGVAATLAPGSRGYRARPPPRRRPGPRWPDPEDLLTPRWQLGPRYAAKQFARYGAASGVVPGSLWPSPEQLRELEAEEREWYPSLATMQESLRVKQLAEEQKRREREQHIAECMAKMPQMIVNWQQQQRENWEKAQADKERRARLQAEAQELLGYQVDPRSARFQELLQDLEKKERKRLKEEKQKRKKEARAAALAAAVAQDPAASGAPSS

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
10	Phosphorylation	ASVRQARSLLGVAAT HHHHHHHHHHHHHHH	30.84	24719451
25	Phosphorylation	LAPGSRGYRARPPPR CCCCCCCCCCCCCCC	10.45	24719451
47	Phosphorylation	PDPEDLLTPRWQLGP CCHHHHCCCCCCCCH	20.36	-
55	Methylation	PRWQLGPRYAAKQFA CCCCCCHHHHHHHHH	31.74	-
59	Ubiquitination	LGPRYAAKQFARYGA CCHHHHHHHHHHHCC	37.46	22817900
59	Acetylation	LGPRYAAKQFARYGA CCHHHHHHHHHHHCC	37.46	27452117
64	Phosphorylation	AAKQFARYGAASGVV HHHHHHHHCCCCCCC	14.00	-
74	Phosphorylation	ASGVVPGSLWPSPEQ CCCCCCCCCCCCHHH	22.61	-
78	Phosphorylation	VPGSLWPSPEQLREL CCCCCCCCHHHHHHH	29.50	-
93	Phosphorylation	EAEEREWYPSLATMQ HHHHHCHHHHHHHHH	4.34	20068231
95	Phosphorylation	EEREWYPSLATMQES HHHCHHHHHHHHHHH	18.23	-
98	Phosphorylation	EWYPSLATMQESLRV CHHHHHHHHHHHHHH	25.36	-
102	Phosphorylation	SLATMQESLRVKQLA HHHHHHHHHHHHHHH	12.46	20068231
113	Ubiquitination	KQLAEEQKRREREQH HHHHHHHHHHHHHHH	57.62	24816145
127	Ubiquitination	HIAECMAKMPQMIVN HHHHHHHHCHHHHHH	24.99	21890473
166	Phosphorylation	EAQELLGYQVDPRSA HHHHHHCCCCCHHHH	12.82	24927040
184	Ubiquitination	ELLQDLEKKERKRLK HHHHHHHHHHHHHHH	68.20	22817900
185	Ubiquitination	LLQDLEKKERKRLKE HHHHHHHHHHHHHHH	54.07	22817900
188	Ubiquitination	DLEKKERKRLKEEKQ HHHHHHHHHHHHHHH	64.27	22817900
221	Phosphorylation	PAASGAPSS------ HHHCCCCCC------	48.42	17069992
222	Phosphorylation	AASGAPSS------- HHCCCCCC-------	43.09	25262027

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
221	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of G45IP_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 G45IP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NR4A1_MOUSE	Nr4a1	physical	15459248
GA45A_HUMAN	GADD45A	physical	12716909
GA45G_HUMAN	GADD45G	physical	12716909
GA45B_HUMAN	GADD45B	physical	12716909
NF2L2_HUMAN	NFE2L2	physical	20427290
A4_HUMAN	APP	physical	21832049
RM12_HUMAN	MRPL12	physical	22939629
TSR1_HUMAN	TSR1	physical	22939629
TM177_HUMAN	TMEM177	physical	22939629
RM11_HUMAN	MRPL11	physical	22939629
RM14_HUMAN	MRPL14	physical	22939629
TAP1_HUMAN	TAP1	physical	22939629
PTH2_HUMAN	PTRH2	physical	22939629
ELF3_HUMAN	ELF3	physical	19801644

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASSSPECTROMETRY.
PubMed: 19369195