1A02_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 1A02_HUMAN
• UniProt AC: P01892
• Protein Name: HLA class I histocompatibility antigen, A-2 alpha chain
• Gene Name: HLA-A
• Organism: Homo sapiens (Human).
• Sequence Length: 365
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Involved in the presentation of foreign antigens to the immune system..
• Protein Sequence: MAVMAPRTLVLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLFGAVITGAVVAAVMWRRKSSDRKGGSYSQAASSDSAQGSDVSLTACKV

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
110	N-linked_Glycosylation	GTLRGYYNQSEAGSH HHHCCCCCCCCCCCC	30.34	19159218
135	Methylation	GSDWRFLRGYHQYAY CCCCHHHCCCEEEEE	40.69	115478757
145	Ubiquitination	HQYAYDGKDYIALKE EEEEECCCCEEEEHH	44.45	21890473
155	Methylation	IALKEDLRSWTAADM EEEHHHHHHCHHHHH	42.33	115478751
168	Ubiquitination	DMAAQTTKHKWEAAH HHHHHHCHHHHHHHH	46.72	21890473
188	Glutathionylation	RAYLEGTCVEWLRRY HHHHHCHHHHHHHHH	3.72	22555962
267	Methylation	AGDGTFQKWAAVVVP CCCCCEEEEEEEEEC	34.31	24623505
292	Ubiquitination	VQHEGLPKPLTLRWE EEECCCCCCEEEECC	58.67	21890473
344	Phosphorylation	SDRKGGSYSQAASSD CCCCCCCCCCCCCCC	14.21	1956339

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
337	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
343	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
344	Y	Phosphorylation	Kinase	SRC	P12931	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of 1A02_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 1A02_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UGGG1_HUMAN	UGGT1	physical	17353931
CD8A_HUMAN	CD8A	physical	9177355
CD8A_HUMAN	CD8A	physical	10809759
COPB_HUMAN	COPB1	physical	11884415
COPG1_HUMAN	COPG1	physical	11884415
TPSN_HUMAN	TAPBP	physical	11884415
TAP1_HUMAN	TAP1	physical	11884415
SYVN1_HUMAN	SYVN1	physical	21245296
UB2J1_HUMAN	UBE2J1	physical	21245296
DERL1_HUMAN	DERL1	physical	21245296
PSMD2_HUMAN	PSMD2	physical	21245296
MAGA4_HUMAN	MAGEA4	physical	21815906
BAP31_HUMAN	BCAP31	physical	17056546
B2MG_HUMAN	B2M	physical	8805302
STAT3_HUMAN	STAT3	physical	21988832
GNAS3_HUMAN	GNAS	physical	9914489
GNAS2_HUMAN	GNAS	physical	9914489
ALEX_HUMAN	GNAS	physical	9914489
GNAS1_HUMAN	GNAS	physical	9914489
BAG6_HUMAN	BAG6	physical	21636303
MEOX2_HUMAN	MEOX2	physical	24722188

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352 AND SER-356, ANDMASS SPECTROMETRY.
PubMed: 19413330

"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 SER-352 AND SER-356, ANDMASS SPECTROMETRY.
PubMed: 18088087