ITAX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ITAX_HUMAN
• UniProt AC: P20702
• Protein Name: Integrin alpha-X
• Gene Name: ITGAX
• Organism: Homo sapiens (Human).
• Sequence Length: 1163
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis..
• Protein Sequence: MTRTRAALLLFTALATSLGFNLDTEELTAFRVDSAGFGDSVVQYANSWVVVGAPQKITAANQTGGLYQCGYSTGACEPIGLQVPPEAVNMSLGLSLASTTSPSQLLACGPTVHHECGRNMYLTGLCFLLGPTQLTQRLPVSRQECPRQEQDIVFLIDGSGSISSRNFATMMNFVRAVISQFQRPSTQFSLMQFSNKFQTHFTFEEFRRSSNPLSLLASVHQLQGFTYTATAIQNVVHRLFHASYGARRDAAKILIVITDGKKEGDSLDYKDVIPMADAAGIIRYAIGVGLAFQNRNSWKELNDIASKPSQEHIFKVEDFDALKDIQNQLKEKIFAIEGTETTSSSSFELEMAQEGFSAVFTPDGPVLGAVGSFTWSGGAFLYPPNMSPTFINMSQENVDMRDSYLGYSTELALWKGVQSLVLGAPRYQHTGKAVIFTQVSRQWRMKAEVTGTQIGSYFGASLCSVDVDSDGSTDLVLIGAPHYYEQTRGGQVSVCPLPRGWRRWWCDAVLYGEQGHPWGRFGAALTVLGDVNGDKLTDVVIGAPGEEENRGAVYLFHGVLGPSISPSHSQRIAGSQLSSRLQYFGQALSGGQDLTQDGLVDLAVGARGQVLLLRTRPVLWVGVSMQFIPAEIPRSAFECREQVVSEQTLVQSNICLYIDKRSKNLLGSRDLQSSVTLDLALDPGRLSPRATFQETKNRSLSRVRVLGLKAHCENFNLLLPSCVEDSVTPITLRLNFTLVGKPLLAFRNLRPMLAADAQRYFTASLPFEKNCGADHICQDNLGISFSFPGLKSLLVGSNLELNAEVMVWNDGEDSYGTTITFSHPAGLSYRYVAEGQKQGQLRSLHLTCDSAPVGSQGTWSTSCRINHLIFRGGAQITFLATFDVSPKAVLGDRLLLTANVSSENNTPRTSKTTFQLELPVKYAVYTVVSSHEQFTKYLNFSESEEKESHVAMHRYQVNNLGQRDLPVSINFWVPVELNQEAVWMDVEVSHPQNPSLRCSSEKIAPPASDFLAHIQKNPVLDCSIAGCLRFRCDVPSFSVQEELDFTLKGNLSFGWVRQILQKKVSVVSVAEITFDTSVYSQLPGQEAFMRAQTTTVLEKYKVHNPTPLIVGSSIGGLLLLALITAVLYKVGFFKRQYKEMMEEANGQIAPENGTQTPSPPSEK

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
61	N-linked_Glycosylation	PQKITAANQTGGLYQ CCEEEEECCCCCEEE	37.17	20033057
89	N-linked_Glycosylation	QVPPEAVNMSLGLSL CCCHHHHCHHHCCCC	22.75	UniProtKB CARBOHYD
209	Phosphorylation	TFEEFRRSSNPLSLL CHHHHHHCCCHHHHH	30.15	22210691
210	Phosphorylation	FEEFRRSSNPLSLLA HHHHHHCCCHHHHHH	40.43	22210691
392	N-linked_Glycosylation	NMSPTFINMSQENVD CCCCCEEECCCCCCC	21.62	20033057
668	Phosphorylation	RSKNLLGSRDLQSSV CCCCCCCCCCCCCCC	23.69	-
673	Phosphorylation	LGSRDLQSSVTLDLA CCCCCCCCCCEEEEE	33.79	-
674	Phosphorylation	GSRDLQSSVTLDLAL CCCCCCCCCEEEEEC	13.22	-
697	N-linked_Glycosylation	ATFQETKNRSLSRVR CCHHHHCCCCCHHEE	46.31	20033057
735	N-linked_Glycosylation	TPITLRLNFTLVGKP CCEEEEEEEEEECCC	22.79	20033057
899	N-linked_Glycosylation	DRLLLTANVSSENNT CEEEEEEEECCCCCC	29.03	20033057
937	Phosphorylation	SHEQFTKYLNFSESE CHHHHHHHHCCCCCH	12.10	27251275
939	N-linked_Glycosylation	EQFTKYLNFSESEEK HHHHHHHCCCCCHHH	35.00	UniProtKB CARBOHYD
941	Phosphorylation	FTKYLNFSESEEKES HHHHHCCCCCHHHHH	38.86	27251275
943	Phosphorylation	KYLNFSESEEKESHV HHHCCCCCHHHHHHE	50.27	27251275
1050	N-linked_Glycosylation	LDFTLKGNLSFGWVR ECEEECCCCCHHHHH	30.81	UniProtKB CARBOHYD
1154	Phosphorylation	QIAPENGTQTPSPPS CCCCCCCCCCCCCCC	40.63	25072903
1156	Phosphorylation	APENGTQTPSPPSEK CCCCCCCCCCCCCCC	26.10	25072903
1158	Phosphorylation	ENGTQTPSPPSEK-- CCCCCCCCCCCCC--	53.48	25072903
1161	Phosphorylation	TQTPSPPSEK----- CCCCCCCCCC-----	62.49	25072903

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ITAX_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 ITAX_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ITAX_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• H00006: Hairy-cell leukemia
• 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

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-899, AND MASSSPECTROMETRY.
PubMed: 19159218