ISL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ISL1_HUMAN
• UniProt AC: P61371
• Protein Name: Insulin gene enhancer protein ISL-1
• Gene Name: ISL1
• Organism: Homo sapiens (Human).
• Sequence Length: 349
• Subcellular Localization: Nucleus .
• Protein Description: DNA-binding transcriptional activator. Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina. Involved in the specification of motor neurons in cooperation with LHX3 and LDB1. Binds to insulin gene enhancer sequences. Essential for heart development. Marker of one progenitor cell population that give rise to the outflow tract, right ventricle, a subset of left ventricular cells, and a large number of atrial cells as well, its function is required for these progenitors to contribute to the heart. Controls the expression of FGF and BMP growth factors in this cell population and is required for proliferation and survival of cells within pharyngeal foregut endoderm and adjacent splanchnic mesoderm as well as for migration of cardiac progenitors into the heart (By similarity)..
• Protein Sequence: MGDMGDPPKKKRLISLCVGCGNQIHDQYILRVSPDLEWHAACLKCAECNQYLDESCTCFVRDGKTYCKRDYIRLYGIKCAKCSIGFSKNDFVMRARSKVYHIECFRCVACSRQLIPGDEFALREDGLFCRADHDVVERASLGAGDPLSPLHPARPLQMAAEPISARQPALRPHVHKQPEKTTRVRTVLNEKQLHTLRTCYAANPRPDALMKEQLVEMTGLSPRVIRVWFQNKRCKDKKRSIMMKQLQQQQPNDKTNIQGMTGTPMVAASPERHDGGLQANPVEVQSYQPPWKVLSDFALQSDIDQPAFQQLVNFSEGGPGSNSTGSEVASMSSQLPDTPNSMVASPIEA

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
33	Phosphorylation	DQYILRVSPDLEWHA HHEEEEECCCCHHHH	13.28	27732954
87	Phosphorylation	AKCSIGFSKNDFVMR CCCEEECCCCCHHHH	25.90	24719451
140	Phosphorylation	HDVVERASLGAGDPL CHHHHHHCCCCCCCC	33.29	24117733
148	Phosphorylation	LGAGDPLSPLHPARP CCCCCCCCCCCCCCC	30.70	26657352
164	Phosphorylation	QMAAEPISARQPALR CCCCCCCCCCCCHHC	28.28	29978859
182	Phosphorylation	HKQPEKTTRVRTVLN CCCCCCCHHHHHHCC	37.93	22817900
191	Ubiquitination	VRTVLNEKQLHTLRT HHHHCCHHHHHHHHH	58.02	32015554
218	Phosphorylation	KEQLVEMTGLSPRVI HHHHHHHHCCCHHHH	22.82	27050516
221	Phosphorylation	LVEMTGLSPRVIRVW HHHHHCCCHHHHHHH	16.41	25159151
255	Phosphorylation	QQQPNDKTNIQGMTG HCCCCCCCCCCCCCC	40.18	27732954
261	Phosphorylation	KTNIQGMTGTPMVAA CCCCCCCCCCCEEEC	44.73	28985074
263	Phosphorylation	NIQGMTGTPMVAASP CCCCCCCCCEEECCC	10.07	24117733
269	Phosphorylation	GTPMVAASPERHDGG CCCEEECCCCCCCCC	19.98	28985074

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO25	Q8TCJ0	PMID:24658274

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ISL1_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 ISL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ISL1_HUMAN	ISL1	physical	9452425
LMX1A_HUMAN	LMX1A	physical	9452425
LHX3_HUMAN	LHX3	physical	9452425
ESR1_HUMAN	ESR1	physical	11043578
PECR_HUMAN	PECR	physical	11043578
COT1_HUMAN	NR2F1	physical	11043578
LDB2_HUMAN	LDB2	physical	20211142
LHX4_HUMAN	LHX4	physical	20211142
SSBP4_HUMAN	SSBP4	physical	20211142
A4_HUMAN	APP	physical	21832049
SMAD3_HUMAN	SMAD3	physical	21988832
TF65_HUMAN	RELA	physical	21988832
KDM1A_HUMAN	KDM1A	physical	23455924
ZN511_HUMAN	ZNF511	physical	25416956

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

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, AND MASSSPECTROMETRY.
PubMed: 18088087