dbPTM

HXA9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HXA9_HUMAN
UniProt AC	P31269
Protein Name	Homeobox protein Hox-A9
Gene Name	HOXA9
Organism	Homo sapiens (Human).
Sequence Length	272
Subcellular Localization	Nucleus.
Protein Description	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation..
Protein Sequence	MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	DELSVGRYAPGTLGQ CCCCCCCCCCCCCCC	15.95	29396449
34	Phosphorylation	VGRYAPGTLGQPPRQ CCCCCCCCCCCCHHH	27.02	29396449
120	Phosphorylation	EPTPGALSFAGLPSS CCCCCCCCCCCCCCC	16.71	-
126	Phosphorylation	LSFAGLPSSRPYGIK CCCCCCCCCCCCCCC	43.98	-
140	Symmetric dimethylarginine	KPEPLSARRGDCPTL CCCCCCCCCCCCCCC	39.47	-
140	Methylation	KPEPLSARRGDCPTL CCCCCCCCCCCCCCC	39.47	22269951
146	Phosphorylation	ARRGDCPTLDTHTLS CCCCCCCCCCCCCEE	43.53	25002506
149	Phosphorylation	GDCPTLDTHTLSLTD CCCCCCCCCCEECCC	21.63	25002506
151	Phosphorylation	CPTLDTHTLSLTDYA CCCCCCCCEECCCCC	21.82	30266825
153	Phosphorylation	TLDTHTLSLTDYACG CCCCCCEECCCCCCC	30.31	30266825
155	Phosphorylation	DTHTLSLTDYACGSP CCCCEECCCCCCCCC	24.48	30266825
157	Phosphorylation	HTLSLTDYACGSPPV CCEECCCCCCCCCCC	9.88	30266825
161	Phosphorylation	LTDYACGSPPVDREK CCCCCCCCCCCCCCC	26.39	23401153
184	Phosphorylation	ENNAENESGGDKPPI CCCCCCCCCCCCCCC	60.71	22496350
205	Phosphorylation	ANWLHARSTRKKRCP HHHHHHHHCCCCCCC	33.09	22817900
209	Ubiquitination	HARSTRKKRCPYTKH HHHHCCCCCCCCCCC	56.81	-
213	Phosphorylation	TRKKRCPYTKHQTLE CCCCCCCCCCCCCHH	31.85	-
215	Ubiquitination	KKRCPYTKHQTLELE CCCCCCCCCCCHHHH	28.07	-
218	Phosphorylation	CPYTKHQTLELEKEF CCCCCCCCHHHHHHH	23.17	-

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
Oops, there are no upstream regulatory protein records of HXA9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
140	R	Methylation		22269951
Methylated on Arg-140 by PRMT5; methylation is critical for E-selectin induction.

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 HXA9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIP6_HUMAN	TRIP6	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
PLS1_HUMAN	PLSCR1	physical	16189514
PBX1_HUMAN	PBX1	physical	10082572
PBX3_HUMAN	PBX3	physical	10082572
PBX2_HUMAN	PBX2	physical	10082572
MEIS1_HUMAN	MEIS1	physical	10082572
SMAD4_HUMAN	SMAD4	physical	11042172
CUL4A_HUMAN	CUL4A	physical	14609952
ANM5_HUMAN	PRMT5	physical	22269951
TRIP6_HUMAN	TRIP6	physical	19060904

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 HXA9_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"HOXA9 methylation by PRMT5 is essential for endothelial cellexpression of leukocyte adhesion molecules."; Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A.,Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.; Mol. Cell. Biol. 32:1202-1213(2012). Cited for: FUNCTION, INTERACTION WITH PRMT5, METHYLATION AT ARG-140, MUTAGENESISOF ARG-140, AND MASS SPECTROMETRY.	22269951 [Abstract]